NCBI Conserved Domain Search

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

30-117

7.09e-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: 7.09e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829  30 PNPGRNLTVETQTTSSISLSWEVPDGLDSQNSNYWVQCTGDGGTT----ETRNTTATNVTVDGLGPGSLYTCSVWVEKDG 105
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                         90
                 ....*....|..
gi 612407829 106 VNSSVGTVTTAT 117
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 ...

670-902

1.37e-163

Pssm-ID: 350467 [Multi-domain] Cd Length: 233 Bit Score: 477.46 E-value: 1.37e-163

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 670 NRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRV 749
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 750 KCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWL 829
Cdd:cd14619   81 KCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQWL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612407829 830 DQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRFL 902
Cdd:cd14619  161 DQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

641-900

3.01e-116

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 355.81 E-value: 3.01e-116

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829   641 GFADEYQQL-SLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPgSDYINASFMPGLWSPQEFIATQGPLP 719
Cdd:smart00194   1 GLEEEFEKLdRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829   720 QTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLD-SQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSV 798
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829   799 RQFHYQAWPDHGVPSSPDTLLAFWRMLRQWldQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMR 878
Cdd:smart00194 160 THYHYTNWPDHGVPESPESILDLIRAVRKS--QSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237

                          250       260
                   ....*....|....*....|..
gi 612407829   879 ESRPLMVQTEAQYVFLHQCILR 900
Cdd:smart00194 238 SQRPGMVQTEEQYIFLYRAILE 259

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

666-899

1.10e-106

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 329.97 E-value: 1.10e-106

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829  666 NNAKNRYRNVLPYDWSRVPLKPihEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCME 745
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTG--DPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829  746 AGRVKCEHYWPLDS-QPCTHGHLRVTLVGEE-VMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWR 823
Cdd:pfam00102  79 KGREKCAQYWPEEEgESLEYGDFTVTLKKEKeDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612407829  824 MLRQWlDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:pfam00102 159 KVRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233

PHA02742

protein tyrosine phosphatase; Provisional

665-901

5.27e-42

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 155.93 E-value: 5.27e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 665 ENNAKNRYRNVLPYDWSRVPLKPihEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCM 744
Cdd:PHA02742  51 KNMKKCRYPDAPCFDRNRVILKI--EDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIM 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 745 EAGRVKCEHYW-PLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWR 823
Cdd:PHA02742 129 EDGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVL 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 824 MLRQwLDQTME---------GGPPI-VHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVF 893
Cdd:PHA02742 209 AVRE-ADLKADvdikgenivKEPPIlVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF 287


                 ....*...
gi 612407829 894 LHQCILRF 901
Cdd:PHA02742 288 CYFIVLIF 295

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

665-907

3.57e-39

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 147.16 E-value: 3.57e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 665 ENNAKNRYRNVLPYDWSRVplkpiheEPGSDYINASFMPGLwSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCM 744
Cdd:COG5599   41 NGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 745 EAG--RVKCEHYWPLDSQPCTHgHLRVTLVGEEV-MENWTVRELLLLQVEE-QKTLSVRQFHYQAWPDHGVPSSpDTLLA 820
Cdd:COG5599  113 EISkpKVKMPVYFRQDGEYGKY-EVSSELTESIQlRDGIEARTYVLTIKGTgQKKIEIPVLHVKNWPDHGAISA-EALKN 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 821 FWRMLRQWLD-QTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLgPFSF---VRKMRESR-PLMVQTEAQYVFLh 895
Cdd:COG5599  191 LADLIDKKEKiKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVQI-TLSVeeiVIDMRTSRnGGMVQTSEQLDVL- 268

                        250
                 ....*....|..
gi 612407829 896 qcILRFLQQSAQ 907
Cdd:COG5599  269 --VKLAEQQIRP 278

FN3

Fibronectin type 3 domain [General function prediction only];

85-509

8.12e-14

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 75.42 E-value: 8.12e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829  85 TVDGLGPGSLYTCSVWVEKDGVNSSVGTVTTATAPNPVRNLTVEAQTNSSIALTWEVPDGPDPQNSTYGVEYTGDGGRAG 164
Cdd:COG3401    7 TSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 165 TRSTAHTNITVDRLE----PGCLYVFSVWVGKNGINSSRETRNATTAPNPVRNLHMETQTNSSIALCWEVPDGPYPQDYT 240
Cdd:COG3401   87 APPTATGLTTLTGSGsvggATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 241 YWVEYTGDGGGTETRNTTNTSVT------AERLEPGTLYTFSVWAEKNGARGSRQN----VSISTVPNAVTSLSKQDWTN 310
Cdd:COG3401  167 GVVVSPDTSATAAVATTSLTVTSttlvdgGGDIEPGTTYYYRVAATDTGGESAPSNevsvTTPTTPPSAPTGLTATADTP 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 311 STIALRWTAPQGPGQSSY------SYWVSWVREGmtdpRTQSTSGTDitlKELEAGSLYHLTVWAE--RNEVRGYNSTLT 382
Cdd:COG3401  247 GSVTLSWDPVTESDATGYrvyrsnSGDGPFTKVA----TVTTTSYTD---TGLTNGTTYYYRVTAVdaAGNESAPSNVVS 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 383 AAT---APNEVTDLQNETQTKNSVMLWWKAPGDPHSQLY-VYwvqwaskghprRGQDPQANWVNQTSRTNETWYKVEALE 458
Cdd:COG3401  320 VTTdltPPAAPSGLTATAVGSSSITLSWTASSDADVTGYnVY-----------RSTSGGGTYTKIAETVTTTSYTDTGLT 388

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 612407829 459 PGTLYNFTVWAERNDVASSTQSLCASTYPDTVTITSCVSTSAGYGVNLIWS 509
Cdd:COG3401  389 PGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVA 439

FN3

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

208-286

4.24e-11

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 60.20 E-value: 4.24e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 208 PNPVRNLHMETQTNSSIALCWEVPDGPYPQDYTYWVEYTGDGGGT----ETRNTTNTSVTAERLEPGTLYTFSVWAEKNG 283
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                 ...
gi 612407829 284 ARG 286
Cdd:cd00063   81 GES 83

FN3

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...

208-280

2.93e-10

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: 57.62 E-value: 2.93e-10

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612407829   208 PNPVRNLHMETQTNSSIALCWEVPDGPYPQDYT--YWVEYTGDGGGTETRNTTN--TSVTAERLEPGTLYTFSVWAE 280
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIvgYRVEYREEGSEWKEVNVTPssTSYTLTGLKPGTEYEFRVRAV 77

FN3

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

30-117

7.09e-09

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 53.65 E-value: 7.09e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829  30 PNPGRNLTVETQTTSSISLSWEVPDGLDSQNSNYWVQCTGDGGTT----ETRNTTATNVTVDGLGPGSLYTCSVWVEKDG 105
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                         90
                 ....*....|..
gi 612407829 106 VNSSVGTVTTAT 117
Cdd:cd00063   81 GESPPSESVTVT 92

fn3

Fibronectin type III domain;

389-467

1.66e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 47.02 E-value: 1.66e-06

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612407829  389 EVTDLQNETQTKNSVMLWWKAPGDPHSQLYVYWVQWASKGHPRRgqdpqanWVNQTSRTNETWYKVEALEPGTLYNFTV 467
Cdd:pfam00041   2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEP-------WNEITVPGTTTSVTLTGLKPGTEYEVRV 73

FN3

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...

30-108

1.06e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 44.53 E-value: 1.06e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829    30 PNPGRNLTVETQTTSSISLSWEVP--DGLDSQNSNYWVQCTGDGGTTE--TRNTTATNVTVDGLGPGSLYTCSVWVEKDG 105
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPpdDGITGYIVGYRVEYREEGSEWKevNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                   ...
gi 612407829   106 VNS 108
Cdd:smart00060  81 GEG 83

fn3

Fibronectin type III domain;

28-99

4.75e-05

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 42.79 E-value: 4.75e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612407829   28 PAPnpgRNLTVETQTTSSISLSWEVPDGLDSQNSNYWVQCTGDGGTTETRNTTATN----VTVDGLGPGSLYTCSV 99
Cdd:pfam00041   1 SAP---SNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGtttsVTLTGLKPGTEYEVRV 73

Name

Accession

Description

Interval

E-value

R-PTPc-H

cd14619

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...

670-902

1.37e-163

Pssm-ID: 350467 [Multi-domain] Cd Length: 233 Bit Score: 477.46 E-value: 1.37e-163

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 670 NRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRV 749
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 750 KCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWL 829
Cdd:cd14619   81 KCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQWL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612407829 830 DQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRFL 902
Cdd:cd14619  161 DQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233

R3-PTPc

cd14548

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...

671-896

1.08e-142

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: 422.92 E-value: 1.08e-142

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 671 RYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVK 750
Cdd:cd14548    1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 751 CEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKtlSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLD 830
Cdd:cd14548   81 CDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVR--SVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIK 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612407829 831 QtmEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQ 896
Cdd:cd14548  159 Q--EKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

641-900

3.01e-116

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 355.81 E-value: 3.01e-116

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829   641 GFADEYQQL-SLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPgSDYINASFMPGLWSPQEFIATQGPLP 719
Cdd:smart00194   1 GLEEEFEKLdRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829   720 QTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLD-SQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSV 798
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829   799 RQFHYQAWPDHGVPSSPDTLLAFWRMLRQWldQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMR 878
Cdd:smart00194 160 THYHYTNWPDHGVPESPESILDLIRAVRKS--QSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237

                          250       260
                   ....*....|....*....|..
gi 612407829   879 ESRPLMVQTEAQYVFLHQCILR 900
Cdd:smart00194 238 SQRPGMVQTEEQYIFLYRAILE 259

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

666-899

1.10e-106

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 329.97 E-value: 1.10e-106

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829  666 NNAKNRYRNVLPYDWSRVPLKPihEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCME 745
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTG--DPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829  746 AGRVKCEHYWPLDS-QPCTHGHLRVTLVGEE-VMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWR 823
Cdd:pfam00102  79 KGREKCAQYWPEEEgESLEYGDFTVTLKKEKeDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612407829  824 MLRQWlDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:pfam00102 159 KVRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233

R-PTPc-V

cd14618

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...

670-899

1.24e-100

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: 313.80 E-value: 1.24e-100

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 670 NRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRV 749
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 750 KCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWL 829
Cdd:cd14618   81 LCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREHV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 830 DQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:cd14618  161 QATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230

R-PTPc-J

cd14615

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...

670-899

1.08e-96

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: 303.28 E-value: 1.08e-96

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 670 NRYRNVLPYDWSRVPLKpIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRV 749
Cdd:cd14615    1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 750 KCEHYWPlDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWL 829
Cdd:cd14615   80 KCEEYWP-SKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYM 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 830 DQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:cd14615  159 KQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCAL 228

PTPc

cd00047

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...

696-896

4.72e-91

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: 287.26 E-value: 4.72e-91

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLD-SQPCTHGHLRVTLVGE 774
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEgGKPLEYGDITVTLVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 775 EVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTmeGGPPIVHCSAGVGRTGTLIA 854
Cdd:cd00047   81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKP--NGPIVVHCSAGVGRTGTFIA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 612407829 855 LDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQ 896
Cdd:cd00047  159 IDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200

R-PTPc-B

cd14617

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...

670-896

3.76e-89

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: 283.35 E-value: 3.76e-89

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 670 NRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRV 749
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 750 KCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQvEEQKTLS--VRQFHYQAWPDHGVPSSPDTLLAFWRMLRQ 827
Cdd:cd14617   81 KCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKICS-EEQLDAPrlVRHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612407829 828 WLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQ 896
Cdd:cd14617  160 YINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228

R-PTPc-LAR-1

cd14553

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...

666-899

7.29e-88

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: 280.44 E-value: 7.29e-88

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 666 NNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCME 745
Cdd:cd14553    3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 746 AGRVKCEHYWPLDSQPcTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRML 825
Cdd:cd14553   83 RSRVKCDQYWPTRGTE-TYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRV 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612407829 826 RQWldQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:cd14553  162 KAC--NPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALL 233

R-PTPc-O

cd14614

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...

666-899

6.16e-87

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: 277.93 E-value: 6.16e-87

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 666 NNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCME 745
Cdd:cd14614   12 NRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 746 AGRVKCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEqkTLSVRQFHYQAWPDHGVPS--SPDTLLAFWR 823
Cdd:cd14614   92 KRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADE--VQDVMHFNYTAWPDHGVPTanAAESILQFVQ 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612407829 824 MLRQWLDQTMegGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:cd14614  170 MVRQQAVKSK--GPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQ 243

PTPc-N9

cd14543

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...

641-895

5.42e-80

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: 260.37 E-value: 5.42e-80

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 641 GFADEYQQLSLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQ 720
Cdd:cd14543    4 GIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 721 TVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPC-THGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVR 799
Cdd:cd14543   84 TYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSlRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVT 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 800 QFHYQAWPDHGVPSSPDTLLAFWRMLRQ---WLDQTM-------EGGPPI-VHCSAGVGRTGTLIALDVLLRQLQSEGLL 868
Cdd:cd14543  164 HFQFTSWPDFGVPSSAAALLDFLGEVRQqqaLAVKAMgdrwkghPPGPPIvVHCSAGIGRTGTFCTLDICLSQLEDVGTL 243

                        250       260
                 ....*....|....*....|....*..
gi 612407829 869 GPFSFVRKMRESRPLMVQTEAQYVFLH 895
Cdd:cd14543  244 NVMQTVRRMRTQRAFSIQTPDQYYFCY 270

R5-PTPc-1

cd14549

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...

696-895

4.14e-79

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: 255.35 E-value: 4.14e-79

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPcTHGHLRVTLVGEE 775
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTE-TYGNIQVTLLSTE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 776 VMENWTVRELLLLQVEEQKTLS------VRQFHYQAWPDHGVPSSPDTLLAFWRmlRQWLDQTMEGGPPIVHCSAGVGRT 849
Cdd:cd14549   80 VLATYTVRTFSLKNLKLKKVKGrsservVYQYHYTQWPDHGVPDYTLPVLSFVR--KSSAANPPGAGPIVVHCSAGVGRT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 612407829 850 GTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLH 895
Cdd:cd14549  158 GTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203

R-PTPc-F-1

cd14626

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...

626-899

7.41e-76

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: 249.57 E-value: 7.41e-76

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 626 DFADHVRKNERDSNCGFADEYQQLSlVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGL 705
Cdd:cd14626    2 DLADNIERLKANDGLKFSQEYESID-PGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 706 WSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPcTHGHLRVTLVGEEVMENWTVREL 785
Cdd:cd14626   81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTE-TYGMIQVTLLDTVELATYSVRTF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 786 LLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWldQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSE 865
Cdd:cd14626  160 ALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKAC--NPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHE 237

                        250       260       270
                 ....*....|....*....|....*....|....
gi 612407829 866 GLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:cd14626  238 KTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALL 271

R-PTPc-Q

cd14616

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...

670-896

2.34e-74

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: 243.66 E-value: 2.34e-74

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 670 NRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRV 749
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 750 KCEHYWPLDSQPCT-HGHLRVTLVGEEVMENWTVRElllLQVEEQ-KTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQ 827
Cdd:cd14616   81 RCHQYWPEDNKPVTvFGDIVITKLMEDVQIDWTIRD---LKIERHgDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRA 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612407829 828 wlDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQ 896
Cdd:cd14616  158 --SRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224

R-PTPc-D-1

cd14624

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...

622-899

3.82e-71

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: 236.94 E-value: 3.82e-71

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 622 IPAEDFADHVRKNERDSNCGFADEYQQLSlVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASF 701
Cdd:cd14624    4 IPILELADHIERLKANDNLKFSQEYESID-PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 702 MPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPcTHGHLRVTLVGEEVMENWT 781
Cdd:cd14624   83 IDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTE-TYGLIQVTLLDTVELATYC 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 782 VRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWldQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQ 861
Cdd:cd14624  162 VRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTC--NPPDAGPMVVHCSAGVGRTGCFIVIDAMLER 239

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 612407829 862 LQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:cd14624  240 IKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALL 277

R-PTPc-T-1

cd14630

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...

665-899

5.11e-71

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: 234.92 E-value: 5.11e-71

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 665 ENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCM 744
Cdd:cd14630    2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 745 EAGRVKCEHYWPLDSQpcTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRM 824
Cdd:cd14630   82 EVGRVKCVRYWPDDTE--VYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQ 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612407829 825 LRqWLDQTmEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:cd14630  160 VK-FLNPP-DAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAIL 232

PTPc-N11_6

cd14544

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...

666-903

1.84e-70

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: 233.89 E-value: 1.84e-70

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 666 NNAKNRYRNVLPYDWSRVPLKPI-HEEPGSDYINASF-MPGLWSPQE------FIATQGPLPQTVGDFWRLVWEQQSHTL 737
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDRdPNVPGSDYINANYiRNENEGPTTdenaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 738 VMLTNCMEAGRVKCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTL-SVRQFHYQAWPDHGVPSSPD 816
Cdd:cd14544   81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPIrEIWHYQYLSWPDHGVPSDPG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 817 TLLAFWRMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSF---VRKMRESRPLMVQTEAQYVF 893
Cdd:cd14544  161 GVLNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIqktIQMVRSQRSGMVQTEAQYKF 240

                        250
                 ....*....|
gi 612407829 894 LHQCILRFLQ 903
Cdd:cd14544  241 IYVAVAQYIE 250

R-PTP-LAR-2

cd14554

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...

661-899

6.44e-70

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: 232.03 E-value: 6.44e-70

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 661 ASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVML 740
Cdd:cd14554    1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 741 TNCMEAGRVKCEHYWPLDsQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLA 820
Cdd:cd14554   81 TKLREMGREKCHQYWPAE-RSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFID 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612407829 821 FWRMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:cd14554  160 FIGQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238

PTPc-N18

cd14603

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...

657-898

9.65e-70

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: 232.41 E-value: 9.65e-70

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 657 SQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHT 736
Cdd:cd14603   21 STVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 737 LVMLTNCMEAGRVKCEHYWPLDSQPCTHGHLRVTLVGEE-VMENWTVRELLLLQVEEQKtlSVRQFHYQAWPDHGVPSSP 815
Cdd:cd14603  101 ILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKrLNEEVILRTLKVTFQKESR--SVSHFQYMAWPDHGIPDSP 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 816 DTLLAFWRMLRQWldQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSF---VRKMRESRPLMVQTEAQYV 892
Cdd:cd14603  179 DCMLAMIELARRL--QGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIfdvVLEMRKQRPAAVQTEEQYE 256


                 ....*.
gi 612407829 893 FLHQCI 898
Cdd:cd14603  257 FLYHTV 262

PTP_fungal

cd18533

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...

696-896

4.27e-69

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: 228.67 E-value: 4.27e-69

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFM-PGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPCTHGHLRVTLVGE 774
Cdd:cd18533    1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 775 EV--MENWTVRELLLlQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTMEGGPPIVHCSAGVGRTGTL 852
Cdd:cd18533   81 EEndDGGFIVREFEL-SKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHCSAGVGRTGTF 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 612407829 853 IALDVLLRQLQSEGLLGP---------FSFVRKMRESRPLMVQTEAQYVFLHQ 896
Cdd:cd18533  160 IALDSLLDELKRGLSDSQdledsedpvYEIVNQLRKQRMSMVQTLRQYIFLYD 212

R-PTPc-S-1

cd14625

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...

622-899

4.80e-69

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: 231.14 E-value: 4.80e-69

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 622 IPAEDFADHVRKNERDSNCGFADEYQQLSlVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASF 701
Cdd:cd14625    4 IPISELAEHTERLKANDNLKLSQEYESID-PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 702 MPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPlDSQPCTHGHLRVTLVGEEVMENWT 781
Cdd:cd14625   83 IDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWP-SRGTETYGMIQVTLLDTIELATFC 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 782 VRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWldQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQ 861
Cdd:cd14625  162 VRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTC--NPPDAGPIVVHCSAGVGRTGCFIVIDAMLER 239

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 612407829 862 LQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:cd14625  240 IKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALL 277

R-PTPc-M-1

cd14633

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...

626-899

7.18e-69

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: 230.31 E-value: 7.18e-69

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 626 DFADHVRKNERDSNCGFADEYQQLsLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGL 705
Cdd:cd14633    1 DLLQHITQMKCAEGYGFKEEYESF-FEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 706 WSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQpcTHGHLRVTLVGEEVMENWTVREL 785
Cdd:cd14633   80 HRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTE--IYKDIKVTLIETELLAEYVIRTF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 786 LLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQwlDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSE 865
Cdd:cd14633  158 AVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS--KSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAERE 235

                        250       260       270
                 ....*....|....*....|....*....|....
gi 612407829 866 GLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:cd14633  236 GVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAIL 269

R-PTPc-A-1

cd14621

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...

622-899

1.44e-68

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: 230.30 E-value: 1.44e-68

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 622 IPAEDFADHVRKNERDSNCGFADEYQQLSLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASF 701
Cdd:cd14621    8 LPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 702 MPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPldSQPC-THGHLRVTLVGEEVMENW 780
Cdd:cd14621   88 INGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWP--DQGCwTYGNIRVSVEDVTVLVDY 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 781 TVRELLLLQV----EEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTmeGGPPIVHCSAGVGRTGTLIALD 856
Cdd:cd14621  166 TVRKFCIQQVgdvtNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQY--AGAIVVHCSAGVGRTGTFIVID 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 612407829 857 VLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:cd14621  244 AMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALL 286

PTPc-N13

cd14597

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...

665-902

3.51e-68

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: 227.02 E-value: 3.51e-68

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 665 ENNAKNRYRNVLPYDWSRVPLKPIHeepgsDYINASFMPGLWSPQEF--IATQGPLPQTVGDFWRLVWEQQSHTLVMLTN 742
Cdd:cd14597    2 ENRKKNRYKNILPYDTTRVPLGDEG-----GYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 743 CMEAGRVKCEHYWP--LDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLA 820
Cdd:cd14597   77 EVEGGKIKCQRYWPeiLGKTTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 821 FWRMLRqwldQTMEGGPPIVHCSAGVGRTGTLIALDVLLrQLQSEGLLGPFS-FVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:cd14597  157 FISYMR----HIHKSGPIITHCSAGIGRSGTLICIDVVL-GLISKDLDFDISdIVRTMRLQRHGMVQTEDQYIFCYQVIL 231


                 ...
gi 612407829 900 RFL 902
Cdd:cd14597  232 YVL 234

PTPc-N3

cd14600

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...

661-900

4.10e-68

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: 228.20 E-value: 4.10e-68

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 661 ASASENNAKNRYRNVLPYDWSRVPLkpiheEPGSDYINASFM----PGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHT 736
Cdd:cd14600   35 AKLPQNMDKNRYKDVLPYDATRVVL-----QGNEDYINASYVnmeiPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 737 LVMLTNCMEAGRVKCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPD 816
Cdd:cd14600  110 IVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSS 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 817 TLLAFWRMLRQwldQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQ 896
Cdd:cd14600  190 DFLEFVNYVRS---KRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCE 266


                 ....
gi 612407829 897 CILR 900
Cdd:cd14600  267 AILR 270

PTPc-KIM

cd14547

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...

670-896

2.97e-66

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: 221.50 E-value: 2.97e-66

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 670 NRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGlWSPQE--FIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAg 747
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRG-YDGEEkaYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 748 RVKCEHYWPlDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKtlSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQ 827
Cdd:cd14547   79 KEKCAQYWP-EEENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKR--YLKHYWYTSWPDHKTPEAAQPLLSLVQEVEE 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612407829 828 WLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQ 896
Cdd:cd14547  156 ARQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224

R-PTPc-E-1

cd14620

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...

672-899

7.26e-66

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: 220.58 E-value: 7.26e-66

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 672 YRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKC 751
Cdd:cd14620    1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 752 EHYWPldSQPC-THGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVR---QFHYQAWPDHGVPSSPDTLLAFWRMLRQ 827
Cdd:cd14620   81 YQYWP--DQGCwTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCKAPRlvtQLHFTSWPDFGVPFTPIGMLKFLKKVKS 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612407829 828 WldQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:cd14620  159 V--NPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228

R-PTPc-G-1

cd17667

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...

642-899

8.41e-66

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: 222.22 E-value: 8.41e-66

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 642 FADEYQQlslVGHSQSQMVASAS-----ENNAKNRYRNVLPYDWSRVPLKPI--HEEPGSDYINASFMPGLWSPQEFIAT 714
Cdd:cd17667    1 FSEDFEE---VQRCTADMNITAEhsnhpDNKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIAT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 715 QGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPcTHGHLRVTLVGEEVMENWTVRELLLLQVEEQK 794
Cdd:cd17667   78 QGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE-EYGNIIVTLKSTKIHACYTVRRFSIRNTKVKK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 795 TL-----------SVRQFHYQAWPDHGVPSSPDTLLAFWRmlRQWLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQ 863
Cdd:cd17667  157 GQkgnpkgrqnerTVIQYHYTQWPDMGVPEYALPVLTFVR--RSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIK 234

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 612407829 864 SEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:cd17667  235 DKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALL 270

PTPc-N3_4

cd14541

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...

695-900

2.53e-64

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: 215.66 E-value: 2.53e-64

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 695 DYINASF----MPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPCTHGHLRVT 770
Cdd:cd14541    1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 771 LVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTMEggPPIVHCSAGVGRTG 850
Cdd:cd14541   81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVE--PTVVHCSAGIGRTG 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 612407829 851 TLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILR 900
Cdd:cd14541  159 VLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILR 208

PTPc-N20_13

cd14538

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...

696-902

4.35e-64

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

Pssm-ID: 350386 [Multi-domain] Cd Length: 207 Bit Score: 214.55 E-value: 4.35e-64

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFM--PGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWP--LDSQPCTHGHLRVTL 771
Cdd:cd14538    1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdsLNKPLICGGRLEVSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 772 VGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDqtmeGGPPIVHCSAGVGRTGT 851
Cdd:cd14538   81 EKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHN----SGPIVVHCSAGIGRTGV 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 612407829 852 LIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRFL 902
Cdd:cd14538  157 LITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207

PTPc-N1_2

cd14545

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...

669-893

2.86e-63

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: 213.41 E-value: 2.86e-63

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 669 KNRYRNVLPYDWSRVPLKpIHEEpGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGR 748
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVK-LKQG-DNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 749 VKCEHYWPLDSQP---CTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRML 825
Cdd:cd14545   79 IKCAQYWPQGEGNamiFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKV 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612407829 826 RQWLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGpfSFVRK----MRESRPLMVQTEAQYVF 893
Cdd:cd14545  159 RESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPSS--VDVKKvlleMRKYRMGLIQTPDQLRF 228

R-PTP-D-2

cd14628

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...

621-902

1.30e-62

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: 213.82 E-value: 1.30e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 621 DIPAEDFADHVRKNER----DSNCGFADEYQQL-SLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSD 695
Cdd:cd14628    2 EVPARNLYAYIQKLTQietgENVTGMELEFKRLaSSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDsQPCTHGHLRVTLVGEE 775
Cdd:cd14628   82 YINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAE-RSARYQYFVVDPMAEY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 776 VMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIAL 855
Cdd:cd14628  161 NMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITL 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 612407829 856 DVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRFL 902
Cdd:cd14628  241 SIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYL 287

R-PTPc-K-1

cd14631

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...

682-899

1.70e-62

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: 210.65 E-value: 1.70e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 682 RVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQp 761
Cdd:cd14631    1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTE- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 762 cTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRqwLDQTMEGGPPIVH 841
Cdd:cd14631   80 -VYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVK--LSNPPSAGPIVVH 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 612407829 842 CSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:cd14631  157 CSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214

R-PTPc-typeIIb-1

cd14555

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...

696-899

2.16e-62

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: 210.16 E-value: 2.16e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQpcTHGHLRVTLVGEE 775
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTE--VYGDIKVTLVETE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 776 VMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRqwLDQTMEGGPPIVHCSAGVGRTGTLIAL 855
Cdd:cd14555   79 PLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVK--ASNPPSAGPIVVHCSAGAGRTGCYIVI 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 612407829 856 DVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:cd14555  157 DIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200

PTPc-N11

cd14605

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...

665-903

4.65e-62

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: 211.03 E-value: 4.65e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 665 ENNAKNRYRNVLPYDWSRVPLkpiHE----EPGSDYINASF-MPGLWS-------PQEFIATQGPLPQTVGDFWRLVWEQ 732
Cdd:cd14605    1 ENKNKNRYKNILPFDHTRVVL---HDgdpnEPVSDYINANIiMPEFETkcnnskpKKSYIATQGCLQNTVNDFWRMVFQE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 733 QSHTLVMLTNCMEAGRVKCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKT-LSVRQFHYQAWPDHGV 811
Cdd:cd14605   78 NSRVIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGNTeRTVWQYHFRTWPDHGV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 812 PSSPDTLLAFWRMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGL---LGPFSFVRKMRESRPLMVQTE 888
Cdd:cd14605  158 PSDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTE 237

                        250
                 ....*....|....*
gi 612407829 889 AQYVFLHQCILRFLQ 903
Cdd:cd14605  238 AQYRFIYMAVQHYIE 252

PTPc-N12

cd14604

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...

665-904

5.47e-62

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: 212.49 E-value: 5.47e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 665 ENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCM 744
Cdd:cd14604   56 ENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREF 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 745 EAGRVKCEHYWPL-DSQPCTHGHLRVTLVGEEVMENWTVRELLllqVE-EQKTLSVRQFHYQAWPDHGVPSSPDTLLAFW 822
Cdd:cd14604  136 EMGRKKCERYWPLyGEEPMTFGPFRISCEAEQARTDYFIRTLL---LEfQNETRRLYQFHYVNWPDHDVPSSFDSILDMI 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 823 RMLRQWldQTMEGGPPIVHCSAGVGRTGTLIALDV---LLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:cd14604  213 SLMRKY--QEHEDVPICIHCSAGCGRTGAICAIDYtwnLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIA 290


                 ....*
gi 612407829 900 RFLQQ 904
Cdd:cd14604  291 QLFEK 295

R-PTP-S-2

cd14627

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...

621-902

7.77e-62

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: 211.52 E-value: 7.77e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 621 DIPAEDFADHVRKNER----DSNCGFADEYQQLS-LVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSD 695
Cdd:cd14627    3 EVPARNLYSYIQKLAQvevgEHVTGMELEFKRLAnSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDsQPCTHGHLRVTLVGEE 775
Cdd:cd14627   83 YINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAE-RSARYQYFVVDPMAEY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 776 VMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIAL 855
Cdd:cd14627  162 NMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITL 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 612407829 856 DVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRFL 902
Cdd:cd14627  242 SIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288

R-PTP-F-2

cd14629

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...

621-902

1.94e-61

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: 210.74 E-value: 1.94e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 621 DIPAEDFADHVRKNER----DSNCGFADEYQQL-SLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSD 695
Cdd:cd14629    3 EVPARNLYAHIQKLTQvppgESVTAMELEFKLLaNSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDsQPCTHGHLRVTLVGEE 775
Cdd:cd14629   83 YINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAE-RSARYQYFVVDPMAEY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 776 VMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIAL 855
Cdd:cd14629  162 NMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITL 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 612407829 856 DVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRFL 902
Cdd:cd14629  242 SIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYL 288

PTPc-N22

cd14602

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...

669-899

5.27e-61

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: 207.39 E-value: 5.27e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 669 KNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGR 748
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 749 VKCEHYWP-LDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTlsVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQ 827
Cdd:cd14602   81 KKCERYWAePGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRT--IYQFHYKNWPDHDVPSSIDPILELIWDVRC 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612407829 828 WldQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQsEGLL----GPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:cd14602  159 Y--QEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAVI 231

PTPc-N6

cd14606

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...

665-903

1.20e-60

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: 207.43 E-value: 1.20e-60

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 665 ENNAKNRYRNVLPYDWSRVPLKPIHEE-PGSDYINASFMPG-LWSPQE----FIATQGPLPQTVGDFWRLVWEQQSHTLV 738
Cdd:cd14606   17 ENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVKNqLLGPDEnaktYIASQGCLEATVNDFWQMAWQENSRVIV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 739 MLTNCMEAGRVKCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEE-QKTLSVRQFHYQAWPDHGVPSSPDT 817
Cdd:cd14606   97 MTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNgELIREIWHYQYLSWPDHGVPSEPGG 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 818 LLAFWRMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSF---VRKMRESRPLMVQTEAQYVFL 894
Cdd:cd14606  177 VLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIqktIQMVRAQRSGMVQTEAQYKFI 256


                 ....*....
gi 612407829 895 HQCILRFLQ 903
Cdd:cd14606  257 YVAIAQFIE 265

PTPc-N22_18_12

cd14542

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...

696-896

1.94e-60

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: 204.58 E-value: 1.94e-60

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPC-THGHLRVTLVGE 774
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlQFGPFKISLEKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 775 EVM-ENWTVRELLLLQVEEQKTlsVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWldQTMEGGPPIVHCSAGVGRTGTLI 853
Cdd:cd14542   81 KRVgPDFLIRTLKVTFQKESRT--VYQFHYTAWPDHGVPSSVDPILDLVRLVRDY--QGSEDVPICVHCSAGCGRTGTIC 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 612407829 854 ALDVLLRQLQSEGL---LGPFSFVRKMRESRPLMVQTEAQYVFLHQ 896
Cdd:cd14542  157 AIDYVWNLLKTGKIpeeFSLFDLVREMRKQRPAMVQTKEQYELVYR 202

R-PTPc-C-1

cd14557

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...

696-896

2.37e-60

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: 204.29 E-value: 2.37e-60

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWP-LDSQPCTHGHLRVTLVGE 774
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsMEEGSRAFGDVVVKINEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 775 EVMENWTVRELLLLQVEEQKT-LSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWldQTMEGGPPIVHCSAGVGRTGTLI 853
Cdd:cd14557   81 KICPDYIIRKLNINNKKEKGSgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAF--NNFFSGPIVVHCSAGVGRTGTYI 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 612407829 854 ALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQ 896
Cdd:cd14557  159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201

R-PTPc-A-E-1

cd14551

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...

696-896

6.86e-60

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: 202.84 E-value: 6.86e-60

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPlDSQPCTHGHLRVTLVGEE 775
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP-DQGCWTYGNLRVRVEDTV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 776 VMENWTVRELLLLQV----EEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLdqTMEGGPPIVHCSAGVGRTGT 851
Cdd:cd14551   80 VLVDYTTRKFCIQKVnrgiGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSAN--PPRAGPIVVHCSAGVGRTGT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 612407829 852 LIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQ 896
Cdd:cd14551  158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202

R-PTPc-U-1

cd14632

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...

696-899

1.14e-59

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: 202.59 E-value: 1.14e-59

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQpcTHGHLRVTLVGEE 775
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSD--TYGDIKITLLKTE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 776 VMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQwlDQTMEGGPPIVHCSAGVGRTGTLIAL 855
Cdd:cd14632   79 TLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKA--STPPDAGPVVVHCSAGAGRTGCYIVL 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 612407829 856 DVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:cd14632  157 DVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200

R-PTPc-A-E-2

cd14552

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...

696-898

2.42e-57

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

Pssm-ID: 350400 [Multi-domain] Cd Length: 202 Bit Score: 195.95 E-value: 2.42e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQpCTHGHLRVTLVGEE 775
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGS-VSSGDITVELKDQT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 776 VMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTmeGGPPI-VHCSAGVGRTGTLIA 854
Cdd:cd14552   80 DYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQS--GNHPItVHCSAGAGRTGTFCA 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 612407829 855 LDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCI 898
Cdd:cd14552  158 LSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201

R-PTPc-A-2

cd14623

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...

671-898

3.60e-57

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: 196.42 E-value: 3.60e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 671 RYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVK 750
Cdd:cd14623    1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 751 CEHYWPLDSQpCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQwlD 830
Cdd:cd14623   81 CAQYWPSDGS-VSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQK--Q 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612407829 831 QTMEGGPPI-VHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCI 898
Cdd:cd14623  158 QQQSGNHPItVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226

R-PTPc-E-2

cd14622

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...

695-901

3.89e-57

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: 195.61 E-value: 3.89e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 695 DYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQpCTHGHLRVTLVGE 774
Cdd:cd14622    1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGS-VTHGEITIEIKND 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 775 EVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTmeGGPPI-VHCSAGVGRTGTLI 853
Cdd:cd14622   80 TLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQT--GNHPIvVHCSAGAGRTGTFI 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 612407829 854 ALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRF 901
Cdd:cd14622  158 ALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205

R-PTPc-Z-1

cd17668

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...

696-899

2.45e-56

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: 193.27 E-value: 2.45e-56

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPcTHGHLRVTLVGEE 775
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE-EYGNFLVTQKSVQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 776 VMENWTVRELLLLQVE----EQKTLS----VRQFHYQAWPDHGVPSSPDTLLAFWRMLRQwlDQTMEGGPPIVHCSAGVG 847
Cdd:cd17668   80 VLAYYTVRNFTLRNTKikkgSQKGRPsgrvVTQYHYTQWPDMGVPEYTLPVLTFVRKASY--AKRHAVGPVVVHCSAGVG 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 612407829 848 RTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:cd17668  158 RTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209

PTPc-N1

cd14608

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...

642-893

2.77e-56

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: 195.63 E-value: 2.77e-56

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 642 FADEYQQLSlvgHSQSQM---VASASENNAKNRYRNVLPYDWSRVPLkpiHEEpGSDYINASFMPGLWSPQEFIATQGPL 718
Cdd:cd14608    1 WAAIYQDIR---HEASDFpcrVAKLPKNKNRNRYRDVSPFDHSRIKL---HQE-DNDYINASLIKMEEAQRSYILTQGPL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 719 PQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQP---CTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKT 795
Cdd:cd14608   74 PNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKemiFEDTNLKLTLISEDIKSYYTVRQLELENLTTQET 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 796 LSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIALD---VLLRQLQSEGLLGPFS 872
Cdd:cd14608  154 REILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADtclLLMDKRKDPSSVDIKK 233

                        250       260
                 ....*....|....*....|.
gi 612407829 873 FVRKMRESRPLMVQTEAQYVF 893
Cdd:cd14608  234 VLLEMRKFRMGLIQTADQLRF 254

R-PTP-C-2

cd14558

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...

696-895

2.19e-54

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

Pssm-ID: 350406 [Multi-domain] Cd Length: 203 Bit Score: 187.60 E-value: 2.19e-54

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQpcTHGHLRVTLVGEE 775
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKK--TYGDIEVELKDTE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 776 VMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTMEGG----PPIVHCSAGVGRTGT 851
Cdd:cd14558   79 KSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSKHgrsvPIVVHCSDGSSRTGI 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 612407829 852 LIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLH 895
Cdd:cd14558  159 FCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202

PTPc-N2

cd14607

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...

654-898

3.24e-54

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: 189.02 E-value: 3.24e-54

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 654 HSQSQMVASASENNAKNRYRNVLPYDWSRVPLkpihEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQ 733
Cdd:cd14607   12 HDYPHRVAKYPENRNRNRYRDVSPYDHSRVKL----QNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 734 SHTLVMLTNCMEAGRVKCEHYWPLDSQPC---THGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHG 810
Cdd:cd14607   88 TKAVVMLNRIVEKDSVKCAQYWPTDEEEVlsfKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWPDFG 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 811 VPSSPDTLLAFWRMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEgllGPFSFVRK-----MRESRPLMV 885
Cdd:cd14607  168 VPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKK---DPDSVDIKqvlldMRKYRMGLI 244

                        250
                 ....*....|...
gi 612407829 886 QTEAQYVFLHQCI 898
Cdd:cd14607  245 QTPDQLRFSYMAV 257

PTPc-N20

cd14596

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...

696-903

1.71e-53

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: 185.34 E-value: 1.71e-53

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASF--MPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLD-SQPCTHGHLRVTLV 772
Cdd:cd14596    1 YINASYitMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETlQEPMELENYQLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 773 GEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRqwldQTMEGGPPIVHCSAGVGRTGTL 852
Cdd:cd14596   81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMR----KVHNTGPIVVHCSAGIGRAGVL 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 612407829 853 IALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRFLQ 903
Cdd:cd14596  157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207

PTPc-N4

cd14601

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...

695-904

7.37e-52

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: 180.91 E-value: 7.37e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 695 DYINASFM----PGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPCTHGHLRVT 770
Cdd:cd14601    1 DYINANYInmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 771 LVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTMEggPPIVHCSAGVGRTG 850
Cdd:cd14601   81 CHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDE--PVVVHCSAGIGRTG 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 612407829 851 TLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRFLQQ 904
Cdd:cd14601  159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYEE 212

R-PTP-N2

cd14610

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...

629-893

3.27e-51

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: 181.79 E-value: 3.27e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 629 DHVRKNERdsncgFADEYQQL-SLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINAS-FMPGLW 706
Cdd:cd14610   11 DHLKNKNR-----LEKEWEALcAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASpIMDHDP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 707 SPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPCTHGHlRVTLVGEEV-MENWTVREL 785
Cdd:cd14610   86 RNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIY-EVNLVSEHIwCEDFLVRSF 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 786 LLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFwrmlRQWLDQTMEGG--PPIVHCSAGVGRTGTLIALDVLLRQL- 862
Cdd:cd14610  165 YLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDF----RRKVNKCYRGRscPIIVHCSDGAGRSGTYILIDMVLNKMa 240

                        250       260       270
                 ....*....|....*....|....*....|.
gi 612407829 863 QSEGLLGPFSFVRKMRESRPLMVQTEAQYVF 893
Cdd:cd14610  241 KGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 271

R-PTP-N

cd14609

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...

629-893

8.24e-51

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: 180.62 E-value: 8.24e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 629 DHVRKNERdsncgFADEYQQLSLVGHSQSQMVASASENN-AKNRYRNVLPYDWSRVPLKPIHEEPGSDYINAS------- 700
Cdd:cd14609    9 DHLRNRDR-----LAKEWQALCAYQAEPNTCSTAQGEANvKKNRNPDFVPYDHARIKLKAESNPSRSDYINASpiiehdp 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 701 FMPGlwspqeFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPCTHGHlRVTLVGEEV-MEN 779
Cdd:cd14609   84 RMPA------YIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIY-EVNLVSEHIwCED 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 780 WTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFwrmlRQWLDQTMEGG--PPIVHCSAGVGRTGTLIALDV 857
Cdd:cd14609  157 FLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDF----RRKVNKCYRGRscPIIVHCSDGAGRTGTYILIDM 232

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 612407829 858 LLRQLqSEGL--LGPFSFVRKMRESRPLMVQTEAQYVF 893
Cdd:cd14609  233 VLNRM-AKGVkeIDIAATLEHVRDQRPGMVRTKDQFEF 269

PTPc-N7

cd14612

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...

668-895

8.85e-50

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: 176.18 E-value: 8.85e-50

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 668 AKNRYRNVLPYDWSRVPLK-PIHEEPGSDYINASFMPGL-WSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCME 745
Cdd:cd14612   17 SKDRYKTILPNPQSRVCLRrAGSQEEEGSYINANYIRGYdGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 746 aGRVKCEHYWPldSQPCTHGHLRVTLVGEEVMENWTVRELLLlQVEEQKTlSVRQFHYQAWPDHGVPSSPDTLLAFWRML 825
Cdd:cd14612   97 -KKEKCVHYWP--EKEGTYGRFEIRVQDMKECDGYTIRDLTI-QLEEESR-SVKHYWFSSWPDHQTPESAGPLLRLVAEV 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 826 RQWLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLH 895
Cdd:cd14612  172 EESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241

PTPc-N21_14

cd14540

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...

696-902

1.18e-47

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.

Pssm-ID: 350388 [Multi-domain] Cd Length: 219 Bit Score: 169.17 E-value: 1.18e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFMPGLWSPQE--FIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPC---THGHLRVT 770
Cdd:cd14540    1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHdalTFGEYKVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 771 LVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFW---RMLRQWLDQTMEG---GPPI-VHCS 843
Cdd:cd14540   81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLeeiNSVRRHTNQDVAGhnrNPPTlVHCS 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 612407829 844 AGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRFL 902
Cdd:cd14540  161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219

PTPc-N14

cd14599

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...

645-903

2.32e-47

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: 170.95 E-value: 2.32e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 645 EYQQLSLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPgSDYINASFMPGLWSPQE--FIATQGPLPQTV 722
Cdd:cd14599   17 EYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENN-TGYINASHIKVTVGGEEwhYIATQGPLPHTC 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 723 GDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWP-LDSQ--PCTHGHLRVTL-----VGEEVMENWTVRELLLLQveeQK 794
Cdd:cd14599   96 HDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPkLGSKhsSATYGKFKVTTkfrtdSGCYATTGLKVKHLLSGQ---ER 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 795 TlsVRQFHYQAWPDHGVPSSPDTLLAFW-------RMLRQWLDQTMEGGPPIV-HCSAGVGRTGTLIALDVLLRQLQSEG 866
Cdd:cd14599  173 T--VWHLQYTDWPDHGCPEEVQGFLSYLeeiqsvrRHTNSMLDSTKNCNPPIVvHCSAGVGRTGVVILTELMIGCLEHNE 250

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 612407829 867 LLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRFLQ 903
Cdd:cd14599  251 KVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287

R-PTPc-R

cd14611

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...

669-896

2.61e-47

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: 168.56 E-value: 2.61e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 669 KNRYRNVLPYDWSRVPLKPIH-EEPGSDYINASFMPGLWSPQE-FIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEA 746
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIRGYGGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 747 GRvKCEHYWPldSQPCTHGHLRVTLVGEEVMENWTVRELLLLQveEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLR 826
Cdd:cd14611   82 NE-KCVLYWP--EKRGIYGKVEVLVNSVKECDNYTIRNLTLKQ--GSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVE 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 827 QWLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQ 896
Cdd:cd14611  157 EDRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226

R-PTPc-typeIIb-2

cd14556

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...

696-896

8.30e-47

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: 166.04 E-value: 8.30e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLtNCMEAGRVKCEHYWPlDSQPCTHGHLRVTLVGEE 775
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWP-DEGSGTYGPIQVEFVSTT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 776 VMENWTVRELLL---LQVEEQKTLsVRQFHYQAWPDHG-VPSSPDTLLAFWRMLRQWLDQTMEgGPPIVHCSAGVGRTGT 851
Cdd:cd14556   79 IDEDVISRIFRLqntTRPQEGYRM-VQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSGE-GPIVVHCLNGVGRSGV 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 612407829 852 LIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQ 896
Cdd:cd14556  157 FCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201

PTPc-N5

cd14613

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...

669-895

2.72e-46

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: 166.58 E-value: 2.72e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 669 KNRYRNVLPYDWSRVPLK-PIHEEPGSDYINASFMPGLWSPQE-FIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEA 746
Cdd:cd14613   28 KNRYKTILPNPHSRVCLTsPDQDDPLSSYINANYIRGYGGEEKvYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 747 GRvKCEHYWPLDSqpCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLsvRQFHYQAWPDHGVPSSPDTLLAFWRMLR 826
Cdd:cd14613  108 NE-KCTEYWPEEQ--VTYEGIEITVKQVIHADDYRLRLITLKSGGEERGL--KHYWYTSWPDQKTPDNAPPLLQLVQEVE 182

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 827 QWLDQTMEG-GPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLH 895
Cdd:cd14613  183 EARQQAEPNcGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVH 252

PTP-N23

cd14539

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...

696-896

4.70e-44

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: 158.32 E-value: 4.70e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFMPGL--WSPQeFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLD-SQPCTHGHLRVTLV 772
Cdd:cd14539    1 YINASLIEDLtpYCPR-FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErGQALVYGAITVSLQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 773 GEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWR-MLRQWLDQTMEGGPPIVHCSAGVGRTGT 851
Cdd:cd14539   80 SVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEeVHSHYLQQRSLQTPIVVHCSSGVGRTGA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 612407829 852 LIALDVLLRQLQSE-GLLGPFSFVRKMRESRPLMVQTEAQYVFLHQ 896
Cdd:cd14539  160 FCLLYAAVQEIEAGnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205

R-PTP-N-N2

cd14546

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...

696-898

6.22e-44

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: 157.99 E-value: 6.22e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFMPGlWSPQE--FIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPCtHGHLRVTLVG 773
Cdd:cd14546    1 YINASTIYD-HDPRNpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEV-YHIYEVHLVS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 774 EEVM-ENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQwlDQTMEGGPPIVHCSAGVGRTGTL 852
Cdd:cd14546   79 EHIWcDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNK--SYRGRSCPIVVHCSDGAGRTGTY 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 612407829 853 IALDVLL-RQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCI 898
Cdd:cd14546  157 ILIDMVLnRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203

PHA02742

protein tyrosine phosphatase; Provisional

665-901

5.27e-42

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 155.93 E-value: 5.27e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 665 ENNAKNRYRNVLPYDWSRVPLKPihEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCM 744
Cdd:PHA02742  51 KNMKKCRYPDAPCFDRNRVILKI--EDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIM 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 745 EAGRVKCEHYW-PLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWR 823
Cdd:PHA02742 129 EDGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVL 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 824 MLRQwLDQTME---------GGPPI-VHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVF 893
Cdd:PHA02742 209 AVRE-ADLKADvdikgenivKEPPIlVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF 287


                 ....*...
gi 612407829 894 LHQCILRF 901
Cdd:PHA02742 288 CYFIVLIF 295

PTPc_plant_PTP1

cd17658

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...

696-893

4.49e-41

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

Pssm-ID: 350496 [Multi-domain] Cd Length: 206 Bit Score: 149.92 E-value: 4.49e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFM--PGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGR-VKCEHYWPL-DSQPCTHGHLRVTL 771
Cdd:cd17658    1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAeENESREFGRISVTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 772 VGEEVMEN-WTVRELLLLQVE-EQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTmegGPPIVHCSAGVGRT 849
Cdd:cd17658   81 KKLKHSQHsITLRVLEVQYIEsEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPPSA---GPIVVHCSAGIGRT 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 612407829 850 GTLIALDVLLRQLqsegLLGPFS------FVRKMRESRPLMVQTEAQYVF 893
Cdd:cd17658  158 GAYCTIHNTIRRI----LEGDMSavdlskTVRKFRSQRIGMVQTQDQYIF 203

PTPc_motif

smart00404

Protein tyrosine phosphatase, catalytic domain motif;

797-899

2.86e-39

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 140.96 E-value: 2.86e-39

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829   797 SVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGL-LGPFSFVR 875
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                           90       100
                   ....*....|....*....|....
gi 612407829   876 KMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALL 104

PTPc_DSPc

smart00012

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...

797-899

2.86e-39

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

Pssm-ID: 214469 [Multi-domain] Cd Length: 105 Bit Score: 140.96 E-value: 2.86e-39

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829   797 SVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGL-LGPFSFVR 875
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                           90       100
                   ....*....|....*....|....
gi 612407829   876 KMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALL 104

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

665-907

3.57e-39

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 147.16 E-value: 3.57e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 665 ENNAKNRYRNVLPYDWSRVplkpiheEPGSDYINASFMPGLwSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCM 744
Cdd:COG5599   41 NGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 745 EAG--RVKCEHYWPLDSQPCTHgHLRVTLVGEEV-MENWTVRELLLLQVEE-QKTLSVRQFHYQAWPDHGVPSSpDTLLA 820
Cdd:COG5599  113 EISkpKVKMPVYFRQDGEYGKY-EVSSELTESIQlRDGIEARTYVLTIKGTgQKKIEIPVLHVKNWPDHGAISA-EALKN 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 821 FWRMLRQWLD-QTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLgPFSF---VRKMRESR-PLMVQTEAQYVFLh 895
Cdd:COG5599  191 LADLIDKKEKiKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVQI-TLSVeeiVIDMRTSRnGGMVQTSEQLDVL- 268

                        250
                 ....*....|..
gi 612407829 896 qcILRFLQQSAQ 907
Cdd:COG5599  269 --VKLAEQQIRP 278

PHA02738

hypothetical protein; Provisional

666-915

8.45e-36

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 138.52 E-value: 8.45e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 666 NNAKNRYRNVLPYDWSRVPLkPIHEEPGsDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCME 745
Cdd:PHA02738  49 NRKLNRYLDAVCFDHSRVIL-PAERNRG-DYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 746 AGRVKCEHYWP-LDSQPCTHGHLRVTLVGEEVMENWtVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRM 824
Cdd:PHA02738 127 NGREKCFPYWSdVEQGSIRFGKFKITTTQVETHPHY-VKSTLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLE 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 825 LRQWL-----------DQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVF 893
Cdd:PHA02738 206 VRQCQkelaqeslqigHNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFF 285

                        250       260
                 ....*....|....*....|..
gi 612407829 894 LHQCILRFLQQSAQAPAEKEVP 915
Cdd:PHA02738 286 CYRAVKRYVNLTVNKVSKKLIP 307

R5-PTP-2

cd14550

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...

696-896

1.94e-35

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: 133.60 E-value: 1.94e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGrvKCEHYWPLDSQPCTHGHLRVTLVGEE 775
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPLECETFKVTLSGED 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 776 VM-----ENWTVRELLLLQVEEQKTLSVRQFHYQAWPDhgvPSSP-DTLLAFWRMLRQWLDQTmeGGPPIVHCSAGVGRT 849
Cdd:cd14550   79 HSclsneIRLIVRDFILESTQDDYVLEVRQFQCPSWPN---PCSPiHTVFELINTVQEWAQQR--DGPIVVHDRYGGVQA 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 612407829 850 GTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQ 896
Cdd:cd14550  154 ATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200

PHA02746

protein tyrosine phosphatase; Provisional

665-898

1.03e-33

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 132.46 E-value: 1.03e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 665 ENNAKNRYRNVLPYDWSRVPLKP-------------------IHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDF 725
Cdd:PHA02746  50 ENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkievTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSEDF 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 726 WRLVWEQQSHTLVMLTNcMEAGRVKCEHYW--PLDSQpCTHGHLRVTLVgeEVME--NWTVRELLLLQVEEQKTLSVRQF 801
Cdd:PHA02746 130 FKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSE-LAFGRFVAKIL--DIIEelSFTKTRLMITDKISDTSREIHHF 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 802 HYQAWPDHGVPSSPDTLLAFW--------RMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSF 873
Cdd:PHA02746 206 WFPDWPDNGIPTGMAEFLELInkvneeqaELIKQADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEI 285

                        250       260
                 ....*....|....*....|....*
gi 612407829 874 VRKMRESRPLMVQTEAQYVFLHQCI 898
Cdd:PHA02746 286 VLKIRKQRHSSVFLPEQYAFCYKAL 310

PHA02747

protein tyrosine phosphatase; Provisional

624-895

1.03e-33

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 132.05 E-value: 1.03e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 624 AEDFADhvRKNERDSNCGFADEYQQLSLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPiHEEPGSDYINASFMP 703
Cdd:PHA02747  11 AIDFLK--RRNQLNCFGIIRDEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDS-GGGSTSDYIHANWID 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 704 GLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCME-AGRVKCEHYWPL--DSQPCTHGHLRVTLvgeevmeNW 780
Cdd:PHA02747  88 GFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKGtNGEEKCYQYWCLneDGNIDMEDFRIETL-------KT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 781 TVRE---LLLLQVEEQKTLSVRQ---FHYQAWPDHGVPSSPDTLLAFWRML---RQ-----WLDQTMEGGPPIVHCSAGV 846
Cdd:PHA02747 161 SVRAkyiLTLIEITDKILKDSRKishFQCSEWFEDETPSDHPDFIKFIKIIdinRKksgklFNPKDALLCPIVVHCSDGV 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 612407829 847 GRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLH 895
Cdd:PHA02747 241 GKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIQ 289

R-PTPc-T-2

cd14634

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...

696-899

1.87e-32

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: 125.13 E-value: 1.87e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLtNCMEAGRVkCEHYWPlDSQPCTHGHLRVTLVGEE 775
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVML-NEMDAAQL-CMQYWP-EKTSCCYGPIQVEFVSAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 776 VMENWTVRELLLLQVEEQKT--LSVRQFHYQAWPDH-GVPSSPDTLLAFWRMLRQWLDQTMEG-GPPIVHCSAGVGRTGT 851
Cdd:cd14634   78 IDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQYDGReGRTVVHCLNGGGRSGT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 612407829 852 LIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:cd14634  158 FCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVAL 205

PTPc-N21

cd14598

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...

696-903

7.05e-32

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: 123.93 E-value: 7.05e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFMPGLWSPQE--FIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWP-LDSQ--PCTHGHLRVT 770
Cdd:cd14598    1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrLGSRhnTVTYGRFKIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 771 LVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFW-------RMLRQWLDQTMEGGPPIVHCS 843
Cdd:cd14598   81 TRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLeeiqsvrRHTNSTIDPKSPNPPVLVHCS 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 844 AGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRFLQ 903
Cdd:cd14598  161 AGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220

R-PTP-Z-2

cd17669

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...

696-899

7.86e-30

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: 117.40 E-value: 7.86e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEhYWPLDSQPCTHGHLRVTLVGEE 775
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEPINCETFKVTLIAEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 776 VM-----ENWTVRELLLLQVEEQKTLSVRQFHYQAWPDhgvPSSP-DTLLAFWRMLRQwlDQTMEGGPPIVHCSAGVGRT 849
Cdd:cd17669   80 HKclsneEKLIIQDFILEATQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISIIKE--EAANRDGPMIVHDEHGGVTA 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 612407829 850 GTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:cd17669  155 GTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204

R-PTPc-K-2

cd14636

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...

696-899

4.50e-28

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: 112.43 E-value: 4.50e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNC-MEAGrvkCEHYWPLDSQpCTHGHLRVTLVGE 774
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWPEEGM-LRYGPIQVECMSC 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 775 EVMENWTVR--ELLLLQVEEQKTLSVRQFHYQAWPDH-GVPSSPDTLLAFWRMLRQWLDQTMEG-GPPIVHCSAGVGRTG 850
Cdd:cd14636   77 SMDCDVISRifRICNLTRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECDEGeGRTIIHCLNGGGRSG 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 612407829 851 TLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:cd14636  157 MFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVAL 205

R-PTP-G-2

cd17670

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...

696-899

1.53e-27

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: 110.92 E-value: 1.53e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNcmEAGRVKCEH-YWPLDSQPCTHGHLRVTLVGE 774
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD--NQGLAEDEFvYWPSREESMNCEAFTVTLISK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 775 EVM-----ENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSpdTLLAFWRMLRQwlDQTMEGGPPIVHCSAGVGRT 849
Cdd:cd17670   79 DRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPIS--STFELINVIKE--EALTRDGPTIVHDEFGAVSA 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 612407829 850 GTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:cd17670  155 GTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204

R-PTPc-M-2

cd14635

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...

696-899

1.64e-27

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

Pssm-ID: 350483 [Multi-domain] Cd Length: 206 Bit Score: 110.93 E-value: 1.64e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRvkCEHYWPlDSQPCTHGHLRVTLVGEE 775
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQL--CPQYWP-ENGVHRHGPIQVEFVSAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 776 VMENWTVRELLLLQVEEQKT--LSVRQFHYQAWPDH-GVPSSPDTLLAFWRMLRQWLDQTMEG-GPPIVHCSAGVGRTGT 851
Cdd:cd14635   78 LEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNGGeGRTVVHCLNGGGRSGT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 612407829 852 LIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:cd14635  158 FCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205

R-PTPc-U-2

cd14637

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...

696-899

5.06e-26

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: 106.53 E-value: 5.06e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 696 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRV-KCEHYWPlDSQPCTHGHLRVTLVGE 774
Cdd:cd14637    1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP-EPGLQQYGPMEVEFVSG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 775 EVMENWTVRELLLLQVE--EQKTLSVRQFHYQAW-PDHGVPSSPDTLLAFWRMLRQWLDQTMEgGPPIVHCSAGVGRTGT 851
Cdd:cd14637   80 SADEDIVTRLFRVQNITrlQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGE-GRTVVHCLNGGGRSGT 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 612407829 852 LIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 899
Cdd:cd14637  159 YCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206

PTP_YopH-like

cd14559

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...

711-894

2.34e-15

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

Pssm-ID: 350407 [Multi-domain] Cd Length: 227 Bit Score: 76.28 E-value: 2.34e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 711 FIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWpldSQPCTHGhlRVTLVGEEVMENWTVRELL---- 786
Cdd:cd14559   31 AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYF---RQSGTYG--SVTVKSKKTGKDELVDGLKadmy 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 787 LLQV-EEQKTLSVRQFHYQAWPDHGVPSSPDTllafwRMLRQWLDQTMEGGP------------------PIVHCSAGVG 847
Cdd:cd14559  106 NLKItDGNKTITIPVVHVTNWPDHTAISSEGL-----KELADLVNKSAEEKRnfykskgssaindknkllPVIHCRAGVG 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 612407829 848 RTGTLIALDVLLRQLQSEGLLgpfSFVRKMRESR-PLMVQTEAQYVFL 894
Cdd:cd14559  181 RTGQLAAAMELNKSPNNLSVE---DIVSDMRTSRnGKMVQKDEQLDTL 225

FN3

Fibronectin type 3 domain [General function prediction only];

85-509

8.12e-14

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 75.42 E-value: 8.12e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829  85 TVDGLGPGSLYTCSVWVEKDGVNSSVGTVTTATAPNPVRNLTVEAQTNSSIALTWEVPDGPDPQNSTYGVEYTGDGGRAG 164
Cdd:COG3401    7 TSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 165 TRSTAHTNITVDRLE----PGCLYVFSVWVGKNGINSSRETRNATTAPNPVRNLHMETQTNSSIALCWEVPDGPYPQDYT 240
Cdd:COG3401   87 APPTATGLTTLTGSGsvggATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 241 YWVEYTGDGGGTETRNTTNTSVT------AERLEPGTLYTFSVWAEKNGARGSRQN----VSISTVPNAVTSLSKQDWTN 310
Cdd:COG3401  167 GVVVSPDTSATAAVATTSLTVTSttlvdgGGDIEPGTTYYYRVAATDTGGESAPSNevsvTTPTTPPSAPTGLTATADTP 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 311 STIALRWTAPQGPGQSSY------SYWVSWVREGmtdpRTQSTSGTDitlKELEAGSLYHLTVWAE--RNEVRGYNSTLT 382
Cdd:COG3401  247 GSVTLSWDPVTESDATGYrvyrsnSGDGPFTKVA----TVTTTSYTD---TGLTNGTTYYYRVTAVdaAGNESAPSNVVS 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 383 AAT---APNEVTDLQNETQTKNSVMLWWKAPGDPHSQLY-VYwvqwaskghprRGQDPQANWVNQTSRTNETWYKVEALE 458
Cdd:COG3401  320 VTTdltPPAAPSGLTATAVGSSSITLSWTASSDADVTGYnVY-----------RSTSGGGTYTKIAETVTTTSYTDTGLT 388

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 612407829 459 PGTLYNFTVWAERNDVASSTQSLCASTYPDTVTITSCVSTSAGYGVNLIWS 509
Cdd:COG3401  389 PGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVA 439

CDKN3-like

cd14505

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...

769-896

9.59e-13

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

Pssm-ID: 350355 [Multi-domain] Cd Length: 163 Bit Score: 66.90 E-value: 9.59e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 769 VTLVGEEVMENWTVRELLllqvEEQKTLSVRQFHYqAWPDHGVPSSpdtlLAFWRMLRQWLDQTMEGGPPIV-HCSAGVG 847
Cdd:cd14505   48 VTLCTDGELEELGVPDLL----EQYQQAGITWHHL-PIPDGGVPSD----IAQWQELLEELLSALENGKKVLiHCKGGLG 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 612407829 848 RTGTLIAldVLLrqLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQ 896
Cdd:cd14505  119 RTGLIAA--CLL--LELGDTLDPEQAIAAVRALRPGAIQTPKQENFLHQ 163

FN3

Fibronectin type 3 domain [General function prediction only];

14-403

7.06e-12

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 69.26 E-value: 7.06e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829  14 LVLLGLCSWTGARAPAPNPGRNLTVETQTTSSISLSWEVPDGLDSQNSNYWVQCTgdggttetRNTTATNVTVDGLGPGS 93
Cdd:COG3401  132 AGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLT--------VTSTTLVDGGGDIEPGT 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829  94 LYTCSVWVEKDGVNSS----VGTVTTATAPNPVRNLTVEAQTNSSIALTWEVPDGPDpqNSTYGVEYTGDGGRAGTR--S 167
Cdd:COG3401  204 TYYYRVAATDTGGESApsneVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD--ATGYRVYRSNSGDGPFTKvaT 281

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 168 TAHTNITVDRLEPGCLYVFSVW-VGKNGINSSR----ETRNATTAPNPVRNLHMETQTNSSIALCWEVPDGPYPQDYTyw 242
Cdd:COG3401  282 VTTTSYTDTGLTNGTTYYYRVTaVDAAGNESAPsnvvSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVTGYN-- 359

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 243 VEYTGDGGGTET---RNTTNTSVTAERLEPGTLYTFSVWAEKNGARGSR-----QNVSISTVPNAVTSLSKQDWTN---S 311
Cdd:COG3401  360 VYRSTSGGGTYTkiaETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESApseevSATTASAASGESLTASVDAVPLtdvA 439

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 312 TIALRWTAPQGPGQSSYSYWVSWVREGMTDPRTQSTSGTDITLKELEAGSLYHLTVWAERNEVRGYNSTLTAATAPNEVT 391
Cdd:COG3401  440 GATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAA 519

                        410
                 ....*....|..
gi 612407829 392 DLQNETQTKNSV 403
Cdd:COG3401  520 VGGAPDGTPNVT 531

PHA02740

protein tyrosine phosphatase; Provisional

618-905

1.28e-11

protein tyrosine phosphatase; Provisional

Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 66.53 E-value: 1.28e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 618 SPGDIPAEDFADHVRKNerDSNCGFADEYQQLsLVGHSQSQMVASASENNAKNRYRNVLP---YDWSRVPLKPiheepGS 694
Cdd:PHA02740   5 DAVDINGMDFINFINKP--DLLSCIIKEYRAI-VPEHEDEANKACAQAENKAKDENLALHitrLLHRRIKLFN-----DE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 695 DYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAgrvKC-EHYWPLDSQPC-THGHLRVTLV 772
Cdd:PHA02740  77 KVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADK---KCfNQFWSLKEGCViTSDKFQIETL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 773 gEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFW----RMLRQWLDQTMEG--GPPIVHCSAGV 846
Cdd:PHA02740 154 -EIIIKPHFNLTLLSLTDKFGQAQKISHFQYTAWPADGFSHDPDAFIDFFcnidDLCADLEKHKADGkiAPIIIDCIDGI 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 612407829 847 GRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRFLQQS 905
Cdd:PHA02740 233 SSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLKEK 291

FN3

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

208-286

4.24e-11

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 60.20 E-value: 4.24e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 208 PNPVRNLHMETQTNSSIALCWEVPDGPYPQDYTYWVEYTGDGGGT----ETRNTTNTSVTAERLEPGTLYTFSVWAEKNG 283
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                 ...
gi 612407829 284 ARG 286
Cdd:cd00063   81 GES 83

CDC14

COG2453

Protein-tyrosine phosphatase [Signal transduction mechanisms];

773-896

6.94e-11

Protein-tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 61.14 E-value: 6.94e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 773 GEEVMENWTVRELLLLQVEEQKTLSVR-----QFHYQAWPDHGVPSSPDtllafWRMLRQWLDQTMEGGPPI-VHCSAGV 846
Cdd:COG2453   17 GEADLKREGIDAVVSLTEEEELLLGLLeeaglEYLHLPIPDFGAPDDEQ-----LQEAVDFIDEALREGKKVlVHCRGGI 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 612407829 847 GRTGTLIALdVLLRQlqseGLlgpfSF---VRKMRESRPLMVQTEAQYVFLHQ 896
Cdd:COG2453   92 GRTGTVAAA-YLVLL----GL----SAeeaLARVRAARPGAVETPAQRAFLER 135

PTP_DSP_cys

cd14494

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...

819-896

2.53e-10

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.

Pssm-ID: 350344 [Multi-domain] Cd Length: 113 Bit Score: 58.52 E-value: 2.53e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 819 LAFWRMLRQWLDQTMEGGPPI-VHCSAGVGRTGTLIALDVLLRQLQSegllgPFSFVRKMRESRP-LMVQTEAQYVFLHQ 896
Cdd:cd14494   39 LAMVDRFLEVLDQAEKPGEPVlVHCKAGVGRTGTLVACYLVLLGGMS-----AEEAVRIVRLIRPgGIPQTIEQLDFLIK 113

FN3

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...

208-280

2.93e-10

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 57.62 E-value: 2.93e-10

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612407829   208 PNPVRNLHMETQTNSSIALCWEVPDGPYPQDYT--YWVEYTGDGGGTETRNTTN--TSVTAERLEPGTLYTFSVWAE 280
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIvgYRVEYREEGSEWKEVNVTPssTSYTLTGLKPGTEYEFRVRAV 77

FN3

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...

387-470

5.52e-10

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 56.85 E-value: 5.52e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829   387 PNEVTDLQNETQTKNSVMLWWKAPGDPHSQLYV--YWVQWASKGHprrgqdpqaNWVNQTSRTNETWYKVEALEPGTLYN 464
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIvgYRVEYREEGS---------EWKEVNVTPSSTSYTLTGLKPGTEYE 71


                   ....*.
gi 612407829   465 FTVWAE 470
Cdd:smart00060  72 FRVRAV 77

FN3

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

119-206

1.47e-09

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 55.58 E-value: 1.47e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 119 PNPVRNLTVEAQTNSSIALTWEVPDGPDPQNSTYGVEYTGDGG----RAGTRSTAHTNITVDRLEPGCLYVFSVW-VGKN 193
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSgdwkEVEVTPGSETSYTLTGLKPGTEYEFRVRaVNGG 80

                         90
                 ....*....|...
gi 612407829 194 GINSSRETRNATT 206
Cdd:cd00063   81 GESPPSESVTVTT 93

FN3

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

387-476

3.41e-09

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 54.81 E-value: 3.41e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 387 PNEVTDLQNETQTKNSVMLWWKAPGDPHSQLYVYWVQWASKGHPRrgqdpqanWVN-QTSRTNETWYKVEALEPGTLYNF 465
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGD--------WKEvEVTPGSETSYTLTGLKPGTEYEF 72

                         90
                 ....*....|.
gi 612407829 466 TVWAERNDVAS 476
Cdd:cd00063   73 RVRAVNGGGES 83

FN3

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

30-117

7.09e-09

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 53.65 E-value: 7.09e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829  30 PNPGRNLTVETQTTSSISLSWEVPDGLDSQNSNYWVQCTGDGGTT----ETRNTTATNVTVDGLGPGSLYTCSVWVEKDG 105
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                         90
                 ....*....|..
gi 612407829 106 VNSSVGTVTTAT 117
Cdd:cd00063   81 GESPPSESVTVT 92

PTP_PTPDC1

cd14506

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...

801-895

6.29e-08

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

Pssm-ID: 350356 [Multi-domain] Cd Length: 206 Bit Score: 53.89 E-value: 6.29e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 801 FHYQAWPDHGVPSsPDTLLAFWRMLRQWLDqtmEGGPPIVHCSAGVGRTGTLIA--LDVLLRqlqseglLGPFSFVRKMR 878
Cdd:cd14506   79 FYNFGWKDYGVPS-LTTILDIVKVMAFALQ---EGGKVAVHCHAGLGRTGVLIAcyLVYALR-------MSADQAIRLVR 147

                         90
                 ....*....|....*..
gi 612407829 879 ESRPLMVQTEAQYVFLH 895
Cdd:cd14506  148 SKRPNSIQTRGQVLCVR 164

FN3

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...

119-190

1.14e-07

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 49.92 E-value: 1.14e-07

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612407829   119 PNPVRNLTVEAQTNSSIALTWEVPdgPDPQNSTYGVEYTGDGGRAG------TRSTAHTNITVDRLEPGCLYVFSVWV 190
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPP--PDDGITGYIVGYRVEYREEGsewkevNVTPSSTSYTLTGLKPGTEYEFRVRA 76

FN3

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

297-385

2.22e-07

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 49.42 E-value: 2.22e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 297 PNAVTSLSKQDWTNSTIALRWTAPQGPGQSSYSYWVSWVREGMTDPR---TQSTSGTDITLKELEAGSLYHLTVWAERNE 373
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKeveVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                         90
                 ....*....|..
gi 612407829 374 VRGYNSTLTAAT 385
Cdd:cd00063   81 GESPPSESVTVT 92

FN3

Fibronectin type 3 domain [General function prediction only];

29-336

3.01e-07

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 54.24 E-value: 3.01e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829  29 APNPGRNLTVETQTTSSISLSWEVPDGLDSqnSNYWV--QCTGDGGTTETRNTTATNVTVDGLGPGSLYTCSVW-VEKDG 105
Cdd:COG3401  232 PPSAPTGLTATADTPGSVTLSWDPVTESDA--TGYRVyrSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTaVDAAG 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 106 V---NSSVGTVTTA-TAPNPVRNLTVEAQTNSSIALTWEVPDGPDPqnSTYGVEYTGDGGR-----AGTRSTahTNITVD 176
Cdd:COG3401  310 NesaPSNVVSVTTDlTPPAAPSGLTATAVGSSSITLSWTASSDADV--TGYNVYRSTSGGGtytkiAETVTT--TSYTDT 385

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 177 RLEPGCLYVFSV-----------------------WVGKNGINSSRETRNATTAPNPVRNLHMETQTNSSIalcWEVPDG 233
Cdd:COG3401  386 GLTPGTTYYYKVtavdaagnesapseevsattasaASGESLTASVDAVPLTDVAGATAAASAASNPGVSAA---VLADGG 462

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 234 PYPQDYTYWVEYTGDGGGTETRNTTNTSVTAERLEPGTLYTFSVWAEKN-GARGSRQNVSISTVPNAVTSLSKQDWTNST 312
Cdd:COG3401  463 DTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSViGASAAAAVGGAPDGTPNVTGASPVTVGAST 542

                        330       340
                 ....*....|....*....|....
gi 612407829 313 iALRWTAPQGPGQSSYSYWVSWVR 336
Cdd:COG3401  543 -GDVLITDLVSLTTSASSSVSGAG 565

fn3

Fibronectin type III domain;

389-467

1.66e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 47.02 E-value: 1.66e-06

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612407829  389 EVTDLQNETQTKNSVMLWWKAPGDPHSQLYVYWVQWASKGHPRRgqdpqanWVNQTSRTNETWYKVEALEPGTLYNFTV 467
Cdd:pfam00041   2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEP-------WNEITVPGTTTSVTLTGLKPGTEYEVRV 73

fn3

Fibronectin type III domain;

210-286

6.39e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 45.10 E-value: 6.39e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829  210 PVRNLHMETQTNSSIALCWEVPDGPYPQDYTYWVEYTGDGGGTETRNTTN----TSVTAERLEPGTLYTFSVWAEKNGAR 285
Cdd:pfam00041   2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVpgttTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                  .
gi 612407829  286 G 286
Cdd:pfam00041  82 G 82

FN3

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...

30-108

1.06e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 44.53 E-value: 1.06e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829    30 PNPGRNLTVETQTTSSISLSWEVP--DGLDSQNSNYWVQCTGDGGTTE--TRNTTATNVTVDGLGPGSLYTCSVWVEKDG 105
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPpdDGITGYIVGYRVEYREEGSEWKevNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                   ...
gi 612407829   106 VNS 108
Cdd:smart00060  81 GEG 83

DUSP23

cd14504

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...

807-896

2.81e-05

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

Pssm-ID: 350354 [Multi-domain] Cd Length: 142 Bit Score: 44.96 E-value: 2.81e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829 807 PDHGVPSSPDTLlafwRMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIALdvllrQLQSEGLLGPFSFVRKMRESRPLMVQ 886
Cdd:cd14504   58 EDYTPPTLEQID----EFLDIVEEANAKNEAVLVHCLAGKGRTGTMLAC-----YLVKTGKISAVDAINEIRRIRPGSIE 128

                         90
                 ....*....|
gi 612407829 887 TEAQYVFLHQ 896
Cdd:cd14504  129 TSEQEKFVIQ 138

fn3

Fibronectin type III domain;

121-201

4.61e-05

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 42.79 E-value: 4.61e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612407829  121 PVRNLTVEAQTNSSIALTWEVPDGPDPQNSTYGVEY----TGDGGRAGTRSTAHTNITVDRLEPGCLYVFSVwVGKNGIN 196
Cdd:pfam00041   2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYrpknSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRV-QAVNGGG 80


                  ....*
gi 612407829  197 SSRET 201
Cdd:pfam00041  81 EGPPS 85

fn3

Fibronectin type III domain;

28-99

4.75e-05

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 42.79 E-value: 4.75e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612407829   28 PAPnpgRNLTVETQTTSSISLSWEVPDGLDSQNSNYWVQCTGDGGTTETRNTTATN----VTVDGLGPGSLYTCSV 99
Cdd:pfam00041   1 SAP---SNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGtttsVTLTGLKPGTEYEVRV 73

CDC14_C

cd14499

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...

807-855

5.65e-05

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

Pssm-ID: 350349 [Multi-domain] Cd Length: 174 Bit Score: 44.75 E-value: 5.65e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 612407829 807 PDHGVPSspdtllafWRMLRQWLDQT-MEGGPPIVHCSAGVGRTGTLIAL 855
Cdd:cd14499   88 PDGSTPS--------DDIVKKFLDICeNEKGAIAVHCKAGLGRTGTLIAC 129

FN3