NCBI Conserved Domain Search

Fibronectin type III domain;

1550-1632

1.39e-11

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 62.43 E-value: 1.39e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1550 SPPSLLSFADVANTSLAITWKGPPDWT-DYNDFELQWFPGDALTIFNPYSSRKSEGR-IVYGLHPGRSYQFSVKTVSGDS 1627
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNgPITGYEVEYRPKNSGEPWNEITVPGTTTSvTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 1907074051 1628 WKTYS 1632
Cdd:pfam00041   81 EGPPS 85

fn3

Fibronectin type III domain;

1644-1723

2.98e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 58.58 E-value: 2.98e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1644 DKIQNLHCRPQNSTAIACSWIPP---DSDFDGYSIECRKMDTQEIEFSRKLEKEKSLLNIMMLVPHKRYLVSIKVQSAGM 1720
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1907074051 1721 TSE 1723
Cdd:pfam00041   81 EGP 83

FN3 super family

cl27307

Fibronectin type 3 domain [General function prediction only];

1341-1674

3.05e-09

Fibronectin type 3 domain [General function prediction only];

The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 62.33 E-value: 3.05e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1341 EDLTPGKKYKMQILTVSGGLFSKESQA----EGRTVPAAVTNLRITENSSRYLSFGWTASEGE-LSWYNIFLYN-PDRTL 1414
Cdd:COG3401    197 GDIEPGTTYYYRVAATDTGGESAPSNEvsvtTPTTPPSAPTGLTATADTPGSVTLSWDPVTESdATGYRVYRSNsGDGPF 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1415 QERAQVDplVQSFSFQNLLQGR--MYKMVIVTHSGELSNESFIF----GRTVPAAVNHLKGShRNTTDSLWFSWSPASG- 1487
Cdd:COG3401    277 TKVATVT--TTSYTDTGLTNGTtyYYRVTAVDAAGNESAPSNVVsvttDLTPPAAPSGLTAT-AVGSSSITLSWTASSDa 353

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1488 DFDFYElILYNPNGTKKENW--KEKDVTEWRFQGLVPGRKYTlYVVT------HSGDLSNKVTGEGRTAPSPPSLLSFAD 1559
Cdd:COG3401    354 DVTGYN-VYRSTSGGGTYTKiaETVTTTSYTDTGLTPGTTYY-YKVTavdaagNESAPSEEVSATTASAASGESLTASVD 431

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1560 VANT---------SLAITWKGPPDWTDYNDFELQWFPGDALTIFNPYSSRKSEGRIVYGLHPGRSYQFSVKTVSGDSWKT 1630
Cdd:COG3401    432 AVPLtdvagataaASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSV 511

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1907074051 1631 YSKPISGSVRTKPDKIQNLHCRPQNS-TAIACSWIPPDSDFDGYS 1674
Cdd:COG3401    512 IGASAAAAVGGAPDGTPNVTGASPVTvGASTGDVLITDLVSLTTS 556

fn3

Fibronectin type III domain;

1020-1096

1.40e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 53.96 E-value: 1.40e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1020 DKVQGISVSNsARSDYLKVSWVHAT---GDFDHYEVTI--KNRESFIQTKTIPKSENECEFIELVPGRLYSVTVSTKSGQ 1094
Cdd:pfam00041    1 SAPSNLTVTD-VTSTSLTVSWTPPPdgnGPITGYEVEYrpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ..
gi 1907074051 1095 YE 1096
Cdd:pfam00041   80 GE 81

FN3 super family

cl27307

Fibronectin type 3 domain [General function prediction only];

856-1309

1.56e-08

Fibronectin type 3 domain [General function prediction only];

The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 60.02 E-value: 1.56e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  856 TSSLFTNWTKALGDVEFYQVLLIHENVVVKNESVSSDTSRYSFRALKPGSLYSVVVTTVSGGISSRQVVAEGRTVPSSVS 935
Cdd:COG3401     61 LSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGT 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  936 GVTVNNSGRNDYLSVSWLPAPGEVDHYVVSLSH-----EGKVDQFLIIAKSVSECSFSsLTPGRLYNVTVTTKSGNYAS- 1009
Cdd:COG3401    141 YALGAGLYGVDGANASGTTASSVAGAGVVVSPDtsataAVATTSLTVTSTTLVDGGGD-IEPGTTYYYRVAATDTGGESa 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1010 ----HSFTEERTVPDKVQGISVSnSARSDYLKVSWV-HATGDFDHYEVTIKNRESfiQTKTIPKSENECEFI--ELVPGR 1082
Cdd:COG3401    220 psneVSVTTPTTPPSAPTGLTAT-ADTPGSVTLSWDpVTESDATGYRVYRSNSGD--GPFTKVATVTTTSYTdtGLTNGT 296

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1083 LYSVTVSTKSGQYEASEQ------GTGRTIPEPVKDLTLLNRSTEDLHVTWS-RANGDVDQYEVQLLFNDMKVFPHIHLV 1155
Cdd:COG3401    297 TYYYRVTAVDAAGNESAPsnvvsvTTDLTPPAAPSGLTATAVGSSSITLSWTaSSDADVTGYNVYRSTSGGGTYTKIAET 376

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1156 NTATEYKFTALTPGRHYKILVLTISGDVQQSAFIEGLTVPSTVKNIHISANGATDR---------LMVTWSPGGGDVDSY 1226
Cdd:COG3401    377 VTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAvpltdvagaTAAASAASNPGVSAA 456

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1227 VVSAFRQDEKVDSQT-------IPKHASEHTFHRLEAGAKYRIAIVSVSGSLRNQIDALGQTVPASVQGVVaANAYSSNS 1299
Cdd:COG3401    457 VLADGGDTGNAVPFTttsstvtATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGT-PNVTGASP 535

                          490
                   ....*....|
gi 1907074051 1300 LTVSWQKALG 1309
Cdd:COG3401    536 VTVGASTGDV 545

fn3

Fibronectin type III domain;

579-658

1.71e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 53.57 E-value: 1.71e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  579 EVSNLKVTNDGRlTSLNVKWQKPP---GDVDSYSITLSHQGTIKESK--TLAPPVTETQFKDLVPGRLYQVTISCISGEL 653
Cdd:pfam00041    2 APSNLTVTDVTS-TSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNeiTVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 1907074051  654 SAEKS 658
Cdd:pfam00041   81 EGPPS 85

fn3

Fibronectin type III domain;

757-835

2.56e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 53.19 E-value: 2.56e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  757 AVLQLRVKHANETSLGITWRAPL---GEWEKYIISL--MDRELLVIHKSLSKDAKEFTFTDLMPGRNYKATVTSMSGDLK 831
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYrpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ....
gi 1907074051  832 QSSS 835
Cdd:pfam00041   82 GPPS 85

FN3

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

398-483

3.33e-08

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

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 52.88 E-value: 3.33e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  398 PLPPARFEVnrEKTASTTLQVRWTPSS---GKVSWYEVQLFDHNNQKIQEVQVQESTTwSQYTFLNLTEGNSYKVAITAV 474
Cdd:cd00063      1 PSPPTNLRV--TDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSE-TSYTLTGLKPGTEYEFRVRAV 77


                   ....*....
gi 1907074051  475 SGEKRSFPV 483
Cdd:cd00063     78 NGGGESPPS 86

fn3

Fibronectin type III domain;

681-742

5.21e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 46.64 E-value: 5.21e-06

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907074051  681 SFTVNWTPPA---GDWEHYRIVLF--NESLVLLNTTVGKEETHYALDGLEliPGRQYEIEVIVESGN 742
Cdd:pfam00041   15 SLTVSWTPPPdgnGPITGYEVEYRpkNSGEPWNEITVPGTTTSVTLTGLK--PGTEYEVRVQAVNGG 79

fn3

Fibronectin type III domain;

492-560

9.00e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 45.87 E-value: 9.00e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907074051  492 SPVKDLGISP-NPNSLLISWSR---GSGNVEQYRLVL--MDKGAIVQDTNVDRRDTSYAFHELTPGHLYNLTIVT 560
Cdd:pfam00041    1 SAPSNLTVTDvTSTSLTVSWTPppdGNGPITGYEVEYrpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75

FN3 super family

cl27307

Fibronectin type 3 domain [General function prediction only];

163-623

2.02e-05

Fibronectin type 3 domain [General function prediction only];

The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 50.00 E-value: 2.02e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  163 RNSAASQIATTANTVPYSPSHISNTTETFLGSTTETLRSTAETLGSTAETLRNTAKT-LGSTAETLRNTAKTLGSTAETL 241
Cdd:COG3401      1 TGSSYLTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVaAGLSSGGGLGTGGRAGTTSGVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  242 GSTAKTLGSTAKTLGSTAKTLGSTSEAYSQSSSKRGLPHLHTAGATDESWSPLTTPPFSSITTETGVAEQvkcNFTLLES 321
Cdd:COG3401     81 AVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGV---DGANASG 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  322 RVSSLSASIQWRTFASPCNFSLIYSSDTSGPMWCHPIridnftygcNPKDLQAGTVYNFRIVSLDG--------EESTLV 393
Cdd:COG3401    158 TTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVD---------GGGDIEPGTTYYYRVAATDTggesapsnEVSVTT 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  394 LQTDPLPPARFEVNREKTASTTLQvrWTPSSGK-VSWYEVQLFDHNNQKIQEVqvqESTTWSQYTFLNLTEGNSYKVAIT 472
Cdd:COG3401    229 PTTPPSAPTGLTATADTPGSVTLS--WDPVTESdATGYRVYRSNSGDGPFTKV---ATVTTTSYTDTGLTNGTTYYYRVT 303

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  473 AV--SGEK--RSFPVYIN-GSTVPSPVKDL-GISPNPNSLLISWSRGSGNVEQYRLVLMDKGAIVQDTNVDR--RDTSYA 544
Cdd:COG3401    304 AVdaAGNEsaPSNVVSVTtDLTPPAAPSGLtATAVGSSSITLSWTASSDADVTGYNVYRSTSGGGTYTKIAEtvTTTSYT 383

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907074051  545 FHELTPGHLYNLTIVTMASGLQNSrwklvrTAPMEVSNLKVTNDGRLTSLNVKWQKPPGDVDSYSITLSHQGTIKESKT 623
Cdd:COG3401    384 DTGLTPGTTYYYKVTAVDAAGNES------APSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAA 456

Name

Accession

Description

Interval

E-value

R-PTPc-B

cd14617

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

2019-2246

8.73e-177

Pssm-ID: 350465 [Multi-domain] Cd Length: 228 Bit Score: 538.74 E-value: 8.73e-177

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2019 NRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRV 2098
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2099 KCDHYWPADQDPLYYGDLILQMVSESVLPEWTIREFKICSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 2178
Cdd:cd14617     81 KCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907074051 2179 INRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2246
Cdd:cd14617    161 INRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

1990-2248

1.06e-115

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 367.37 E-value: 1.06e-115

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  1990 LLSKEYEDLKDVGRS-QSCDIALLPENRGKNRYNNILPYDASRVKLcNVDDDPCSDYINASYIPGNNFRREYIATQGPLP 2068
Cdd:smart00194    1 GLEEEFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKL-KPPPGEGSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  2069 GTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQ-DPLYYGDLILQMVSESVLPEWTIREFKICSEEQlDAHRL 2147
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGC-SETRT 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  2148 IRHFHYTVWPDHGVPETTQSLIQFVRTVRDYinRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDL 2227
Cdd:smart00194  159 VTHYHYTNWPDHGVPESPESILDLIRAVRKS--QSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKEL 236

                           250       260
                    ....*....|....*....|.
gi 1907074051  2228 RLHRVHMVQTECQYVYLHQCV 2248
Cdd:smart00194  237 RSQRPGMVQTEEQYIFLYRAI 257

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

2015-2248

3.45e-101

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 324.58 E-value: 3.45e-101

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2015 NRGKNRYNNILPYDASRVKLcnVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVE 2094
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL--TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2095 KGRVKCDHYWP-ADQDPLYYGDLILQMVSE-SVLPEWTIREFKIcSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFV 2172
Cdd:pfam00102   79 KGREKCAQYWPeEEGESLEYGDFTVTLKKEkEDEKDYTVRTLEV-SNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907074051 2173 RTVRDYiNRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2248
Cdd:pfam00102  158 RKVRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232

beta-trefoil_Ricin_PTPRB-like

cd23409

ricin B-type lectin domain, beta-trefoil fold, found in receptor-type tyrosine-protein ...

18-133

7.52e-53

ricin B-type lectin domain, beta-trefoil fold, found in receptor-type tyrosine-protein phosphatase beta (PTPRB) isoform e and similar proteins; PTPRB (EC 3.1.3.48), also called protein-tyrosine phosphatase beta, R-PTP-beta, vascular endothelial protein tyrosine phosphatase, or VE-PTP, plays an important role in blood vessel remodeling and angiogenesis. It is not necessary for the initial formation of blood vessels but is essential for their maintenance and remodeling. It is also essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells, which requires the presence of plakoglobin. The subfamily corresponds to PTPRB isoform e, which contains an extra ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.

Pssm-ID: 467787 Cd Length: 117 Bit Score: 181.48 E-value: 7.52e-53

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051   18 LEGFQIVHVRKQQCLSINQKVVMGFCNGSSRNQQWLSTEDGKFLHIKSGLCLGISNSSRGPFQPAVATPCAQAPRWTCHA 97
Cdd:cd23409      1 SEGFLILHVQKQQCLFGNKTVSVGKCNATSPNQQWQWTEDGKLLHVKSGQCLGISNSSAFHSRRAILLDCSQAPRWTCHE 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1907074051   98 QEGFLEVENTSLFLKKQNHKVVVKKISKYLDSWMKL 133
Cdd:cd23409     81 NEGLLEVANSSLFLTKQGQRVVVKQGKKYLHNWMKY 116

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

2013-2266

1.00e-41

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 155.63 E-value: 1.00e-41

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2013 PENRGKNRYNNILPYDASRVKlcnvDDDPcsdYINASYIPGNNFRReYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQC 2092
Cdd:COG5599     40 INGSPLNRFRDIQPYKETALR----ANLG---YLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASD 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2093 VE--KGRVKCDHYWPADqdplyyGDLILQMVS------ESVLPEWTIREFKI----CSEEQLDahrlIRHFHYTVWPDHG 2160
Cdd:COG5599    112 DEisKPKVKMPVYFRQD------GEYGKYEVSseltesIQLRDGIEARTYVLtikgTGQKKIE----IPVLHVKNWPDHG 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2161 VPETTQsLIQFVRTVRDYIN-RSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKD--SVDIYGAVHDLRLHR-VHMVQ 2236
Cdd:COG5599    182 AISAEA-LKNLADLIDKKEKiKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQ 260

                          250       260       270
                   ....*....|....*....|....*....|
gi 1907074051 2237 TECQYvylhqcvrDVLraKKLRNEQENPLF 2266
Cdd:COG5599    261 TSEQL--------DVL--VKLAEQQIRPLL 280

PHA02742

protein tyrosine phosphatase; Provisional

1972-2257

2.53e-41

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 155.55 E-value: 2.53e-41

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1972 KINQFEGHFMKLQADSN--YLLSKEYEDLKDVGRSQSCDIALLPENRGKNRYNNILPYDASRVKLCNvdDDPCSDYINAS 2049
Cdd:PHA02742     7 KKNSFAKNCEQLIEESNlaEILKEEHEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILKI--EDGGDDFINAS 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2050 YIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYW-PADQDPLYYGDLILQMVSESVLPE 2128
Cdd:PHA02742    85 YVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRN 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2129 WTIREFKIcSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVR--DYINRSPGAG-------PTVVHCSAGVGRT 2199
Cdd:PHA02742   165 YAVTNLCL-TDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVReaDLKADVDIKGenivkepPILVHCSAGLDRA 243

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907074051 2200 GTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYlhqCVRDVLRAKKL 2257
Cdd:PHA02742   244 GAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF---CYFIVLIFAKL 298

PTP_tm

pfam18861

TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases ...

1761-1898

1.04e-33

Pssm-ID: 465889 Cd Length: 126 Bit Score: 126.95 E-value: 1.04e-33

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1761 VNCSWFSDTNGAVKYFAVVVREADSmdELKPEQQHPLPSYLEYRhNASIRVYQTNYFASKCAeSPDSSSKSFNIKLGAEM 1840
Cdd:pfam18861    1 IQFSLFNSSNGPIKAYGVIVTTNDS--LNRPLKEYLNKTYYDWK-YKKTDSYLATVTPNPFT-SPRSSSRSLTVPVGTGS 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907074051 1841 DSlggkcdpsqQKFCDGPLKPHTAYRISIRAFTQL-FDEDLKEFTKPLYSDTFFSMPIT 1898
Cdd:pfam18861   77 KW---------QGYCNGPLKPLGSYRFSVAAFTRLeFDDGLIDGEESYVSFTPFSEPIA 126

fn3

Fibronectin type III domain;

1550-1632

1.39e-11

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 62.43 E-value: 1.39e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1550 SPPSLLSFADVANTSLAITWKGPPDWT-DYNDFELQWFPGDALTIFNPYSSRKSEGR-IVYGLHPGRSYQFSVKTVSGDS 1627
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNgPITGYEVEYRPKNSGEPWNEITVPGTTTSvTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 1907074051 1628 WKTYS 1632
Cdd:pfam00041   81 EGPPS 85

fn3

Fibronectin type III domain;

1644-1723

2.98e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 58.58 E-value: 2.98e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1644 DKIQNLHCRPQNSTAIACSWIPP---DSDFDGYSIECRKMDTQEIEFSRKLEKEKSLLNIMMLVPHKRYLVSIKVQSAGM 1720
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1907074051 1721 TSE 1723
Cdd:pfam00041   81 EGP 83

FN3

Fibronectin type 3 domain [General function prediction only];

1341-1674

3.05e-09

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 62.33 E-value: 3.05e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1341 EDLTPGKKYKMQILTVSGGLFSKESQA----EGRTVPAAVTNLRITENSSRYLSFGWTASEGE-LSWYNIFLYN-PDRTL 1414
Cdd:COG3401    197 GDIEPGTTYYYRVAATDTGGESAPSNEvsvtTPTTPPSAPTGLTATADTPGSVTLSWDPVTESdATGYRVYRSNsGDGPF 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1415 QERAQVDplVQSFSFQNLLQGR--MYKMVIVTHSGELSNESFIF----GRTVPAAVNHLKGShRNTTDSLWFSWSPASG- 1487
Cdd:COG3401    277 TKVATVT--TTSYTDTGLTNGTtyYYRVTAVDAAGNESAPSNVVsvttDLTPPAAPSGLTAT-AVGSSSITLSWTASSDa 353

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1488 DFDFYElILYNPNGTKKENW--KEKDVTEWRFQGLVPGRKYTlYVVT------HSGDLSNKVTGEGRTAPSPPSLLSFAD 1559
Cdd:COG3401    354 DVTGYN-VYRSTSGGGTYTKiaETVTTTSYTDTGLTPGTTYY-YKVTavdaagNESAPSEEVSATTASAASGESLTASVD 431

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1560 VANT---------SLAITWKGPPDWTDYNDFELQWFPGDALTIFNPYSSRKSEGRIVYGLHPGRSYQFSVKTVSGDSWKT 1630
Cdd:COG3401    432 AVPLtdvagataaASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSV 511

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1907074051 1631 YSKPISGSVRTKPDKIQNLHCRPQNS-TAIACSWIPPDSDFDGYS 1674
Cdd:COG3401    512 IGASAAAAVGGAPDGTPNVTGASPVTvGASTGDVLITDLVSLTTS 556

fn3

Fibronectin type III domain;

1020-1096

1.40e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 53.96 E-value: 1.40e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1020 DKVQGISVSNsARSDYLKVSWVHAT---GDFDHYEVTI--KNRESFIQTKTIPKSENECEFIELVPGRLYSVTVSTKSGQ 1094
Cdd:pfam00041    1 SAPSNLTVTD-VTSTSLTVSWTPPPdgnGPITGYEVEYrpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ..
gi 1907074051 1095 YE 1096
Cdd:pfam00041   80 GE 81

FN3

Fibronectin type 3 domain [General function prediction only];

856-1309

1.56e-08

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 60.02 E-value: 1.56e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  856 TSSLFTNWTKALGDVEFYQVLLIHENVVVKNESVSSDTSRYSFRALKPGSLYSVVVTTVSGGISSRQVVAEGRTVPSSVS 935
Cdd:COG3401     61 LSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGT 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  936 GVTVNNSGRNDYLSVSWLPAPGEVDHYVVSLSH-----EGKVDQFLIIAKSVSECSFSsLTPGRLYNVTVTTKSGNYAS- 1009
Cdd:COG3401    141 YALGAGLYGVDGANASGTTASSVAGAGVVVSPDtsataAVATTSLTVTSTTLVDGGGD-IEPGTTYYYRVAATDTGGESa 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1010 ----HSFTEERTVPDKVQGISVSnSARSDYLKVSWV-HATGDFDHYEVTIKNRESfiQTKTIPKSENECEFI--ELVPGR 1082
Cdd:COG3401    220 psneVSVTTPTTPPSAPTGLTAT-ADTPGSVTLSWDpVTESDATGYRVYRSNSGD--GPFTKVATVTTTSYTdtGLTNGT 296

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1083 LYSVTVSTKSGQYEASEQ------GTGRTIPEPVKDLTLLNRSTEDLHVTWS-RANGDVDQYEVQLLFNDMKVFPHIHLV 1155
Cdd:COG3401    297 TYYYRVTAVDAAGNESAPsnvvsvTTDLTPPAAPSGLTATAVGSSSITLSWTaSSDADVTGYNVYRSTSGGGTYTKIAET 376

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1156 NTATEYKFTALTPGRHYKILVLTISGDVQQSAFIEGLTVPSTVKNIHISANGATDR---------LMVTWSPGGGDVDSY 1226
Cdd:COG3401    377 VTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAvpltdvagaTAAASAASNPGVSAA 456

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1227 VVSAFRQDEKVDSQT-------IPKHASEHTFHRLEAGAKYRIAIVSVSGSLRNQIDALGQTVPASVQGVVaANAYSSNS 1299
Cdd:COG3401    457 VLADGGDTGNAVPFTttsstvtATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGT-PNVTGASP 535

                          490
                   ....*....|
gi 1907074051 1300 LTVSWQKALG 1309
Cdd:COG3401    536 VTVGASTGDV 545

fn3

Fibronectin type III domain;

579-658

1.71e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 53.57 E-value: 1.71e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  579 EVSNLKVTNDGRlTSLNVKWQKPP---GDVDSYSITLSHQGTIKESK--TLAPPVTETQFKDLVPGRLYQVTISCISGEL 653
Cdd:pfam00041    2 APSNLTVTDVTS-TSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNeiTVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 1907074051  654 SAEKS 658
Cdd:pfam00041   81 EGPPS 85

fn3

Fibronectin type III domain;

1109-1182

2.12e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 53.19 E-value: 2.12e-08

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907074051 1109 PVKDLTLLNRSTEDLHVTWSRA---NGDVDQYEVQLL-FNDMKVFPHIHLVNTATEYKFTALTPGRHYKILVLTISGD 1182
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

fn3

Fibronectin type III domain;

1473-1536

2.39e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 53.19 E-value: 2.39e-08

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907074051 1473 NTTDSLWFSWSPA---SGDFDFYELILYNPNGTKKENWKE--KDVTEWRFQGLVPGRKYTLYVVTHSGD 1536
Cdd:pfam00041   11 VTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITvpGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

fn3

Fibronectin type III domain;

757-835

2.56e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 53.19 E-value: 2.56e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  757 AVLQLRVKHANETSLGITWRAPL---GEWEKYIISL--MDRELLVIHKSLSKDAKEFTFTDLMPGRNYKATVTSMSGDLK 831
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYrpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ....
gi 1907074051  832 QSSS 835
Cdd:pfam00041   82 GPPS 85

FN3

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

398-483

3.33e-08

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 52.88 E-value: 3.33e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  398 PLPPARFEVnrEKTASTTLQVRWTPSS---GKVSWYEVQLFDHNNQKIQEVQVQESTTwSQYTFLNLTEGNSYKVAITAV 474
Cdd:cd00063      1 PSPPTNLRV--TDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSE-TSYTLTGLKPGTEYEFRVRAV 77


                   ....*....
gi 1907074051  475 SGEKRSFPV 483
Cdd:cd00063     78 NGGGESPPS 86

Ricin_B_lectin

pfam00652

Ricin-type beta-trefoil lectin domain;

22-93

3.45e-07

Ricin-type beta-trefoil lectin domain;

Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 51.38 E-value: 3.45e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051   22 QIVHVRKQQCLSINQ-----KVVMGFCNGSSRNQQWLSTEDGKFL-HIKSGLCLGISNSSRGPFQPAVATPCAQAP--RW 93
Cdd:pfam00652   47 TIRSVASDLCLDVGStadgaKVVLWPCHPGNGNQRWRYDEDGTQIrNPQSGKCLDVSGAGTSNGKVILWTCDSGNPnqQW 126

FN3

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

1643-1731

1.01e-06

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 49.03 E-value: 1.01e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1643 PDKIQNLHCRPQNSTAIACSWIPPDSD---FDGYSIECRKMDTQEIEFSRKLEKEKSLLNIMMLVPHKRYLVSIKVQSAG 1719
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDggpITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|..
gi 1907074051 1720 MTSEVVEDSTIT 1731
Cdd:cd00063     81 GESPPSESVTVT 92

fn3

Fibronectin type III domain;

413-482

1.63e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 48.18 E-value: 1.63e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907074051  413 STTLQVRWTPS---SGKVSWYEVQLFDHN-NQKIQEVQVQESTTwsQYTFLNLTEGNSYKVAITAVSGEKRSFP 482
Cdd:pfam00041   13 STSLTVSWTPPpdgNGPITGYEVEYRPKNsGEPWNEITVPGTTT--SVTLTGLKPGTEYEVRVQAVNGGGEGPP 84

FN3

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

1549-1636

2.28e-06

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 47.88 E-value: 2.28e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1549 PSPPSLLSFADVANTSLAITWKGPPDWTDYND-FELQWFPGDALTIFNPYSSRKSEGR-IVYGLHPGRSYQFSVKTVSGD 1626
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITgYVVEYREKGSGDWKEVEVTPGSETSyTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|
gi 1907074051 1627 SWKTYSKPIS 1636
Cdd:cd00063     81 GESPPSESVT 90

fn3

Fibronectin type III domain;

681-742

5.21e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 46.64 E-value: 5.21e-06

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907074051  681 SFTVNWTPPA---GDWEHYRIVLF--NESLVLLNTTVGKEETHYALDGLEliPGRQYEIEVIVESGN 742
Cdd:pfam00041   15 SLTVSWTPPPdgnGPITGYEVEYRpkNSGEPWNEITVPGTTTSVTLTGLK--PGTEYEVRVQAVNGG 79

FN3

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

577-652

6.05e-06

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 46.72 E-value: 6.05e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  577 PMEVSNLKVTNDGRlTSLNVKWQKPPGD---VDSYSITLS--HQGTIKESKTLAPPVTETQFKDLVPGRLYQVTISCISG 651
Cdd:cd00063      1 PSPPTNLRVTDVTS-TSVTLSWTPPEDDggpITGYVVEYRekGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79


                   .
gi 1907074051  652 E 652
Cdd:cd00063     80 G 80

fn3

Fibronectin type III domain;

492-560

9.00e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 45.87 E-value: 9.00e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907074051  492 SPVKDLGISP-NPNSLLISWSR---GSGNVEQYRLVL--MDKGAIVQDTNVDRRDTSYAFHELTPGHLYNLTIVT 560
Cdd:pfam00041    1 SAPSNLTVTDvTSTSLTVSWTPppdGNGPITGYEVEYrpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75

FN3

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

491-560

1.39e-05

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

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 45.30 E-value: 1.39e-05

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907074051   491 PSPVKDLGISP-NPNSLLISWSR-----GSGNVEQYRLVLMDKGAIVQDTNVDRRDTSYAFHELTPGHLYNLTIVT 560
Cdd:smart00060    1 PSPPSNLRVTDvTSTSVTLSWEPppddgITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRA 76

FN3

Fibronectin type 3 domain [General function prediction only];

163-623

2.02e-05

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 50.00 E-value: 2.02e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  163 RNSAASQIATTANTVPYSPSHISNTTETFLGSTTETLRSTAETLGSTAETLRNTAKT-LGSTAETLRNTAKTLGSTAETL 241
Cdd:COG3401      1 TGSSYLTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVaAGLSSGGGLGTGGRAGTTSGVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  242 GSTAKTLGSTAKTLGSTAKTLGSTSEAYSQSSSKRGLPHLHTAGATDESWSPLTTPPFSSITTETGVAEQvkcNFTLLES 321
Cdd:COG3401     81 AVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGV---DGANASG 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  322 RVSSLSASIQWRTFASPCNFSLIYSSDTSGPMWCHPIridnftygcNPKDLQAGTVYNFRIVSLDG--------EESTLV 393
Cdd:COG3401    158 TTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVD---------GGGDIEPGTTYYYRVAATDTggesapsnEVSVTT 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  394 LQTDPLPPARFEVNREKTASTTLQvrWTPSSGK-VSWYEVQLFDHNNQKIQEVqvqESTTWSQYTFLNLTEGNSYKVAIT 472
Cdd:COG3401    229 PTTPPSAPTGLTATADTPGSVTLS--WDPVTESdATGYRVYRSNSGDGPFTKV---ATVTTTSYTDTGLTNGTTYYYRVT 303

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  473 AV--SGEK--RSFPVYIN-GSTVPSPVKDL-GISPNPNSLLISWSRGSGNVEQYRLVLMDKGAIVQDTNVDR--RDTSYA 544
Cdd:COG3401    304 AVdaAGNEsaPSNVVSVTtDLTPPAAPSGLtATAVGSSSITLSWTASSDADVTGYNVYRSTSGGGTYTKIAEtvTTTSYT 383

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907074051  545 FHELTPGHLYNLTIVTMASGLQNSrwklvrTAPMEVSNLKVTNDGRLTSLNVKWQKPPGDVDSYSITLSHQGTIKESKT 623
Cdd:COG3401    384 DTGLTPGTTYYYKVTAVDAAGNES------APSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAA 456

FN3

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

577-651

2.10e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 44.91 E-value: 2.10e-05

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051   577 PMEVSNLKVTNDGRlTSLNVKWQKPPGD-----VDSYSITLSHQGTIKESKTLAPPVTETQFKDLVPGRLYQVTISCISG 651
Cdd:smart00060    1 PSPPSNLRVTDVTS-TSVTLSWEPPPDDgitgyIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

FN3

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

1549-1628

2.55e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 44.53 E-value: 2.55e-05

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  1549 PSPPSLLSFADVANTSLAITWKGPPD--WTDYND-FELQWFPGDALTIFNPYSSRKSEGRIVyGLHPGRSYQFSVKTVSG 1625
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDdgITGYIVgYRVEYREEGSEWKEVNVTPSSTSYTLT-GLKPGTEYEFRVRAVNG 79


                    ...
gi 1907074051  1626 DSW 1628
Cdd:smart00060   80 AGE 82

Herpes_BLLF1

pfam05109

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...

158-352

2.65e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.

Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 49.53 E-value: 2.65e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  158 SVRTARNSAASQIATTANTVPYSPSHISNTTETFLGSTTETLRSTAETLGSTAETLRNTAKTLGSTAETLRNTAKTLGST 237
Cdd:pfam05109  512 AVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNAT 591

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  238 AETLGSTAKTLGSTAKTLGSTAKTLGSTSEAYSQSSSKRGLPHLHTAGATdeswSPLTTPPFS-SITTETGVAEQVKCNF 316
Cdd:pfam05109  592 SPTVGETSPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSST----SSMSLRPSSiSETLSPSTSDNSTSHM 667

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1907074051  317 TLLESRVSSLSASIQWRTFASPCNFSLIYSSDTSGP 352
Cdd:pfam05109  668 PLLTSAHPTGGENITQVTPASTSTHHVSTSSPAPRP 703

RICIN

smart00458

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.

23-74

4.17e-05

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.

Pssm-ID: 214672 [Multi-domain] Cd Length: 118 Bit Score: 45.19 E-value: 4.17e-05

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1907074051    23 IVHVRKQQCLSI---NQKVVMGFCNGSSRNQQWLSTEDGKFLHIKSGLCLGISNS 74
Cdd:smart00458    1 IISGNTGKCLDVngnKNPVGLFDCHGTGGNQLWKLTSDGAIRIKDTDLCLTANGN 55

FN3

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

398-480

5.81e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 43.76 E-value: 5.81e-05

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051   398 PLPPARFEVnrEKTASTTLQVRWT-PSSGKVSWYEVQLFDHNNQK-IQEVQVQESTTWSQYTFLNLTEGNSYKVAITAVS 475
Cdd:smart00060    1 PSPPSNLRV--TDVTSTSVTLSWEpPPDDGITGYIVGYRVEYREEgSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 1907074051   476 GEKRS 480
Cdd:smart00060   79 GAGEG 83

FN3

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

755-828

2.65e-04

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 41.83 E-value: 2.65e-04

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907074051   755 PLAVLQLRVKHANETSLGITWRAP-----LGEWEKYIISLMDRELLVIHKSLSKDAKEFTFTDLMPGRNYKATVTSMSG 828
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPpddgiTGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

FN3

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

755-840

4.02e-04

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 41.33 E-value: 4.02e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  755 PLAVLQLRVKHANETSLGITWRAPL---GEWEKYIISL--MDRELLVIHKSLSKDAKEFTFTDLMPGRNYKATVTSMSGD 829
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYreKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|...
gi 1907074051  830 L--KQSSSIKGRT 840
Cdd:cd00063     81 GesPPSESVTVTT 93

FN3

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

931-1009

4.98e-04

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 41.33 E-value: 4.98e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  931 PSSVSGVTVNNSGRnDYLSVSWLPAP---GEVDHYVVSLSHEGKVDQFLIIAKSVSECSF--SSLTPGRLYNVTVTTKSG 1005
Cdd:cd00063      1 PSPPTNLRVTDVTS-TSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYtlTGLKPGTEYEFRVRAVNG 79


                   ....
gi 1907074051 1006 NYAS 1009
Cdd:cd00063     80 GGES 83

FN3

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

1019-1105

5.03e-04

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 41.33 E-value: 5.03e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1019 PDKVQGISVSNSaRSDYLKVSWVHATGD---FDHYEVTIK--NRESFIQTKTIPKSENECEFIELVPGRLYSVTVS--TK 1091
Cdd:cd00063      1 PSPPTNLRVTDV-TSTSVTLSWTPPEDDggpITGYVVEYRekGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRavNG 79

                           90
                   ....*....|....
gi 1907074051 1092 SGQYEASEQGTGRT 1105
Cdd:cd00063     80 GGESPPSESVTVTT 93

PRK12688

flagellin; Reviewed

152-268

5.91e-04

flagellin; Reviewed

Pssm-ID: 171664 [Multi-domain] Cd Length: 751 Bit Score: 45.25 E-value: 5.91e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  152 GLGTEVSVRTARNS----------AASQIATTA--NTVPYSPShiSNTTETFLGSTTETLRSTAETLGSTAETLRNTAKT 219
Cdd:PRK12688    66 GIGNGVQILQAANTgitslqklidSAKSIANQAlqTVVGYSTK--SNVSTTISGATADDLRGTTSYASATASSNVLYDGA 143

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1907074051  220 LGSTaeTLRNTAKTLGSTAETLGSTAKTLGSTAKTLGSTAKTLGSTSEA 268
Cdd:PRK12688   144 AGGA--TAATGATTLGGTAGSLAGTGATAGDGTTALTGTITLIATNGTT 190

FN3

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

491-559

1.43e-03

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 39.79 E-value: 1.43e-03

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907074051  491 PSPVKDLGISP-NPNSLLISWSR---GSGNVEQYRLVLMDKGA--IVQDTNVDRRDTSYAFHELTPGHLYNLTIV 559
Cdd:cd00063      1 PSPPTNLRVTDvTSTSVTLSWTPpedDGGPITGYVVEYREKGSgdWKEVEVTPGSETSYTLTGLKPGTEYEFRVR 75

FN3

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

665-742

2.17e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 39.13 E-value: 2.17e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051   665 PEKVRNLVSYNeIWMKSFTVNWTPPAGDWE-----HYRIVLFNESLVLLNTTVGKEETHYALDGLEliPGRQYEIEVIVE 739
Cdd:smart00060    1 PSPPSNLRVTD-VTSTSVTLSWEPPPDDGItgyivGYRVEYREEGSEWKEVNVTPSSTSYTLTGLK--PGTEYEFRVRAV 77


                    ...
gi 1907074051   740 SGN 742
Cdd:smart00060   78 NGA 80

FN3

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

1461-1553

2.45e-03

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 39.40 E-value: 2.45e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1461 PAAVNHLKGSHrNTTDSLWFSWSPASGD---FDFYELILYNPNGTKKENWKEKDV--TEWRFQGLVPGRKYTLYVVThsg 1535
Cdd:cd00063      1 PSPPTNLRVTD-VTSTSVTLSWTPPEDDggpITGYVVEYREKGSGDWKEVEVTPGseTSYTLTGLKPGTEYEFRVRA--- 76

                           90
                   ....*....|....*...
gi 1907074051 1536 dlsnkVTGEGRTAPSPPS 1553
Cdd:cd00063     77 -----VNGGGESPPSESV 89

FN3

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

1461-1535

2.72e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 38.75 E-value: 2.72e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  1461 PAAVNHLKGSHrNTTDSLWFSWSPASGDFDFYELILYNP-NGTKKENWKEKDV----TEWRFQGLVPGRKYTLYVVTHSG 1535
Cdd:smart00060    1 PSPPSNLRVTD-VTSTSVTLSWEPPPDDGITGYIVGYRVeYREEGSEWKEVNVtpssTSYTLTGLKPGTEYEFRVRAVNG 79

FN3

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

931-1006

4.19e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 38.36 E-value: 4.19e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051   931 PSSVSGVTVNNSGRNdYLSVSWLPAP-----GEVDHYVVSLSHEGKVDQFLIIAKSVSECSFSSLTPGRLYNVTVTTKSG 1005
Cdd:smart00060    1 PSPPSNLRVTDVTST-SVTLSWEPPPddgitGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    .
gi 1907074051  1006 N 1006
Cdd:smart00060   80 A 80

FN3

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

1019-1094

5.68e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 37.98 E-value: 5.68e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  1019 PDKVQGISVSNSArSDYLKVSWVHATGD-FDHYEV--TIKNRESFIQTKTIPKSENECEFI--ELVPGRLYSVTVSTKSG 1093
Cdd:smart00060    1 PSPPSNLRVTDVT-STSVTLSWEPPPDDgITGYIVgyRVEYREEGSEWKEVNVTPSSTSYTltGLKPGTEYEFRVRAVNG 79


                    .
gi 1907074051  1094 Q 1094
Cdd:smart00060   80 A 80

FN3

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

665-742

6.25e-03

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 38.25 E-value: 6.25e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  665 PEKVRNLvSYNEIWMKSFTVNWTPPAGD---WEHYRIVLF--NESLVLLNTTVGKEETHYALDGLEliPGRQYEIEVIVE 739
Cdd:cd00063      1 PSPPTNL-RVTDVTSTSVTLSWTPPEDDggpITGYVVEYRekGSGDWKEVEVTPGSETSYTLTGLK--PGTEYEFRVRAV 77


                   ...
gi 1907074051  740 SGN 742
Cdd:cd00063     78 NGG 80

Name

Accession

Description

Interval

E-value

R-PTPc-B

cd14617

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

2019-2246

8.73e-177

Pssm-ID: 350465 [Multi-domain] Cd Length: 228 Bit Score: 538.74 E-value: 8.73e-177

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2019 NRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRV 2098
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2099 KCDHYWPADQDPLYYGDLILQMVSESVLPEWTIREFKICSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 2178
Cdd:cd14617     81 KCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907074051 2179 INRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2246
Cdd:cd14617    161 INRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228

R3-PTPc

cd14548

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

2020-2246

3.87e-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: 441.41 E-value: 3.87e-142

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2020 RYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVK 2099
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2100 CDHYWPADQDPLYYGDLILQMVSESVLPEWTIREFKICseeQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYI 2179
Cdd:cd14548     81 CDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLE---RGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYI 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907074051 2180 NRspGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2246
Cdd:cd14548    158 KQ--EKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

1990-2248

1.06e-115

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 367.37 E-value: 1.06e-115

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  1990 LLSKEYEDLKDVGRS-QSCDIALLPENRGKNRYNNILPYDASRVKLcNVDDDPCSDYINASYIPGNNFRREYIATQGPLP 2068
Cdd:smart00194    1 GLEEEFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKL-KPPPGEGSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  2069 GTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQ-DPLYYGDLILQMVSESVLPEWTIREFKICSEEQlDAHRL 2147
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGC-SETRT 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  2148 IRHFHYTVWPDHGVPETTQSLIQFVRTVRDYinRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDL 2227
Cdd:smart00194  159 VTHYHYTNWPDHGVPESPESILDLIRAVRKS--QSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKEL 236

                           250       260
                    ....*....|....*....|.
gi 1907074051  2228 RLHRVHMVQTECQYVYLHQCV 2248
Cdd:smart00194  237 RSQRPGMVQTEEQYIFLYRAI 257

R-PTPc-J

cd14615

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

2019-2250

1.27e-112

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: 357.20 E-value: 1.27e-112

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2019 NRYNNILPYDASRVKLCNvDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRV 2098
Cdd:cd14615      1 NRYNNVLPYDISRVKLSV-QSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2099 KCDHYWPADQdPLYYGDLILQMVSESVLPEWTIREFKIcSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 2178
Cdd:cd14615     80 KCEEYWPSKQ-KKDYGDITVTMTSEIVLPEWTIRDFTV-KNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREY 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907074051 2179 INRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRD 2250
Cdd:cd14615    158 MKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229

R-PTPc-O

cd14614

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

2008-2249

4.15e-106

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: 339.17 E-value: 4.15e-106

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2008 DIALLPENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIV 2087
Cdd:cd14614      5 FAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIV 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2088 MVTQCVEKGRVKCDHYWPADQDPLYYGDLILQMVSESVLPEWTIREFKIcseEQLDAHRLIRHFHYTVWPDHGVP--ETT 2165
Cdd:cd14614     85 MLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRV---SYADEVQDVMHFNYTAWPDHGVPtaNAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2166 QSLIQFVRTVRDYINRSPgaGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 2245
Cdd:cd14614    162 ESILQFVQMVRQQAVKSK--GPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 239


                   ....
gi 1907074051 2246 QCVR 2249
Cdd:cd14614    240 QCVQ 243

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

2015-2248

3.45e-101

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 324.58 E-value: 3.45e-101

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2015 NRGKNRYNNILPYDASRVKLcnVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVE 2094
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL--TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2095 KGRVKCDHYWP-ADQDPLYYGDLILQMVSE-SVLPEWTIREFKIcSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFV 2172
Cdd:pfam00102   79 KGREKCAQYWPeEEGESLEYGDFTVTLKKEkEDEKDYTVRTLEV-SNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907074051 2173 RTVRDYiNRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2248
Cdd:pfam00102  158 RKVRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232

R-PTPc-H

cd14619

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

2019-2252

5.13e-101

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.

Pssm-ID: 350467 [Multi-domain] Cd Length: 233 Bit Score: 324.15 E-value: 5.13e-101

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2019 NRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRV 2098
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2099 KCDHYWPADQDPLYYGDLILQMVSESVLPEWTIREFKICSEEQlDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 2178
Cdd:cd14619     81 KCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEE-QKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQW 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907074051 2179 INRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVL 2252
Cdd:cd14619    160 LDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233

R-PTPc-V

cd14618

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

2019-2248

9.79e-97

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: 311.88 E-value: 9.79e-97

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2019 NRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRV 2098
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2099 KCDHYWPADQDPLYYGDLILQMVSESVLPEWTIREFKIcSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 2178
Cdd:cd14618     81 LCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKL-WHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREH 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2179 INRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2248
Cdd:cd14618    160 VQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229

PTPc

cd00047

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

2045-2246

4.26e-89

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: 288.41 E-value: 4.26e-89

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2045 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQD-PLYYGDLILQMVSE 2123
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGkPLEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2124 SVLPEWTIREFKIcSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYinRSPGAGPTVVHCSAGVGRTGTFV 2203
Cdd:cd00047     81 EELSDYTIRTLEL-SPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKE--ARKPNGPIVVHCSAGVGRTGTFI 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1907074051 2204 ALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2246
Cdd:cd00047    158 AIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200

R-PTPc-LAR-1

cd14553

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

2015-2248

7.57e-89

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: 289.68 E-value: 7.57e-89

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2015 NRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVE 2094
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2095 KGRVKCDHYWPADqDPLYYGDLILQMVSESVLPEWTIREFKICSEEQLDaHRLIRHFHYTVWPDHGVPETTQSLIQFVRT 2174
Cdd:cd14553     83 RSRVKCDQYWPTR-GTETYGLIQVTLLDTVELATYTVRTFALHKNGSSE-KREVRQFQFTAWPDHGVPEHPTPFLAFLRR 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907074051 2175 VRDYinRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2248
Cdd:cd14553    161 VKAC--NPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232

R-PTPc-Q

cd14616

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

2019-2246

2.69e-83

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: 272.94 E-value: 2.69e-83

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2019 NRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRV 2098
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2099 KCDHYWPADQDPL-YYGDLILQMVSESVLPEWTIREFKIcseEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRd 2177
Cdd:cd14616     81 RCHQYWPEDNKPVtVFGDIVITKLMEDVQIDWTIRDLKI---ERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVR- 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907074051 2178 yINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2246
Cdd:cd14616    157 -ASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224

PTPc-N9

cd14543

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

1993-2245

3.33e-83

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: 274.63 E-value: 3.33e-83

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1993 KEYEDLKDVGRSQSCDIALLPENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKD 2072
Cdd:cd14543      7 EEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYS 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2073 DFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDP-LYYGDLILQMVSESVLPEWTIREFKICSEEQlDAHRLIRHF 2151
Cdd:cd14543     87 DFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSsLRYGDLTVTNLSVENKEHYKKTTLEIHNTET-DESRQVTHF 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2152 HYTVWPDHGVPETTQSLIQFVRTVRDYINRS-----------PGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDI 2220
Cdd:cd14543    166 QFTSWPDFGVPSSAAALLDFLGEVRQQQALAvkamgdrwkghPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNV 245

                          250       260
                   ....*....|....*....|....*
gi 1907074051 2221 YGAVHDLRLHRVHMVQTECQYVYLH 2245
Cdd:cd14543    246 MQTVRRMRTQRAFSIQTPDQYYFCY 270

R5-PTPc-1

cd14549

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

2045-2245

2.09e-82

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: 269.61 E-value: 2.09e-82

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2045 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDPlYYGDLILQMVSES 2124
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTE-TYGNIQVTLLSTE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2125 VLPEWTIREF-----KICSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYinRSPGAGPTVVHCSAGVGRT 2199
Cdd:cd14549     80 VLATYTVRTFslknlKLKKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAA--NPPGAGPIVVHCSAGVGRT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1907074051 2200 GTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 2245
Cdd:cd14549    158 GTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203

R-PTPc-T-1

cd14630

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

2014-2248

3.89e-75

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: 250.33 E-value: 3.89e-75

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2014 ENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCV 2093
Cdd:cd14630      2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2094 EKGRVKCDHYWPADQDplYYGDLILQMVSESVLPEWTIREFKICSEEQLDAhRLIRHFHYTVWPDHGVPETTQSLIQFVR 2173
Cdd:cd14630     82 EVGRVKCVRYWPDDTE--VYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEI-REIRQFHFTSWPDHGVPCYATGLLGFVR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907074051 2174 TVRdYINrSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2248
Cdd:cd14630    159 QVK-FLN-PPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAI 231

R-PTPc-F-1

cd14626

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

1979-2248

8.71e-75

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: 250.72 E-value: 8.71e-75

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1979 HFMKLQADSNYLLSKEYEDLkDVGRSQSCDIALLPENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRR 2058
Cdd:cd14626      6 NIERLKANDGLKFSQEYESI-DPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQN 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2059 EYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPAdQDPLYYGDLILQMVSESVLPEWTIREF---K 2135
Cdd:cd14626     85 AYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPI-RGTETYGMIQVTLLDTVELATYSVRTFalyK 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2136 ICSEEQldahRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRdyINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSK 2215
Cdd:cd14626    164 NGSSEK----REVRQFQFMAWPDHGVPEYPTPILAFLRRVK--ACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHE 237

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1907074051 2216 DSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2248
Cdd:cd14626    238 KTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEAL 270

R-PTPc-G-1

cd17667

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

2013-2252

7.96e-74

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: 248.03 E-value: 7.96e-74

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2013 PENRGKNRYNNILPYDASRVKLCNV--DDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVT 2090
Cdd:cd17667     25 PDNKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMIT 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2091 QCVEKGRVKCDHYWPADQDPlYYGDLILQMVSESVLPEWTIREFKICSEEQLDAH----------RLIRHFHYTVWPDHG 2160
Cdd:cd17667    105 NLVEKGRRKCDQYWPTENSE-EYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQkgnpkgrqneRTVIQYHYTQWPDMG 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2161 VPETTQSLIQFVRtvRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQ 2240
Cdd:cd17667    184 VPEYALPVLTFVR--RSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQ 261

                          250
                   ....*....|..
gi 1907074051 2241 YVYLHQCVRDVL 2252
Cdd:cd17667    262 YIFIHDALLEAI 273

PTPc-KIM

cd14547

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

2019-2246

2.76e-73

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: 244.23 E-value: 2.76e-73

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2019 NRYNNILPYDASRVKLCNVDDDPCSDYINASYIPG-NNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKgR 2097
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGyDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2098 VKCDHYWPADQdPLYYGDLILQMVSESVLPEWTIREFKICSEEQldaHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRD 2177
Cdd:cd14547     80 EKCAQYWPEEE-NETYGDFEVTVQSVKETDGYTVRKLTLKYGGE---KRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEE 155

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907074051 2178 YINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2246
Cdd:cd14547    156 ARQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224

PTPc-N11_6

cd14544

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

2015-2248

4.69e-72

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: 241.98 E-value: 4.69e-72

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2015 NRGKNRYNNILPYDASRVKLCNVDDD-PCSDYINASYI-PGNNFRRE------YIATQGPLPGTKDDFWKMAWEQNVHNI 2086
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRDPNvPGSDYINANYIrNENEGPTTdenaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2087 VMVTQCVEKGRVKCDHYWPADQDPLYYGDLILQMVSESVLPEWTIREFKICSEEQLDAHRLIRHFHYTVWPDHGVPETTQ 2166
Cdd:cd14544     81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPIREIWHYQYLSWPDHGVPSDPG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2167 SLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKD---SVDIYGAVHDLRLHRVHMVQTECQYVY 2243
Cdd:cd14544    161 GVLNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQTEAQYKF 240


                   ....*
gi 1907074051 2244 LHQCV 2248
Cdd:cd14544    241 IYVAV 245

R-PTPc-A-1

cd14621

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

1964-2248

6.81e-72

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).

Pssm-ID: 350469 [Multi-domain] Cd Length: 296 Bit Score: 243.39 E-value: 6.81e-72

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1964 NRKTScPIKINQFEGHFMKLQADSNYLLSKEYEDLKDVGRSQSCDIALLPENRGKNRYNNILPYDASRVKLCNVDDDPCS 2043
Cdd:cd14621      2 NRKYP-PLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2044 DYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPaDQDPLYYGDLILQMVSE 2123
Cdd:cd14621     81 DYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWP-DQGCWTYGNIRVSVEDV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2124 SVLPEWTIREFkiCSEEQLDA-----HRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRdyiNRSPG-AGPTVVHCSAGVG 2197
Cdd:cd14621    160 TVLVDYTVRKF--CIQQVGDVtnkkpQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVK---NCNPQyAGAIVVHCSAGVG 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907074051 2198 RTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2248
Cdd:cd14621    235 RTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQAL 285

R-PTPc-M-1

cd14633

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

1979-2248

2.09e-71

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: 241.10 E-value: 2.09e-71

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1979 HFMKLQADSNYLLSKEYEDLKDvGRSQSCDIALLPENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRR 2058
Cdd:cd14633      5 HITQMKCAEGYGFKEEYESFFE-GQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPN 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2059 EYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDplYYGDLILQMVSESVLPEWTIREFKIcs 2138
Cdd:cd14633     84 HYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTE--IYKDIKVTLIETELLAEYVIRTFAV-- 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2139 eEQLDAH--RLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDyiNRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKD 2216
Cdd:cd14633    160 -EKRGVHeiREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS--KSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREG 236

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1907074051 2217 SVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2248
Cdd:cd14633    237 VVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 268

R-PTP-LAR-2

cd14554

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

2010-2246

3.02e-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: 236.27 E-value: 3.02e-70

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2010 ALLPENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMV 2089
Cdd:cd14554      1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2090 TQCVEKGRVKCDHYWPADQDpLYYGDLILQMVSESVLPEWTIREFKIcSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLI 2169
Cdd:cd14554     81 TKLREMGREKCHQYWPAERS-ARYQYFVVDPMAEYNMPQYILREFKV-TDARDGQSRTVRQFQFTDWPEQGVPKSGEGFI 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907074051 2170 QFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2246
Cdd:cd14554    159 DFIGQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYR 235

PTP_fungal

cd18533

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

2045-2246

7.52e-70

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: 234.07 E-value: 7.52e-70

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2045 YINASYI-PGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDPLYYGDLILQMVSE 2123
Cdd:cd18533      1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2124 SVLPEW--TIREFKICSEEQldAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGT 2201
Cdd:cd18533     81 EENDDGgfIVREFELSKEDG--KVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHCSAGVGRTGT 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907074051 2202 FVALDRILQQLDS--------KDSVD-IYGAVHDLRLHRVHMVQTECQYVYLHQ 2246
Cdd:cd18533    159 FIALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212

R-PTPc-D-1

cd14624

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

1970-2248

6.08e-69

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: 234.24 E-value: 6.08e-69

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1970 PIKINQFEGHFMKLQADSNYLLSKEYEDLkDVGRSQSCDIALLPENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINAS 2049
Cdd:cd14624      3 PIPILELADHIERLKANDNLKFSQEYESI-DPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2050 YIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPAdQDPLYYGDLILQMVSESVLPEW 2129
Cdd:cd14624     82 YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPS-RGTETYGLIQVTLLDTVELATY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2130 TIREFKICSEEQLDaHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRdyINRSPGAGPTVVHCSAGVGRTGTFVALDRIL 2209
Cdd:cd14624    161 CVRTFALYKNGSSE-KREVRQFQFTAWPDHGVPEHPTPFLAFLRRVK--TCNPPDAGPMVVHCSAGVGRTGCFIVIDAML 237

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1907074051 2210 QQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2248
Cdd:cd14624    238 ERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276

R-PTPc-S-1

cd14625

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

1970-2248

7.66e-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: 233.83 E-value: 7.66e-69

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1970 PIKINQFEGHFMKLQADSNYLLSKEYEDLkDVGRSQSCDIALLPENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINAS 2049
Cdd:cd14625      3 PIPISELAEHTERLKANDNLKLSQEYESI-DPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2050 YIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPaDQDPLYYGDLILQMVSESVLPEW 2129
Cdd:cd14625     82 YIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWP-SRGTETYGMIQVTLLDTIELATF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2130 TIREFKIcSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRdyINRSPGAGPTVVHCSAGVGRTGTFVALDRIL 2209
Cdd:cd14625    161 CVRTFSL-HKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVK--TCNPPDAGPIVVHCSAGVGRTGCFIVIDAML 237

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1907074051 2210 QQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2248
Cdd:cd14625    238 ERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276

PTPc-N1

cd14608

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

1995-2244

7.57e-67

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: 227.99 E-value: 7.57e-67

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1995 YEDLKDVGRSQSCDIALLPENRGKNRYNNILPYDASRVKLcnvdDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDF 2074
Cdd:cd14608      5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2075 WKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQD-PLYYGD--LILQMVSESVLPEWTIREFKIcseEQLDAH--RLIR 2149
Cdd:cd14608     81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEkEMIFEDtnLKLTLISEDIKSYYTVRQLEL---ENLTTQetREIL 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2150 HFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSK---DSVDIYGAVHD 2226
Cdd:cd14608    158 HFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRkdpSSVDIKKVLLE 237

                          250       260
                   ....*....|....*....|
gi 1907074051 2227 LRLHRVHMVQT--ECQYVYL 2244
Cdd:cd14608    238 MRKFRMGLIQTadQLRFSYL 257

R-PTPc-E-1

cd14620

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

2021-2246

9.10e-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: 222.89 E-value: 9.10e-66

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2021 YNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKC 2100
Cdd:cd14620      1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2101 DHYWPaDQDPLYYGDLILQMVSESVLPEWTIREFkiCSEEQLD----AHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVR 2176
Cdd:cd14620     81 YQYWP-DQGCWTYGNIRVAVEDCVVLVDYTIRKF--CIQPQLPdgckAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVK 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907074051 2177 dyiNRSPG-AGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2246
Cdd:cd14620    158 ---SVNPVhAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQ 225

PTPc-N6

cd14606

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

2013-2248

2.51e-65

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: 223.22 E-value: 2.51e-65

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2013 PENRGKNRYNNILPYDASRVKLCNVDDD-PCSDYINASYI------PGNNFRReYIATQGPLPGTKDDFWKMAWEQNVHN 2085
Cdd:cd14606     16 PENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVknqllgPDENAKT-YIASQGCLEATVNDFWQMAWQENSRV 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2086 IVMVTQCVEKGRVKCDHYWPADQDPLYYGDLILQMVSESVLPEWTIREFKICSEEQLDAHRLIRHFHYTVWPDHGVPETT 2165
Cdd:cd14606     95 IVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELIREIWHYQYLSWPDHGVPSEP 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2166 QSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSK--DS-VDIYGAVHDLRLHRVHMVQTECQYV 2242
Cdd:cd14606    175 GGVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKglDCdIDIQKTIQMVRAQRSGMVQTEAQYK 254


                   ....*.
gi 1907074051 2243 YLHQCV 2248
Cdd:cd14606    255 FIYVAI 260

R-PTPc-Z-1

cd17668

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

2045-2245

6.67e-65

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: 219.85 E-value: 6.67e-65

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2045 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDPlYYGDLILQMVSES 2124
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE-EYGNFLVTQKSVQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2125 VLPEWTIREF-------KICSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDyiNRSPGAGPTVVHCSAGVG 2197
Cdd:cd17668     80 VLAYYTVRNFtlrntkiKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASY--AKRHAVGPVVVHCSAGVG 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1907074051 2198 RTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 2245
Cdd:cd17668    158 RTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 205

PTPc-N20_13

cd14538

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

2045-2252

8.29e-65

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: 219.17 E-value: 8.29e-65

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2045 YINASYI--PGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWP--ADQDPLYYGDLILQM 2120
Cdd:cd14538      1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdsLNKPLICGGRLEVSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2121 VSESVLPEWTIREFKIcSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRtvrdYINRSPGAGPTVVHCSAGVGRTG 2200
Cdd:cd14538     81 EKYQSLQDFVIRRISL-RDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIR----YMRRIHNSGPIVVHCSAGIGRTG 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907074051 2201 TFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVL 2252
Cdd:cd14538    156 VLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207

R-PTPc-C-1

cd14557

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

2045-2246

1.58e-64

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: 218.16 E-value: 1.58e-64

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2045 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPA-DQDPLYYGDLILQMVSE 2123
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmEEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2124 SVLPEWTIREFKICSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRspGAGPTVVHCSAGVGRTGTFV 2203
Cdd:cd14557     81 KICPDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNF--FSGPIVVHCSAGVGRTGTYI 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1907074051 2204 ALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2246
Cdd:cd14557    159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201

PTPc-N18

cd14603

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

2013-2248

4.67e-64

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: 219.70 E-value: 4.67e-64

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2013 PENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQC 2092
Cdd:cd14603     28 KENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACRE 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2093 VEKGRVKCDHYWPADQDPLYYGDLILQMVSESVL-PEWTIREFKI--CSEEqldahRLIRHFHYTVWPDHGVPETTQSLI 2169
Cdd:cd14603    108 IEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLnEEVILRTLKVtfQKES-----RSVSHFQYMAWPDHGIPDSPDCML 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2170 QFVRTVRDYINRSPgaGPTVVHCSAGVGRTGTFVALDRILQQLDSK---DSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2246
Cdd:cd14603    183 AMIELARRLQGSGP--EPLCVHCSAGCGRTGVICTVDYVRQLLLTQripPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYH 260


                   ..
gi 1907074051 2247 CV 2248
Cdd:cd14603    261 TV 262

R-PTPc-typeIIb-1

cd14555

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

2045-2248

5.10e-64

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: 217.09 E-value: 5.10e-64

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2045 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDplYYGDLILQMVSES 2124
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTE--VYGDIKVTLVETE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2125 VLPEWTIREFKIcSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRdyINRSPGAGPTVVHCSAGVGRTGTFVA 2204
Cdd:cd14555     79 PLAEYVVRTFAL-ERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVK--ASNPPSAGPIVVHCSAGAGRTGCYIV 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1907074051 2205 LDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2248
Cdd:cd14555    156 IDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAI 199

PTPc-N1_2

cd14545

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

2018-2240

1.32e-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: 216.87 E-value: 1.32e-63

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2018 KNRYNNILPYDASRVKLCNVDDDpcSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGR 2097
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2098 VKCDHYWPADQDPLY---YGDLILQMVSESVLPEWTIREFKIcseEQLDAH--RLIRHFHYTVWPDHGVPETTQSLIQFV 2172
Cdd:cd14545     79 IKCAQYWPQGEGNAMifeDTGLKVTLLSEEDKSYYTVRTLEL---ENLKTQetREVLHFHYTTWPDFGVPESPAAFLNFL 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2173 RTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKD--SVDIYGAVHDLRLHRVHMVQTECQ 2240
Cdd:cd14545    156 QKVRESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQ 225

PTPc-N7

cd14612

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

2012-2245

3.17e-63

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: 216.24 E-value: 3.17e-63

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2012 LPENRGKNRYNNILPYDASRVKLCNV-DDDPCSDYINASYIPGNNFR-REYIATQGPLPGTKDDFWKMAWEQNVHNIVMV 2089
Cdd:cd14612     12 IPGHASKDRYKTILPNPQSRVCLRRAgSQEEEGSYINANYIRGYDGKeKAYIATQGPMLNTVSDFWEMVWQEECPIIVMI 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2090 TQCVEKgRVKCDHYWPADQDPlyYGDLILQMVSESVLPEWTIREFKICSEEqldAHRLIRHFHYTVWPDHGVPETTQSLI 2169
Cdd:cd14612     92 TKLKEK-KEKCVHYWPEKEGT--YGRFEIRVQDMKECDGYTIRDLTIQLEE---ESRSVKHYWFSSWPDHQTPESAGPLL 165

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907074051 2170 QFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 2245
Cdd:cd14612    166 RLVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241

R-PTPc-K-1

cd14631

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

2031-2248

1.92e-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: 212.96 E-value: 1.92e-62

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2031 RVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDp 2110
Cdd:cd14631      1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTE- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2111 lYYGDLILQMVSESVLPEWTIREFKIcSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRdyINRSPGAGPTVV 2190
Cdd:cd14631     80 -VYGDFKVTCVEMEPLAEYVVRTFTL-ERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVK--LSNPPSAGPIVV 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907074051 2191 HCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2248
Cdd:cd14631    156 HCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213

PTPc-N2

cd14607

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

1995-2240

2.35e-62

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: 214.44 E-value: 2.35e-62

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1995 YEDLKDVGRSQSCDIALLPENRGKNRYNNILPYDASRVKLCNVDDDpcsdYINASYIPGNNFRREYIATQGPLPGTKDDF 2074
Cdd:cd14607      4 YLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEND----YINASLVVIEEAQRSYILTQGPLPNTCCHF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2075 WKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPA-DQDPLYYGD--LILQMVSESVLPEWTIREFKIcSEEQLDAHRLIRHF 2151
Cdd:cd14607     80 WLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTdEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQL-ENINSGETRTISHF 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2152 HYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKD--SVDIYGAVHDLRL 2229
Cdd:cd14607    159 HYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRK 238

                          250
                   ....*....|.
gi 1907074051 2230 HRVHMVQTECQ 2240
Cdd:cd14607    239 YRMGLIQTPDQ 249

PTPc-N13

cd14597

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

2014-2252

2.61e-61

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.

Pssm-ID: 350445 [Multi-domain] Cd Length: 234 Bit Score: 210.46 E-value: 2.61e-61

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2014 ENRGKNRYNNILPYDASRVKLCNVdddpcSDYINASYI--PGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQ 2091
Cdd:cd14597      2 ENRKKNRYKNILPYDTTRVPLGDE-----GGYINASFIkmPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2092 CVEKGRVKCDHYWP-ADQDPLYYGD-LILQMVSESVLPEWTIREFKIcSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLI 2169
Cdd:cd14597     77 EVEGGKIKCQRYWPeILGKTTMVDNrLQLTLVRMQQLKNFVIRVLEL-EDIQTREVRHITHLNFTAWPDHDTPSQPEQLL 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2170 QFVRTVRdYINRSpgaGPTVVHCSAGVGRTGTFVALDRILqQLDSKD-SVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2248
Cdd:cd14597    156 TFISYMR-HIHKS---GPIITHCSAGIGRSGTLICIDVVL-GLISKDlDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230


                   ....
gi 1907074051 2249 RDVL 2252
Cdd:cd14597    231 LYVL 234

PTPc-N3_4

cd14541

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

2044-2248

3.66e-61

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: 209.11 E-value: 3.66e-61

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2044 DYINASY----IPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDPLYYGDLILQ 2119
Cdd:cd14541      1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2120 MVSESVLPEWTIREFKICSEEQLDAhRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYinRSPGAGPTVVHCSAGVGRT 2199
Cdd:cd14541     81 CVSEEVTPSFAFREFILTNTNTGEE-RHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQN--RVGMVEPTVVHCSAGIGRT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1907074051 2200 GTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2248
Cdd:cd14541    158 GVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAI 206

PTPc-N11

cd14605

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

2014-2249

5.48e-60

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: 207.18 E-value: 5.48e-60

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2014 ENRGKNRYNNILPYDASRVKLCNVD-DDPCSDYINASYI-PGNNF-------RREYIATQGPLPGTKDDFWKMAWEQNVH 2084
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRVVLHDGDpNEPVSDYINANIImPEFETkcnnskpKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2085 NIVMVTQCVEKGRVKCDHYWPADQDPLYYGDLILQMVSESVLPEWTIREFKICSEEQLDAHRLIRHFHYTVWPDHGVPET 2164
Cdd:cd14605     81 VIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGNTERTVWQYHFRTWPDHGVPSD 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2165 TQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKD---SVDIYGAVHDLRLHRVHMVQTECQY 2241
Cdd:cd14605    161 PGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRSQRSGMVQTEAQY 240


                   ....*...
gi 1907074051 2242 VYLHQCVR 2249
Cdd:cd14605    241 RFIYMAVQ 248

R-PTPc-U-1

cd14632

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

2045-2248

5.96e-60

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: 205.29 E-value: 5.96e-60

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2045 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDplYYGDLILQMVSES 2124
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSD--TYGDIKITLLKTE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2125 VLPEWTIREFKIcSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDyiNRSPGAGPTVVHCSAGVGRTGTFVA 2204
Cdd:cd14632     79 TLAEYSVRTFAL-ERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKA--STPPDAGPVVVHCSAGAGRTGCYIV 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1907074051 2205 LDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2248
Cdd:cd14632    156 LDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAI 199

R-PTPc-A-E-1

cd14551

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

2045-2246

1.31e-59

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: 204.38 E-value: 1.31e-59

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2045 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPaDQDPLYYGDLILQMVSES 2124
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP-DQGCWTYGNLRVRVEDTV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2125 VLPEWTIREFkiCSEEQLD-----AHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYInrSPGAGPTVVHCSAGVGRT 2199
Cdd:cd14551     80 VLVDYTTRKF--CIQKVNRgigekRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSAN--PPRAGPIVVHCSAGVGRT 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1907074051 2200 GTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2246
Cdd:cd14551    156 GTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202

R-PTP-S-2

cd14627

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

2010-2252

8.70e-59

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: 205.35 E-value: 8.70e-59

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2010 ALLPENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMV 2089
Cdd:cd14627     48 ANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVML 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2090 TQCVEKGRVKCDHYWPADQDPlYYGDLILQMVSESVLPEWTIREFKIcSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLI 2169
Cdd:cd14627    128 TKLREMGREKCHQYWPAERSA-RYQYFVVDPMAEYNMPQYILREFKV-TDARDGQSRTVRQFQFTDWPEQGVPKSGEGFI 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2170 QFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVR 2249
Cdd:cd14627    206 DFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAAL 285


                   ...
gi 1907074051 2250 DVL 2252
Cdd:cd14627    286 EYL 288

R-PTP-D-2

cd14628

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

2010-2252

2.20e-58

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: 204.19 E-value: 2.20e-58

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2010 ALLPENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMV 2089
Cdd:cd14628     47 ANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2090 TQCVEKGRVKCDHYWPADQDPlYYGDLILQMVSESVLPEWTIREFKIcSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLI 2169
Cdd:cd14628    127 TKLREMGREKCHQYWPAERSA-RYQYFVVDPMAEYNMPQYILREFKV-TDARDGQSRTVRQFQFTDWPEQGVPKSGEGFI 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2170 QFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVR 2249
Cdd:cd14628    205 DFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAAL 284


                   ...
gi 1907074051 2250 DVL 2252
Cdd:cd14628    285 EYL 287

PTPc-N3

cd14600

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

1994-2253

3.96e-58

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: 202.77 E-value: 3.96e-58

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1994 EYEDL--KDVGRSQSCdiALLPENRGKNRYNNILPYDASRVKLcnvddDPCSDYINASY----IPGNNFRREYIATQGPL 2067
Cdd:cd14600     19 QFEQLyrKKPGLAITC--AKLPQNMDKNRYKDVLPYDATRVVL-----QGNEDYINASYvnmeIPSANIVNKYIATQGPL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2068 PGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDPLYYGDLILQMVSESVLPEWTIREFKICSEEQLDAHRL 2147
Cdd:cd14600     92 PHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTV 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2148 IrHFHYTVWPDHGVPETTQSLIQFVRTVRdyiNRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDL 2227
Cdd:cd14600    172 T-HLQYVAWPDHGVPDDSSDFLEFVNYVR---SKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKM 247

                          250       260
                   ....*....|....*....|....*.
gi 1907074051 2228 RLHRVHMVQTECQYVYLHQCVRDVLR 2253
Cdd:cd14600    248 RDQRAMMVQTSSQYKFVCEAILRVYE 273

R-PTP-F-2

cd14629

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

2010-2252

6.74e-58

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: 202.65 E-value: 6.74e-58

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2010 ALLPENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMV 2089
Cdd:cd14629     48 ANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2090 TQCVEKGRVKCDHYWPADQDPlYYGDLILQMVSESVLPEWTIREFKIcSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLI 2169
Cdd:cd14629    128 TKLREMGREKCHQYWPAERSA-RYQYFVVDPMAEYNMPQYILREFKV-TDARDGQSRTIRQFQFTDWPEQGVPKTGEGFI 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2170 QFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYvylHQCVR 2249
Cdd:cd14629    206 DFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQY---QLCYR 282


                   ...
gi 1907074051 2250 DVL 2252
Cdd:cd14629    283 AAL 285

PTPc-N20

cd14596

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

2045-2253

5.46e-57

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: 196.89 E-value: 5.46e-57

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2045 YINASYI--PGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPAD-QDPLYYGDLILQMV 2121
Cdd:cd14596      1 YINASYItmPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETlQEPMELENYQLRLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2122 SESVLPEWTIREFKICSEEQLDAHrLIRHFHYTVWPDHGVPETTQSLIQFVRtvrdYINRSPGAGPTVVHCSAGVGRTGT 2201
Cdd:cd14596     81 NYQALQYFIIRIIKLVEKETGENR-LIKHLQFTTWPDHGTPQSSDQLVKFIC----YMRKVHNTGPIVVHCSAGIGRAGV 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907074051 2202 FVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVLR 2253
Cdd:cd14596    156 LICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207

R-PTPc-A-E-2

cd14552

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

2045-2248

1.05e-55

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: 192.87 E-value: 1.05e-55

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2045 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADqDPLYYGDLILQMVSES 2124
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPED-GSVSSGDITVELKDQT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2125 VLPEWTIREFKIcSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSpGAGPTVVHCSAGVGRTGTFVA 2204
Cdd:cd14552     80 DYEDYTLRDFLV-TKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQS-GNHPITVHCSAGAGRTGTFCA 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1907074051 2205 LDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2248
Cdd:cd14552    158 LSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201

R-PTPc-E-2

cd14622

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

2044-2250

3.95e-55

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: 191.37 E-value: 3.95e-55

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2044 DYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPAdQDPLYYGDLILQMVSE 2123
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPS-EGSVTHGEITIEIKND 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2124 SVLPEWTIREFkICSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSpGAGPTVVHCSAGVGRTGTFV 2203
Cdd:cd14622     80 TLLETISIRDF-LVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQT-GNHPIVVHCSAGAGRTGTFI 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1907074051 2204 ALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRD 2250
Cdd:cd14622    158 ALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQD 204

PTPc-N22_18_12

cd14542

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

2045-2246

6.75e-54

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: 187.63 E-value: 6.75e-54

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2045 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQ-DPLYYGDLILQMVSE 2123
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGeEQLQFGPFKISLEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2124 S-VLPEWTIREFKI-CSEEQldahRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYinRSPGAGPTVVHCSAGVGRTGT 2201
Cdd:cd14542     81 KrVGPDFLIRTLKVtFQKES----RTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDY--QGSEDVPICVHCSAGCGRTGT 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1907074051 2202 FVALD---RILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2246
Cdd:cd14542    155 ICAIDyvwNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202

PTPc-N12

cd14604

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

1974-2248

5.79e-53

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: 188.99 E-value: 5.79e-53

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1974 NQFEGHFMKLQAdsnylLSKEYEDLK----DVGRSQscdiallpENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINAS 2049
Cdd:cd14604     25 DNFASDFMRLRR-----LSTKYRTEKiyptATGEKE--------ENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINAN 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2050 YIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPA-DQDPLYYGDLILQMVSESVLPE 2128
Cdd:cd14604     92 FIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLyGEEPMTFGPFRISCEAEQARTD 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2129 WTIREFKIcsEEQLDAHRLIRhFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSpgAGPTVVHCSAGVGRTGTFVALD-- 2206
Cdd:cd14604    172 YFIRTLLL--EFQNETRRLYQ-FHYVNWPDHDVPSSFDSILDMISLMRKYQEHE--DVPICIHCSAGCGRTGAICAIDyt 246

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1907074051 2207 -RILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2248
Cdd:cd14604    247 wNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289

beta-trefoil_Ricin_PTPRB-like

cd23409

ricin B-type lectin domain, beta-trefoil fold, found in receptor-type tyrosine-protein ...

18-133

7.52e-53

Pssm-ID: 467787 Cd Length: 117 Bit Score: 181.48 E-value: 7.52e-53

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051   18 LEGFQIVHVRKQQCLSINQKVVMGFCNGSSRNQQWLSTEDGKFLHIKSGLCLGISNSSRGPFQPAVATPCAQAPRWTCHA 97
Cdd:cd23409      1 SEGFLILHVQKQQCLFGNKTVSVGKCNATSPNQQWQWTEDGKLLHVKSGQCLGISNSSAFHSRRAILLDCSQAPRWTCHE 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1907074051   98 QEGFLEVENTSLFLKKQNHKVVVKKISKYLDSWMKL 133
Cdd:cd23409     81 NEGLLEVANSSLFLTKQGQRVVVKQGKKYLHNWMKY 116

PTPc-N22

cd14602

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

2018-2248

1.72e-52

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: 185.04 E-value: 1.72e-52

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2018 KNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGR 2097
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2098 VKCDHYWP-ADQDPLYYGDLILQMVSESVLPEWTIREFKI-CSEEQldahRLIRHFHYTVWPDHGVPETTQSLIQFVRTV 2175
Cdd:cd14602     81 KKCERYWAePGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVkFNSET----RTIYQFHYKNWPDHDVPSSIDPILELIWDV 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907074051 2176 RDYinRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLdsKDSV-----DIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2248
Cdd:cd14602    157 RCY--QEDDSVPICIHCSAGCGRTGVICAIDYTWMLL--KDGIipenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAV 230

R-PTPc-A-2

cd14623

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

2020-2250

3.06e-52

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: 184.09 E-value: 3.06e-52

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2020 RYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVK 2099
Cdd:cd14623      1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2100 CDHYWPADqDPLYYGDLILQMVSESVLPEWTIREFKICSEEQlDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYI 2179
Cdd:cd14623     81 CAQYWPSD-GSVSYGDITIELKKEEECESYTVRDLLVTNTRE-NKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQ 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907074051 2180 NRSpGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRD 2250
Cdd:cd14623    159 QQS-GNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228

PTPc-N5

cd14613

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

2018-2245

6.44e-52

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: 184.30 E-value: 6.44e-52

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2018 KNRYNNILPYDASRVKLCNVD-DDPCSDYINASYIPG-NNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEK 2095
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTSPDqDDPLSSYINANYIRGyGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2096 GRvKCDHYWPADQdPLYYGdliLQMVSESVLPE--WTIREFKICSEEQldaHRLIRHFHYTVWPDHGVPETTQSLIQFVR 2173
Cdd:cd14613    108 NE-KCTEYWPEEQ-VTYEG---IEITVKQVIHAddYRLRLITLKSGGE---ERGLKHYWYTSWPDQKTPDNAPPLLQLVQ 179

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907074051 2174 TVRDYINRS-PGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 2245
Cdd:cd14613    180 EVEEARQQAePNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVH 252

R-PTPc-R

cd14611

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

2018-2246

1.47e-51

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: 182.04 E-value: 1.47e-51

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2018 KNRYNNILPYDASRVKLCNVD-DDPCSDYINASYIPG-NNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEK 2095
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIRGyGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2096 GRvKCDHYWPADQDplYYGDLILQMVSESVLPEWTIREFKIcseEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTV 2175
Cdd:cd14611     82 NE-KCVLYWPEKRG--IYGKVEVLVNSVKECDNYTIRNLTL---KQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDV 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907074051 2176 RDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2246
Cdd:cd14611    156 EEDRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226

PTPc-N21_14

cd14540

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

2045-2246

4.07e-51

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: 180.34 E-value: 4.07e-51

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2045 YINASYIP---GNNFRReYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPA---DQDPLYYGDLIL 2118
Cdd:cd14540      1 YINASHITatvGGKQRF-YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTlggEHDALTFGEYKV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2119 QMVSESVLPEWTIREFKIcSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQF---VRTVRDYI-------NRSPgagPT 2188
Cdd:cd14540     80 STKFSVSSGCYTTTGLRV-KHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeINSVRRHTnqdvaghNRNP---PT 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907074051 2189 VVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2246
Cdd:cd14540    156 LVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYN 213

R-PTP-N2

cd14610

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

1991-2243

5.38e-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: 182.56 E-value: 5.38e-51

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1991 LSKEYEDLKDV-GRSQSCDIALLPENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRR-EYIATQGPLP 2068
Cdd:cd14610     19 LEKEWEALCAYqAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHDPRNpAYIATQGPLP 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2069 GTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDPLYYgDLILQMVSESVLPE-WTIREFKIcSEEQLDAHRL 2147
Cdd:cd14610     99 ATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYH-IYEVNLVSEHIWCEdFLVRSFYL-KNLQTNETRT 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2148 IRHFHYTVWPDHGVPETTQSLIQFVRTVRD-YINRSpgaGPTVVHCSAGVGRTGTFVALDRILQQL-DSKDSVDIYGAVH 2225
Cdd:cd14610    177 VTQFHFLSWNDQGVPASTRSLLDFRRKVNKcYRGRS---CPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLE 253

                          250
                   ....*....|....*...
gi 1907074051 2226 DLRLHRVHMVQTECQYVY 2243
Cdd:cd14610    254 HLRDQRPGMVQTKEQFEF 271

R-PTP-N

cd14609

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

1991-2243

1.29e-48

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: 175.61 E-value: 1.29e-48

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1991 LSKEYEDLKDV-GRSQSCDIALLPENRGKNRYNNILPYDASRVKLcNVDDDPC-SDYINASYIPGNNFRR-EYIATQGPL 2067
Cdd:cd14609     17 LAKEWQALCAYqAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKL-KAESNPSrSDYINASPIIEHDPRMpAYIATQGPL 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2068 PGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDPLYYgDLILQMVSESVLPE-WTIREFKIcSEEQLDAHR 2146
Cdd:cd14609     96 SHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYH-IYEVNLVSEHIWCEdFLVRSFYL-KNVQTQETR 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2147 LIRHFHYTVWPDHGVPETTQSLIQFVRTV-RDYINRSpgaGPTVVHCSAGVGRTGTFVALDRILQQL-DSKDSVDIYGAV 2224
Cdd:cd14609    174 TLTQFHFLSWPAEGIPSSTRPLLDFRRKVnKCYRGRS---CPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATL 250

                          250
                   ....*....|....*....
gi 1907074051 2225 HDLRLHRVHMVQTECQYVY 2243
Cdd:cd14609    251 EHVRDQRPGMVRTKDQFEF 269

PTPc-N4

cd14601

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

2044-2253

3.59e-48

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: 171.67 E-value: 3.59e-48

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2044 DYINASYI----PGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDPLYYGDLILQ 2119
Cdd:cd14601      1 DYINANYInmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2120 MVSESVLPEWTIREFKICSEEQLDAhRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDyiNRSPGAGPTVVHCSAGVGRT 2199
Cdd:cd14601     81 CHSEEGNPAYVFREMTLTNLEKNES-RPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRN--KRAGKDEPVVVHCSAGIGRT 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907074051 2200 GTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVLR 2253
Cdd:cd14601    158 GVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYE 211

R-PTP-C-2

cd14558

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

2045-2245

8.19e-48

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: 170.27 E-value: 8.19e-48

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2045 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDPlyYGDLILQMVSES 2124
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT--YGDIEVELKDTE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2125 VLPEWTIREFKIcSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVR----DYINRSPGAGPTVVHCSAGVGRTG 2200
Cdd:cd14558     79 KSPTYTVRVFEI-THLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKqklpYKNSKHGRSVPIVVHCSDGSSRTG 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907074051 2201 TFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 2245
Cdd:cd14558    158 IFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202

PTPc-N14

cd14599

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

1994-2246

4.40e-46

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: 168.64 E-value: 4.40e-46

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1994 EYEDLKDVGRSQSCDIALLPENRGKNRYNNILPYDASRVKLCNVDDDPcSDYINASYIPGNNFRRE--YIATQGPLPGTK 2071
Cdd:cd14599     17 EYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENN-TGYINASHIKVTVGGEEwhYIATQGPLPHTC 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2072 DDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWP---ADQDPLYYG--DLILQMVSESVLPEWTIREFKICSEEQldaHR 2146
Cdd:cd14599     96 HDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPklgSKHSSATYGkfKVTTKFRTDSGCYATTGLKVKHLLSGQ---ER 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2147 LIRHFHYTVWPDHGVPETTQSLIQF---VRTVRDYINRSPGAG-----PTVVHCSAGVGRTGTFVALDRILQQLDSKDSV 2218
Cdd:cd14599    173 TVWHLQYTDWPDHGCPEEVQGFLSYleeIQSVRRHTNSMLDSTkncnpPIVVHCSAGVGRTGVVILTELMIGCLEHNEKV 252

                          250       260
                   ....*....|....*....|....*...
gi 1907074051 2219 DIYGAVHDLRLHRVHMVQTECQYVYLHQ 2246
Cdd:cd14599    253 EVPVMLRHLREQRMFMIQTIAQYKFVYQ 280

R-PTPc-typeIIb-2

cd14556

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

2045-2246

5.39e-46

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: 165.27 E-value: 5.39e-46

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2045 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQcVEKGRVKCDHYWPaDQDPLYYGDLILQMVSES 2124
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQ-LDPKDQSCPQYWP-DEGSGTYGPIQVEFVSTT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2125 VLPEWTIREFKICSEEQL-DAHRLIRHFHYTVWPDHG-VPETTQSLIQFVRTVRDYINRSpGAGPTVVHCSAGVGRTGTF 2202
Cdd:cd14556     79 IDEDVISRIFRLQNTTRPqEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQS-GEGPIVVHCLNGVGRSGVF 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1907074051 2203 VALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2246
Cdd:cd14556    158 CAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201

R-PTP-N-N2

cd14546

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

2045-2248

1.85e-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: 161.07 E-value: 1.85e-44

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2045 YINASYIPGNNFRRE-YIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDPLyYGDLILQMVSE 2123
Cdd:cd14546      1 YINASTIYDHDPRNPaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEV-YHIYEVHLVSE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2124 SVLPE-WTIREFKIcSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTV-RDYINRSpgaGPTVVHCSAGVGRTGT 2201
Cdd:cd14546     80 HIWCDdYLVRSFYL-KNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVnKSYRGRS---CPIVVHCSDGAGRTGT 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1907074051 2202 FVALDRILQQL-DSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2248
Cdd:cd14546    156 YILIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203

PTPc_plant_PTP1

cd17658

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

2045-2243

3.67e-44

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: 159.94 E-value: 3.67e-44

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2045 YINASYIPGNNFRR--EYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGR-VKCDHYWPA-DQDPLYYGDLilqm 2120
Cdd:cd17658      1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAeENESREFGRI---- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2121 vseSVLPEW--------TIREFKICSEEQLDAHRLIRHFHYTVWPDHGVPETTqsliqfvRTVRDYINRS----PGAGPT 2188
Cdd:cd17658     77 ---SVTNKKlkhsqhsiTLRVLEVQYIESEEPPLSVLHIQYPEWPDHGVPKDT-------RSVRELLKRLygipPSAGPI 146

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907074051 2189 VVHCSAGVGRTGTFVALDRILQQLDSKD--SVDIYGAVHDLRLHRVHMVQTECQYVY 2243
Cdd:cd17658    147 VVHCSAGIGRTGAYCTIHNTIRRILEGDmsAVDLSKTVRKFRSQRIGMVQTQDQYIF 203

PTP-N23

cd14539

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

2045-2246

2.12e-43

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: 157.93 E-value: 2.12e-43

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2045 YINASYIPG-NNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQ-DPLYYGDLILQMVS 2122
Cdd:cd14539      1 YINASLIEDlTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERgQALVYGAITVSLQS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2123 ESVLPEWTIREFKICSEEQlDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRS-PGAGPTVVHCSAGVGRTGT 2201
Cdd:cd14539     81 VRTTPTHVERIISIQHKDT-RLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQrSLQTPIVVHCSSGVGRTGA 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1907074051 2202 FVALDRILQQLDSKDSV-DIYGAVHDLRLHRVHMVQTECQYVYLHQ 2246
Cdd:cd14539    160 FCLLYAAVQEIEAGNGIpDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

2013-2266

1.00e-41

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 155.63 E-value: 1.00e-41

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2013 PENRGKNRYNNILPYDASRVKlcnvDDDPcsdYINASYIPGNNFRReYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQC 2092
Cdd:COG5599     40 INGSPLNRFRDIQPYKETALR----ANLG---YLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASD 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2093 VE--KGRVKCDHYWPADqdplyyGDLILQMVS------ESVLPEWTIREFKI----CSEEQLDahrlIRHFHYTVWPDHG 2160
Cdd:COG5599    112 DEisKPKVKMPVYFRQD------GEYGKYEVSseltesIQLRDGIEARTYVLtikgTGQKKIE----IPVLHVKNWPDHG 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2161 VPETTQsLIQFVRTVRDYIN-RSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKD--SVDIYGAVHDLRLHR-VHMVQ 2236
Cdd:COG5599    182 AISAEA-LKNLADLIDKKEKiKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQ 260

                          250       260       270
                   ....*....|....*....|....*....|
gi 1907074051 2237 TECQYvylhqcvrDVLraKKLRNEQENPLF 2266
Cdd:COG5599    261 TSEQL--------DVL--VKLAEQQIRPLL 280

PHA02742

protein tyrosine phosphatase; Provisional

1972-2257

2.53e-41

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 155.55 E-value: 2.53e-41

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1972 KINQFEGHFMKLQADSN--YLLSKEYEDLKDVGRSQSCDIALLPENRGKNRYNNILPYDASRVKLCNvdDDPCSDYINAS 2049
Cdd:PHA02742     7 KKNSFAKNCEQLIEESNlaEILKEEHEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILKI--EDGGDDFINAS 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2050 YIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYW-PADQDPLYYGDLILQMVSESVLPE 2128
Cdd:PHA02742    85 YVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRN 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2129 WTIREFKIcSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVR--DYINRSPGAG-------PTVVHCSAGVGRT 2199
Cdd:PHA02742   165 YAVTNLCL-TDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVReaDLKADVDIKGenivkepPILVHCSAGLDRA 243

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907074051 2200 GTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYlhqCVRDVLRAKKL 2257
Cdd:PHA02742   244 GAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF---CYFIVLIFAKL 298

PTPc_motif

smart00404

Protein tyrosine phosphatase, catalytic domain motif;

2148-2248

3.25e-40

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 144.81 E-value: 3.25e-40

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  2148 IRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDS-KDSVDIYGAVHD 2226
Cdd:smart00404    2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDTVKE 81

                            90       100
                    ....*....|....*....|..
gi 1907074051  2227 LRLHRVHMVQTECQYVYLHQCV 2248
Cdd:smart00404   82 LRSQRPGMVQTEEQYLFLYRAL 103

PTPc_DSPc

smart00012

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

2148-2248

3.25e-40

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: 144.81 E-value: 3.25e-40

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  2148 IRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDS-KDSVDIYGAVHD 2226
Cdd:smart00012    2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDTVKE 81

                            90       100
                    ....*....|....*....|..
gi 1907074051  2227 LRLHRVHMVQTECQYVYLHQCV 2248
Cdd:smart00012   82 LRSQRPGMVQTEEQYLFLYRAL 103

PHA02747

protein tyrosine phosphatase; Provisional

2013-2245

9.09e-39

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 148.23 E-value: 9.09e-39

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2013 PENRGKNRYNNILPYDASRVKLcNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQC 2092
Cdd:PHA02747    49 PENQPKNRYWDIPCWDHNRVIL-DSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPT 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2093 -VEKGRVKCDHYW-PADQDPLYYGDLILQMVSESVLPEWTIREFKIcSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQ 2170
Cdd:PHA02747   128 kGTNGEEKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEI-TDKILKDSRKISHFQCSEWFEDETPSDHPDFIK 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2171 FVRTV--------RDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYV 2242
Cdd:PHA02747   207 FIKIIdinrkksgKLFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYL 286


                   ...
gi 1907074051 2243 YLH 2245
Cdd:PHA02747   287 FIQ 289

PHA02738

hypothetical protein; Provisional

2015-2249

1.06e-37

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 145.45 E-value: 1.06e-37

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2015 NRGKNRYNNILPYDASRVKLCNVDDDpcSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVE 2094
Cdd:PHA02738    49 NRKLNRYLDAVCFDHSRVILPAERNR--GDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2095 KGRVKCDHYWP-ADQDPLYYGDLILQMVSESVLPEWTirEFKICSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVR 2173
Cdd:PHA02738   127 NGREKCFPYWSdVEQGSIRFGKFKITTTQVETHPHYV--KSTLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVL 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2174 TVRD-----YINR------SPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYV 2242
Cdd:PHA02738   205 EVRQcqkelAQESlqighnRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYF 284


                   ....*..
gi 1907074051 2243 YLHQCVR 2249
Cdd:PHA02738   285 FCYRAVK 291

PHA02746

protein tyrosine phosphatase; Provisional

1990-2257

6.20e-37

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 143.25 E-value: 6.20e-37

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1990 LLSKEYEDLKDVGRSQSCDIALLPENRGKNRYNNILPYDASRV--------KLCNVDD-----------DPCSDYINASY 2050
Cdd:PHA02746    26 FVLLEHAEVMDIPIRGTTNHFLKKENLKKNRFHDIPCWDHSRVvinaheslKMFDVGDsdgkkievtseDNAENYIHANF 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2051 IPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQcVEKGRVKCDHYWPADQD-PLYYGDL---ILQMVSESVL 2126
Cdd:PHA02746   106 VDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWTKEEDsELAFGRFvakILDIIEELSF 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2127 PEWTIREFKICSeeqlDAHRLIRHFHYTVWPDHGVPETTQSLIQFV--------RTVRDYINRSPGAGPTVVHCSAGVGR 2198
Cdd:PHA02746   185 TKTRLMITDKIS----DTSREIHHFWFPDWPDNGIPTGMAEFLELInkvneeqaELIKQADNDPQTLGPIVVHCSAGIGR 260

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907074051 2199 TGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVL--RAKKL 2257
Cdd:PHA02746   261 AGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAIieEAKKK 321

PTPc-N21

cd14598

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

2045-2253

1.82e-36

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: 138.57 E-value: 1.82e-36

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2045 YINASYIPGNNFRRE--YIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWP---ADQDPLYYG--DLI 2117
Cdd:cd14598      1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgSRHNTVTYGrfKIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2118 LQMVSESVLPEWTIREFKICSEEQldaHRLIRHFHYTVWPDHGVPETTQSLIQF---VRTVRDYIN-----RSPGAgPTV 2189
Cdd:cd14598     81 TRFRTDSGCYATTGLKIKHLLTGQ---ERTVWHLQYTDWPEHGCPEDLKGFLSYleeIQSVRRHTNstidpKSPNP-PVL 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907074051 2190 VHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVLR 2253
Cdd:cd14598    157 VHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220

PTP_tm

pfam18861

TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases ...

1761-1898

1.04e-33

Pssm-ID: 465889 Cd Length: 126 Bit Score: 126.95 E-value: 1.04e-33

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1761 VNCSWFSDTNGAVKYFAVVVREADSmdELKPEQQHPLPSYLEYRhNASIRVYQTNYFASKCAeSPDSSSKSFNIKLGAEM 1840
Cdd:pfam18861    1 IQFSLFNSSNGPIKAYGVIVTTNDS--LNRPLKEYLNKTYYDWK-YKKTDSYLATVTPNPFT-SPRSSSRSLTVPVGTGS 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907074051 1841 DSlggkcdpsqQKFCDGPLKPHTAYRISIRAFTQL-FDEDLKEFTKPLYSDTFFSMPIT 1898
Cdd:pfam18861   77 KW---------QGYCNGPLKPLGSYRFSVAAFTRLeFDDGLIDGEESYVSFTPFSEPIA 126

R5-PTP-2

cd14550

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

2045-2246

1.06e-33

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: 129.75 E-value: 1.06e-33

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2045 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCdhYWPADQDPLYYGDLILQMVSES 2124
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTKEKPLECETFKVTLSGED 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2125 VLPEW-----TIREFKIcsEEQLDAHRL-IRHFHYTVWPDHGVP-ETTQSLIQFVRtvRDYINRSpgaGPTVVHCSAGVG 2197
Cdd:cd14550     79 HSCLSneirlIVRDFIL--ESTQDDYVLeVRQFQCPSWPNPCSPiHTVFELINTVQ--EWAQQRD---GPIVVHDRYGGV 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1907074051 2198 RTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2246
Cdd:cd14550    152 QAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200

R-PTPc-T-2

cd14634

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

2045-2246

4.87e-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: 4.87e-32

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2045 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQcVEKGRVkCDHYWPaDQDPLYYGDLILQMVSES 2124
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNE-MDAAQL-CMQYWP-EKTSCCYGPIQVEFVSAD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2125 VLPEWTIREFKICSEEQ-LDAHRLIRHFHYTVWPDH-GVPETTQSLIQFVRTVRDYINRSPGA-GPTVVHCSAGVGRTGT 2201
Cdd:cd14634     78 IDEDIISRIFRICNMARpQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQYDGReGRTVVHCLNGGGRSGT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907074051 2202 FVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2246
Cdd:cd14634    158 FCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYE 202

R-PTP-G-2

cd17670

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

2045-2248

2.71e-26

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: 108.61 E-value: 2.71e-26

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2045 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQcvEKGRVKCDH-YWPADQDPLYYGDLILQMVSE 2123
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD--NQGLAEDEFvYWPSREESMNCEAFTVTLISK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2124 SVL-----PEWTIREFkICSEEQLDAHRLIRHFHYTVWPDHGVP-ETTQSLIQFVRtvRDYINRSpgaGPTVVHCSAGVG 2197
Cdd:cd17670     79 DRLclsneEQIIIHDF-ILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVIK--EEALTRD---GPTIVHDEFGAV 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907074051 2198 RTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2248
Cdd:cd17670    153 SAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203

R-PTPc-U-2

cd14637

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

2045-2248

5.24e-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: 108.07 E-value: 5.24e-26

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2045 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRV-KCDHYWPaDQDPLYYGDLILQMVSE 2123
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP-EPGLQQYGPMEVEFVSG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2124 SVLPEWTIREFKICSEEQL-DAHRLIRHFHYTVW-PDHGVPETTQSLIQFVRTVRDYiNRSPGAGPTVVHCSAGVGRTGT 2201
Cdd:cd14637     80 SADEDIVTRLFRVQNITRLqEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKW-QRESGEGRTVVHCLNGGGRSGT 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1907074051 2202 FVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2248
Cdd:cd14637    159 YCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIA 205

R-PTPc-K-2

cd14636

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

2045-2245

1.48e-25

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: 106.65 E-value: 1.48e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2045 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQC-VEKGrvkCDHYWPaDQDPLYYGDLILQMVSE 2123
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWP-EEGMLRYGPIQVECMSC 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2124 SVLPEWTIREFKICS-EEQLDAHRLIRHFHYTVWPDH-GVPETTQSLIQFVRTVRDYINR-SPGAGPTVVHCSAGVGRTG 2200
Cdd:cd14636     77 SMDCDVISRIFRICNlTRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEEcDEGEGRTIIHCLNGGGRSG 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907074051 2201 TFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 2245
Cdd:cd14636    157 MFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCY 201

R-PTP-Z-2

cd17669

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

2045-2248

4.37e-25

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: 105.08 E-value: 4.37e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2045 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCdHYWPADQDPLYYGDLILQMVSE- 2123
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKDEPINCETFKVTLIAEe 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2124 ----SVLPEWTIREFkICSEEQLDAHRLIRHFHYTVWPDHGVP-ETTQSLIQFVRtvRDYINRSpgaGPTVVHCSAGVGR 2198
Cdd:cd17669     80 hkclSNEEKLIIQDF-ILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISIIK--EEAANRD---GPMIVHDEHGGVT 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2199 TGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2248
Cdd:cd17669    154 AGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203

R-PTPc-M-2

cd14635

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

2045-2246

1.05e-24

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: 104.00 E-value: 1.05e-24

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2045 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQcVEKGRVkCDHYWPaDQDPLYYGDLILQMVSES 2124
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLND-VDPAQL-CPQYWP-ENGVHRHGPIQVEFVSAD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2125 VLPEWTIREFKICSEEQ-LDAHRLIRHFHYTVWPDH-GVPETTQSLIQFVRTVRDYINRSPGA-GPTVVHCSAGVGRTGT 2201
Cdd:cd14635     78 LEEDIISRIFRIYNAARpQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNGGeGRTVVHCLNGGGRSGT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907074051 2202 FVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2246
Cdd:cd14635    158 FCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 202

beta-trefoil_Ricin_MRC-like

cd23385

ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...

19-132

2.22e-19

Pssm-ID: 467784 [Multi-domain] Cd Length: 119 Bit Score: 85.73 E-value: 2.22e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051   19 EGFQIVHVRKQQCLSINQ---KVVMGFCNGSSRNQQWLSTEDGKFLHIKSGLCLGISNSSRGPfqPAVATPC---AQAPR 92
Cdd:cd23385      1 DSFLIYNEDLGKCLAARSsssKVSLSTCNPNSPNQQWKWTSGHRLFNVGTGKCLGVSSSSPSS--PLRLFECdseDELQK 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1907074051   93 WTCHAQEGFLEVENTSLFLK-KQNHKVVVKKISKYLDSWMK 132
Cdd:cd23385     79 WKCSKDGLLLLKGLGLLLLYdKSGKNVVVSKGSGLSSRWKI 119

PHA02740

protein tyrosine phosphatase; Provisional

1971-2255

2.23e-14

protein tyrosine phosphatase; Provisional

Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 76.16 E-value: 2.23e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1971 IKINQFEGHFMKlqADSNYLLSKEYEDL---KDVGRSQSCDIAllpENRGKNRYN--NILPYDASRVKLCNVDDdpcsdY 2045
Cdd:PHA02740     9 INGMDFINFINK--PDLLSCIIKEYRAIvpeHEDEANKACAQA---ENKAKDENLalHITRLLHRRIKLFNDEK-----V 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2046 INASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKgrvKC-DHYWPADQDPL-YYGDLILQMVSE 2123
Cdd:PHA02740    79 LDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADK---KCfNQFWSLKEGCViTSDKFQIETLEI 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2124 SVLPEWTIREFKIcsEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDY---INRSPG---AGPTVVHCSAGVG 2197
Cdd:PHA02740   156 IIKPHFNLTLLSL--TDKFGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLcadLEKHKAdgkIAPIIIDCIDGIS 233

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907074051 2198 RTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVLRAK 2255
Cdd:PHA02740   234 SSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLKEK 291

CDC14

COG2453

Protein-tyrosine phosphatase [Signal transduction mechanisms];

2148-2246

8.66e-12

Protein-tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 64.61 E-value: 8.66e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2148 IRHFHYTvWPDHGVPETTQsLIQFVRTVRDYINRSpgaGPTVVHCSAGVGRTGTFVALDRILQQLDSKDsvdiygAVHDL 2227
Cdd:COG2453     48 LEYLHLP-IPDFGAPDDEQ-LQEAVDFIDEALREG---KKVLVHCRGGIGRTGTVAAAYLVLLGLSAEE------ALARV 116

                           90
                   ....*....|....*....
gi 1907074051 2228 RLHRVHMVQTECQYVYLHQ 2246
Cdd:COG2453    117 RAARPGAVETPAQRAFLER 135

fn3

Fibronectin type III domain;

1550-1632

1.39e-11

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 62.43 E-value: 1.39e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1550 SPPSLLSFADVANTSLAITWKGPPDWT-DYNDFELQWFPGDALTIFNPYSSRKSEGR-IVYGLHPGRSYQFSVKTVSGDS 1627
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNgPITGYEVEYRPKNSGEPWNEITVPGTTTSvTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 1907074051 1628 WKTYS 1632
Cdd:pfam00041   81 EGPPS 85

fn3

Fibronectin type III domain;

1644-1723

2.98e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 58.58 E-value: 2.98e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1644 DKIQNLHCRPQNSTAIACSWIPP---DSDFDGYSIECRKMDTQEIEFSRKLEKEKSLLNIMMLVPHKRYLVSIKVQSAGM 1720
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1907074051 1721 TSE 1723
Cdd:pfam00041   81 EGP 83

PTP_YopH-like

cd14559

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

2151-2244

2.68e-09

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: 59.72 E-value: 2.68e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2151 FHYTVWPDHG-------------VPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVAldrILQQLDSKDS 2217
Cdd:cd14559    121 VHVTNWPDHTaisseglkeladlVNKSAEEKRNFYKSKGSSAINDKNKLLPVIHCRAGVGRTGQLAA---AMELNKSPNN 197

                           90       100
                   ....*....|....*....|....*...
gi 1907074051 2218 VDIYGAVHDLRLHR-VHMVQTECQYVYL 2244
Cdd:cd14559    198 LSVEDIVSDMRTSRnGKMVQKDEQLDTL 225

FN3

Fibronectin type 3 domain [General function prediction only];

1341-1674

3.05e-09

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 62.33 E-value: 3.05e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1341 EDLTPGKKYKMQILTVSGGLFSKESQA----EGRTVPAAVTNLRITENSSRYLSFGWTASEGE-LSWYNIFLYN-PDRTL 1414
Cdd:COG3401    197 GDIEPGTTYYYRVAATDTGGESAPSNEvsvtTPTTPPSAPTGLTATADTPGSVTLSWDPVTESdATGYRVYRSNsGDGPF 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1415 QERAQVDplVQSFSFQNLLQGR--MYKMVIVTHSGELSNESFIF----GRTVPAAVNHLKGShRNTTDSLWFSWSPASG- 1487
Cdd:COG3401    277 TKVATVT--TTSYTDTGLTNGTtyYYRVTAVDAAGNESAPSNVVsvttDLTPPAAPSGLTAT-AVGSSSITLSWTASSDa 353

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1488 DFDFYElILYNPNGTKKENW--KEKDVTEWRFQGLVPGRKYTlYVVT------HSGDLSNKVTGEGRTAPSPPSLLSFAD 1559
Cdd:COG3401    354 DVTGYN-VYRSTSGGGTYTKiaETVTTTSYTDTGLTPGTTYY-YKVTavdaagNESAPSEEVSATTASAASGESLTASVD 431

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1560 VANT---------SLAITWKGPPDWTDYNDFELQWFPGDALTIFNPYSSRKSEGRIVYGLHPGRSYQFSVKTVSGDSWKT 1630
Cdd:COG3401    432 AVPLtdvagataaASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSV 511

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1907074051 1631 YSKPISGSVRTKPDKIQNLHCRPQNS-TAIACSWIPPDSDFDGYS 1674
Cdd:COG3401    512 IGASAAAAVGGAPDGTPNVTGASPVTvGASTGDVLITDLVSLTTS 556

fn3

Fibronectin type III domain;

1020-1096

1.40e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 53.96 E-value: 1.40e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1020 DKVQGISVSNsARSDYLKVSWVHAT---GDFDHYEVTI--KNRESFIQTKTIPKSENECEFIELVPGRLYSVTVSTKSGQ 1094
Cdd:pfam00041    1 SAPSNLTVTD-VTSTSLTVSWTPPPdgnGPITGYEVEYrpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ..
gi 1907074051 1095 YE 1096
Cdd:pfam00041   80 GE 81

FN3

Fibronectin type 3 domain [General function prediction only];

856-1309

1.56e-08

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 60.02 E-value: 1.56e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  856 TSSLFTNWTKALGDVEFYQVLLIHENVVVKNESVSSDTSRYSFRALKPGSLYSVVVTTVSGGISSRQVVAEGRTVPSSVS 935
Cdd:COG3401     61 LSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGT 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  936 GVTVNNSGRNDYLSVSWLPAPGEVDHYVVSLSH-----EGKVDQFLIIAKSVSECSFSsLTPGRLYNVTVTTKSGNYAS- 1009
Cdd:COG3401    141 YALGAGLYGVDGANASGTTASSVAGAGVVVSPDtsataAVATTSLTVTSTTLVDGGGD-IEPGTTYYYRVAATDTGGESa 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1010 ----HSFTEERTVPDKVQGISVSnSARSDYLKVSWV-HATGDFDHYEVTIKNRESfiQTKTIPKSENECEFI--ELVPGR 1082
Cdd:COG3401    220 psneVSVTTPTTPPSAPTGLTAT-ADTPGSVTLSWDpVTESDATGYRVYRSNSGD--GPFTKVATVTTTSYTdtGLTNGT 296

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1083 LYSVTVSTKSGQYEASEQ------GTGRTIPEPVKDLTLLNRSTEDLHVTWS-RANGDVDQYEVQLLFNDMKVFPHIHLV 1155
Cdd:COG3401    297 TYYYRVTAVDAAGNESAPsnvvsvTTDLTPPAAPSGLTATAVGSSSITLSWTaSSDADVTGYNVYRSTSGGGTYTKIAET 376

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1156 NTATEYKFTALTPGRHYKILVLTISGDVQQSAFIEGLTVPSTVKNIHISANGATDR---------LMVTWSPGGGDVDSY 1226
Cdd:COG3401    377 VTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAvpltdvagaTAAASAASNPGVSAA 456

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1227 VVSAFRQDEKVDSQT-------IPKHASEHTFHRLEAGAKYRIAIVSVSGSLRNQIDALGQTVPASVQGVVaANAYSSNS 1299
Cdd:COG3401    457 VLADGGDTGNAVPFTttsstvtATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGT-PNVTGASP 535

                          490
                   ....*....|
gi 1907074051 1300 LTVSWQKALG 1309
Cdd:COG3401    536 VTVGASTGDV 545

fn3

Fibronectin type III domain;

579-658

1.71e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 53.57 E-value: 1.71e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  579 EVSNLKVTNDGRlTSLNVKWQKPP---GDVDSYSITLSHQGTIKESK--TLAPPVTETQFKDLVPGRLYQVTISCISGEL 653
Cdd:pfam00041    2 APSNLTVTDVTS-TSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNeiTVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 1907074051  654 SAEKS 658
Cdd:pfam00041   81 EGPPS 85

fn3

Fibronectin type III domain;

1109-1182

2.12e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 53.19 E-value: 2.12e-08

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907074051 1109 PVKDLTLLNRSTEDLHVTWSRA---NGDVDQYEVQLL-FNDMKVFPHIHLVNTATEYKFTALTPGRHYKILVLTISGD 1182
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

fn3

Fibronectin type III domain;

1473-1536

2.39e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 53.19 E-value: 2.39e-08

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907074051 1473 NTTDSLWFSWSPA---SGDFDFYELILYNPNGTKKENWKE--KDVTEWRFQGLVPGRKYTLYVVTHSGD 1536
Cdd:pfam00041   11 VTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITvpGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

fn3

Fibronectin type III domain;

757-835

2.56e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 53.19 E-value: 2.56e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  757 AVLQLRVKHANETSLGITWRAPL---GEWEKYIISL--MDRELLVIHKSLSKDAKEFTFTDLMPGRNYKATVTSMSGDLK 831
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYrpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ....
gi 1907074051  832 QSSS 835
Cdd:pfam00041   82 GPPS 85

FN3

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

398-483

3.33e-08

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 52.88 E-value: 3.33e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  398 PLPPARFEVnrEKTASTTLQVRWTPSS---GKVSWYEVQLFDHNNQKIQEVQVQESTTwSQYTFLNLTEGNSYKVAITAV 474
Cdd:cd00063      1 PSPPTNLRV--TDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSE-TSYTLTGLKPGTEYEFRVRAV 77


                   ....*....
gi 1907074051  475 SGEKRSFPV 483
Cdd:cd00063     78 NGGGESPPS 86

PTP_DSP_cys

cd14494

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

2170-2246

6.12e-08

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: 53.12 E-value: 6.12e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2170 QFVRTVRDYINR--SPGaGPTVVHCSAGVGRTGTFVALDRILQQLDS-KDSVDIYGavhdlRLHRVHMVQTECQYVYLHQ 2246
Cdd:cd14494     40 AMVDRFLEVLDQaeKPG-EPVLVHCKAGVGRTGTLVACYLVLLGGMSaEEAVRIVR-----LIRPGGIPQTIEQLDFLIK 113

fn3

Fibronectin type III domain;

1196-1269

6.34e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 52.03 E-value: 6.34e-08

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907074051 1196 STVKNIHISANGATDrLMVTWSP---GGGDVDSYVVSAFRQD--EKVDSQTIPKHASEHTFHRLEAGAKYRIAIVSVSG 1269
Cdd:pfam00041    1 SAPSNLTVTDVTSTS-LTVSWTPppdGNGPITGYEVEYRPKNsgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

fn3

Fibronectin type III domain;

932-1010

8.02e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 51.65 E-value: 8.02e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  932 SSVSGVTVNNSGrNDYLSVSWLPAP---GEVDHYVVSLSHEGKVDQF--LIIAKSVSECSFSSLTPGRLYNVTVTTKSGN 1006
Cdd:pfam00041    1 SAPSNLTVTDVT-STSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWneITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....
gi 1907074051 1007 YASH 1010
Cdd:pfam00041   80 GEGP 83

fn3

Fibronectin type III domain;

844-917

1.80e-07

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 50.88 E-value: 1.80e-07

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907074051  844 QVTDLHVNNQGmTSSLFTNWTKAL---GDVEFYQVLLIHEN--VVVKNESVSSDTSRYSFRALKPGSLYSVVVTTVSGG 917
Cdd:pfam00041    2 APSNLTVTDVT-STSLTVSWTPPPdgnGPITGYEVEYRPKNsgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

CDKN3-like

cd14505

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

2137-2246

1.86e-07

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: 53.04 E-value: 1.86e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2137 CSEEQLDAHRL-----------IRHFHYTVwPDHGVPETTQsliQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVAl 2205
Cdd:cd14505     51 CTDGELEELGVpdlleqyqqagITWHHLPI-PDGGVPSDIA---QWQELLEELLSALENGKKVLIHCKGGLGRTGLIAA- 125

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1907074051 2206 dRILQQLDSKDSVDiyGAVHDLRLHRVHMVQTECQYVYLHQ 2246
Cdd:cd14505    126 -CLLLELGDTLDPE--QAIAAVRALRPGAIQTPKQENFLHQ 163

Ricin_B_lectin

pfam00652

Ricin-type beta-trefoil lectin domain;

22-93

3.45e-07

Ricin-type beta-trefoil lectin domain;

Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 51.38 E-value: 3.45e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051   22 QIVHVRKQQCLSINQ-----KVVMGFCNGSSRNQQWLSTEDGKFL-HIKSGLCLGISNSSRGPFQPAVATPCAQAP--RW 93
Cdd:pfam00652   47 TIRSVASDLCLDVGStadgaKVVLWPCHPGNGNQRWRYDEDGTQIrNPQSGKCLDVSGAGTSNGKVILWTCDSGNPnqQW 126

PTP_VSP_TPTE

cd14510

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...

2134-2245

4.86e-07

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

Pssm-ID: 350360 [Multi-domain] Cd Length: 177 Bit Score: 51.98 E-value: 4.86e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2134 FKICSEEQLDAhrliRHFHYTV----WPDHGVPeTTQSLIQFVRTVRDYINRSPgAGPTVVHCSAGVGRTGTFVA--LDR 2207
Cdd:cd14510     59 YNLCSERGYDP----KYFHNRVervpIDDHNVP-TLDEMLSFTAEVREWMAADP-KNVVAIHCKGGKGRTGTMVCawLIY 132

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1907074051 2208 ILQQLDSKDSVDIYGAVH-DLRL-HRVHMVQTECQYVYLH 2245
Cdd:cd14510    133 SGQFESAKEALEYFGERRtDKSVsSKFQGVETPSQSRYVG 172

FN3

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

1643-1731

1.01e-06

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 49.03 E-value: 1.01e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1643 PDKIQNLHCRPQNSTAIACSWIPPDSD---FDGYSIECRKMDTQEIEFSRKLEKEKSLLNIMMLVPHKRYLVSIKVQSAG 1719
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDggpITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|..
gi 1907074051 1720 MTSEVVEDSTIT 1731
Cdd:cd00063     81 GESPPSESVTVT 92

PTP_PTEN

cd14509

protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...

2137-2223

1.59e-06

protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; Phosphatase and tensin homolog (PTEN), also phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN or mutated in multiple advanced cancers 1 (MMAC1), is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It is a critical endogenous inhibitor of phosphoinositide signaling. It dephosphorylates phosphoinositide trisphosphate, and therefore, has the function of negatively regulating Akt. The PTEN/PI3K/AKT pathway regulates the signaling of multiple biological processes such as apoptosis, metabolism, cell proliferation, and cell growth. PTEN contains an N-terminal PIP-binding domain, a protein tyrosine phosphatase (PTP)-like catalytic domain, a regulatory C2 domain responsible for its cellular location, a C-tail containing phosphorylation sites, and a C-terminal PDZ domain.

Pssm-ID: 350359 [Multi-domain] Cd Length: 158 Bit Score: 50.28 E-value: 1.59e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2137 CSEEQLDAHRlirhFHYTV----WPDHGVPeTTQSLIQFVRTVRDYINRSPGAgPTVVHCSAGVGRTGTFVA--LDRILQ 2210
Cdd:cd14509     48 CSERSYDPSK----FNGRVaeypFDDHNPP-PLELIKPFCEDVDEWLKEDEKN-VAAVHCKAGKGRTGVMICcyLLYLGK 121

                           90
                   ....*....|...
gi 1907074051 2211 QLDSKDSVDIYGA 2223
Cdd:cd14509    122 FPSAKEALDFYGA 134

fn3

Fibronectin type III domain;

413-482

1.63e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 48.18 E-value: 1.63e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907074051  413 STTLQVRWTPS---SGKVSWYEVQLFDHN-NQKIQEVQVQESTTwsQYTFLNLTEGNSYKVAITAVSGEKRSFP 482
Cdd:pfam00041   13 STSLTVSWTPPpdgNGPITGYEVEYRPKNsGEPWNEITVPGTTT--SVTLTGLKPGTEYEVRVQAVNGGGEGPP 84

fn3

Fibronectin type III domain;

1375-1448

2.06e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 47.79 E-value: 2.06e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907074051 1375 AVTNLRITENSSRYLSFGWTASE---GELSWYNIFLYNPDRTLQERAQVDPLVQ-SFSFQNLLQGRMYKMVIVTHSGE 1448
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGG 79

FN3

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

1549-1636

2.28e-06

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 47.88 E-value: 2.28e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1549 PSPPSLLSFADVANTSLAITWKGPPDWTDYND-FELQWFPGDALTIFNPYSSRKSEGR-IVYGLHPGRSYQFSVKTVSGD 1626
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITgYVVEYREKGSGDWKEVEVTPGSETSyTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|
gi 1907074051 1627 SWKTYSKPIS 1636
Cdd:cd00063     81 GESPPSESVT 90

FN3

Fibronectin type 3 domain [General function prediction only];

570-1030

2.30e-06

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 53.08 E-value: 2.30e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  570 WKLVRTAPMEVSNLKVTNDGRLTSLNVKWQKPPGDVDSYSITLSHQGTIKESKTLAPPVTETqfkdLVPGRLYQVTISCI 649
Cdd:COG3401     49 KESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTG----LTSSDEVPSPAVGT 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  650 SGELSAEKSAAGRTVPEKVRNLVSYNEIWMKSFTVNWTPPAGDWEHYRIVLFNESLVLLNTTVGKEEThyALDGLELIPG 729
Cdd:COG3401    125 ATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTL--VDGGGDIEPG 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  730 RQYE--IEVIVESGNLRNSERC---QGRTVPLAVLQLRVKHANETSLGITWRAPLGEWEK-YIIslmdrellviHKSLSK 803
Cdd:COG3401    203 TTYYyrVAATDTGGESAPSNEVsvtTPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATgYRV----------YRSNSG 272

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  804 DAK----------EFTFTDLMPGRNYKATVTSM------SGDLKQSSSIKGRTVPAQVTDLHVNNQGMTS-SLftNWTKA 866
Cdd:COG3401    273 DGPftkvatvtttSYTDTGLTNGTTYYYRVTAVdaagneSAPSNVVSVTTDLTPPAAPSGLTATAVGSSSiTL--SWTAS 350

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  867 LG-DVEFYQVL--LIHENVVVKNESVSSDTSrYSFRALKPGSLYSVVVTTV-SGGISSRQvvaegrtvPSSVSGVTVNNS 942
Cdd:COG3401    351 SDaDVTGYNVYrsTSGGGTYTKIAETVTTTS-YTDTGLTPGTTYYYKVTAVdAAGNESAP--------SEEVSATTASAA 421

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  943 GRNDYLSVSWLPAPGEVDHYVVSLSHEGKVDQFLIIAKSVSECSFSSLTPGRLYNVTVTTKSGNYASHSFTEERTVPDKV 1022
Cdd:COG3401    422 SGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSG 501


                   ....*...
gi 1907074051 1023 QGISVSNS 1030
Cdd:COG3401    502 ASSVTNSV 509

FN3

Fibronectin type 3 domain [General function prediction only];

1154-1505

2.76e-06

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 52.70 E-value: 2.76e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1154 LVNTATEYKFTALTPGR--HYKILVLTISGDVQQSAFIEGL---TVPSTVKNIHISANGaTDRLMVTWSP-GGGDVDSYV 1227
Cdd:COG3401    187 VTSTTLVDGGGDIEPGTtyYYRVAATDTGGESAPSNEVSVTtptTPPSAPTGLTATADT-PGSVTLSWDPvTESDATGYR 265

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1228 VsaFRQDEKVDS-QTIPK-HASEHTFHRLEAGAKYRIAIVSVSGS-----LRNQIDA-LGQTVPASVQGVVAANAySSNS 1299
Cdd:COG3401    266 V--YRSNSGDGPfTKVATvTTTSYTDTGLTNGTTYYYRVTAVDAAgnesaPSNVVSVtTDLTPPAAPSGLTATAV-GSSS 342

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1300 LTVSWQKALGV-AERYDILLLNENGLLLSNVSEPATARQHKFEDLTPGKKYKMQILTV-SGGLFSKESQ--------AEG 1369
Cdd:COG3401    343 ITLSWTASSDAdVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVdAAGNESAPSEevsattasAAS 422

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1370 RTVPAAVTNLRITENSSRYLSFGWTASEGELSWYNIFLYNPDRTLQERAQVDPLVQSFSFQNLLQG-RMYKMVIVTHSGE 1448
Cdd:COG3401    423 GESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANlSVTTGSLVGGSGA 502

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907074051 1449 LSNESFIFGRTVPAAVNHlkGSHRNTTDSLWFSWSPASGDFDFYELILYNPNGTKKE 1505
Cdd:COG3401    503 SSVTNSVSVIGASAAAAV--GGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSA 557

beta-trefoil_Ricin_GALNT1-like

cd23433

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...

31-94

3.04e-06

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 1 (GALNT1)-like subfamily; The GALNT1-like subfamily includes GALNT1 and GALNT13. They catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT1 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. GALNT13 has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. It can glycosylate SDC3. It may be responsible for the synthesis of Tn antigen in neuronal cells. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467311 [Multi-domain] Cd Length: 127 Bit Score: 48.46 E-value: 3.04e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051   31 CL---SINQKVVMGFCNGSSRNQQWL-STEDGKFLHIKSGLCLGISNsSRGPFQPAVAtPCAQAP--RWT 94
Cdd:cd23433     57 CLdasRKGGPVKLEKCHGMGGNQEWEyDKETKQIRHVNSGLCLTAPN-EDDPNEPVLR-PCDGGPsqKWE 124

fn3

Fibronectin type III domain;

681-742

5.21e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 46.64 E-value: 5.21e-06

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907074051  681 SFTVNWTPPA---GDWEHYRIVLF--NESLVLLNTTVGKEETHYALDGLEliPGRQYEIEVIVESGN 742
Cdd:pfam00041   15 SLTVSWTPPPdgnGPITGYEVEYRpkNSGEPWNEITVPGTTTSVTLTGLK--PGTEYEVRVQAVNGG 79

FN3

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

577-652

6.05e-06

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 46.72 E-value: 6.05e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  577 PMEVSNLKVTNDGRlTSLNVKWQKPPGD---VDSYSITLS--HQGTIKESKTLAPPVTETQFKDLVPGRLYQVTISCISG 651
Cdd:cd00063      1 PSPPTNLRVTDVTS-TSVTLSWTPPEDDggpITGYVVEYRekGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79


                   .
gi 1907074051  652 E 652
Cdd:cd00063     80 G 80

fn3

Fibronectin type III domain;

492-560

9.00e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 45.87 E-value: 9.00e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907074051  492 SPVKDLGISP-NPNSLLISWSR---GSGNVEQYRLVL--MDKGAIVQDTNVDRRDTSYAFHELTPGHLYNLTIVT 560
Cdd:pfam00041    1 SAPSNLTVTDvTSTSLTVSWTPppdGNGPITGYEVEYrpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75

fn3

Fibronectin type III domain;

1285-1365

1.07e-05

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 45.87 E-value: 1.07e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1285 SVQGVVAANAySSNSLTVSWQKAL---GVAERYDIL-LLNENGLLLSNVSEPATARQHKFEDLTPGKKYKMQILTVSGGL 1360
Cdd:pfam00041    2 APSNLTVTDV-TSTSLTVSWTPPPdgnGPITGYEVEyRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 1907074051 1361 FSKES 1365
Cdd:pfam00041   81 EGPPS 85

FN3

Fibronectin type 3 domain [General function prediction only];

370-545

1.27e-05

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 50.39 E-value: 1.27e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  370 KDLQAGTVYNFRIVSLD--GEES----TLVLQTDPLPPAR-FEVNREKTASTTLQVRWTPSSGK-VSWYEVQLFDHNNQK 441
Cdd:COG3401    290 TGLTNGTTYYYRVTAVDaaGNESapsnVVSVTTDLTPPAApSGLTATAVGSSSITLSWTASSDAdVTGYNVYRSTSGGGT 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  442 IQEVQVQESTTWsqYTFLNLTEGNSYKVAITAV--SGEK--RSFPVYINGSTVPSPVKDLGISP----NPNSLLISWSRG 513
Cdd:COG3401    370 YTKIAETVTTTS--YTDTGLTPGTTYYYKVTAVdaAGNEsaPSEEVSATTASAASGESLTASVDavplTDVAGATAAASA 447

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1907074051  514 SGNVEQYRLVLMDKGAIVQDTNVDRRDTSYAF 545
Cdd:COG3401    448 ASNPGVSAAVLADGGDTGNAVPFTTTSSTVTA 479

FN3

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

491-560

1.39e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 45.30 E-value: 1.39e-05

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907074051   491 PSPVKDLGISP-NPNSLLISWSR-----GSGNVEQYRLVLMDKGAIVQDTNVDRRDTSYAFHELTPGHLYNLTIVT 560
Cdd:smart00060    1 PSPPSNLRVTDvTSTSVTLSWEPppddgITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRA 76

FN3

Fibronectin type 3 domain [General function prediction only];

163-623

2.02e-05

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 50.00 E-value: 2.02e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  163 RNSAASQIATTANTVPYSPSHISNTTETFLGSTTETLRSTAETLGSTAETLRNTAKT-LGSTAETLRNTAKTLGSTAETL 241
Cdd:COG3401      1 TGSSYLTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVaAGLSSGGGLGTGGRAGTTSGVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  242 GSTAKTLGSTAKTLGSTAKTLGSTSEAYSQSSSKRGLPHLHTAGATDESWSPLTTPPFSSITTETGVAEQvkcNFTLLES 321
Cdd:COG3401     81 AVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGV---DGANASG 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  322 RVSSLSASIQWRTFASPCNFSLIYSSDTSGPMWCHPIridnftygcNPKDLQAGTVYNFRIVSLDG--------EESTLV 393
Cdd:COG3401    158 TTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVD---------GGGDIEPGTTYYYRVAATDTggesapsnEVSVTT 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  394 LQTDPLPPARFEVNREKTASTTLQvrWTPSSGK-VSWYEVQLFDHNNQKIQEVqvqESTTWSQYTFLNLTEGNSYKVAIT 472
Cdd:COG3401    229 PTTPPSAPTGLTATADTPGSVTLS--WDPVTESdATGYRVYRSNSGDGPFTKV---ATVTTTSYTDTGLTNGTTYYYRVT 303

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  473 AV--SGEK--RSFPVYIN-GSTVPSPVKDL-GISPNPNSLLISWSRGSGNVEQYRLVLMDKGAIVQDTNVDR--RDTSYA 544
Cdd:COG3401    304 AVdaAGNEsaPSNVVSVTtDLTPPAAPSGLtATAVGSSSITLSWTASSDADVTGYNVYRSTSGGGTYTKIAEtvTTTSYT 383

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907074051  545 FHELTPGHLYNLTIVTMASGLQNSrwklvrTAPMEVSNLKVTNDGRLTSLNVKWQKPPGDVDSYSITLSHQGTIKESKT 623
Cdd:COG3401    384 DTGLTPGTTYYYKVTAVDAAGNES------APSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAA 456

FN3

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

577-651

2.10e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 44.91 E-value: 2.10e-05

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051   577 PMEVSNLKVTNDGRlTSLNVKWQKPPGD-----VDSYSITLSHQGTIKESKTLAPPVTETQFKDLVPGRLYQVTISCISG 651
Cdd:smart00060    1 PSPPSNLRVTDVTS-TSVTLSWEPPPDDgitgyIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

beta-trefoil_Ricin_laminarinase

cd23451

ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...

37-94

2.44e-05

ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and similar proteins; Glucan endo-1,3-beta-glucosidase (EC 3.2.1.39), also called (1->3)-beta-glucan endohydrolase, or (1->3)-beta-glucanase, or laminarinase, belongs to the glycosyl hydrolase 64 (GH64) family. It catalyzes hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans. It has been implicated in the defense against fungal pathogens. Glucan endo-1,3-beta-glucosidase contains a C-terminal ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467329 [Multi-domain] Cd Length: 125 Bit Score: 45.79 E-value: 2.44e-05

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051   37 KVVMGFCNGSSrNQQWLSTEDGKFLHIKSGLCLGISNSSRGPFQPAVATPC--AQAPRWT 94
Cdd:cd23451     67 LVQLWDCNGTG-AQKWVPRADGTLYNPQSGKCLDAPGGSTTDGTQLQLYTCngTAAQQWT 125

beta-trefoil_Ricin_XLN-like

cd23418

ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...

26-96

2.46e-05

ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1,4-beta-xylanase and similar proteins; The family includes Streptomyces olivaceoviridis endo-1,4-beta-xylanase (XLN, EC 3.2.1.8), Streptomyces avermitilis beta-L-arabinopyranosidase (EC 3.2.1.185), and Streptomyces coelicolor extracellular exo-alpha-L-arabinofuranosidase (ABF, EC 3.2.1.55). XLN, also called xylanase, or 1,4-beta-D-xylan xylanohydrolase, belongs to the glycosyl hydrolase 10 (cellulase F) family. It contributes to hydrolyze hemicellulose, the major component of plant cell walls. XLN contains a (beta/alpha)8-barrel as a catalytic domain, a family 13 carbohydrate binding module (CBM13) as a xylan binding domain (XBD) and a Gly/Pro-rich linker between them. Beta-L-arabinopyranosidase belongs to the glycosyl hydrolase 27 (GH27) family. It has a GH27 catalytic domain, an antiparallel beta-domain containing Greek key motifs, another antiparallel beta-domain forming a jellyroll structure, and a CBM13 module. ScAraf62A, also called ABF, or arabinosidase, or arabinoxylan arabinofuranohydrolase, belongs to the glycosyl hydrolase 62 (GH62) family. It is involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. It acts synergistically with xylanases and binds specifically to xylan. ScAraf62A comprises a CBM13 module at its N-terminus and a catalytic domain at its C-terminus. This model corresponds to the CBM13 module, which is a ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding pocket.

Pssm-ID: 467297 [Multi-domain] Cd Length: 130 Bit Score: 45.80 E-value: 2.46e-05

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907074051   26 VRKQQCLSI-------NQKVVMGFCNGSSrNQQWLSTEDGKFLHIKSGLCLGISNSSRGPFQPAVAtpcaqaprWTCH 96
Cdd:cd23418     53 VGGDKCLDAagggttnGTPVVIWPCNGGA-NQKWRFNSDGTIRNVNSGLCLDVAGGGTANGTRLIL--------WSCN 121

FN3

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

1549-1628

2.55e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 44.53 E-value: 2.55e-05

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  1549 PSPPSLLSFADVANTSLAITWKGPPD--WTDYND-FELQWFPGDALTIFNPYSSRKSEGRIVyGLHPGRSYQFSVKTVSG 1625
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDdgITGYIVgYRVEYREEGSEWKEVNVTPSSTSYTLT-GLKPGTEYEFRVRAVNG 79


                    ...
gi 1907074051  1626 DSW 1628
Cdd:smart00060   80 AGE 82

Herpes_BLLF1

pfam05109

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...

158-352

2.65e-05

Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 49.53 E-value: 2.65e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  158 SVRTARNSAASQIATTANTVPYSPSHISNTTETFLGSTTETLRSTAETLGSTAETLRNTAKTLGSTAETLRNTAKTLGST 237
Cdd:pfam05109  512 AVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNAT 591

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  238 AETLGSTAKTLGSTAKTLGSTAKTLGSTSEAYSQSSSKRGLPHLHTAGATdeswSPLTTPPFS-SITTETGVAEQVKCNF 316
Cdd:pfam05109  592 SPTVGETSPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSST----SSMSLRPSSiSETLSPSTSDNSTSHM 667

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1907074051  317 TLLESRVSSLSASIQWRTFASPCNFSLIYSSDTSGP 352
Cdd:pfam05109  668 PLLTSAHPTGGENITQVTPASTSTHHVSTSSPAPRP 703

beta-trefoil_Ricin-like

cd00161

ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...

21-100

3.81e-05

ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a carbohydrate-binding domain formed from presumed gene triplication. It shows a beta-trefoil fold characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain was originally found in Ricin, which is a legume lectin from the seeds of the castor bean plant, Ricinus communis. It is also found in many carbohydrate-recognition proteins like plant and bacterial AB-toxins, glycosidases, or proteases, which serve diverse functions such as inhibitory toxicity, enzymatic activity, and signal transduction. The ricin B-type lectin domain can be present in one or more copies and has been shown in some instances to bind simple sugars, such as galactose or lactose. The most characteristic, though not completely conserved, sequence feature is the presence of a Q-W pattern. Consequently, the ricin B-type lectin domain has also been referred as the (QxW)3 domain and the three homologous regions as the QxW repeats. A disulfide bond is also conserved in some QxW repeats.

Pssm-ID: 467293 [Multi-domain] Cd Length: 134 Bit Score: 45.44 E-value: 3.81e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051   21 FQIVHVRKQQCLSI-------NQKVVMGFCNGSSrNQQW----LSTEDGKFLHIKSGLCLGISNSSRGPFQPAVATPCAQ 89
Cdd:cd00161      3 YRIVNAASGKCLDVaggstanGAPVQQWTCNGGA-NQQWtltpVGDGYYTIRNVASGKCLDVAGGSTANGANVQQWTCNG 81

                           90
                   ....*....|...
gi 1907074051   90 AP--RWTCHAQEG 100
Cdd:cd00161     82 GDnqQWRLEPVGD 94

RICIN

smart00458

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.

23-74

4.17e-05

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.

Pssm-ID: 214672 [Multi-domain] Cd Length: 118 Bit Score: 45.19 E-value: 4.17e-05

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1907074051    23 IVHVRKQQCLSI---NQKVVMGFCNGSSRNQQWLSTEDGKFLHIKSGLCLGISNS 74
Cdd:smart00458    1 IISGNTGKCLDVngnKNPVGLFDCHGTGGNQLWKLTSDGAIRIKDTDLCLTANGN 55

FN3

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

398-480

5.81e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 43.76 E-value: 5.81e-05

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051   398 PLPPARFEVnrEKTASTTLQVRWT-PSSGKVSWYEVQLFDHNNQK-IQEVQVQESTTWSQYTFLNLTEGNSYKVAITAVS 475
Cdd:smart00060    1 PSPPSNLRV--TDVTSTSVTLSWEpPPDDGITGYIVGYRVEYREEgSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 1907074051   476 GEKRS 480
Cdd:smart00060   79 GAGEG 83

Ricin_B_lectin

pfam00652

Ricin-type beta-trefoil lectin domain;

21-94

5.93e-05

Ricin-type beta-trefoil lectin domain;

Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 44.83 E-value: 5.93e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051   21 FQIVHVRKQQCLSINQK------VVMGFCNGSSRNQQWLSTEDGKFLHIKSGLCLGISNSSRGpfQPAVATPCAQAP--- 91
Cdd:pfam00652    3 GRIRNRASGKCLDVPGGssaggpVGLYPCHGSNGNQLWTLTGDGTIRSVASDLCLDVGSTADG--AKVVLWPCHPGNgnq 80


                   ...
gi 1907074051   92 RWT 94
Cdd:pfam00652   81 RWR 83

Herpes_BLLF1

pfam05109

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...

154-351

7.49e-05

Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 47.99 E-value: 7.49e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  154 GTEVSVRTARNSAASQIATTANTVPYSPSHISNTTEtflgSTTETLRSTAETLGSTAETLRNTAKTLGSTAETLRNTAKT 233
Cdd:pfam05109  498 GTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPN----ATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPT 573

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  234 LGSTAETLGSTAKTLGSTAKTLGSTAKTLGSTSeaysqssskrglphlHTAGATdeSWSPLTTPPFSSITT--ETGVAEQ 311
Cdd:pfam05109  574 LGKTSPTSAVTTPTPNATSPTVGETSPQANTTN---------------HTLGGT--SSTPVVTSPPKNATSavTTGQHNI 636

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1907074051  312 VKCNFTLLESRVSSLSASIQWRTF-ASPCNFSLIYSSDTSG 351
Cdd:pfam05109  637 TSSSTSSMSLRPSSISETLSPSTSdNSTSHMPLLTSAHPTG 677

beta-trefoil_Ricin-like

cd00161

ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...

21-93

1.55e-04

Pssm-ID: 467293 [Multi-domain] Cd Length: 134 Bit Score: 43.90 E-value: 1.55e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051   21 FQIVHVRKQQCLSI-------NQKVVMGFCNGSSrNQQW----LSTEDGKFLHIKSGLCLGISNSSRGPFQPAVATPCAQ 89
Cdd:cd00161     50 YTIRNVASGKCLDVaggstanGANVQQWTCNGGD-NQQWrlepVGDGYYRIVNKHSGKCLDVSGGSTANGANVQQWTCNG 128


                   ....*.
gi 1907074051   90 AP--RW 93
Cdd:cd00161    129 GAnqQW 134

DUSP23

cd14504

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

2142-2204

1.77e-04

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

Pssm-ID: 350354 [Multi-domain] Cd Length: 142 Bit Score: 43.81 E-value: 1.77e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907074051 2142 LDAHRLIRHFHYTVwPDHGVPeTTQSLIQFVRTVRDYINRSpgaGPTVVHCSAGVGRTGTFVA 2204
Cdd:cd14504     44 SDTCPGLRYHHIPI-EDYTPP-TLEQIDEFLDIVEEANAKN---EAVLVHCLAGKGRTGTMLA 101

FN3

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

755-828

2.65e-04

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 41.83 E-value: 2.65e-04

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907074051   755 PLAVLQLRVKHANETSLGITWRAP-----LGEWEKYIISLMDRELLVIHKSLSKDAKEFTFTDLMPGRNYKATVTSMSG 828
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPpddgiTGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

TpbA-like

cd14529

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...

2148-2229

3.36e-04

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

Pssm-ID: 350378 [Multi-domain] Cd Length: 158 Bit Score: 43.52 E-value: 3.36e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 2148 IRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRspgaGPTVVHCSAGVGRTGTFVALDRILQQLDSKDsvdiygAVHDL 2227
Cdd:cd14529     56 IDGVKYVNLPLSATRPTESDVQSFLLIMDLKLAP----GPVLIHCKHGKDRTGLVSALYRIVYGGSKEE------ANEDY 125


                   ..
gi 1907074051 2228 RL 2229
Cdd:cd14529    126 RL 127

FN3

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

755-840

4.02e-04

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 41.33 E-value: 4.02e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  755 PLAVLQLRVKHANETSLGITWRAPL---GEWEKYIISL--MDRELLVIHKSLSKDAKEFTFTDLMPGRNYKATVTSMSGD 829
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYreKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|...
gi 1907074051  830 L--KQSSSIKGRT 840
Cdd:cd00063     81 GesPPSESVTVTT 93

FN3

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

931-1009

4.98e-04

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 41.33 E-value: 4.98e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  931 PSSVSGVTVNNSGRnDYLSVSWLPAP---GEVDHYVVSLSHEGKVDQFLIIAKSVSECSF--SSLTPGRLYNVTVTTKSG 1005
Cdd:cd00063      1 PSPPTNLRVTDVTS-TSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYtlTGLKPGTEYEFRVRAVNG 79


                   ....
gi 1907074051 1006 NYAS 1009
Cdd:cd00063     80 GGES 83

FN3

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

1019-1105

5.03e-04

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 41.33 E-value: 5.03e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1019 PDKVQGISVSNSaRSDYLKVSWVHATGD---FDHYEVTIK--NRESFIQTKTIPKSENECEFIELVPGRLYSVTVS--TK 1091
Cdd:cd00063      1 PSPPTNLRVTDV-TSTSVTLSWTPPEDDggpITGYVVEYRekGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRavNG 79

                           90
                   ....*....|....
gi 1907074051 1092 SGQYEASEQGTGRT 1105
Cdd:cd00063     80 GGESPPSESVTVTT 93

RICIN

smart00458

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.

22-75

5.36e-04

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.

Pssm-ID: 214672 [Multi-domain] Cd Length: 118 Bit Score: 41.73 E-value: 5.36e-04

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907074051    22 QIVHVRKQQCLSINQ----KVVMGFCNGSSRNQQWLSTEDGKFLHIKSGLCLGISNSS 75
Cdd:smart00458   40 AIRIKDTDLCLTANGntgsTVTLYSCDGTNDNQYWEVNKDGTIRNPDSGKCLDVKDGN 97

FN3

Fibronectin type 3 domain [General function prediction only];

1521-1778

5.73e-04

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 44.99 E-value: 5.73e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1521 VPGRKYTLYVVTHSGDLSNKVTGEGRTAPSPPSLLSFADVANTSLAITWKGPPDW-----TDYNDFELQWFPGDALTIFN 1595
Cdd:COG3401    105 GATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTassvaGAGVVVSPDTSATAAVATTS 184

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1596 PYSSRKSEGRIVYGLHPGRSYQFSVKTVSGDSWKTYSKPISGSV-RTKPDKIQNLHCRPQNSTAIACSWIP-PDSDFDGY 1673
Cdd:COG3401    185 LTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTpTTPPSAPTGLTATADTPGSVTLSWDPvTESDATGY 264

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1674 SIEcRKMDTQEiEFSRKLEKEKSLLNIMMLVPHKRYLVSIK-VQSAGMTSEVVEDSTITMIDRPPQPPPHIRVnekdVLI 1752
Cdd:COG3401    265 RVY-RSNSGDG-PFTKVATVTTTSYTDTGLTNGTTYYYRVTaVDAAGNESAPSNVVSVTTDLTPPAAPSGLTA----TAV 338

                          250       260
                   ....*....|....*....|....*.
gi 1907074051 1753 SKSSINFtvncSWFSDTNGAVKYFAV 1778
Cdd:COG3401    339 GSSSITL----SWTASSDADVTGYNV 360

PRK12688

flagellin; Reviewed

152-268

5.91e-04

flagellin; Reviewed

Pssm-ID: 171664 [Multi-domain] Cd Length: 751 Bit Score: 45.25 E-value: 5.91e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  152 GLGTEVSVRTARNS----------AASQIATTA--NTVPYSPShiSNTTETFLGSTTETLRSTAETLGSTAETLRNTAKT 219
Cdd:PRK12688    66 GIGNGVQILQAANTgitslqklidSAKSIANQAlqTVVGYSTK--SNVSTTISGATADDLRGTTSYASATASSNVLYDGA 143

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1907074051  220 LGSTaeTLRNTAKTLGSTAETLGSTAKTLGSTAKTLGSTAKTLGSTSEA 268
Cdd:PRK12688   144 AGGA--TAATGATTLGGTAGSLAGTGATAGDGTTALTGTITLIATNGTT 190

DSPc

smart00195

Dual specificity phosphatase, catalytic domain;

2150-2228

7.13e-04

Dual specificity phosphatase, catalytic domain;

Pssm-ID: 214551 [Multi-domain] Cd Length: 138 Bit Score: 41.88 E-value: 7.13e-04

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  2150 HFHYTVWPdhgVPETTQSLI-QFVRTVRDYINRS-PGAGPTVVHCSAGVGRTGTFVAldRILQQLDSKDSVDIYGAVHDL 2227
Cdd:smart00195   44 DFTYLGVP---IDDNTETKIsPYFPEAVEFIEDAeSKGGKVLVHCQAGVSRSATLII--AYLMKTRNMSLNDAYDFVKDR 118


                    .
gi 1907074051  2228 R 2228
Cdd:smart00195  119 R 119

COG4733

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

380-554

7.59e-04

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

Pssm-ID: 443767 [Multi-domain] Cd Length: 978 Bit Score: 44.94 E-value: 7.59e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  380 FRIVSL-DGEESTLVLQ----------------TDPLPPA----------RFEVNREKTASTTLQVRWTPSSGKVSwYEV 432
Cdd:COG4733    491 FRVVSIeENEDGTYTITavqhapekyaaidagaFDDVPPQwppvnvttseSLSVVAQGTAVTTLTVSWDAPAGAVA-YEV 569

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  433 QLFDHNNqkiqEVQVQESTTWSQYTFLNLTEGNsYKVAITAVS-GEKRSFPVY-----ING-STVPSPVKDLGISPNPNS 505
Cdd:COG4733    570 EWRRDDG----NWVSVPRTSGTSFEVPGIYAGD-YEVRVRAINaLGVSSAWAAssettVTGkTAPPPAPTGLTATGGLGG 644

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907074051  506 LLISWSRGSG-NVEQYRLVLMDKG--AIVQDTNVDRRDTSYAFHELTPGHLY 554
Cdd:COG4733    645 ITLSWSFPVDaDTLRTEIRYSTTGdwASATVAQALYPGNTYTLAGLKAGQTY 696

beta-trefoil_Ricin_MRC1

cd23407

ricin B-type lectin domain, beta-trefoil fold, found in macrophage mannose receptor 1 (MRC1) ...

21-135

7.97e-04

ricin B-type lectin domain, beta-trefoil fold, found in macrophage mannose receptor 1 (MRC1) and similar proteins; MRC1, also called MMR, C-type lectin domain family 13 member D (CLEC13D), C-type lectin domain family 13 member D-like (CLEC13DL), macrophage mannose receptor 1-like protein 1 (MRC1L1), or CD206, mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains. MRC1 acts as phagocytic receptor for bacteria, fungi and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC1 contains a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.

Pssm-ID: 467785 Cd Length: 123 Bit Score: 41.58 E-value: 7.97e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051   21 FQIVHVRKQQCL--SINQKVVMGFCNGSSRNQQWLSTEDGKFLHIKSGLCLGISNSSRGpfqpAVAT--PCAQAP---RW 93
Cdd:cd23407      3 FLIYNEDHNRCVqaRSSSSVTTATCNPNAESQKFRWVSGSQILSVAFKLCLGVPSKKDW----VTVTlfPCNEKSelqKW 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907074051   94 TCHaQEGFLEVENTSLFL--KKQNHKVVVkkISKYLDSWMKLVI 135
Cdd:cd23407     79 ECK-NDTLLALKGEDLYFnyGNRQEKNVM--LYKGSGLWSRWKI 119

beta-trefoil_Ricin_GALNT14-like

cd23441

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...

30-94

1.11e-03

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14)-like subfamily; The GALNT14-like subfamily includes GALNT14 and GALNT16. They act as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT14 displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). It may be involved in O-glycosylation in the kidney. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467319 [Multi-domain] Cd Length: 122 Bit Score: 40.85 E-value: 1.11e-03

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907074051   30 QCLSI-----NQKVVMGFCNGSsRNQQWLSTeDGKFLHIKSGLCLgisnSSRGPFQPAVaTPC---AQAPRWT 94
Cdd:cd23441     55 LCLTVdssskDLPVVLETCSDD-PKQKWTRT-GRQLVHSESGLCL----DSRKKKGLVV-SPCrsgAPSQKWD 120

PTP_PTEN-like

cd14497

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...

2156-2204

1.36e-03

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins; Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity.

Pssm-ID: 350347 [Multi-domain] Cd Length: 160 Bit Score: 41.41 E-value: 1.36e-03

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907074051 2156 WPDHGVPeTTQSLIQFVRTVRDYINRSPG--AgptVVHCSAGVGRTGTFVA 2204
Cdd:cd14497     68 FPDHHPP-PLGLLLEIVDDIDSWLSEDPNnvA---VVHCKAGKGRTGTVIC 114

FN3

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

491-559

1.43e-03

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 39.79 E-value: 1.43e-03

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907074051  491 PSPVKDLGISP-NPNSLLISWSR---GSGNVEQYRLVLMDKGA--IVQDTNVDRRDTSYAFHELTPGHLYNLTIV 559
Cdd:cd00063      1 PSPPTNLRVTDvTSTSVTLSWTPpedDGGPITGYVVEYREKGSgdWKEVEVTPGSETSYTLTGLKPGTEYEFRVR 75

beta-trefoil_Ricin_Pgant9-like

cd23462

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...

21-52

1.54e-03

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 9 (Pgant9) and similar proteins; The subfamily includes Pgant9 (also called pp-GaNTase 9, protein-UDP acetylgalactosaminyltransferase 9, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9), Pgant4 (also called pp-GaNTase 4, N-acetylgalactosaminyltransferase 4, protein-UDP acetylgalactosaminyltransferase 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4) and Pgant6 (also called pp-GaNTase 6, N-acetylgalactosaminyltransferase 6, protein-UDP acetylgalactosaminyltransferase 6, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6). They function as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant9 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Pgant4 and Pgant6 do not act as a peptide transferase, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. They prefer the diglycosylated Muc5AC-3/13 as a substrate. Pgant6 may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467340 [Multi-domain] Cd Length: 126 Bit Score: 40.81 E-value: 1.54e-03

                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1907074051   21 FQIVHVRKQQCLSIN---QKVVMGFCNGSSRNQQW 52
Cdd:cd23462     89 KQIVHGTSKKCLELSddsSKLVMEPCNGSSPRQQW 123

beta-trefoil_Ricin_unchar

cd23412

ricin B-type lectin domain, beta-trefoil fold, found in uncharacterized macrophage mannose ...

20-122

2.00e-03

ricin B-type lectin domain, beta-trefoil fold, found in uncharacterized macrophage mannose receptor (MRC)-like proteins; The subfamily corresponds to a group of uncharacterized ricin B-type lectin beta-trefoil domain-containing proteins from Gnathostomata. They show high sequence similarity with macrophage mannose receptor (MRC) family proteins.

Pssm-ID: 467790 Cd Length: 127 Bit Score: 40.46 E-value: 2.00e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051   20 GFQIVHVRKQQCLSINQ----KVVMGFCNGSSRNQQWLSTEDGKFL-HIKSGLCLGISNSSRgpFQPAVATPCA----QA 90
Cdd:cd23412      4 GFMIRNVQLEKCIQVDHgeseRVSLAECKPHSEHQQWSWDPETRALsSLHTGECLTVLKIQE--FGSVRLEPCGsrepQA 81

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1907074051   91 prWTChAQEGFLEVENTSLFL--KKQNHKVVVKK 122
Cdd:cd23412     82 --WSC-SKKGHLTLQGLGLHLsaRHSSHKVFVSK 112

beta-trefoil_Ricin_GALNT11

cd23440

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...

43-92

2.02e-03

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 11 (GALNT11) and similar proteins; GALNT11 (EC 2.4.1.41), also called polypeptide GalNAc transferase 11, GalNAc-T11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes its activation, modulating the balance between motile and immotile (sensory) cilia at the left-right organizer (LRO). GALNT11 displays the same enzyme activity toward MUC1, MUC4, and EA2 as GALNT1. It is not involved in glycosylation of erythropoietin (EPO). GALNT11 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467318 [Multi-domain] Cd Length: 127 Bit Score: 40.44 E-value: 2.02e-03

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907074051   43 CNGSSRNQQWLSTEDGKFLHIKSGLCLGISNSSRGpfQPAVATPCAQAPR 92
Cdd:cd23440     75 CHGSGGSQQWRFKKDNRLYNPASGQCLAASKNGTS--GYVTMDICSDSPS 122

FN3

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

665-742

2.17e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 39.13 E-value: 2.17e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051   665 PEKVRNLVSYNeIWMKSFTVNWTPPAGDWE-----HYRIVLFNESLVLLNTTVGKEETHYALDGLEliPGRQYEIEVIVE 739
Cdd:smart00060    1 PSPPSNLRVTD-VTSTSVTLSWEPPPDDGItgyivGYRVEYREEGSEWKEVNVTPSSTSYTLTGLK--PGTEYEFRVRAV 77


                    ...
gi 1907074051   740 SGN 742
Cdd:smart00060   78 NGA 80

FN3

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

1107-1182

2.22e-03

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 39.40 E-value: 2.22e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1107 PEPVKDLTLLNRSTEDLHVTWSRA---NGDVDQYEVQL-LFNDMKVFPHIHLVNTATEYKFTALTPGRHYKILVLTISGD 1182
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPeddGGPITGYVVEYrEKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

FN3

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

1461-1553

2.45e-03

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 39.40 E-value: 2.45e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1461 PAAVNHLKGSHrNTTDSLWFSWSPASGD---FDFYELILYNPNGTKKENWKEKDV--TEWRFQGLVPGRKYTLYVVThsg 1535
Cdd:cd00063      1 PSPPTNLRVTD-VTSTSVTLSWTPPEDDggpITGYVVEYREKGSGDWKEVEVTPGseTSYTLTGLKPGTEYEFRVRA--- 76

                           90
                   ....*....|....*...
gi 1907074051 1536 dlsnkVTGEGRTAPSPPS 1553
Cdd:cd00063     77 -----VNGGGESPPSESV 89

FN3

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

1461-1535

2.72e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 38.75 E-value: 2.72e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  1461 PAAVNHLKGSHrNTTDSLWFSWSPASGDFDFYELILYNP-NGTKKENWKEKDV----TEWRFQGLVPGRKYTLYVVTHSG 1535
Cdd:smart00060    1 PSPPSNLRVTD-VTSTSVTLSWEPPPDDGITGYIVGYRVeYREEGSEWKEVNVtpssTSYTLTGLKPGTEYEFRVRAVNG 79

beta-trefoil_Ricin_Pgant3-like

cd23460

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...

22-69

3.20e-03

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 3 (Pgant3) and similar proteins; Pgant3, also called pp-GaNTase 3, protein-UDP acetylgalactosaminyltransferase 3, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, functions as a GalNAc transferase (EC 2.4.1.41) that catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant3 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers EA2 as a substrate and has weak activity toward Muc5AC-3, -13 and -3/13 substrates. Pgant3 plays a critical role in the regulation of integrin-mediated cell adhesion during wing development by influencing, via glycosylation, the secretion and localization of the integrin ligand Tig to the basal cell layer interface. It may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Together with Pgant35A, Pgant3 regulates integrin levels and activity-dependent integrin signaling at the synapse in neurons and muscles. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467338 [Multi-domain] Cd Length: 121 Bit Score: 39.73 E-value: 3.20e-03

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907074051   22 QIVHVRkqQCLSINQ--KVVMGFCNGSSRNQQWLSTEDGK-FLHIKSGLCL 69
Cdd:cd23460     47 QIRQDH--LCLTADEgnKVTLRECADQLPSQEWSYDEKTGtIRHRSTGLCL 95

beta-trefoil_Ricin_Pgant9-like

cd23462

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...

31-87

3.87e-03

Pssm-ID: 467340 [Multi-domain] Cd Length: 126 Bit Score: 39.66 E-value: 3.87e-03

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907074051   31 CLSIN---QKVVMGFCNGSSRNQQWL-STEDGKFLHIKSGLCLGISNSSRGPfqpaVATPC 87
Cdd:cd23462     58 CLDYAggsGDVTLYPCHGMKGNQFWIyDEETKQIVHGTSKKCLELSDDSSKL----VMEPC 114

FN3

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

931-1006

4.19e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 38.36 E-value: 4.19e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051   931 PSSVSGVTVNNSGRNdYLSVSWLPAP-----GEVDHYVVSLSHEGKVDQFLIIAKSVSECSFSSLTPGRLYNVTVTTKSG 1005
Cdd:smart00060    1 PSPPSNLRVTDVTST-SVTLSWEPPPddgitGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    .
gi 1907074051  1006 N 1006
Cdd:smart00060   80 A 80

beta-trefoil_Ricin_GALNT2

cd23434

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...

31-75

4.23e-03

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 2 (GALNT2) and similar proteins; GALNT2 (EC 2.4.1.41), also called polypeptide GalNAc transferase 2, GalNAc-T2, pp-GaNTase 2, protein-UDP acetylgalactosaminyltransferase 2, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT2 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. It is probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region. It is also involved in O-linked glycosylation of APOC-III, ANGPTL3 and PLTP. It participates in the regulation of HDL-C metabolism. GALNT2 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467312 [Multi-domain] Cd Length: 121 Bit Score: 39.23 E-value: 4.23e-03

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907074051   31 CLSI-----NQKVVMGFCNGSSRNQQWLSTEDGKFL-HIKSGLCLGISNSS 75
Cdd:cd23434     51 CLTVvdrapGSLVTLQPCREDDSNQKWEQIENNSKLrHVGSNLCLDSRNAK 101

beta-trefoil_Ricin_GALNT7

cd23437

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...

22-52

5.22e-03

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 7 (GALNT7) and similar proteins; GALNT7 (EC 2.4.1.41), also called polypeptide GalNAc transferase 7, GalNAc-T7, pp-GaNTase 7, protein-UDP acetylgalactosaminyltransferase 7, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7, acts as glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Its appropriate peptide substrate remains unidentified. GALNT7 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467315 [Multi-domain] Cd Length: 124 Bit Score: 39.20 E-value: 5.22e-03

                           10        20        30
                   ....*....|....*....|....*....|....
gi 1907074051   22 QIVHVRKQQCLSIN---QKVVMGFCNGSSRNQQW 52
Cdd:cd23437     87 QIRHKGTGKCLDLNegtNKLILQPCDSSSPSQKW 120

FN3

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

1283-1368

5.29e-03

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 38.25 E-value: 5.29e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051 1283 PASVQGVVAANAySSNSLTVSWQKAL---GVAERYDILLLNENGLLLSNV-SEPATARQHKFEDLTPGKKYKMQILTVSG 1358
Cdd:cd00063      1 PSPPTNLRVTDV-TSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                           90
                   ....*....|
gi 1907074051 1359 GLFSKESQAE 1368
Cdd:cd00063     80 GGESPPSESV 89

beta-trefoil_Ricin_MRC2

cd23408

ricin B-type lectin domain, beta-trefoil fold, found in macrophage mannose receptor 2 (MRC2) ...

21-118

5.40e-03

ricin B-type lectin domain, beta-trefoil fold, found in macrophage mannose receptor 2 (MRC2) and similar proteins; MRC2, also called C-type mannose receptor 2, C-type lectin domain family 13 member E (CLEC13E), endocytic receptor 180 (Endo180), urokinase-type plasminogen activator receptor-associated protein (UPARAP), UPAR-associated protein, urokinase receptor-associated protein, or CD280, may play a role as endocytotic lectin receptor displaying calcium-dependent lectin activity. It internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. It may be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. It may contribute to cellular uptake, remodeling, and degradation of extracellular collagen matrices. It may play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. It may participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). MRC2 contains an atypical ricin B-type lectin domain at the N-terminus. The typical ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. In contrast, the ninth, tenth and eleventh beta strands, comprising the gamma subdomain, are missing in the ricin B-type lectin domain of MRC2.

Pssm-ID: 467786 Cd Length: 124 Bit Score: 39.00 E-value: 5.40e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051   21 FQIVHVRKQQCLSINQKVV--MGFCNGSSRNQQWLSTEDGKFLHIKSGLCLGISNSSRGPFQPAVAT-PCAQAP---RWT 94
Cdd:cd23408      3 FLIYSDGAQGCLEVRDSVVrlSPACNTSSPAQQWKWVSRNRLFNLGSMQCLGVSGPNGSGTSATLGTyECDRESvnmRWH 82

                           90       100
                   ....*....|....*....|....
gi 1907074051   95 ChaqEGFLEVENTSLFLKKQNHKV 118
Cdd:cd23408     83 C---RTLGEQLSQHLGARTANGNP 103

FN3

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

1019-1094

5.68e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 37.98 E-value: 5.68e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  1019 PDKVQGISVSNSArSDYLKVSWVHATGD-FDHYEV--TIKNRESFIQTKTIPKSENECEFI--ELVPGRLYSVTVSTKSG 1093
Cdd:smart00060    1 PSPPSNLRVTDVT-STSVTLSWEPPPDDgITGYIVgyRVEYREEGSEWKEVNVTPSSTSYTltGLKPGTEYEFRVRAVNG 79


                    .
gi 1907074051  1094 Q 1094
Cdd:smart00060   80 A 80

FN3

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

665-742

6.25e-03

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 38.25 E-value: 6.25e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  665 PEKVRNLvSYNEIWMKSFTVNWTPPAGD---WEHYRIVLF--NESLVLLNTTVGKEETHYALDGLEliPGRQYEIEVIVE 739
Cdd:cd00063      1 PSPPTNL-RVTDVTSTSVTLSWTPPEDDggpITGYVVEYRekGSGDWKEVEVTPGSETSYTLTGLK--PGTEYEFRVRAV 77


                   ...
gi 1907074051  740 SGN 742
Cdd:cd00063     78 NGG 80

FN3

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

1195-1269

7.12e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 37.59 E-value: 7.12e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074051  1195 PSTVKNIHISANGATdRLMVTWSP-----GGGDVDSYVVSAFRQDEKVDSQTIPKHASEHTFHRLEAGAKYRIAIVSVSG 1269
Cdd:smart00060    1 PSPPSNLRVTDVTST-SVTLSWEPppddgITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

FN3