NCBI Conserved Domain Search

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

583-671

8.44e-14

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: 68.68 E-value: 8.44e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  583 PNPPRNMTIETVRSNSVLVHWSPPES--GEFTEYSIRYRTDSEQQWVRL--PSVRSTEADITDMTKGEKYTIQVNTVSFG 658
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDdgGPITGYVVEYREKGSGDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|...
gi 442615984  659 VESPVPQEVNTTV 671
Cdd:cd00063    81 GESPPSESVTVTT 93

FN3 super family

cl27307

Fibronectin type 3 domain [General function prediction only];

278-734

5.14e-11

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: 67.72 E-value: 5.14e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  278 AFKGLVPGRAYNISVQTMSEDEISLPTTAQYRTVPLRPLNVTFDRDFITSNSFRVLW-EAPKGISEFDKYQVSVATTRRQ 356
Cdd:COG3401     9 LDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGgLGTGGRAGTTSGVAAVAVAAAP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  357 STVPRSNEPVAFFDFRDIAEPGKTFNVIVKTVSGkvtSWPATGDVTLRPLPVRNLRSINDDKTNTMIITWEADPASTQdE 436
Cdd:COG3401    89 PTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAV---GTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSV-A 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  437 YRIVYHELETFNGDTSTLTTDRTRFTLES-----LLPGRNYSLSVQAVSKKMESNETSIFVVTR----PSSPiiEDLKSI 507
Cdd:COG3401   165 GAGVVVSPDTSATAAVATTSLTVTSTTLVdgggdIEPGTTYYYRVAATDTGGESAPSNEVSVTTpttpPSAP--TGLTAT 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  508 RMGLN---ISWKSDVNSKQEQYEVLYSRNGTSDLRT-QKTKESRLVIKNLQPGAGYELKVFAVSHD-LRSEPHAYFQAV- 581
Cdd:COG3401   243 ADTPGsvtLSWDPVTESDATGYRVYRSNSGDGPFTKvATVTTTSYTDTGLTNGTTYYYRVTAVDAAgNESAPSNVVSVTt 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  582 ---YPNPPRNMTIETVRSNSVLVHWSPPESGEFTEYSIRYRTDSEQQWVRL-PSVRSTEADITDMTKGEKYTIQVNTV-S 656
Cdd:COG3401   323 dltPPAAPSGLTATAVGSSSITLSWTASSDADVTGYNVYRSTSGGGTYTKIaETVTTTSYTDTGLTPGTTYYYKVTAVdA 402

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442615984  657 FGVESPVPQEVNTTVPPNPVSNIIQLVdsrniTLEWPKPEGRVESYILKWWPSDNPGRVQTKNVSENKSADDLSTVRV 734
Cdd:COG3401   403 AGNESAPSEEVSATTASAASGESLTAS-----VDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSS 475

PTP_tm super family

cl40142

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

1083-1187

7.29e-11

TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases (PTPs) are known to be signaling molecules that regulate a variety of cellular processes, including cell growth, differentiation, mitotic cycle, and oncogenic transformation. PTP receptor type J possesses an extracellular region containing five fibronectin type III repeats, the transmembrane region included in this Pfam entry, and a intracytoplasmic catalytic domain. This entry probably contains part of a Fn3 domain at the N-terminus.

The actual alignment was detected with superfamily member pfam18861:

Pssm-ID: 465889 Cd Length: 126 Bit Score: 61.47 E-value: 7.29e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  1083 FSDQNGQVRMYTIIVAEDDAKNASGLEMPSwldvQSYSVWLpYQAIDPY--YPFENRSVE--------DFTIGTENCDNh 1152
Cdd:pfam18861    6 FNSSNGPIKAYGVIVTTNDSLNRPLKEYLN----KTYYDWK-YKKTDSYlaTVTPNPFTSprsssrslTVPVGTGSKWQ- 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 442615984  1153 kiGYCNGPLKSGTTYRVKVRAFT------GADKFTDTAYSF 1187
Cdd:pfam18861   80 --GYCNGPLKPLGSYRFSVAAFTrlefddGLIDGEESYVSF 118

fn3

Fibronectin type III domain;

959-1043

7.84e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 57.04 E-value: 7.84e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984   959 GRVERFHPTDVQPSEINFEWSlPSSEANGVIRQFSIAYTNINNLTDAGMQDFESEEAFGVIKNLKPGETYVFKIQAKTAI 1038
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWT-PPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*
gi 442615984  1039 GFGPE 1043
Cdd:pfam00041   80 GEGPP 84

fn3

Fibronectin type III domain;

866-935

2.14e-09

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 55.88 E-value: 2.14e-09

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442615984   866 PITQLHATNITDTEISLRWDLPK---GEYNDFDIAYLTADNLLAQNMTT----RNEITISDLRPHRNYTFTVVVRSG 935
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITvpgtTTSVTLTGLKPGTEYEVRVQAVNG 78

fn3

Fibronectin type III domain;

220-304

6.27e-09

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 54.73 E-value: 6.27e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984   220 PGKFIVWFRNETTLLVLWQPP-YPAGIYTHYKVSIEPPDANDSVLYVEkegEPPGPAQAAFKGLVPGRAYNISVQTMSED 298
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPpDGNGPITGYEVEYRPKNSGEPWNEIT---VPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*.
gi 442615984   299 EISLPT 304
Cdd:pfam00041   80 GEGPPS 85

fn3

Fibronectin type III domain;

124-205

6.04e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 52.03 E-value: 6.04e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984   124 DPPSNLSVQVRSGKNAIILWSPPTQGS--YTAFKIKVLGLSEasSSYNRTFQVNDNTFQHSVKELTPGATYQVQAYTIYD 201
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNgpITGYEVEYRPKNS--GEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78


                   ....
gi 442615984   202 GKES 205
Cdd:pfam00041   79 GGEG 82

fn3

Fibronectin type III domain;

787-850

3.30e-04

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 41.25 E-value: 3.30e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442615984   787 DTITLSYTPTPQSSSKFDIYR--FSLGDAEIRDKEKLANDTDRKVTFTGLVPGRLYNITVWTVSGG 850
Cdd:pfam00041   14 TSLTVSWTPPPDGNGPITGYEveYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

Name

Accession

Description

Interval

E-value

R3-PTPc

cd14548

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

1301-1522

9.71e-148

Pssm-ID: 350396 [Multi-domain] Cd Length: 222 Bit Score: 455.28 E-value: 9.71e-148

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1301 RFTNILPYDHSRFKLQPVDDDEGSDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREK 1380
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1381 CDQYWPNDTVPVFYGDIKVQILNDSHYADWVMTEFMLCRGSEQRILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAE 1460
Cdd:cd14548    81 CDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIKQE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442615984 1461 QRPIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQ 1522
Cdd:cd14548   161 KGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

1272-1525

9.93e-115

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 364.29 E-value: 9.93e-115

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984   1272 FSEEFEELKHVGR-DQPCTFADLPCNRPKNRFTNILPYDHSRFKLQPvDDDEGSDYINANYVPGHNSPREFIVTQGPLHS 1350
Cdd:smart00194    2 LEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKP-PPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984   1351 TRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDTV-PVFYGDIKVQILNDSHYADWVMTEFMLCRG--SEQRILR 1427
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGePLTYGDITVTLKSVEKVDDYTIRTLEVTNTgcSETRTVT 160

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984   1428 HFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAEQRPIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKER 1507
Cdd:smart00194  161 HYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQR 240

                           250
                    ....*....|....*...
gi 442615984   1508 VWMVQTEQQYICIHQCLL 1525
Cdd:smart00194  241 PGMVQTEEQYIFLYRAIL 258

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

1296-1525

2.88e-101

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 324.58 E-value: 2.88e-101

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  1296 NRPKNRFTNILPYDHSRFKLQPVDDDegSDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFE 1375
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  1376 KGREKCDQYWPNDT-VPVFYGDIKVQILN-DSHYADWVMTEFMLCRG--SEQRILRHFHFTTWPDFGVPNPPQTLVRFVR 1451
Cdd:pfam00102   79 KGREKCAQYWPEEEgESLEYGDFTVTLKKeKEDEKDYTVRTLEVSNGgsEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442615984  1452 AFRD-RIGAEQRPIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLL 1525
Cdd:pfam00102  159 KVRKsSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233

PHA02742

protein tyrosine phosphatase; Provisional

1296-1529

7.05e-45

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 165.56 E-value: 7.05e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1296 NRPKNRFTNILPYDHSRFKLQPvdDDEGSDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFE 1375
Cdd:PHA02742   52 NMKKCRYPDAPCFDRNRVILKI--EDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1376 KGREKCDQYW-PNDTVPVFYGDIKVQILNDSHYADWVMTEFMLCRGSEQRIL--RHFHFTTWPDFGVPNPPQTLVRFVRA 1452
Cdd:PHA02742  130 DGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLdiKHFAYEDWPHGGLPRDPNKFLDFVLA 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1453 FRDR-------IGAEQR----PIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICih 1521
Cdd:PHA02742  210 VREAdlkadvdIKGENIvkepPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF-- 287


                  ....*...
gi 442615984 1522 qCLLAVLE 1529
Cdd:PHA02742  288 -CYFIVLI 294

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

1246-1520

2.40e-37

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 142.92 E-value: 2.40e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1246 IEQNRPILIKNFAEHYRLmsadsdfRFSEEFEELKHVGRDQpcTFADLPCNRPKNRFTNILPYDHSRfkLQPVDDdegsd 1325
Cdd:COG5599     1 VSPKNPIAIKSEEEKINS-------RLSTLTNELAPSHNDP--QYLQNINGSPLNRFRDIQPYKETA--LRANLG----- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYVPGHNsPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFE--KGREKCDQYWPNDTVpvfYGDIKVQILN 1403
Cdd:COG5599    65 YLNANYIQVIG-NHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEisKPKVKMPVYFRQDGE---YGKYEVSSEL 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1404 DSHYAdwVMTEFML------CRGS--EQRILRHFHFTTWPDFGVPNPPQTLvrfvrAFRDRIGAEQR-------PIVVHC 1468
Cdd:COG5599   141 TESIQ--LRDGIEArtyvltIKGTgqKKIEIPVLHVKNWPDHGAISAEALK-----NLADLIDKKEKikdpdklLPVVHC 213

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442615984 1469 SAGVGRSGTFITLDRILQQINT--SDYVDIFGIVYAMRKERVW-MVQTEQQYICI 1520
Cdd:COG5599   214 RAGVGRTGTLIACLALSKSINAlvQITLSVEEIVIDMRTSRNGgMVQTSEQLDVL 268

FN3

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

583-671

8.44e-14

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 68.68 E-value: 8.44e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  583 PNPPRNMTIETVRSNSVLVHWSPPES--GEFTEYSIRYRTDSEQQWVRL--PSVRSTEADITDMTKGEKYTIQVNTVSFG 658
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDdgGPITGYVVEYREKGSGDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|...
gi 442615984  659 VESPVPQEVNTTV 671
Cdd:cd00063    81 GESPPSESVTVTT 93

FN3

Fibronectin type 3 domain [General function prediction only];

552-704

8.57e-14

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 76.58 E-value: 8.57e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  552 NLQPGAGYELKVFAVSHDLRSEPHAYFQAVY----PNPPRNMTIETVRSNSVLVHWSPPESGEFTEYSIRYRTDSEQQWV 627
Cdd:COG3401   198 DIEPGTTYYYRVAATDTGGESAPSNEVSVTTpttpPSAPTGLTATADTPGSVTLSWDPVTESDATGYRVYRSNSGDGPFT 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  628 RLPSVRSTEADITDMTKGEKYTIQVNTV-SFGVESPVPQEVNTTV---PPNPVSNI-IQLVDSRNITLEW-PKPEGRVES 701
Cdd:COG3401   278 KVATVTTTSYTDTGLTNGTTYYYRVTAVdAAGNESAPSNVVSVTTdltPPAAPSGLtATAVGSSSITLSWtASSDADVTG 357


                  ...
gi 442615984  702 YIL 704
Cdd:COG3401   358 YNV 360

fn3

Fibronectin type III domain;

585-662

8.90e-13

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 65.51 E-value: 8.90e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984   585 PPRNMTIETVRSNSVLVHWSPPE--SGEFTEYSIRYRT-DSEQQWVRLPSVRST-EADITDMTKGEKYTIQVNTVSFGVE 660
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgNGPITGYEVEYRPkNSGEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ..
gi 442615984   661 SP 662
Cdd:pfam00041   82 GP 83

FN3

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

583-661

4.54e-11

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: 60.71 E-value: 4.54e-11

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984    583 PNPPRNMTIETVRSNSVLVHWSPPESGEFTEYSIRYR---TDSEQQWVRLP-SVRSTEADITDMTKGEKYTIQVNTVSFG 658
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRveyREEGSEWKEVNvTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 442615984    659 VES 661
Cdd:smart00060   81 GEG 83

FN3

Fibronectin type 3 domain [General function prediction only];

278-734

5.14e-11

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 67.72 E-value: 5.14e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  278 AFKGLVPGRAYNISVQTMSEDEISLPTTAQYRTVPLRPLNVTFDRDFITSNSFRVLW-EAPKGISEFDKYQVSVATTRRQ 356
Cdd:COG3401     9 LDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGgLGTGGRAGTTSGVAAVAVAAAP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  357 STVPRSNEPVAFFDFRDIAEPGKTFNVIVKTVSGkvtSWPATGDVTLRPLPVRNLRSINDDKTNTMIITWEADPASTQdE 436
Cdd:COG3401    89 PTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAV---GTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSV-A 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  437 YRIVYHELETFNGDTSTLTTDRTRFTLES-----LLPGRNYSLSVQAVSKKMESNETSIFVVTR----PSSPiiEDLKSI 507
Cdd:COG3401   165 GAGVVVSPDTSATAAVATTSLTVTSTTLVdgggdIEPGTTYYYRVAATDTGGESAPSNEVSVTTpttpPSAP--TGLTAT 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  508 RMGLN---ISWKSDVNSKQEQYEVLYSRNGTSDLRT-QKTKESRLVIKNLQPGAGYELKVFAVSHD-LRSEPHAYFQAV- 581
Cdd:COG3401   243 ADTPGsvtLSWDPVTESDATGYRVYRSNSGDGPFTKvATVTTTSYTDTGLTNGTTYYYRVTAVDAAgNESAPSNVVSVTt 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  582 ---YPNPPRNMTIETVRSNSVLVHWSPPESGEFTEYSIRYRTDSEQQWVRL-PSVRSTEADITDMTKGEKYTIQVNTV-S 656
Cdd:COG3401   323 dltPPAAPSGLTATAVGSSSITLSWTASSDADVTGYNVYRSTSGGGTYTKIaETVTTTSYTDTGLTPGTTYYYKVTAVdA 402

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442615984  657 FGVESPVPQEVNTTVPPNPVSNIIQLVdsrniTLEWPKPEGRVESYILKWWPSDNPGRVQTKNVSENKSADDLSTVRV 734
Cdd:COG3401   403 AGNESAPSEEVSATTASAASGESLTAS-----VDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSS 475

PTP_tm

pfam18861

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

1083-1187

7.29e-11

Pssm-ID: 465889 Cd Length: 126 Bit Score: 61.47 E-value: 7.29e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  1083 FSDQNGQVRMYTIIVAEDDAKNASGLEMPSwldvQSYSVWLpYQAIDPY--YPFENRSVE--------DFTIGTENCDNh 1152
Cdd:pfam18861    6 FNSSNGPIKAYGVIVTTNDSLNRPLKEYLN----KTYYDWK-YKKTDSYlaTVTPNPFTSprsssrslTVPVGTGSKWQ- 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 442615984  1153 kiGYCNGPLKSGTTYRVKVRAFT------GADKFTDTAYSF 1187
Cdd:pfam18861   80 --GYCNGPLKPLGSYRFSVAAFTrlefddGLIDGEESYVSF 118

fn3

Fibronectin type III domain;

959-1043

7.84e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 57.04 E-value: 7.84e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984   959 GRVERFHPTDVQPSEINFEWSlPSSEANGVIRQFSIAYTNINNLTDAGMQDFESEEAFGVIKNLKPGETYVFKIQAKTAI 1038
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWT-PPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*
gi 442615984  1039 GFGPE 1043
Cdd:pfam00041   80 GEGPP 84

fn3

Fibronectin type III domain;

866-935

2.14e-09

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 55.88 E-value: 2.14e-09

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442615984   866 PITQLHATNITDTEISLRWDLPK---GEYNDFDIAYLTADNLLAQNMTT----RNEITISDLRPHRNYTFTVVVRSG 935
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITvpgtTTSVTLTGLKPGTEYEVRVQAVNG 78

fn3

Fibronectin type III domain;

220-304

6.27e-09

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 54.73 E-value: 6.27e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984   220 PGKFIVWFRNETTLLVLWQPP-YPAGIYTHYKVSIEPPDANDSVLYVEkegEPPGPAQAAFKGLVPGRAYNISVQTMSED 298
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPpDGNGPITGYEVEYRPKNSGEPWNEIT---VPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*.
gi 442615984   299 EISLPT 304
Cdd:pfam00041   80 GEGPPS 85

FN3

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

405-494

1.97e-08

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 53.65 E-value: 1.97e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  405 PLPVRNLRsINDDKTNTMIITWEA--DPASTQDEYRIVYHELETFNGDT-STLTTDRTRFTLESLLPGRNYSLSVQAVSK 481
Cdd:cd00063     1 PSPPTNLR-VTDVTSTSVTLSWTPpeDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                          90
                  ....*....|...
gi 442615984  482 KMESNETSIFVVT 494
Cdd:cd00063    80 GGESPPSESVTVT 92

fn3

Fibronectin type III domain;

407-488

4.17e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 52.42 E-value: 4.17e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984   407 PVRNLRsINDDKTNTMIITWEA--DPASTQDEYRIVYHELETFNGDTS-TLTTDRTRFTLESLLPGRNYSLSVQAVSKKM 483
Cdd:pfam00041    2 APSNLT-VTDVTSTSLTVSWTPppDGNGPITGYEVEYRPKNSGEPWNEiTVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 442615984   484 ESNET 488
Cdd:pfam00041   81 EGPPS 85

fn3

Fibronectin type III domain;

124-205

6.04e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 52.03 E-value: 6.04e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984   124 DPPSNLSVQVRSGKNAIILWSPPTQGS--YTAFKIKVLGLSEasSSYNRTFQVNDNTFQHSVKELTPGATYQVQAYTIYD 201
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNgpITGYEVEYRPKNS--GEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78


                   ....
gi 442615984   202 GKES 205
Cdd:pfam00041   79 GGEG 82

FN3

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

405-485

1.26e-07

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 51.08 E-value: 1.26e-07

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984    405 PLPVRNLRSINDDKTnTMIITWEADPASTQDEYRIVYHELETFNGD---TSTLTTDRTRFTLESLLPGRNYSLSVQAVSK 481
Cdd:smart00060    1 PSPPSNLRVTDVTST-SVTLSWEPPPDDGITGYIVGYRVEYREEGSewkEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 442615984    482 KMES 485
Cdd:smart00060   80 AGEG 83

FN3

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

864-939

6.60e-07

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 49.03 E-value: 6.60e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  864 PEPITQLHATNITDTEISLRWDLPKGEYNDFD---IAYLTADNLLAQNMT----TRNEITISDLRPHRNYTFTVVVRSGT 936
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITgyvVEYREKGSGDWKEVEvtpgSETSYTLTGLKPGTEYEFRVRAVNGG 80


                  ...
gi 442615984  937 ESS 939
Cdd:cd00063    81 GES 83

FN3

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

123-205

7.05e-07

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 48.76 E-value: 7.05e-07

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984    123 PDPPSNLSVQVRSGKNAIILWSPPTQGSYTAFKIKVLGLSEASSSYNRTFQVNDNTFQHSVKELTPGATYQVQAYTIYDG 202
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 442615984    203 KES 205
Cdd:smart00060   81 GEG 83

FN3

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

958-1042

1.34e-06

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 48.26 E-value: 1.34e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  958 PGRVERFHPTDVQPSEINFEWSLPSSEaNGVIRQFSIAYTNINNLTDAGMQDFESEEAFGVIKNLKPGETYVFKIQAKTA 1037
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDD-GGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79


                  ....*
gi 442615984 1038 IGFGP 1042
Cdd:cd00063    80 GGESP 84

FN3

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

123-215

2.05e-06

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 47.88 E-value: 2.05e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  123 PDPPSNLSVQVRSGKNAIILWSPP--TQGSYTAFKIKVLGLSEASSSYNRTFQVNDNTFQhsVKELTPGATYQVQAYTIY 200
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPedDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYT--LTGLKPGTEYEFRVRAVN 78

                          90
                  ....*....|....*
gi 442615984  201 DGKESVAYTSRNFTT 215
Cdd:cd00063    79 GGGESPPSESVTVTT 93

FN3

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

864-939

3.12e-06

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 46.84 E-value: 3.12e-06

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984    864 PEPITQLHATNITDTEISLRWDLPKGEYNDFDIAYLT-------ADNLLAQNMTTRNEITISDLRPHRNYTFTVVVRSGT 936
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRveyreegSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 442615984    937 ESS 939
Cdd:smart00060   81 GEG 83

FN3

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

217-305

6.60e-06

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 46.34 E-value: 6.60e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  217 PNTPGKFIVWFRNETTLLVLWQPP-YPAGIYTHYKVSIEPPDANDSVLYVEKEGEPPgpaQAAFKGLVPGRAYNISVQTM 295
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPeDDGGPITGYVVEYREKGSGDWKEVEVTPGSET---SYTLTGLKPGTEYEFRVRAV 77

                          90
                  ....*....|
gi 442615984  296 SEDEISLPTT 305
Cdd:cd00063    78 NGGGESPPSE 87

FN3

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

958-1041

3.82e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 43.76 E-value: 3.82e-05

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984    958 PGRVERFHPTDVQPSEINFEWSLPSSE-ANGVIRQFSIAYTNINNLTDAGMQDFESEEAfgVIKNLKPGETYVFKIQAKT 1036
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDgITGYIVGYRVEYREEGSEWKEVNVTPSSTSY--TLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 442615984   1037 AIGFG 1041
Cdd:smart00060   79 GAGEG 83

fn3

Fibronectin type III domain;

787-850

3.30e-04

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 41.25 E-value: 3.30e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442615984   787 DTITLSYTPTPQSSSKFDIYR--FSLGDAEIRDKEKLANDTDRKVTFTGLVPGRLYNITVWTVSGG 850
Cdd:pfam00041   14 TSLTVSWTPPPDGNGPITGYEveYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

FN3

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

217-301

1.28e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 39.52 E-value: 1.28e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984    217 PNTPGKFIVWFRNETTLLVLWQPPYPAGIyTHYKVSIEPPDANDSVLYVEKEGEPPGPaQAAFKGLVPGRAYNISVQTMS 296
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGI-TGYIVGYRVEYREEGSEWKEVNVTPSST-SYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 442615984    297 EDEIS 301
Cdd:smart00060   79 GAGEG 83

FN3

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

782-857

2.54e-03

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 39.02 E-value: 2.54e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442615984  782 KEDERDTITLSYTPTPQSSSKFDIYRFSLGDAEIRDKEKLAND--TDRKVTFTGLVPGRLYNITVWTVSGGVASLPIQ 857
Cdd:cd00063    10 TDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTpgSETSYTLTGLKPGTEYEFRVRAVNGGGESPPSE 87

FN3

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

786-850

4.72e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 37.98 E-value: 4.72e-03

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442615984    786 RDTITLSYTPTPQSSSKFDIYRFSLGDAEIRDKEKLAN--DTDRKVTFTGLVPGRLYNITVWTVSGG 850
Cdd:smart00060   14 STSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNvtPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

Name

Accession

Description

Interval

E-value

R3-PTPc

cd14548

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

1301-1522

9.71e-148

Pssm-ID: 350396 [Multi-domain] Cd Length: 222 Bit Score: 455.28 E-value: 9.71e-148

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1301 RFTNILPYDHSRFKLQPVDDDEGSDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREK 1380
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1381 CDQYWPNDTVPVFYGDIKVQILNDSHYADWVMTEFMLCRGSEQRILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAE 1460
Cdd:cd14548    81 CDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIKQE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442615984 1461 QRPIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQ 1522
Cdd:cd14548   161 KGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

1272-1525

9.93e-115

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 364.29 E-value: 9.93e-115

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984   1272 FSEEFEELKHVGR-DQPCTFADLPCNRPKNRFTNILPYDHSRFKLQPvDDDEGSDYINANYVPGHNSPREFIVTQGPLHS 1350
Cdd:smart00194    2 LEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKP-PPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984   1351 TRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDTV-PVFYGDIKVQILNDSHYADWVMTEFMLCRG--SEQRILR 1427
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGePLTYGDITVTLKSVEKVDDYTIRTLEVTNTgcSETRTVT 160

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984   1428 HFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAEQRPIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKER 1507
Cdd:smart00194  161 HYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQR 240

                           250
                    ....*....|....*...
gi 442615984   1508 VWMVQTEQQYICIHQCLL 1525
Cdd:smart00194  241 PGMVQTEEQYIFLYRAIL 258

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

1296-1525

2.88e-101

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 324.58 E-value: 2.88e-101

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  1296 NRPKNRFTNILPYDHSRFKLQPVDDDegSDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFE 1375
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  1376 KGREKCDQYWPNDT-VPVFYGDIKVQILN-DSHYADWVMTEFMLCRG--SEQRILRHFHFTTWPDFGVPNPPQTLVRFVR 1451
Cdd:pfam00102   79 KGREKCAQYWPEEEgESLEYGDFTVTLKKeKEDEKDYTVRTLEVSNGgsEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442615984  1452 AFRD-RIGAEQRPIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLL 1525
Cdd:pfam00102  159 KVRKsSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233

R-PTPc-O

cd14614

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

1285-1525

5.89e-99

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: 318.76 E-value: 5.89e-99

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1285 DQPCTFADLPCNRPKNRFTNILPYDHSRFKLQPVDDDEGSDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNS 1364
Cdd:cd14614     1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1365 RAIVMLTRCFEKGREKCDQYWPNDTVPVFYGDIKVQILNDSHYADWVMTEFMLCRGSEQRILRHFHFTTWPDFGVP--NP 1442
Cdd:cd14614    81 QIIVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPtaNA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1443 PQTLVRFVRAFRDRIGAEQRPIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQ 1522
Cdd:cd14614   161 AESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240


                  ...
gi 442615984 1523 CLL 1525
Cdd:cd14614   241 CVQ 243

R-PTPc-B

cd14617

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

1300-1522

1.06e-97

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.

Pssm-ID: 350465 [Multi-domain] Cd Length: 228 Bit Score: 314.16 E-value: 1.06e-97

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1300 NRFTNILPYDHSRFKLQPVDDDEGSDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGRE 1379
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1380 KCDQYWPNDTVPVFYGDIKVQILNDSHYADWVMTEFMLCrGSEQ----RILRHFHFTTWPDFGVPNPPQTLVRFVRAFRD 1455
Cdd:cd14617    81 KCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKIC-SEEQldapRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442615984 1456 RIG--AEQRPIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQ 1522
Cdd:cd14617   160 YINrtPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228

R-PTPc-LAR-1

cd14553

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

1294-1525

7.84e-93

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: 300.85 E-value: 7.84e-93

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1294 PCNRPKNRFTNILPYDHSRFKLQPVDDDEGSDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRC 1373
Cdd:cd14553     1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1374 FEKGREKCDQYWPNDTVPVfYGDIKVQILNDSHYADWVMTEFMLCRG--SEQRILRHFHFTTWPDFGVPNPPQTLVRFVR 1451
Cdd:cd14553    81 EERSRVKCDQYWPTRGTET-YGLIQVTLLDTVELATYTVRTFALHKNgsSEKREVRQFQFTAWPDHGVPEHPTPFLAFLR 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442615984 1452 AFRDRIGAEQRPIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLL 1525
Cdd:cd14553   160 RVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALL 233

R-PTPc-H

cd14619

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

1300-1528

6.66e-88

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: 286.40 E-value: 6.66e-88

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1300 NRFTNILPYDHSRFKLQPVDDDEGSDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGRE 1379
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1380 KCDQYWPNDTVPVFYGDIKVQILNDSHYADWVMTEFMLCRGSEQ--RILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRI 1457
Cdd:cd14619    81 KCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQktLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQWL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442615984 1458 GA--EQRPIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLLAVL 1528
Cdd:cd14619   161 DQtmSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233

PTPc

cd00047

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

1326-1522

3.38e-87

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: 283.02 E-value: 3.38e-87

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDT-VPVFYGDIKVQILND 1404
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGgKPLEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1405 SHYADWVMTEFMLCRG--SEQRILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAEQRPIVVHCSAGVGRSGTFITLD 1482
Cdd:cd00047    81 EELSDYTIRTLELSPKgcSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAID 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 442615984 1483 RILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQ 1522
Cdd:cd00047   161 ILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200

R-PTPc-J

cd14615

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

1300-1525

9.68e-86

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: 280.16 E-value: 9.68e-86

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1300 NRFTNILPYDHSRFKLQpVDDDEGSDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGRE 1379
Cdd:cd14615     1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1380 KCDQYWPNDTvPVFYGDIKVQILNDSHYADWVMTEFML--CRGSEQRILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRI 1457
Cdd:cd14615    80 KCEEYWPSKQ-KKDYGDITVTMTSEIVLPEWTIRDFTVknAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYM 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1458 GAEQR--PIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLL 1525
Cdd:cd14615   159 KQNPPnsPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCAL 228

R-PTPc-V

cd14618

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

1300-1525

1.45e-85

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: 279.52 E-value: 1.45e-85

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1300 NRFTNILPYDHSRFKLQPVDDDEGSDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGRE 1379
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1380 KCDQYWPNDTVPVFYGDIKVQILNDSHYADWVMTEFMLCRGSE--QRILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRI 1457
Cdd:cd14618    81 LCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLrkERRVKHLHYTAWPDHGIPESTSSLMAFRELVREHV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1458 GAEQR--PIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLL 1525
Cdd:cd14618   161 QATKGkgPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230

R-PTPc-Q

cd14616

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

1300-1522

7.89e-79

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: 259.84 E-value: 7.89e-79

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1300 NRFTNILPYDHSRFKLQPVDDDEGSDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGRE 1379
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1380 KCDQYWPNDTVPV-FYGDIKVQILNDSHYADWVMTEFMLCRGSEQRILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRIG 1458
Cdd:cd14616    81 RCHQYWPEDNKPVtVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRASRA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442615984 1459 AEQRPIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQ 1522
Cdd:cd14616   161 HDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224

PTPc-N9

cd14543

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

1274-1517

3.03e-78

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.

Pssm-ID: 350391 [Multi-domain] Cd Length: 271 Bit Score: 260.37 E-value: 3.03e-78

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1274 EEFEELKhvgRDQPC-TF--ADLPCNRPKNRFTNILPYDHSRFKLQPVDDDEGSDYINANYVPGHNSPREFIVTQGPLHS 1350
Cdd:cd14543     7 EEYEDIR---REPPAgTFlcSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1351 TRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDT-VPVFYGDIKVQILNDSHYADWVMTEFML--CRGSEQRILR 1427
Cdd:cd14543    84 TYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEgSSLRYGDLTVTNLSVENKEHYKKTTLEIhnTETDESRQVT 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1428 HFHFTTWPDFGVPNPPQTLVRF-----------VRAFRDRIGAEQR--PIVVHCSAGVGRSGTFITLDRILQQINTSDYV 1494
Cdd:cd14543   164 HFQFTSWPDFGVPSSAAALLDFlgevrqqqalaVKAMGDRWKGHPPgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTL 243

                         250       260
                  ....*....|....*....|...
gi 442615984 1495 DIFGIVYAMRKERVWMVQTEQQY 1517
Cdd:cd14543   244 NVMQTVRRMRTQRAFSIQTPDQY 266

R-PTPc-F-1

cd14626

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

1256-1525

1.21e-76

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).

Pssm-ID: 350474 [Multi-domain] Cd Length: 276 Bit Score: 255.73 E-value: 1.21e-76

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1256 NFAEHYRLMSADSDFRFSEEFEELKHvGRDQPCTFADLPCNRPKNRFTNILPYDHSRFKLQPVDDDEGSDYINANYVPGH 1335
Cdd:cd14626     2 DLADNIERLKANDGLKFSQEYESIDP-GQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1336 NSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDTVPVfYGDIKVQILNDSHYADWVMTEF 1415
Cdd:cd14626    81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTET-YGMIQVTLLDTVELATYSVRTF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1416 MLCR--GSEQRILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAEQRPIVVHCSAGVGRSGTFITLDRILQQINTSDY 1493
Cdd:cd14626   160 ALYKngSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKT 239

                         250       260       270
                  ....*....|....*....|....*....|..
gi 442615984 1494 VDIFGIVYAMRKERVWMVQTEQQYICIHQCLL 1525
Cdd:cd14626   240 VDIYGHVTCMRSQRNYMVQTEDQYIFIHEALL 271

R5-PTPc-1

cd14549

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

1326-1521

5.13e-76

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: 251.12 E-value: 5.13e-76

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDTVPVfYGDIKVQILNDS 1405
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTET-YGNIQVTLLSTE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1406 HYADWVMTEFML--------CRGSEQRILRHFHFTTWPDFGVPNPPQTLVRFVR--AFRDRIGAEqrPIVVHCSAGVGRS 1475
Cdd:cd14549    80 VLATYTVRTFSLknlklkkvKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRksSAANPPGAG--PIVVHCSAGVGRT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 442615984 1476 GTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIH 1521
Cdd:cd14549   158 GTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203

R-PTPc-G-1

cd17667

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

1272-1525

2.81e-75

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: 251.88 E-value: 2.81e-75

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1272 FSEEFEELKHVGRDQPCT--FADLPCNRPKNRFTNILPYDHSRFKLQPV--DDDEGSDYINANYVPGHNSPREFIVTQGP 1347
Cdd:cd17667     1 FSEDFEEVQRCTADMNITaeHSNHPDNKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1348 LHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDTVPVfYGDIKVQILNDSHYADWVMTEFM-----LCRGSE 1422
Cdd:cd17667    81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEE-YGNIIVTLKSTKIHACYTVRRFSirntkVKKGQK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1423 --------QRILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAEQRPIVVHCSAGVGRSGTFITLDRILQQINTSDYV 1494
Cdd:cd17667   160 gnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTV 239

                         250       260       270
                  ....*....|....*....|....*....|.
gi 442615984 1495 DIFGIVYAMRKERVWMVQTEQQYICIHQCLL 1525
Cdd:cd17667   240 NVLGFLKHIRTQRNYLVQTEEQYIFIHDALL 270

R-PTPc-S-1

cd14625

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

1251-1525

3.61e-75

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: 251.94 E-value: 3.61e-75

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1251 PILIKNFAEHYRLMSADSDFRFSEEFEELKHvGRDQPCTFADLPCNRPKNRFTNILPYDHSRFKLQPVDDDEGSDYINAN 1330
Cdd:cd14625     3 PIPISELAEHTERLKANDNLKLSQEYESIDP-GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1331 YVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDTVPVfYGDIKVQILNDSHYADW 1410
Cdd:cd14625    82 YIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTET-YGMIQVTLLDTIELATF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1411 VMTEFMLCR--GSEQRILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAEQRPIVVHCSAGVGRSGTFITLDRILQQI 1488
Cdd:cd14625   161 CVRTFSLHKngSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERI 240

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 442615984 1489 NTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLL 1525
Cdd:cd14625   241 KHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALL 277

R-PTP-LAR-2

cd14554

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

1291-1528

7.30e-72

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: 240.50 E-value: 7.30e-72

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1291 ADLPCNRPKNRFTNILPYDHSRFKLQPVDDDEGSDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVML 1370
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1371 TRCFEKGREKCDQYWPNDTvPVFYGDIKVQILNDSHYADWVMTEFML--CRGSEQRILRHFHFTTWPDFGVPNPPQTLVR 1448
Cdd:cd14554    81 TKLREMGREKCHQYWPAER-SARYQYFVVDPMAEYNMPQYILREFKVtdARDGQSRTVRQFQFTDWPEQGVPKSGEGFID 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1449 F---VRAFRDRIGAEQrPIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYiciHQCLL 1525
Cdd:cd14554   160 FigqVHKTKEQFGQEG-PITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQY---QFCYR 235


                  ...
gi 442615984 1526 AVL 1528
Cdd:cd14554   236 AAL 238

R-PTPc-D-1

cd14624

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

1251-1525

4.77e-71

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

Pssm-ID: 350472 [Multi-domain] Cd Length: 284 Bit Score: 240.02 E-value: 4.77e-71

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1251 PILIKNFAEHYRLMSADSDFRFSEEFEELKHvGRDQPCTFADLPCNRPKNRFTNILPYDHSRFKLQPVDDDEGSDYINAN 1330
Cdd:cd14624     3 PIPILELADHIERLKANDNLKFSQEYESIDP-GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1331 YVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDTVPVfYGDIKVQILNDSHYADW 1410
Cdd:cd14624    82 YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTET-YGLIQVTLLDTVELATY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1411 VMTEFMLCR--GSEQRILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAEQRPIVVHCSAGVGRSGTFITLDRILQQI 1488
Cdd:cd14624   161 CVRTFALYKngSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERI 240

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 442615984 1489 NTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLL 1525
Cdd:cd14624   241 KHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALL 277

R-PTPc-T-1

cd14630

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

1296-1525

3.06e-70

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: 236.08 E-value: 3.06e-70

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1296 NRPKNRFTNILPYDHSRFKLQPVDDDEGSDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFE 1375
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1376 KGREKCDQYWPNDTvpVFYGDIKVQILNDSHYADWVMTEFMLCRGS--EQRILRHFHFTTWPDFGVPNPPQTLVRFVRAF 1453
Cdd:cd14630    83 VGRVKCVRYWPDDT--EVYGDIKVTLIETEPLAEYVIRTFTVQKKGyhEIREIRQFHFTSWPDHGVPCYATGLLGFVRQV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442615984 1454 RDRIGAEQRPIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLL 1525
Cdd:cd14630   161 KFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAIL 232

R-PTPc-M-1

cd14633

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

1256-1525

6.46e-69

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

Pssm-ID: 350481 [Multi-domain] Cd Length: 273 Bit Score: 233.78 E-value: 6.46e-69

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1256 NFAEHYRLMSADSDFRFSEEFEELKHvGRDQPCTFADLPCNRPKNRFTNILPYDHSRFKLQPVDDDEGSDYINANYVPGH 1335
Cdd:cd14633     1 DLLQHITQMKCAEGYGFKEEYESFFE-GQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1336 NSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDTvpVFYGDIKVQILNDSHYADWVMTEF 1415
Cdd:cd14633    80 HRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDT--EIYKDIKVTLIETELLAEYVIRTF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1416 ML-CRGS-EQRILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAEQRPIVVHCSAGVGRSGTFITLDRILQQINTSDY 1493
Cdd:cd14633   158 AVeKRGVhEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGV 237

                         250       260       270
                  ....*....|....*....|....*....|..
gi 442615984 1494 VDIFGIVYAMRKERVWMVQTEQQYICIHQCLL 1525
Cdd:cd14633   238 VDIYNCVRELRSRRVNMVQTEEQYVFIHDAIL 269

PTPc-KIM

cd14547

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

1300-1522

1.93e-68

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: 230.36 E-value: 1.93e-68

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1300 NRFTNILPYDHSRFKLQPVDDDEGSDYINANYVPGHNSPRE-FIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKgR 1378
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKaYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1379 EKCDQYWPnDTVPVFYGDIKVQILNDSHYADWVMTEFMLCRGSEQRILRHFHFTTWPDFGVPNPPQTLVRFVR-AFRDRI 1457
Cdd:cd14547    80 EKCAQYWP-EEENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQeVEEARQ 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442615984 1458 GAEQR-PIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQ 1522
Cdd:cd14547   159 TEPHRgPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224

PTPc-N11_6

cd14544

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

1296-1517

1.46e-67

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: 228.89 E-value: 1.46e-67

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1296 NRPKNRFTNILPYDHSRFKLQPVDDDE-GSDYINANYVPGHNSPRE-------FIVTQGPLHSTRDDFWRMCWESNSRAI 1367
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDPNVpGSDYINANYIRNENEGPTtdenaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1368 VMLTRCFEKGREKCDQYWPNDTVPVFYGDIKVQILNDSHYADWVMTEFMLCRGSEQ---RILRHFHFTTWPDFGVPNPPQ 1444
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGdpiREIWHYQYLSWPDHGVPSDPG 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442615984 1445 TLVRFVRAFRDRIGA--EQRPIVVHCSAGVGRSGTFITLDRILQQINTSDY---VDIFGIVYAMRKERVWMVQTEQQY 1517
Cdd:cd14544   161 GVLNFLEDVNQRQESlpHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQY 238

R-PTPc-A-1

cd14621

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

1251-1525

1.99e-66

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: 227.21 E-value: 1.99e-66

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1251 PILIKNFAEHYRLMSADSDFRFSEEFEELKHVGRDQPCTFADLPCNRPKNRFTNILPYDHSRFKLQPVDDDEGSDYINAN 1330
Cdd:cd14621     7 PLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINAS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1331 YVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDTVPVfYGDIKVQILNDSHYADW 1410
Cdd:cd14621    87 FINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWT-YGNIRVSVEDVTVLVDY 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1411 VMTEFMLCRGSE------QRILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAEQRPIVVHCSAGVGRSGTFITLDRI 1484
Cdd:cd14621   166 TVRKFCIQQVGDvtnkkpQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAM 245

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 442615984 1485 LQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLL 1525
Cdd:cd14621   246 LDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALL 286

PTP_fungal

cd18533

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

1326-1522

2.21e-66

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: 223.66 E-value: 2.21e-66

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYV-PGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDTVPVFYGDIKVQILND 1404
Cdd:cd18533     1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1405 SHYADW--VMTEF-MLCRGSEQRILRHFHFTTWPDFGVPNPPQ---TLVRFVRAFRDRiGAEQRPIVVHCSAGVGRSGTF 1478
Cdd:cd18533    81 EENDDGgfIVREFeLSKEDGKVKKVYHIQYKSWPDFGVPDSPEdllTLIKLKRELNDS-ASLDPPIIVHCSAGVGRTGTF 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 442615984 1479 ITLDRILQ----QINTSDYVD-----IFGIVYAMRKERVWMVQTEQQYICIHQ 1522
Cdd:cd18533   160 IALDSLLDelkrGLSDSQDLEdsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212

PTPc-N1_2

cd14545

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

1296-1516

1.74e-65

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.

Pssm-ID: 350393 [Multi-domain] Cd Length: 231 Bit Score: 221.88 E-value: 1.74e-65

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1296 NRpkNRFTNILPYDHSRFKLQpvddDEGSDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFE 1375
Cdd:cd14545     2 NR--YRDRDPYDHDRSRVKLK----QGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLME 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1376 KGREKCDQYWPNDTVPVF---YGDIKVQILNDSHYADWVMTEFMLCR--GSEQRILRHFHFTTWPDFGVPNPPQTLVRFV 1450
Cdd:cd14545    76 KGQIKCAQYWPQGEGNAMifeDTGLKVTLLSEEDKSYYTVRTLELENlkTQETREVLHFHYTTWPDFGVPESPAAFLNFL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1451 RAFRDR--IGAEQRPIVVHCSAGVGRSGTFITLDRILQQINTSDY--VDIFGIVYAMRKERVWMVQTEQQ 1516
Cdd:cd14545   156 QKVRESgsLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQ 225

R-PTPc-E-1

cd14620

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

1302-1525

6.04e-65

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1).

Pssm-ID: 350468 [Multi-domain] Cd Length: 229 Bit Score: 220.58 E-value: 6.04e-65

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1302 FTNILPYDHSRFKLQPVDDDEGSDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKC 1381
Cdd:cd14620     1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1382 DQYWPNDTVPVfYGDIKVQILNDSHYADWVMTEF----MLCRGSE-QRILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDR 1456
Cdd:cd14620    81 YQYWPDQGCWT-YGNIRVAVEDCVVLVDYTIRKFciqpQLPDGCKaPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442615984 1457 IGAEQRPIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLL 1525
Cdd:cd14620   160 NPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228

PTPc-N1

cd14608

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

1276-1538

3.97e-64

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: 219.90 E-value: 3.97e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1276 FEELKHVGRDQPCTFADLPCNRPKNRFTNILPYDHSRFKLQpvddDEGSDYINANYVPGHNSPREFIVTQGPLHSTRDDF 1355
Cdd:cd14608     5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLH----QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1356 WRMCWESNSRAIVMLTRCFEKGREKCDQYWPN-DTVPVFYGD--IKVQILNDSHYADWVMTEFML--CRGSEQRILRHFH 1430
Cdd:cd14608    81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQkEEKEMIFEDtnLKLTLISEDIKSYYTVRQLELenLTTQETREILHFH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1431 FTTWPDFGVPNPPQTLVRFVRAFRDR--IGAEQRPIVVHCSAGVGRSGTFITLDR---ILQQINTSDYVDIFGIVYAMRK 1505
Cdd:cd14608   161 YTTWPDFGVPESPASFLNFLFKVRESgsLSPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRK 240

                         250       260       270
                  ....*....|....*....|....*....|...
gi 442615984 1506 ERVWMVQTEQQyicIHQCLLAVLEGKENIVGPA 1538
Cdd:cd14608   241 FRMGLIQTADQ---LRFSYLAVIEGAKFIMGDS 270

R-PTP-S-2

cd14627

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

1291-1528

1.23e-62

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

Pssm-ID: 350475 [Multi-domain] Cd Length: 290 Bit Score: 216.14 E-value: 1.23e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1291 ADLPCNRPKNRFTNILPYDHSRFKLQPVDDDEGSDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVML 1370
Cdd:cd14627    48 ANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVML 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1371 TRCFEKGREKCDQYWPNDTvPVFYGDIKVQILNDSHYADWVMTEFML--CRGSEQRILRHFHFTTWPDFGVPNPPQTLVR 1448
Cdd:cd14627   128 TKLREMGREKCHQYWPAER-SARYQYFVVDPMAEYNMPQYILREFKVtdARDGQSRTVRQFQFTDWPEQGVPKSGEGFID 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1449 F---VRAFRDRIGaEQRPIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLL 1525
Cdd:cd14627   207 FigqVHKTKEQFG-QDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAAL 285


                  ...
gi 442615984 1526 AVL 1528
Cdd:cd14627   286 EYL 288

R-PTPc-K-1

cd14631

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

1312-1525

1.66e-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: 1.66e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1312 RFKLQPVDDDEGSDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDTvp 1391
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDT-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1392 VFYGDIKVQILNDSHYADWVMTEFMLCRG--SEQRILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAEQRPIVVHCS 1469
Cdd:cd14631    79 EVYGDFKVTCVEMEPLAEYVVRTFTLERRgyNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCS 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 442615984 1470 AGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLL 1525
Cdd:cd14631   159 AGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214

R-PTP-D-2

cd14628

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

1291-1517

5.13e-62

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

Pssm-ID: 350476 [Multi-domain] Cd Length: 292 Bit Score: 214.60 E-value: 5.13e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1291 ADLPCNRPKNRFTNILPYDHSRFKLQPVDDDEGSDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVML 1370
Cdd:cd14628    47 ANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1371 TRCFEKGREKCDQYWPNDTvPVFYGDIKVQILNDSHYADWVMTEFML--CRGSEQRILRHFHFTTWPDFGVPNPPQTLVR 1448
Cdd:cd14628   127 TKLREMGREKCHQYWPAER-SARYQYFVVDPMAEYNMPQYILREFKVtdARDGQSRTVRQFQFTDWPEQGVPKSGEGFID 205

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442615984 1449 F---VRAFRDRIGaEQRPIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQY 1517
Cdd:cd14628   206 FigqVHKTKEQFG-QDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQY 276

R-PTPc-C-1

cd14557

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

1326-1522

5.20e-62

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: 210.84 E-value: 5.20e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPN-DTVPVFYGDIKVQILND 1404
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1405 SHYADWVMTEFMLCRGSEQRILR---HFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAEQRPIVVHCSAGVGRSGTFITL 1481
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKGSGRevtHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 442615984 1482 DRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQ 1522
Cdd:cd14557   161 DAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201

R-PTP-F-2

cd14629

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

1291-1529

5.56e-62

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: 214.20 E-value: 5.56e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1291 ADLPCNRPKNRFTNILPYDHSRFKLQPVDDDEGSDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVML 1370
Cdd:cd14629    48 ANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1371 TRCFEKGREKCDQYWPNDTvPVFYGDIKVQILNDSHYADWVMTEFML--CRGSEQRILRHFHFTTWPDFGVPNPPQTLVR 1448
Cdd:cd14629   128 TKLREMGREKCHQYWPAER-SARYQYFVVDPMAEYNMPQYILREFKVtdARDGQSRTIRQFQFTDWPEQGVPKTGEGFID 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1449 F---VRAFRDRIGaEQRPIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYiciHQCLL 1525
Cdd:cd14629   207 FigqVHKTKEQFG-QDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQY---QLCYR 282


                  ....
gi 442615984 1526 AVLE 1529
Cdd:cd14629   283 AALE 286

R-PTPc-typeIIb-1

cd14555

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

1326-1525

7.14e-62

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

Pssm-ID: 350403 [Multi-domain] Cd Length: 204 Bit Score: 210.54 E-value: 7.14e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDTVpvFYGDIKVQILNDS 1405
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTE--VYGDIKVTLVETE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1406 HYADWVMTEFMLCRG--SEQRILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAEQRPIVVHCSAGVGRSGTFITLDR 1483
Cdd:cd14555    79 PLAEYVVRTFALERRgyHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVIDI 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 442615984 1484 ILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLL 1525
Cdd:cd14555   159 MLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200

R-PTPc-Z-1

cd17668

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

1326-1525

2.89e-61

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: 209.06 E-value: 2.89e-61

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDTVPVfYGDIKVQILNDS 1405
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEE-YGNFLVTQKSVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1406 HYADWVMTEFML-----CRGSEQ-----RILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAEQRPIVVHCSAGVGRS 1475
Cdd:cd17668    80 VLAYYTVRNFTLrntkiKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRT 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 442615984 1476 GTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLL 1525
Cdd:cd17668   160 GTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209

R-PTPc-A-E-1

cd14551

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

1326-1522

8.68e-60

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).

Pssm-ID: 350399 [Multi-domain] Cd Length: 202 Bit Score: 204.38 E-value: 8.68e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPnDTVPVFYGDIKVQILNDS 1405
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP-DQGCWTYGNLRVRVEDTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1406 HYADWVMTEFML--------CRgsEQRILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAEQRPIVVHCSAGVGRSGT 1477
Cdd:cd14551    80 VLVDYTTRKFCIqkvnrgigEK--RVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 442615984 1478 FITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQ 1522
Cdd:cd14551   158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202

PTPc-N18

cd14603

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

1273-1517

1.21e-59

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: 206.60 E-value: 1.21e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1273 SEEFEELKH----VGRDQPCTF--ADLPCNRPKNRFTNILPYDHSRFKLQPVDDDEGSDYINANYVPGHNSPREFIVTQG 1346
Cdd:cd14603     1 AGEFSEIRAcsaaFKADYVCSTvaGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1347 PLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDTVPVFYGDIKVQILNDSHY-ADWVMTEFMLCRGSEQRI 1425
Cdd:cd14603    81 PLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLnEEVILRTLKVTFQKESRS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1426 LRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAEQRPIVVHCSAGVGRSGTFITLDRILQQINTS---DYVDIFGIVYA 1502
Cdd:cd14603   161 VSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQripPDFSIFDVVLE 240

                         250
                  ....*....|....*
gi 442615984 1503 MRKERVWMVQTEQQY 1517
Cdd:cd14603   241 MRKQRPAAVQTEEQY 255

PTPc-N20_13

cd14538

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

1326-1528

1.35e-59

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: 204.15 E-value: 1.35e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYV--PGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPN--DTVPVFYGDIKVQI 1401
Cdd:cd14538     1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDslNKPLICGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1402 LNDSHYADWVMTEFML--CRGSEQRILRHFHFTTWPDFGVPNPPQTLVRFVRAFRdRIgAEQRPIVVHCSAGVGRSGTFI 1479
Cdd:cd14538    81 EKYQSLQDFVIRRISLrdKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMR-RI-HNSGPIVVHCSAGIGRTGVLI 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 442615984 1480 TLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLLAVL 1528
Cdd:cd14538   159 TIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207

PTPc-N2

cd14607

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

1278-1516

8.37e-58

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: 200.96 E-value: 8.37e-58

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1278 ELKHVGRDQPCTFADLPCNRPKNRFTNILPYDHSRFKLQPVDDDegsdYINANYVPGHNSPREFIVTQGPLHSTRDDFWR 1357
Cdd:cd14607     6 EIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEND----YINASLVVIEEAQRSYILTQGPLPNTCCHFWL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1358 MCWESNSRAIVMLTRCFEKGREKCDQYWPNDTVPV-FYGD--IKVQILND---SHYADWVMtEFMLCRGSEQRILRHFHF 1431
Cdd:cd14607    82 MVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVlSFKEtgFSVKLLSEdvkSYYTVHLL-QLENINSGETRTISHFHY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1432 TTWPDFGVPNPPQTLVRFVRAFRDR--IGAEQRPIVVHCSAGVGRSGTFITLDR--ILQQINTSDYVDIFGIVYAMRKER 1507
Cdd:cd14607   161 TTWPDFGVPESPASFLNFLFKVRESgsLSPEHGPAVVHCSAGIGRSGTFSLVDTclVLMEKKDPDSVDIKQVLLDMRKYR 240


                  ....*....
gi 442615984 1508 VWMVQTEQQ 1516
Cdd:cd14607   241 MGLIQTPDQ 249

PTPc-N11

cd14605

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

1296-1529

5.46e-57

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: 198.70 E-value: 5.46e-57

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1296 NRPKNRFTNILPYDHSRFKLQPVDDDE-GSDYINANYV-PGHNS-------PREFIVTQGPLHSTRDDFWRMCWESNSRA 1366
Cdd:cd14605     2 NKNKNRYKNILPFDHTRVVLHDGDPNEpVSDYINANIImPEFETkcnnskpKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1367 IVMLTRCFEKGREKCDQYWPNDTVPVFYGDIKVQILNDSHYADWVMTEFMLCR---GSEQRILRHFHFTTWPDFGVPNPP 1443
Cdd:cd14605    82 IVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLSKvgqGNTERTVWQYHFRTWPDHGVPSDP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1444 QTLVRF---VRAFRDRIgAEQRPIVVHCSAGVGRSGTFITLDRILQQINTSDY---VDIFGIVYAMRKERVWMVQTEQQY 1517
Cdd:cd14605   162 GGVLDFleeVHHKQESI-MDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEAQY 240

                         250
                  ....*....|..
gi 442615984 1518 ICIHQCLLAVLE 1529
Cdd:cd14605   241 RFIYMAVQHYIE 252

PTPc-N6

cd14606

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

1294-1529

1.10e-56

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: 198.18 E-value: 1.10e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1294 PCNRPKNRFTNILPYDHSRFKLQPVDDD-EGSDYINANYVPGH-----NSPREFIVTQGPLHSTRDDFWRMCWESNSRAI 1367
Cdd:cd14606    16 PENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVKNQllgpdENAKTYIASQGCLEATVNDFWQMAWQENSRVI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1368 VMLTRCFEKGREKCDQYWPNDTVPVFYGDIKVQILNDSHYADWVMTEFMLC---RGSEQRILRHFHFTTWPDFGVPNPPQ 1444
Cdd:cd14606    96 VMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSpldNGELIREIWHYQYLSWPDHGVPSEPG 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1445 TlvrfVRAFRDRIGAEQR------PIVVHCSAGVGRSGTFITLDRILQQINTSDY---VDIFGIVYAMRKERVWMVQTEQ 1515
Cdd:cd14606   176 G----VLSFLDQINQRQEslphagPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQTEA 251

                         250
                  ....*....|....
gi 442615984 1516 QYICIHQCLLAVLE 1529
Cdd:cd14606   252 QYKFIYVAIAQFIE 265

PTPc-N22_18_12

cd14542

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

1326-1522

5.98e-56

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: 193.41 E-value: 5.98e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDTVPVF-YGDIKVQILND 1404
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLqFGPFKISLEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1405 ShyadWVMTEFML-----CRGSEQRILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAEQRPIVVHCSAGVGRSGTFI 1479
Cdd:cd14542    81 K----RVGPDFLIrtlkvTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTIC 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 442615984 1480 TLD---RILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQ 1522
Cdd:cd14542   157 AIDyvwNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202

R-PTPc-U-1

cd14632

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

1326-1525

2.06e-55

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: 192.19 E-value: 2.06e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDTVpvFYGDIKVQILNDS 1405
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSD--TYGDIKITLLKTE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1406 HYADWVMTEFMLCRG--SEQRILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAEQRPIVVHCSAGVGRSGTFITLDR 1483
Cdd:cd14632    79 TLAEYSVRTFALERRgySARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLDV 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 442615984 1484 ILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLL 1525
Cdd:cd14632   159 MLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200

PTPc-N7

cd14612

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

1292-1524

4.60e-55

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: 192.74 E-value: 4.60e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1292 DLPCNRPKNRFTNILPYDHSRFKLQ-PVDDDEGSDYINANYVPGHN-SPREFIVTQGPLHSTRDDFWRMCWESNSRAIVM 1369
Cdd:cd14612    11 DIPGHASKDRYKTILPNPQSRVCLRrAGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVM 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1370 LTRCFEKgREKCDQYWPNDTVPvfYGDIKVQILNDSHYADWVMTEFMLCRGSEQRILRHFHFTTWPDFGVPNPPQTLVRF 1449
Cdd:cd14612    91 ITKLKEK-KEKCVHYWPEKEGT--YGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPESAGPLLRL 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442615984 1450 VRAFRDR--IGAEQRPIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCL 1524
Cdd:cd14612   168 VAEVEESrqTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTL 244

R-PTPc-A-E-2

cd14552

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

1326-1517

5.88e-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: 190.56 E-value: 5.88e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDTVpVFYGDIKVQILNDS 1405
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGS-VSSGDITVELKDQT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1406 HYADWVMTEFMLC--RGSEQRILRHFHFTTWPDFGVPNPPQTLVrfvrafrDRIGAEQR--------PIVVHCSAGVGRS 1475
Cdd:cd14552    80 DYEDYTLRDFLVTkgKGGSTRTVRQFHFHGWPEVGIPDNGKGMI-------DLIAAVQKqqqqsgnhPITVHCSAGAGRT 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 442615984 1476 GTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQY 1517
Cdd:cd14552   153 GTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQY 194

PTPc-N3_4

cd14541

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

1325-1530

6.57e-55

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: 191.00 E-value: 6.57e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1325 DYINANYV----PGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDTVPVFYGDIKVQ 1400
Cdd:cd14541     1 DYINANYVnmeiPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1401 ILNDSHYADWVMTEFMLC--RGSEQRILRHFHFTTWPDFGVPNPPQTLVRFV-RAFRDRIGAEQrPIVVHCSAGVGRSGT 1477
Cdd:cd14541    81 CVSEEVTPSFAFREFILTntNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVkRVRQNRVGMVE-PTVVHCSAGIGRTGV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 442615984 1478 FITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLLAVLEG 1530
Cdd:cd14541   160 LITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRVYEE 212

PTPc-N12

cd14604

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

1253-1529

1.82e-54

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: 192.84 E-value: 1.82e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1253 LIKNFAEHYRLMSA---DSDFRFSEEFEELKHVG------RDQPCTFADLPCNRPKNRFTNILPYDHSRFKLQPVDDDEG 1323
Cdd:cd14604     5 ILKKFIERVQAMKStdhNGEDNFASDFMRLRRLStkyrteKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1324 SDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPN-DTVPVFYGDIKVQIL 1402
Cdd:cd14604    85 SDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLyGEEPMTFGPFRISCE 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1403 NDSHYADWVMTEFMLCRGSEQRILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAEQRPIVVHCSAGVGRSGTFITLD 1482
Cdd:cd14604   165 AEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAID 244

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 442615984 1483 ---RILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLLAVLE 1529
Cdd:cd14604   245 ytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFE 294

PTPc-N13

cd14597

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

1296-1528

6.12e-54

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: 188.89 E-value: 6.12e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1296 NRPKNRFTNILPYDHSRFKLqpvdDDEGsDYINANYV--PGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRC 1373
Cdd:cd14597     3 NRKKNRYKNILPYDTTRVPL----GDEG-GYINASFIkmPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1374 FEKGREKCDQYWPND-TVPVFYGD-IKVQILNDSHYADWVMTEFML--CRGSEQRILRHFHFTTWPDFGVPNPPQTLVRF 1449
Cdd:cd14597    78 VEGGKIKCQRYWPEIlGKTTMVDNrLQLTLVRMQQLKNFVIRVLELedIQTREVRHITHLNFTAWPDHDTPSQPEQLLTF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1450 VRAFRD--RIGaeqrPIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLLAV 1527
Cdd:cd14597   158 ISYMRHihKSG----PIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVILYV 233


                  .
gi 442615984 1528 L 1528
Cdd:cd14597   234 L 234

PTPc-N3

cd14600

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

1275-1529

1.20e-53

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: 189.68 E-value: 1.20e-53

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1275 EFEELKHVGRDQPCTFADLPCNRPKNRFTNILPYDHSRFKLQpvdddEGSDYINANYV----PGHNSPREFIVTQGPLHS 1350
Cdd:cd14600    19 QFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQ-----GNEDYINASYVnmeiPSANIVNKYIATQGPLPH 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1351 TRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDTVPVFYGDIKVQILNDSHYADWVMTEFMLC--RGSEQRILRH 1428
Cdd:cd14600    94 TCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTntQTGEERTVTH 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1429 FHFTTWPDFGVPNPPQTLVRFVRAFRDRiGAEQRPIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERV 1508
Cdd:cd14600   174 LQYVAWPDHGVPDDSSDFLEFVNYVRSK-RVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRA 252

                         250       260
                  ....*....|....*....|.
gi 442615984 1509 WMVQTEQQYICIHQCLLAVLE 1529
Cdd:cd14600   253 MMVQTSSQYKFVCEAILRVYE 273

R-PTPc-A-2

cd14623

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

1301-1517

2.08e-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: 184.48 E-value: 2.08e-52

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1301 RFTNILPYDHSRFKLQPVDDDEGSDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREK 1380
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1381 CDQYWPNDTVpVFYGDIKVQILNDSHYADWVMTEFMLC--RGSEQRILRHFHFTTWPDFGVPNPPQTLVRFVRAF-RDRI 1457
Cdd:cd14623    81 CAQYWPSDGS-VSYGDITIELKKEEECESYTVRDLLVTntRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVqKQQQ 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1458 GAEQRPIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQY 1517
Cdd:cd14623   160 QSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQY 219

PTPc-N5

cd14613

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

1292-1524

2.57e-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: 185.45 E-value: 2.57e-52

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1292 DLPCNRPKNRFTNILPYDHSRFKLQPVD-DDEGSDYINANYVPGHNSP-REFIVTQGPLHSTRDDFWRMCWESNSRAIVM 1369
Cdd:cd14613    21 DIPGLVRKNRYKTILPNPHSRVCLTSPDqDDPLSSYINANYIRGYGGEeKVYIATQGPTVNTVGDFWRMVWQERSPIIVM 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1370 LTRCFEKGrEKCDQYWPNDTVpvFYGDIKVQILNDSHYADWVMTEFMLCRGSEQRILRHFHFTTWPDFGVPN--PPQ-TL 1446
Cdd:cd14613   101 ITNIEEMN-EKCTEYWPEEQV--TYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYTSWPDQKTPDnaPPLlQL 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442615984 1447 VRFVRAFRDRIGAEQRPIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCL 1524
Cdd:cd14613   178 VQEVEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255

PTPc-N22

cd14602

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

1299-1517

4.91e-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: 183.50 E-value: 4.91e-52

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1299 KNRFTNILPYDHSRFKLQPVDDDEGSDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGR 1378
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1379 EKCDQYWPN-DTVPVFYGDIKVQILNDSHYADWVMTEFMLCRGSEQRILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRI 1457
Cdd:cd14602    81 KKCERYWAEpGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442615984 1458 GAEQRPIVVHCSAGVGRSGTFITLD---RILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQY 1517
Cdd:cd14602   161 EDDSVPICIHCSAGCGRTGVICAIDytwMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQY 223

R-PTPc-R

cd14611

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

1299-1522

8.68e-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: 179.73 E-value: 8.68e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1299 KNRFTNILPYDHSRFKLQPVD-DDEGSDYINANYVPGH-NSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEK 1376
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIRGYgGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1377 GrEKCDQYWPNDTVpvFYGDIKVQILNDSHYADWVMTEFMLCRGSEQRILRHFHFTTWPDFGVPNPPQTLVRFVRAFR-D 1455
Cdd:cd14611    82 N-EKCVLYWPEKRG--IYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEeD 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442615984 1456 RIGAEQR-PIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQ 1522
Cdd:cd14611   159 RLASPGRgPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226

R-PTPc-E-2

cd14622

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

1325-1517

1.28e-50

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: 178.28 E-value: 1.28e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1325 DYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDTvPVFYGDIKVQILND 1404
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEG-SVTHGEITIEIKND 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1405 SHYADWVMTEFMLCRGSEQ--RILRHFHFTTWPDFGVPNPPQTLVRFVRAF-RDRIGAEQRPIVVHCSAGVGRSGTFITL 1481
Cdd:cd14622    80 TLLETISIRDFLVTYNQEKqtRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVqKQQQQTGNHPIVVHCSAGAGRTGTFIAL 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 442615984 1482 DRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQY 1517
Cdd:cd14622   160 SNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQY 195

PTPc-N20

cd14596

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

1326-1529

3.11e-49

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: 174.55 E-value: 3.11e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYVPGHNSPRE--FIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPND-TVPVFYGDIKVQIL 1402
Cdd:cd14596     1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETlQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1403 NDSHYADWVMTEFMLCRGS--EQRILRHFHFTTWPDFGVPNPPQTLVRFVRAFRdRIGAEQrPIVVHCSAGVGRSGTFIT 1480
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKEtgENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMR-KVHNTG-PIVVHCSAGIGRAGVLIC 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 442615984 1481 LDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLLAVLE 1529
Cdd:cd14596   159 VDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207

R-PTP-N2

cd14610

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

1271-1517

6.00e-49

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: 176.40 E-value: 6.00e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1271 RFSEEFEEL-KHVGRDQPCTFADLPCNRPKNRFTNILPYDHSRFKLQPVDDDEGSDYINANYVPGHNsPRE--FIVTQGP 1347
Cdd:cd14610    18 RLEKEWEALcAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHD-PRNpaYIATQGP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1348 LHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPnDTVPVFYGDIKVQILNDSHYA-DWVMTEFML--CRGSEQR 1424
Cdd:cd14610    97 LPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWP-DEGSNLYHIYEVNLVSEHIWCeDFLVRSFYLknLQTNETR 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1425 ILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAEQRPIVVHCSAGVGRSGTFITLDRILQQI-NTSDYVDIFGIVYAM 1503
Cdd:cd14610   176 TVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHL 255

                         250
                  ....*....|....
gi 442615984 1504 RKERVWMVQTEQQY 1517
Cdd:cd14610   256 RDQRPGMVQTKEQF 269

R-PTP-N

cd14609

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

1271-1517

3.04e-47

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: 171.37 E-value: 3.04e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1271 RFSEEFEEL-KHVGRDQPCTFADLPCNRPKNRFTNILPYDHSRFKLQPVDDDEGSDYINANYVPGHNsPR--EFIVTQGP 1347
Cdd:cd14609    16 RLAKEWQALcAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIEHD-PRmpAYIATQGP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1348 LHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPnDTVPVFYGDIKVQILNDSHYA-DWVMTEFML--CRGSEQR 1424
Cdd:cd14609    95 LSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWP-DEGSSLYHIYEVNLVSEHIWCeDFLVRSFYLknVQTQETR 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1425 ILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAEQRPIVVHCSAGVGRSGTFITLDRILQQINTS-DYVDIFGIVYAM 1503
Cdd:cd14609   174 TLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHV 253

                         250
                  ....*....|....
gi 442615984 1504 RKERVWMVQTEQQY 1517
Cdd:cd14609   254 RDQRPGMVRTKDQF 267

PTPc-N4

cd14601

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

1325-1529

7.48e-46

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: 165.12 E-value: 7.48e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1325 DYINANY----VPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDTVPVFYGDIKVQ 1400
Cdd:cd14601     1 DYINANYinmeIPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1401 ILNDSHYADWVMTEFMLC--RGSEQRILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAEQRPIVVHCSAGVGRSGTF 1478
Cdd:cd14601    81 CHSEEGNPAYVFREMTLTnlEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGVL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 442615984 1479 ITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLLAVLE 1529
Cdd:cd14601   161 ITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYE 211

R-PTP-C-2

cd14558

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

1326-1517

7.53e-46

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: 164.49 E-value: 7.53e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDTVPvfYGDIKVQILNDS 1405
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT--YGDIEVELKDTE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1406 HYADWVMTEFML--CRGSEQRILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAEQ------RPIVVHCSAGVGRSGT 1477
Cdd:cd14558    79 KSPTYTVRVFEIthLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNskhgrsVPIVVHCSDGSSRTGI 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 442615984 1478 FITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQY 1517
Cdd:cd14558   159 FCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQY 198

PHA02742

protein tyrosine phosphatase; Provisional

1296-1529

7.05e-45

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 165.56 E-value: 7.05e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1296 NRPKNRFTNILPYDHSRFKLQPvdDDEGSDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFE 1375
Cdd:PHA02742   52 NMKKCRYPDAPCFDRNRVILKI--EDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1376 KGREKCDQYW-PNDTVPVFYGDIKVQILNDSHYADWVMTEFMLCRGSEQRIL--RHFHFTTWPDFGVPNPPQTLVRFVRA 1452
Cdd:PHA02742  130 DGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLdiKHFAYEDWPHGGLPRDPNKFLDFVLA 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1453 FRDR-------IGAEQR----PIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICih 1521
Cdd:PHA02742  210 VREAdlkadvdIKGENIvkepPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF-- 287


                  ....*...
gi 442615984 1522 qCLLAVLE 1529
Cdd:PHA02742  288 -CYFIVLI 294

PHA02738

hypothetical protein; Provisional

1256-1518

5.38e-44

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 163.56 E-value: 5.38e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1256 NFAEHYRLMSAdSDFRFSEEFEELKHVGRDQPCTFADLPCNRPKNRFTNILPYDHSRFKLqPVDDDEGsDYINANYVPGH 1335
Cdd:PHA02738   10 KYAEFLALMEK-SDCEEVITREHQKVISEKVDGTFNAEKKNRKLNRYLDAVCFDHSRVIL-PAERNRG-DYINANYVDGF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1336 NSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPN-DTVPVFYGDIKVQILNDSHYADWVMTE 1414
Cdd:PHA02738   87 EYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDvEQGSIRFGKFKITTTQVETHPHYVKST 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1415 FMLCRGSEQ-RILRHFHFTTWPDFGVPNPPQTLVRFVRAFRD----------RIGAEQR---PIVVHCSAGVGRSGTFIT 1480
Cdd:PHA02738  167 LLLTDGTSAtQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQcqkelaqeslQIGHNRLqppPIVVHCNAGLGRTPCYCV 246

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 442615984 1481 LDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYI 1518
Cdd:PHA02738  247 VDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYF 284

PTPc-N21_14

cd14540

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

1326-1528

1.15e-43

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: 158.77 E-value: 1.15e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYVPGH--NSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDT---VPVFYGDIKVQ 1400
Cdd:cd14540     1 YINASHITATvgGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGgehDALTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1401 ILNDSHYADWVMTEFMLCRGSE--QRILRHFHFTTWPDFGVPNPPQTLVRF---VRAFRDRIGAEQR------PIVVHCS 1469
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHTLSgqSRTVWHLQYTDWPDHGCPEDVSGFLDFleeINSVRRHTNQDVAghnrnpPTLVHCS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 442615984 1470 AGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLLAVL 1528
Cdd:cd14540   161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219

R-PTP-N-N2

cd14546

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

1326-1517

1.64e-41

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: 152.21 E-value: 1.64e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYVPGHNsPRE--FIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDTVPVfYGDIKVQILN 1403
Cdd:cd14546     1 YINASTIYDHD-PRNpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEV-YHIYEVHLVS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1404 DSHY-ADWVMTEFML--CRGSEQRILRHFHFTTWPDFGVPNPPQTLVRFVR----AFRDRIgaeqRPIVVHCSAGVGRSG 1476
Cdd:cd14546    79 EHIWcDDYLVRSFYLknLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRkvnkSYRGRS----CPIVVHCSDGAGRTG 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 442615984 1477 TFITLDRILQQINTS-DYVDIFGIVYAMRKERVWMVQTEQQY 1517
Cdd:cd14546   155 TYILIDMVLNRMAKGaKEIDIAATLEHLRDQRPGMVKTKDQF 196

PHA02747

protein tyrosine phosphatase; Provisional

1294-1538

1.08e-40

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 153.62 E-value: 1.08e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1294 PCNRPKNRFTNILPYDHSRFKLQpVDDDEGSDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRC 1373
Cdd:PHA02747   49 PENQPKNRYWDIPCWDHNRVILD-SGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPT 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1374 -FEKGREKCDQYW-PNDTVPVFYGDIKVQILNDSHYADWVMTEFMLCRGS--EQRILRHFHFTTWPDFGVPNPPQTLVRF 1449
Cdd:PHA02747  128 kGTNGEEKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKIlkDSRKISHFQCSEWFEDETPSDHPDFIKF 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1450 VRAF---RDRIGAEQR-------PIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYIC 1519
Cdd:PHA02747  208 IKIIdinRKKSGKLFNpkdallcPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLF 287

                         250       260
                  ....*....|....*....|..
gi 442615984 1520 I---HQCLLAVLEGKENIVGPA 1538
Cdd:PHA02747  288 IqpgYEVLHYFLSKIKAIDKIK 309

PTP-N23

cd14539

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

1326-1518

2.15e-40

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: 149.07 E-value: 2.15e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYVPGHN--SPReFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDT-VPVFYGDIKV--Q 1400
Cdd:cd14539     1 YINASLIEDLTpyCPR-FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERgQALVYGAITVslQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1401 ILNDSHYadWVmtEFMLC----RGSEQRILRHFHFTTWPDFGVPNPPQTLVRF---VRAFRDRIGAEQRPIVVHCSAGVG 1473
Cdd:cd14539    80 SVRTTPT--HV--ERIISiqhkDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFieeVHSHYLQQRSLQTPIVVHCSSGVG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 442615984 1474 RSGTFITLDRILQQINTSD-YVDIFGIVYAMRKERVWMVQTEQQYI 1518
Cdd:cd14539   156 RTGAFCLLYAAVQEIEAGNgIPDLPQLVRKMRQQRKYMLQEKEHLK 201

R-PTPc-typeIIb-2

cd14556

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

1326-1522

1.36e-39

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: 146.40 E-value: 1.36e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRcFEKGREKCDQYWPNDTVPVfYGDIKVQILNDS 1405
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQ-LDPKDQSCPQYWPDEGSGT-YGPIQVEFVSTT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1406 HYADWVMTEFMLC---RGSEQ-RILRHFHFTTWPDFG-VPNPPQ---TLVRFVRAFRDRIGAEqrPIVVHCSAGVGRSGT 1477
Cdd:cd14556    79 IDEDVISRIFRLQnttRPQEGyRMVQQFQFLGWPRDRdTPPSKRallKLLSEVEKWQEQSGEG--PIVVHCLNGVGRSGV 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 442615984 1478 FITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQ 1522
Cdd:cd14556   157 FCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201

PTPc-N14

cd14599

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

1275-1529

1.90e-39

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: 149.38 E-value: 1.90e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1275 EFEELKHVGRDQPCTFADLPCNRPKNRFTNILPYDHSRFKLQPVDDDEgSDYINANYVPGHNSPRE--FIVTQGPLHSTR 1352
Cdd:cd14599    17 EYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENN-TGYINASHIKVTVGGEEwhYIATQGPLPHTC 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1353 DDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWP---NDTVPVFYGDIKV--QILNDSH-YADWVMTEFMLCRGSEqRIL 1426
Cdd:cd14599    96 HDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPklgSKHSSATYGKFKVttKFRTDSGcYATTGLKVKHLLSGQE-RTV 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1427 RHFHFTTWPDFGVPNPPQTLVRFVRAFR----------DRIGAEQRPIVVHCSAGVGRSGTFITLDRILQQINTSDYVDI 1496
Cdd:cd14599   175 WHLQYTDWPDHGCPEEVQGFLSYLEEIQsvrrhtnsmlDSTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEV 254

                         250       260       270
                  ....*....|....*....|....*....|...
gi 442615984 1497 FGIVYAMRKERVWMVQTEQQYICIHQCLLAVLE 1529
Cdd:cd14599   255 PVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

1246-1520

2.40e-37

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 142.92 E-value: 2.40e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1246 IEQNRPILIKNFAEHYRLmsadsdfRFSEEFEELKHVGRDQpcTFADLPCNRPKNRFTNILPYDHSRfkLQPVDDdegsd 1325
Cdd:COG5599     1 VSPKNPIAIKSEEEKINS-------RLSTLTNELAPSHNDP--QYLQNINGSPLNRFRDIQPYKETA--LRANLG----- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYVPGHNsPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFE--KGREKCDQYWPNDTVpvfYGDIKVQILN 1403
Cdd:COG5599    65 YLNANYIQVIG-NHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEisKPKVKMPVYFRQDGE---YGKYEVSSEL 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1404 DSHYAdwVMTEFML------CRGS--EQRILRHFHFTTWPDFGVPNPPQTLvrfvrAFRDRIGAEQR-------PIVVHC 1468
Cdd:COG5599   141 TESIQ--LRDGIEArtyvltIKGTgqKKIEIPVLHVKNWPDHGAISAEALK-----NLADLIDKKEKikdpdklLPVVHC 213

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442615984 1469 SAGVGRSGTFITLDRILQQINT--SDYVDIFGIVYAMRKERVW-MVQTEQQYICI 1520
Cdd:COG5599   214 RAGVGRTGTLIACLALSKSINAlvQITLSVEEIVIDMRTSRNGgMVQTSEQLDVL 268

PTPc_motif

smart00404

Protein tyrosine phosphatase, catalytic domain motif;

1425-1525

2.76e-37

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 136.33 E-value: 2.76e-37

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984   1425 ILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAEQR--PIVVHCSAGVGRSGTFITLDRILQQINTSDY-VDIFGIVY 1501
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                            90       100
                    ....*....|....*....|....
gi 442615984   1502 AMRKERVWMVQTEQQYICIHQCLL 1525
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALL 104

PTPc_DSPc

smart00012

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

1425-1525

2.76e-37

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

Pssm-ID: 214469 [Multi-domain] Cd Length: 105 Bit Score: 136.33 E-value: 2.76e-37

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984   1425 ILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAEQR--PIVVHCSAGVGRSGTFITLDRILQQINTSDY-VDIFGIVY 1501
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                            90       100
                    ....*....|....*....|....
gi 442615984   1502 AMRKERVWMVQTEQQYICIHQCLL 1525
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALL 104

PTPc_plant_PTP1

cd17658

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

1326-1518

4.09e-37

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: 139.52 E-value: 4.09e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYV--PGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGR-EKCDQYWP-NDTVPVFYGDIKVQI 1401
Cdd:cd17658     1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPaEENESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1402 LNDSHYADWVMTEFMLCRGSEQ----RILRHFHFTTWPDFGVPNPpqtlVRFVRAFRDR---IGAEQRPIVVHCSAGVGR 1474
Cdd:cd17658    81 KKLKHSQHSITLRVLEVQYIESeeppLSVLHIQYPEWPDHGVPKD----TRSVRELLKRlygIPPSAGPIVVHCSAGIGR 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 442615984 1475 SGTFITLDRILQQINTSDY--VDIFGIVYAMRKERVWMVQTEQQYI 1518
Cdd:cd17658   157 TGAYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYI 202

PHA02746

protein tyrosine phosphatase; Provisional

1294-1517

2.24e-36

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 141.32 E-value: 2.24e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1294 PCNRPKNRFTNILPYDHSRF-------------------KLQPVDDDEGSDYINANYVPGHNSPREFIVTQGPLHSTRDD 1354
Cdd:PHA02746   49 KENLKKNRFHDIPCWDHSRVvinaheslkmfdvgdsdgkKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSED 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1355 FWRMCWESNSRAIVMLTRcFEKGREKCDQYW--PNDTVPVFyGDIKVQILNDSHYADWVMTEFMLCRGSEQ--RILRHFH 1430
Cdd:PHA02746  129 FFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELAF-GRFVAKILDIIEELSFTKTRLMITDKISDtsREIHHFW 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1431 FTTWPDFGVPNPPQTLVRfvraFRDRIGAEQR--------------PIVVHCSAGVGRSGTFITLDRILQQINTSDYVDI 1496
Cdd:PHA02746  207 FPDWPDNGIPTGMAEFLE----LINKVNEEQAelikqadndpqtlgPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCL 282

                         250       260
                  ....*....|....*....|.
gi 442615984 1497 FGIVYAMRKERVWMVQTEQQY 1517
Cdd:PHA02746  283 GEIVLKIRKQRHSSVFLPEQY 303

R5-PTP-2

cd14550

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

1326-1509

1.21e-35

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

Pssm-ID: 350398 [Multi-domain] Cd Length: 200 Bit Score: 135.14 E-value: 1.21e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKgrEKCDQYWPNDTVPVFYGDIKVQILNDS 1405
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELN--EDEPIYWPTKEKPLECETFKVTLSGED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1406 H-----YADWVMTEFMLCRGSEQRIL--RHFHFTTWPDfgVPNPPQTLVRFVRAFRDRigAEQR--PIVVHCSAGVGRSG 1476
Cdd:cd14550    79 HsclsnEIRLIVRDFILESTQDDYVLevRQFQCPSWPN--PCSPIHTVFELINTVQEW--AQQRdgPIVVHDRYGGVQAA 154

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 442615984 1477 TFITLDRILQQINTSDYVDIFGIV--YAMRKERVW 1509
Cdd:cd14550   155 TFCALTTLHQQLEHESSVDVYQVAklYHLMRPGVF 189

R-PTPc-T-2

cd14634

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

1326-1525

1.93e-31

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: 123.21 E-value: 1.93e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCfeKGREKCDQYWPNDTvPVFYGDIKVQILNDS 1405
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKT-SCCYGPIQVEFVSAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1406 HYADWVMTEFMLCRGSEQ----RILRHFHFTTWPDFGvPNPPQ-----TLVRFVRAFRDRIGAEQRPIVVHCSAGVGRSG 1476
Cdd:cd14634    78 IDEDIISRIFRICNMARPqdgyRIVQHLQYIGWPAYR-DTPPSkrsilKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 442615984 1477 TFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLL 1525
Cdd:cd14634   157 TFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVAL 205

PTPc-N21

cd14598

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

1326-1529

2.59e-31

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.

Pssm-ID: 350446 [Multi-domain] Cd Length: 220 Bit Score: 123.55 E-value: 2.59e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYVPGHNSPRE--FIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWP-----NDTVPvfYGDIK 1398
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsrHNTVT--YGRFK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1399 VQI--LNDSH-YADWVMTEFMLCRGSEqRILRHFHFTTWPDFGVPNPpqtlVRFVRAFRDRIGAEQR------------- 1462
Cdd:cd14598    79 ITTrfRTDSGcYATTGLKIKHLLTGQE-RTVWHLQYTDWPEHGCPED----LKGFLSYLEEIQSVRRhtnstidpkspnp 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442615984 1463 PIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLLAVLE 1529
Cdd:cd14598   154 PVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220

R-PTP-Z-2

cd17669

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

1326-1525

5.72e-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: 104.69 E-value: 5.72e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCdQYWPNDTVPVFYGDIKVQILNDS 1405
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKDEPINCETFKVTLIAEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1406 HYA-----DWVMTEFMLCRGSEQRIL--RHFHFTTWPDfgvPNPP-QTLVRFVRAFRDRIGAEQRPIVVHCSAGVGRSGT 1477
Cdd:cd17669    80 HKClsneeKLIIQDFILEATQDDYVLevRHFQCPKWPN---PDSPiSKTFELISIIKEEAANRDGPMIVHDEHGGVTAGT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 442615984 1478 FITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLL 1525
Cdd:cd17669   157 FCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204

R-PTPc-K-2

cd14636

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

1326-1517

8.79e-23

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: 98.56 E-value: 8.79e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRC-FEKGrekCDQYWPNDTVpVFYGDIKVQILND 1404
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWPEEGM-LRYGPIQVECMSC 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1405 SHYADWVMTEFMLCRGSEQR----ILRHFHFTTWPDF-GVPNPPQTLVRF---VRAFRDRIGAEQRPIVVHCSAGVGRSG 1476
Cdd:cd14636    77 SMDCDVISRIFRICNLTRPQegylMVQQFQYLGWASHrEVPGSKRSFLKLilqVEKWQEECDEGEGRTIIHCLNGGGRSG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 442615984 1477 TFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQY 1517
Cdd:cd14636   157 MFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQY 197

R-PTPc-U-2

cd14637

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

1326-1529

2.15e-22

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: 97.29 E-value: 2.15e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGRE-KCDQYWPNDTVPVfYGDIKVQILND 1404
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQ-YGPMEVEFVSG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1405 SHYADWVMTEFM---LCRGSEQRIL-RHFHFTTWPDF-GVPNPPQTLVRFVrAFRDRIGAEQRP--IVVHCSAGVGRSGT 1477
Cdd:cd14637    80 SADEDIVTRLFRvqnITRLQEGHLMvRHFQFLRWSAYrDTPDSKKAFLHLL-ASVEKWQRESGEgrTVVHCLNGGGRSGT 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442615984 1478 FITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYiciHQCLLAVLE 1529
Cdd:cd14637   159 YCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQY---RFCYEIALE 207

R-PTP-G-2

cd17670

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

1326-1526

3.14e-21

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: 93.97 E-value: 3.14e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCdQYWPNDTVPVFYGDIKVQILND- 1404
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEF-VYWPSREESMNCEAFTVTLISKd 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1405 ----SHYADWVMTEFMLCRGSEQRIL--RHFHFTTWPDfgvPNPP-QTLVRFVRAFRDRIGAEQRPIVVHCSAGVGRSGT 1477
Cdd:cd17670    80 rlclSNEEQIIIHDFILEATQDDYVLevRHFQCPKWPN---PDAPiSSTFELINVIKEEALTRDGPTIVHDEFGAVSAGT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 442615984 1478 FITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLLA 1526
Cdd:cd17670   157 LCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205

R-PTPc-M-2

cd14635

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

1326-1517

6.88e-21

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: 92.83 E-value: 6.88e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1326 YINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCfeKGREKCDQYWPNDTVPVfYGDIKVQILNDS 1405
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENGVHR-HGPIQVEFVSAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1406 HYADWVMTEFMLCRGSEQ----RILRHFHFTTWPDF-GVPNPPQTLVRFVRAF----RDRIGAEQRpIVVHCSAGVGRSG 1476
Cdd:cd14635    78 LEEDIISRIFRIYNAARPqdgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVdkwqEEYNGGEGR-TVVHCLNGGGRSG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 442615984 1477 TFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQY 1517
Cdd:cd14635   157 TFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQY 197

PHA02740

protein tyrosine phosphatase; Provisional

1295-1535

1.12e-15

protein tyrosine phosphatase; Provisional

Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 80.01 E-value: 1.12e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1295 CNRPKNRF---TNILP---YDHSRFKLQpvdDDEgsDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIV 1368
Cdd:PHA02740   46 CAQAENKAkdeNLALHitrLLHRRIKLF---NDE--KVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1369 MLTRCFEKgreKC-DQYWP-NDTVPVFYGDIKVQILNDSHYADWVMTEFMLC--RGSEQRIlRHFHFTTWPDFGVPNPPQ 1444
Cdd:PHA02740  121 LISRHADK---KCfNQFWSlKEGCVITSDKFQIETLEIIIKPHFNLTLLSLTdkFGQAQKI-SHFQYTAWPADGFSHDPD 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1445 TLVRFVRAFRDRIGAEQR--------PIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQ 1516
Cdd:PHA02740  197 AFIDFFCNIDDLCADLEKhkadgkiaPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDD 276

                         250
                  ....*....|....*....
gi 442615984 1517 YICIHQCLLAVLEGKENIV 1535
Cdd:PHA02740  277 YVFCYHLIAAYLKEKFDIL 295

FN3

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

583-671

8.44e-14

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 68.68 E-value: 8.44e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  583 PNPPRNMTIETVRSNSVLVHWSPPES--GEFTEYSIRYRTDSEQQWVRL--PSVRSTEADITDMTKGEKYTIQVNTVSFG 658
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDdgGPITGYVVEYREKGSGDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|...
gi 442615984  659 VESPVPQEVNTTV 671
Cdd:cd00063    81 GESPPSESVTVTT 93

FN3

Fibronectin type 3 domain [General function prediction only];

552-704

8.57e-14

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 76.58 E-value: 8.57e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  552 NLQPGAGYELKVFAVSHDLRSEPHAYFQAVY----PNPPRNMTIETVRSNSVLVHWSPPESGEFTEYSIRYRTDSEQQWV 627
Cdd:COG3401   198 DIEPGTTYYYRVAATDTGGESAPSNEVSVTTpttpPSAPTGLTATADTPGSVTLSWDPVTESDATGYRVYRSNSGDGPFT 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  628 RLPSVRSTEADITDMTKGEKYTIQVNTV-SFGVESPVPQEVNTTV---PPNPVSNI-IQLVDSRNITLEW-PKPEGRVES 701
Cdd:COG3401   278 KVATVTTTSYTDTGLTNGTTYYYRVTAVdAAGNESAPSNVVSVTTdltPPAAPSGLtATAVGSSSITLSWtASSDADVTG 357


                  ...
gi 442615984  702 YIL 704
Cdd:COG3401   358 YNV 360

fn3

Fibronectin type III domain;

585-662

8.90e-13

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 65.51 E-value: 8.90e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984   585 PPRNMTIETVRSNSVLVHWSPPE--SGEFTEYSIRYRT-DSEQQWVRLPSVRST-EADITDMTKGEKYTIQVNTVSFGVE 660
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgNGPITGYEVEYRPkNSGEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ..
gi 442615984   661 SP 662
Cdd:pfam00041   82 GP 83

FN3

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

583-661

4.54e-11

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 60.71 E-value: 4.54e-11

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984    583 PNPPRNMTIETVRSNSVLVHWSPPESGEFTEYSIRYR---TDSEQQWVRLP-SVRSTEADITDMTKGEKYTIQVNTVSFG 658
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRveyREEGSEWKEVNvTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 442615984    659 VES 661
Cdd:smart00060   81 GEG 83

FN3

Fibronectin type 3 domain [General function prediction only];

278-734

5.14e-11

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 67.72 E-value: 5.14e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  278 AFKGLVPGRAYNISVQTMSEDEISLPTTAQYRTVPLRPLNVTFDRDFITSNSFRVLW-EAPKGISEFDKYQVSVATTRRQ 356
Cdd:COG3401     9 LDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGgLGTGGRAGTTSGVAAVAVAAAP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  357 STVPRSNEPVAFFDFRDIAEPGKTFNVIVKTVSGkvtSWPATGDVTLRPLPVRNLRSINDDKTNTMIITWEADPASTQdE 436
Cdd:COG3401    89 PTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAV---GTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSV-A 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  437 YRIVYHELETFNGDTSTLTTDRTRFTLES-----LLPGRNYSLSVQAVSKKMESNETSIFVVTR----PSSPiiEDLKSI 507
Cdd:COG3401   165 GAGVVVSPDTSATAAVATTSLTVTSTTLVdgggdIEPGTTYYYRVAATDTGGESAPSNEVSVTTpttpPSAP--TGLTAT 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  508 RMGLN---ISWKSDVNSKQEQYEVLYSRNGTSDLRT-QKTKESRLVIKNLQPGAGYELKVFAVSHD-LRSEPHAYFQAV- 581
Cdd:COG3401   243 ADTPGsvtLSWDPVTESDATGYRVYRSNSGDGPFTKvATVTTTSYTDTGLTNGTTYYYRVTAVDAAgNESAPSNVVSVTt 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  582 ---YPNPPRNMTIETVRSNSVLVHWSPPESGEFTEYSIRYRTDSEQQWVRL-PSVRSTEADITDMTKGEKYTIQVNTV-S 656
Cdd:COG3401   323 dltPPAAPSGLTATAVGSSSITLSWTASSDADVTGYNVYRSTSGGGTYTKIaETVTTTSYTDTGLTPGTTYYYKVTAVdA 402

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442615984  657 FGVESPVPQEVNTTVPPNPVSNIIQLVdsrniTLEWPKPEGRVESYILKWWPSDNPGRVQTKNVSENKSADDLSTVRV 734
Cdd:COG3401   403 AGNESAPSEEVSATTASAASGESLTAS-----VDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSS 475

PTP_tm

pfam18861

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

1083-1187

7.29e-11

Pssm-ID: 465889 Cd Length: 126 Bit Score: 61.47 E-value: 7.29e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  1083 FSDQNGQVRMYTIIVAEDDAKNASGLEMPSwldvQSYSVWLpYQAIDPY--YPFENRSVE--------DFTIGTENCDNh 1152
Cdd:pfam18861    6 FNSSNGPIKAYGVIVTTNDSLNRPLKEYLN----KTYYDWK-YKKTDSYlaTVTPNPFTSprsssrslTVPVGTGSKWQ- 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 442615984  1153 kiGYCNGPLKSGTTYRVKVRAFT------GADKFTDTAYSF 1187
Cdd:pfam18861   80 --GYCNGPLKPLGSYRFSVAAFTrlefddGLIDGEESYVSF 118

PTP_YopH-like

cd14559

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

1300-1526

3.53e-10

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: 62.03 E-value: 3.53e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1300 NRFTNIlpydHSRFKLQpvdDDEGsdyINANYVPGHNSPReFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGRE 1379
Cdd:cd14559     1 NRFTNI----QTRVSTP---VGKN---LNANRVQIGNKNV-AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRK 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1380 KCDQYW-PNDTvpvfYGDIKVQILNDSHYADWVMTEF----MLCRGSEQRI-LRHFHFTTWPDFGVPNPPQT--LVRFVR 1451
Cdd:cd14559    70 GLPPYFrQSGT----YGSVTVKSKKTGKDELVDGLKAdmynLKITDGNKTItIPVVHVTNWPDHTAISSEGLkeLADLVN 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1452 AFRD--RIGAEQRPI-----------VVHCSAGVGRSGTFITLDRILQQINTSDYVDifgIVYAMRKER-VWMVQTEQQY 1517
Cdd:cd14559   146 KSAEekRNFYKSKGSsaindknkllpVIHCRAGVGRTGQLAAAMELNKSPNNLSVED---IVSDMRTSRnGKMVQKDEQL 222


                  ....*....
gi 442615984 1518 icihQCLLA 1526
Cdd:cd14559   223 ----DTLKE 227

fn3

Fibronectin type III domain;

959-1043

7.84e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 57.04 E-value: 7.84e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984   959 GRVERFHPTDVQPSEINFEWSlPSSEANGVIRQFSIAYTNINNLTDAGMQDFESEEAFGVIKNLKPGETYVFKIQAKTAI 1038
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWT-PPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*
gi 442615984  1039 GFGPE 1043
Cdd:pfam00041   80 GEGPP 84

fn3

Fibronectin type III domain;

866-935

2.14e-09

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 55.88 E-value: 2.14e-09

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442615984   866 PITQLHATNITDTEISLRWDLPK---GEYNDFDIAYLTADNLLAQNMTT----RNEITISDLRPHRNYTFTVVVRSG 935
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITvpgtTTSVTLTGLKPGTEYEVRVQAVNG 78

fn3

Fibronectin type III domain;

220-304

6.27e-09

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 54.73 E-value: 6.27e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984   220 PGKFIVWFRNETTLLVLWQPP-YPAGIYTHYKVSIEPPDANDSVLYVEkegEPPGPAQAAFKGLVPGRAYNISVQTMSED 298
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPpDGNGPITGYEVEYRPKNSGEPWNEIT---VPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*.
gi 442615984   299 EISLPT 304
Cdd:pfam00041   80 GEGPPS 85

CDC14

COG2453

Protein-tyrosine phosphatase [Signal transduction mechanisms];

1422-1517

1.05e-08

Protein-tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 55.75 E-value: 1.05e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1422 EQRILRHFHFTtWPDFGVPNPPQtLVRFVRAFRDRIgAEQRPIVVHCSAGVGRSGTF---------ITLDRILQQIntsd 1492
Cdd:COG2453    44 EEAGLEYLHLP-IPDFGAPDDEQ-LQEAVDFIDEAL-REGKKVLVHCRGGIGRTGTVaaaylvllgLSAEEALARV---- 116

                          90       100
                  ....*....|....*....|....*
gi 442615984 1493 yvdifgivyamRKERVWMVQTEQQY 1517
Cdd:COG2453   117 -----------RAARPGAVETPAQR 130

FN3

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

405-494

1.97e-08

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 53.65 E-value: 1.97e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  405 PLPVRNLRsINDDKTNTMIITWEA--DPASTQDEYRIVYHELETFNGDT-STLTTDRTRFTLESLLPGRNYSLSVQAVSK 481
Cdd:cd00063     1 PSPPTNLR-VTDVTSTSVTLSWTPpeDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                          90
                  ....*....|...
gi 442615984  482 KMESNETSIFVVT 494
Cdd:cd00063    80 GGESPPSESVTVT 92

fn3

Fibronectin type III domain;

407-488

4.17e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 52.42 E-value: 4.17e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984   407 PVRNLRsINDDKTNTMIITWEA--DPASTQDEYRIVYHELETFNGDTS-TLTTDRTRFTLESLLPGRNYSLSVQAVSKKM 483
Cdd:pfam00041    2 APSNLT-VTDVTSTSLTVSWTPppDGNGPITGYEVEYRPKNSGEPWNEiTVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 442615984   484 ESNET 488
Cdd:pfam00041   81 EGPPS 85

fn3

Fibronectin type III domain;

124-205

6.04e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 52.03 E-value: 6.04e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984   124 DPPSNLSVQVRSGKNAIILWSPPTQGS--YTAFKIKVLGLSEasSSYNRTFQVNDNTFQHSVKELTPGATYQVQAYTIYD 201
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNgpITGYEVEYRPKNS--GEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78


                   ....
gi 442615984   202 GKES 205
Cdd:pfam00041   79 GGEG 82

FN3

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

405-485

1.26e-07

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 51.08 E-value: 1.26e-07

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984    405 PLPVRNLRSINDDKTnTMIITWEADPASTQDEYRIVYHELETFNGD---TSTLTTDRTRFTLESLLPGRNYSLSVQAVSK 481
Cdd:smart00060    1 PSPPSNLRVTDVTST-SVTLSWEPPPDDGITGYIVGYRVEYREEGSewkEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 442615984    482 KMES 485
Cdd:smart00060   80 AGEG 83

PTP_DSP_cys

cd14494

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

1446-1522

2.27e-07

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: 51.20 E-value: 2.27e-07

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442615984 1446 LVRFVRAFRDRIGAEQRPIVVHCSAGVGRSGTFITLDRILQQINTSDyvDIFGIVYAMRKERvwMVQTEQQYICIHQ 1522
Cdd:cd14494    41 MVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAE--EAVRIVRLIRPGG--IPQTIEQLDFLIK 113

FN3

Fibronectin type 3 domain [General function prediction only];

639-1199

2.64e-07

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 55.78 E-value: 2.64e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  639 ITDMTKGEKYTIQVNTVSFGVESPVPQEVNTTVPPNPVSNIIQLVDSRNITLEWPKPEGRVESYILKWWPSDNPGRVQTK 718
Cdd:COG3401     6 LTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  719 NVSENKSADDLSTVRVLIGELMPGVQYKFDIQTTSYGILSGITSLYPRTMPLIQSDVVVANgeKEDERDTITLSYTPTPQ 798
Cdd:COG3401    86 AAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAG--LYGVDGANASGTTASSV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  799 SSSKFDIYRFSLGDAEIRDKEKLANDTDRKVTFTGLVPGRLYNITVWTVSGGVASLPIQR----QDRLYPEPITQLHATN 874
Cdd:COG3401   164 AGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEvsvtTPTTPPSAPTGLTATA 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  875 ITDTEISLRWDLPKGEYND-FDIAYLTADN----LLAQnmTTRNEITISDLRPHRNYTFTVVV--RSGTESSvlrSSSPL 947
Cdd:COG3401   244 DTPGSVTLSWDPVTESDATgYRVYRSNSGDgpftKVAT--VTTTSYTDTGLTNGTTYYYRVTAvdAAGNESA---PSNVV 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  948 SAsfTTNEAVPGRVERFHPTDVQPSEINFEWSlPSSEANgvIRQFSIAYTNINNLTDAGMQDFESEEAFgVIKNLKPGET 1027
Cdd:COG3401   319 SV--TTDLTPPAAPSGLTATAVGSSSITLSWT-ASSDAD--VTGYNVYRSTSGGGTYTKIAETVTTTSY-TDTGLTPGTT 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1028 YVFKIQAKTAIGFGPER-EYRQTMPILAPPRPATQVVPTEVYR---SSSTIQIRFRKNYfSDQNGQVRMYTIIVAEDDAK 1103
Cdd:COG3401   393 YYYKVTAVDAAGNESAPsEEVSATTASAASGESLTASVDAVPLtdvAGATAAASAASNP-GVSAAVLADGGDTGNAVPFT 471

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1104 NASGLEMPSWLDVQSYSVWLPYQAIDPYYPFENRSVEDFTIGTENCDNHKIGYcNGPLKSGTTYRVKVRAFTGADKFTDT 1183
Cdd:COG3401   472 TTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAP-DGTPNVTGASPVTVGASTGDVLITDL 550

                         570
                  ....*....|....*.
gi 442615984 1184 AYSFPIQTDQDNTSLI 1199
Cdd:COG3401   551 VSLTTSASSSVSGAGL 566

FN3

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

864-939

6.60e-07

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 49.03 E-value: 6.60e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  864 PEPITQLHATNITDTEISLRWDLPKGEYNDFD---IAYLTADNLLAQNMT----TRNEITISDLRPHRNYTFTVVVRSGT 936
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITgyvVEYREKGSGDWKEVEvtpgSETSYTLTGLKPGTEYEFRVRAVNGG 80


                  ...
gi 442615984  937 ESS 939
Cdd:cd00063    81 GES 83

FN3

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

123-205

7.05e-07

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 48.76 E-value: 7.05e-07

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984    123 PDPPSNLSVQVRSGKNAIILWSPPTQGSYTAFKIKVLGLSEASSSYNRTFQVNDNTFQHSVKELTPGATYQVQAYTIYDG 202
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 442615984    203 KES 205
Cdd:smart00060   81 GEG 83

FN3

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

958-1042

1.34e-06

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 48.26 E-value: 1.34e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  958 PGRVERFHPTDVQPSEINFEWSLPSSEaNGVIRQFSIAYTNINNLTDAGMQDFESEEAFGVIKNLKPGETYVFKIQAKTA 1037
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDD-GGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79


                  ....*
gi 442615984 1038 IGFGP 1042
Cdd:cd00063    80 GGESP 84

FN3

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

123-215

2.05e-06

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 47.88 E-value: 2.05e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  123 PDPPSNLSVQVRSGKNAIILWSPP--TQGSYTAFKIKVLGLSEASSSYNRTFQVNDNTFQhsVKELTPGATYQVQAYTIY 200
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPedDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYT--LTGLKPGTEYEFRVRAVN 78

                          90
                  ....*....|....*
gi 442615984  201 DGKESVAYTSRNFTT 215
Cdd:cd00063    79 GGGESPPSESVTVTT 93

FN3

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

864-939

3.12e-06

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 46.84 E-value: 3.12e-06

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984    864 PEPITQLHATNITDTEISLRWDLPKGEYNDFDIAYLT-------ADNLLAQNMTTRNEITISDLRPHRNYTFTVVVRSGT 936
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRveyreegSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 442615984    937 ESS 939
Cdd:smart00060   81 GEG 83

fn3

Fibronectin type III domain;

683-751

3.74e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 46.64 E-value: 3.74e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442615984   683 VDSRNITLEWPKPE---GRVESYILKWWPSDNPGRVQTKNVSENksaddlsTVRVLIGELMPGVQYKFDIQT 751
Cdd:pfam00041   11 VTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITVPGT-------TTSVTLTGLKPGTEYEVRVQA 75

FN3

Fibronectin type 3 domain [General function prediction only];

48-410

6.25e-06

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 51.16 E-value: 6.25e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984   48 SIPNNPGLDDGASYRLDYSPPFGYPEPNTTIASREIGDEIQfsRALPGTKYNFWLYYTNFTHHDWLTWTVTIT---TAPD 124
Cdd:COG3401   157 GTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGG--DIEPGTTYYYRVAATDTGGESAPSNEVSVTtptTPPS 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  125 PPSNLSVQVRSGKNAIILWSPPTQGSYTAFKIKVlglseaSSSYNRTFQ----VNDNTFQhsVKELTPGATY--QVQAYT 198
Cdd:COG3401   235 APTGLTATADTPGSVTLSWDPVTESDATGYRVYR------SNSGDGPFTkvatVTTTSYT--DTGLTNGTTYyyRVTAVD 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  199 iYDGKES----VAYTSRNfTTKPNTPGKFIVWFRNETTLLVLWQPPYPAGIyTHYKV--SIEPPDANDSVlyvekeGEPP 272
Cdd:COG3401   307 -AAGNESapsnVVSVTTD-LTPPAAPSGLTATAVGSSSITLSWTASSDADV-TGYNVyrSTSGGGTYTKI------AETV 377

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  273 GPAQAAFKGLVPGRAYNISVQTMSEDEISLPTTAQYRTVPLRPLN-------VTFDRDFITSNSFRVLWEAPKGISEFDK 345
Cdd:COG3401   378 TTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASgesltasVDAVPLTDVAGATAAASAASNPGVSAAV 457

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442615984  346 YQVSVATTRRQSTVPRSNEPVAFFDFRDIAEPGKTFNVIVKTVSGKVTSWPATGDVTLRPLPVRN 410
Cdd:COG3401   458 LADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGG 522

FN3

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

217-305

6.60e-06

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 46.34 E-value: 6.60e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  217 PNTPGKFIVWFRNETTLLVLWQPP-YPAGIYTHYKVSIEPPDANDSVLYVEKEGEPPgpaQAAFKGLVPGRAYNISVQTM 295
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPeDDGGPITGYVVEYREKGSGDWKEVEVTPGSET---SYTLTGLKPGTEYEFRVRAV 77

                          90
                  ....*....|
gi 442615984  296 SEDEISLPTT 305
Cdd:cd00063    78 NGGGESPPSE 87

DUSP23

cd14504

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

1435-1479

8.11e-06

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: 47.27 E-value: 8.11e-06

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 442615984 1435 PDFGVPNPPQtLVRFVRAFRDRIgAEQRPIVVHCSAGVGRSGTFI 1479
Cdd:cd14504    58 EDYTPPTLEQ-IDEFLDIVEEAN-AKNEAVLVHCLAGKGRTGTML 100

FN3

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

958-1041

3.82e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 43.76 E-value: 3.82e-05

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984    958 PGRVERFHPTDVQPSEINFEWSLPSSE-ANGVIRQFSIAYTNINNLTDAGMQDFESEEAfgVIKNLKPGETYVFKIQAKT 1036
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDgITGYIVGYRVEYREEGSEWKEVNVTPSSTSY--TLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 442615984   1037 AIGFG 1041
Cdd:smart00060   79 GAGEG 83

FN3

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

511-574

3.94e-05

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 44.02 E-value: 3.94e-05

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442615984  511 LNISWK--SDVNSKQEQYEVLYSRNGTSD---LRTQKTKESRLVIKNLQPGAGYELKVFAVSHDLRSEP 574
Cdd:cd00063    17 VTLSWTppEDDGGPITGYVVEYREKGSGDwkeVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPP 85

fn3

Fibronectin type III domain;

315-391

8.29e-05

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 42.79 E-value: 8.29e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984   315 PLNVTFDrdFITSNSFRVLWEAPK-GISEFDKYQVSVATTRRQSTVPRSNEP--VAFFDFRDIaEPGKTFNVIVKTVSGK 391
Cdd:pfam00041    3 PSNLTVT--DVTSTSLTVSWTPPPdGNGPITGYEVEYRPKNSGEPWNEITVPgtTTSVTLTGL-KPGTEYEVRVQAVNGG 79

CDKN3-like

cd14505

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

1405-1522

1.01e-04

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: 44.95 E-value: 1.01e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1405 SHYADWVMTefmLCRGSE---------QRILRHFHFTTW----PDFGVPNPPQTLVRFVRAFRDRIGAEQRpIVVHCSAG 1471
Cdd:cd14505    41 DQGVDDVVT---LCTDGEleelgvpdlLEQYQQAGITWHhlpiPDGGVPSDIAQWQELLEELLSALENGKK-VLIHCKGG 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442615984 1472 VGRSGTFITldRILQQIN-TSDYVDIFGIVYAMRKeRVwmVQTEQQYICIHQ 1522
Cdd:cd14505   117 LGRTGLIAA--CLLLELGdTLDPEQAIAAVRALRP-GA--IQTPKQENFLHQ 163

fn3

Fibronectin type III domain;

511-575

1.31e-04

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 42.40 E-value: 1.31e-04

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984   511 LNISWK--SDVNSKQEQYEVLYS-RNGTSDLRTQKTK--ESRLVIKNLQPGAGYELKVFAVSHDLRSEPH 575
Cdd:pfam00041   16 LTVSWTppPDGNGPITGYEVEYRpKNSGEPWNEITVPgtTTSVTLTGLKPGTEYEVRVQAVNGGGEGPPS 85

fn3

Fibronectin type III domain;

787-850

3.30e-04

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 41.25 E-value: 3.30e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442615984   787 DTITLSYTPTPQSSSKFDIYR--FSLGDAEIRDKEKLANDTDRKVTFTGLVPGRLYNITVWTVSGG 850
Cdd:pfam00041   14 TSLTVSWTPPPDGNGPITGYEveYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

FN3

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

673-758

5.23e-04

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 40.94 E-value: 5.23e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984  673 PNPVSNI-IQLVDSRNITLEWPKPE---GRVESYILKWWPSDNPGRVQTKNVSENKSaddlstvRVLIGELMPGVQYKFD 748
Cdd:cd00063     1 PSPPTNLrVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSET-------SYTLTGLKPGTEYEFR 73

                          90
                  ....*....|
gi 442615984  749 IQTTSYGILS 758
Cdd:cd00063    74 VRAVNGGGES 83

PTP_PTPDC1

cd14506

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

1429-1521

5.49e-04

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

Pssm-ID: 350356 [Multi-domain] Cd Length: 206 Bit Score: 43.49 E-value: 5.49e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984 1429 FHFTTWPDFGVPnPPQTLVRFVRAFrDRIGAEQRPIVVHCSAGVGRSGTFITLDRI-LQQINTSDYVDIFgivyamRKER 1507
Cdd:cd14506    79 FYNFGWKDYGVP-SLTTILDIVKVM-AFALQEGGKVAVHCHAGLGRTGVLIACYLVyALRMSADQAIRLV------RSKR 150

                          90
                  ....*....|....
gi 442615984 1508 VWMVQTEQQYICIH 1521
Cdd:cd14506   151 PNSIQTRGQVLCVR 164

FN3

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

672-747

1.14e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 39.91 E-value: 1.14e-03

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442615984    672 PPNPVSNIIQLVDSRNITLEW-PKPEGRVESYILKWWPSDNPGRVQTKNVSENKSaddlsTVRVLIGELMPGVQYKF 747
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWePPPDDGITGYIVGYRVEYREEGSEWKEVNVTPS-----STSYTLTGLKPGTEYEF 72

FN3

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

217-301

1.28e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 39.52 E-value: 1.28e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615984    217 PNTPGKFIVWFRNETTLLVLWQPPYPAGIyTHYKVSIEPPDANDSVLYVEKEGEPPGPaQAAFKGLVPGRAYNISVQTMS 296
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGI-TGYIVGYRVEYREEGSEWKEVNVTPSST-SYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 442615984    297 EDEIS 301
Cdd:smart00060   79 GAGEG 83

FN3

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

782-857

2.54e-03

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 39.02 E-value: 2.54e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442615984  782 KEDERDTITLSYTPTPQSSSKFDIYRFSLGDAEIRDKEKLAND--TDRKVTFTGLVPGRLYNITVWTVSGGVASLPIQ 857
Cdd:cd00063    10 TDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTpgSETSYTLTGLKPGTEYEFRVRAVNGGGESPPSE 87

FN3

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

786-850

4.72e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 37.98 E-value: 4.72e-03

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442615984    786 RDTITLSYTPTPQSSSKFDIYRFSLGDAEIRDKEKLAN--DTDRKVTFTGLVPGRLYNITVWTVSGG 850
Cdd:smart00060   14 STSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNvtPSSTSYTLTGLKPGTEYEFRVRAVNGA 80

FN3