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Conserved domains on  [gi|665389652|ref|NP_001284875|]
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protein tyrosine phosphatase 4E, isoform H [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1358-1579 2.31e-134

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


:

Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 416.37  E-value: 2.31e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1358 RFTNILPYDHSRFKLQPVDDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREK 1437
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1438 CDQYWPVDRVAMFYGDIKVQLIIDTHYHDWSISEFMVSRNCESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTD 1517
Cdd:cd14548    81 CDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIKQE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665389652 1518 MRPIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQ 1579
Cdd:cd14548   161 KGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
fn3 pfam00041
Fibronectin type III domain;
902-978 8.82e-11

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.74  E-value: 8.82e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   902 PISDLKAIQVAAREITLHWTAPA---GEYTDFELQYLSADEEAPQLLQNVTKNT-EITLQGLRPYHNYTFTVVVRSGSIQ 977
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   .
gi 665389652   978 G 978
Cdd:pfam00041   82 G 82
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
319-749 1.01e-10

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 66.56  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  319 VQTVSEDETSSVPTTARYLTVPERVLNVTFDEAYTTSSSFRVRWEP-PRTYSEFDAYQVMLS--TSRRIFNVPRAANGDS 395
Cdd:COG3401    26 LSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGrAGTTSGVAAVAVAAAppTATGLTTLTGSGSVGG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  396 VYFDYPDILEPGRTYEVVVKTIADNVNSWPASGEVTLRPRPVRSLGGFLDDRSNALHISWEPAETGRQDSYrisyheqtn 475
Cdd:COG3401   106 ATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSA--------- 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  476 asevPAPFPVAAESQITTNLTEYTLDsLLAGRRYLIAVQALSKGVASNASD----ITRYTRPAAPliQELRSIDQG---L 548
Cdd:COG3401   177 ----TAAVATTSLTVTSTTLVDGGGD-IEPGTTYYYRVAATDTGGESAPSNevsvTTPTTPPSAP--TGLTATADTpgsV 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  549 MLSWRSDVNSRQDRYEVhYQRNGTREERTM--ATNETSLTIHYLHPGSGYEVKVHAI-SHGVRSEPHSYFQAV----FPK 621
Cdd:COG3401   250 TLSWDPVTESDATGYRV-YRSNSGDGPFTKvaTVTTTSYTDTGLTNGTTYYYRVTAVdAAGNESAPSNVVSVTtdltPPA 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  622 PPQNLTLQTVHTNLVVLHWQAPEGSDFSEYVVrYRTDAS--PWQRI-SGLHENEARIKDMHYGERYLVQVNTV-SFGVES 697
Cdd:COG3401   329 APSGLTATAVGSSSITLSWTASSDADVTGYNV-YRSTSGggTYTKIaETVTTTSYTDTGLTPGTTYYYKVTAVdAAGNES 407

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665389652  698 PHPLELNVTMPPQPVSNVVPLVdsrnlTLEWPRPDGHVDFYTLKWWPTDEED 749
Cdd:COG3401   408 APSEEVSATTASAASGESLTAS-----VDAVPLTDVAGATAAASAASNPGVS 454
fn3 pfam00041
Fibronectin type III domain;
247-328 7.26e-10

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.04  E-value: 7.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   247 PGKFIVWFRNETTLLVLWQPPFPA-GIYTHYRVSITPDDAIQSVLYVEregEPPGPAQAAFKGLVPGREYNISVQTVSED 325
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPPDGnGPITGYEVEYRPKNSGEPWNEIT---VPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ...
gi 665389652   326 ETS 328
Cdd:pfam00041   80 GEG 82
fn3 pfam00041
Fibronectin type III domain;
1013-1092 1.25e-09

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 56.65  E-value: 1.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  1013 FQPSDVQPGEVTFEWSlEPAEQHGPIDYFRITCQNADDAADVSSYEFPVNATQGKIDGLVPGNHYIFRIQAKSALGYGAE 1092
Cdd:pfam00041    6 LTVTDVTSTSLTVSWT-PPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
PTP_tm super family cl40142
TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases ...
 1127-1247 1.70e-09

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: 57.23  E-value: 1.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  1127 FRQGYFSNAHGMVRSYTIIIAEDVGKNASGLEMPS--WQD-----VQAY-TVWLPyqaiepyNPFlTSNGSRKSSLEAEh 1198
Cdd:pfam18861    1 IQFSLFNSSNGPIKAYGVIVTTNDSLNRPLKEYLNktYYDwkykkTDSYlATVTP-------NPF-TSPRSSSRSLTVP- 71

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  1199 ftIGTANCDKhqaGYCNGPLRAGTTYRIKIRAFTD-----------EDKFTDTVYSSPIT 1247
Cdd:pfam18861   72 --VGTGSKWQ---GYCNGPLKPLGSYRFSVAAFTRlefddglidgeESYVSFTPFSEPIA 126
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
94-334 7.34e-08

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 57.32  E-value: 7.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   94 SPPFGFPEPNTTIPASDIGKDIKFSRALPGTEYNFWLYYTNSTHREQLTWTVNIT---TAPDPPANLSVQLRSSKSAFIT 170
Cdd:COG3401   173 DTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTtptTPPSAPTGLTATADTPGSVTLS 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  171 WRPPGSGRYSGFRIRVLGLTDLPFERSYSLEGNEtlqLSAKELTPGGSY--QVQAYSvYQGKES----VAYTSRNfTTKP 244
Cdd:COG3401   253 WDPVTESDATGYRVYRSNSGDGPFTKVATVTTTS---YTDTGLTNGTTYyyRVTAVD-AAGNESapsnVVSVTTD-LTPP 327

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  245 NTPGKFIVWFRNETTLLVLWQPPFPAGIyTHYRV--SITPDDAIQSVlyvereGEPPGPAQAAFKGLVPGREYNISVQTV 322
Cdd:COG3401   328 AAPSGLTATAVGSSSITLSWTASSDADV-TGYNVyrSTSGGGTYTKI------AETVTTTSYTDTGLTPGTTYYYKVTAV 400

                         250
                  ....*....|..
gi 665389652  323 SEDETSSVPTTA 334
Cdd:COG3401   401 DAAGNESAPSEE 412
fn3 pfam00041
Fibronectin type III domain;
708-796 3.45e-07

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 49.72  E-value: 3.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   708 PPQPVSnVVPlVDSRNLTLEWPRP---DGHVDFYTLKWWPTDEEDrvefknVTQLEDLSSPSVRIPIEDLSPGRQYRFEV 784
Cdd:pfam00041    2 APSNLT-VTD-VTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGE------PWNEITVPGTTTSVTLTGLKPGTEYEVRV 73

                           90
                   ....*....|..
gi 665389652   785 QASSNGIRSGTT 796
Cdd:pfam00041   74 QAVNGGGEGPPS 85
 
Name Accession Description Interval E-value
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1358-1579 2.31e-134

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 416.37  E-value: 2.31e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1358 RFTNILPYDHSRFKLQPVDDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREK 1437
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1438 CDQYWPVDRVAMFYGDIKVQLIIDTHYHDWSISEFMVSRNCESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTD 1517
Cdd:cd14548    81 CDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIKQE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665389652 1518 MRPIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQ 1579
Cdd:cd14548   161 KGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1329-1582 2.79e-110

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 351.19  E-value: 2.79e-110
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   1329 FSEEFEELKHVGR-DQACSFANLPCNRPKNRFTNILPYDHSRFKLQPvDDDDGSDYINANYMPGHNSPREFIVTQGPLHS 1407
Cdd:smart00194    2 LEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKP-PPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   1408 TREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPVD-RVAMFYGDIKVQLIIDTHYHDWSISEFMVSRNC--ESRIMR 1484
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGcsETRTVT 160

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   1485 HFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDMRPIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKER 1564
Cdd:smart00194  161 HYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQR 240

                           250
                    ....*....|....*...
gi 665389652   1565 VFMVQTEQQYVCIHQCLL 1582
Cdd:smart00194  241 PGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1353-1582 6.18e-103

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 329.20  E-value: 6.18e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  1353 NRPKNRFTNILPYDHSRFKLQpvDDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFE 1432
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  1433 KGREKCDQYWPVDR-VAMFYGDIKVQLI-IDTHYHDWSISEFMVSRNC--ESRIMRHFHFTTWPDFGVPEPPQSLVRFVR 1508
Cdd:pfam00102   79 KGREKCAQYWPEEEgESLEYGDFTVTLKkEKEDEKDYTVRTLEVSNGGseETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665389652  1509 AFRDVIGTDMR-PIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLL 1582
Cdd:pfam00102  159 KVRKSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1353-1586 2.49e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 157.86  E-value: 2.49e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1353 NRPKNRFTNILPYDHSRFKLQPvdDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFE 1432
Cdd:PHA02742   52 NMKKCRYPDAPCFDRNRVILKI--EDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1433 KGREKCDQYW-PVDRVAMFYGDIKVQLIIDTHYHDWSISEFMVSRNCESRIM--RHFHFTTWPDFGVPEPPQSLVRFVRA 1509
Cdd:PHA02742  130 DGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLdiKHFAYEDWPHGGLPRDPNKFLDFVLA 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1510 FRDVIGT-----------DMRPIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCih 1578
Cdd:PHA02742  210 VREADLKadvdikgenivKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF-- 287


                  ....*...
gi 665389652 1579 qCLLAVLE 1586
Cdd:PHA02742  288 -CYFIVLI 294
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1303-1577 3.00e-35

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 136.76  E-value: 3.00e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1303 ITPNRPVHVKDFSEHYRImsadsdfRFSEEFEELKHVGRDQacSFANLPCNRPKNRFTNILPYDHSRfklqpVDDDDGsd 1382
Cdd:COG5599     1 VSPKNPIAIKSEEEKINS-------RLSTLTNELAPSHNDP--QYLQNINGSPLNRFRDIQPYKETA-----LRANLG-- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANYMPGHNsPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFE--KGREKCDQYWPVD-RVAMFygDIKVQLI 1459
Cdd:COG5599    65 YLNANYIQVIG-NHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEisKPKVKMPVYFRQDgEYGKY--EVSSELT 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1460 ----IDTHYHdwsISEFMVSRNC---ESRIMRHFHFTTWPDFGVPEPPQ--SLVRFVRAFRDVIGTDMRPIIVHCSAGVG 1530
Cdd:COG5599   142 esiqLRDGIE---ARTYVLTIKGtgqKKIEIPVLHVKNWPDHGAISAEAlkNLADLIDKKEKIKDPDKLLPVVHCRAGVG 218

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 665389652 1531 RSGTFIALDRILQHI--HKSDYVDIFGIVFAMRKER-VFMVQTEQQYVCI 1577
Cdd:COG5599   219 RTGTLIACLALSKSInaLVQITLSVEEIVIDMRTSRnGGMVQTSEQLDVL 268
fn3 pfam00041
Fibronectin type III domain;
902-978 8.82e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.74  E-value: 8.82e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   902 PISDLKAIQVAAREITLHWTAPA---GEYTDFELQYLSADEEAPQLLQNVTKNT-EITLQGLRPYHNYTFTVVVRSGSIQ 977
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   .
gi 665389652   978 G 978
Cdd:pfam00041   82 G 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
319-749 1.01e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 66.56  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  319 VQTVSEDETSSVPTTARYLTVPERVLNVTFDEAYTTSSSFRVRWEP-PRTYSEFDAYQVMLS--TSRRIFNVPRAANGDS 395
Cdd:COG3401    26 LSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGrAGTTSGVAAVAVAAAppTATGLTTLTGSGSVGG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  396 VYFDYPDILEPGRTYEVVVKTIADNVNSWPASGEVTLRPRPVRSLGGFLDDRSNALHISWEPAETGRQDSYrisyheqtn 475
Cdd:COG3401   106 ATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSA--------- 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  476 asevPAPFPVAAESQITTNLTEYTLDsLLAGRRYLIAVQALSKGVASNASD----ITRYTRPAAPliQELRSIDQG---L 548
Cdd:COG3401   177 ----TAAVATTSLTVTSTTLVDGGGD-IEPGTTYYYRVAATDTGGESAPSNevsvTTPTTPPSAP--TGLTATADTpgsV 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  549 MLSWRSDVNSRQDRYEVhYQRNGTREERTM--ATNETSLTIHYLHPGSGYEVKVHAI-SHGVRSEPHSYFQAV----FPK 621
Cdd:COG3401   250 TLSWDPVTESDATGYRV-YRSNSGDGPFTKvaTVTTTSYTDTGLTNGTTYYYRVTAVdAAGNESAPSNVVSVTtdltPPA 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  622 PPQNLTLQTVHTNLVVLHWQAPEGSDFSEYVVrYRTDAS--PWQRI-SGLHENEARIKDMHYGERYLVQVNTV-SFGVES 697
Cdd:COG3401   329 APSGLTATAVGSSSITLSWTASSDADVTGYNV-YRSTSGggTYTKIaETVTTTSYTDTGLTPGTTYYYKVTAVdAAGNES 407

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665389652  698 PHPLELNVTMPPQPVSNVVPLVdsrnlTLEWPRPDGHVDFYTLKWWPTDEED 749
Cdd:COG3401   408 APSEEVSATTASAASGESLTAS-----VDAVPLTDVAGATAAASAASNPGVS 454
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 900-988 1.92e-10

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 59.05  E-value: 1.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  900 PLPISDLKAIQVAAREITLHWTAPA---GEYTDFELQYLSADEEAPQLLQ-NVTKNTEITLQGLRPYHNYTFTVVVRSGS 975
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEvTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|...
gi 665389652  976 IQGTDFADVSVST 988
Cdd:cd00063    81 GESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
247-328 7.26e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.04  E-value: 7.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   247 PGKFIVWFRNETTLLVLWQPPFPA-GIYTHYRVSITPDDAIQSVLYVEregEPPGPAQAAFKGLVPGREYNISVQTVSED 325
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPPDGnGPITGYEVEYRPKNSGEPWNEIT---VPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ...
gi 665389652   326 ETS 328
Cdd:pfam00041   80 GEG 82
fn3 pfam00041
Fibronectin type III domain;
1013-1092 1.25e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 56.65  E-value: 1.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  1013 FQPSDVQPGEVTFEWSlEPAEQHGPIDYFRITCQNADDAADVSSYEFPVNATQGKIDGLVPGNHYIFRIQAKSALGYGAE 1092
Cdd:pfam00041    6 LTVTDVTSTSLTVSWT-PPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
PTP_tm pfam18861
TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases ...
 1127-1247 1.70e-09

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.


Pssm-ID: 465889  Cd Length: 126  Bit Score: 57.23  E-value: 1.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  1127 FRQGYFSNAHGMVRSYTIIIAEDVGKNASGLEMPS--WQD-----VQAY-TVWLPyqaiepyNPFlTSNGSRKSSLEAEh 1198
Cdd:pfam18861    1 IQFSLFNSSNGPIKAYGVIVTTNDSLNRPLKEYLNktYYDwkykkTDSYlATVTP-------NPF-TSPRSSSRSLTVP- 71

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  1199 ftIGTANCDKhqaGYCNGPLRAGTTYRIKIRAFTD-----------EDKFTDTVYSSPIT 1247
Cdd:pfam18861   72 --VGTGSKWQ---GYCNGPLKPLGSYRFSVAAFTRlefddglidgeESYVSFTPFSEPIA 126
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1007-1098 4.52e-09

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 55.20  E-value: 4.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1007 PGKVDYFQPSDVQPGEVTFEWSlEPAEQHGPIDYFRITCQNADDAADVSSYEFPVNATQGKIDGLVPGNHYIFRIQAKSA 1086
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWT-PPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                          90
                  ....*....|....
gi 665389652 1087 LGYG--AEREHIQT 1098
Cdd:cd00063    80 GGESppSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 620-706 2.83e-08

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 52.88  E-value: 2.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  620 PKPPQNLTLQTVHTNLVVLHWQAPE--GSDFSEYVVRYR-TDASPWQRISG--LHENEARIKDMHYGERYLVQVNTVSFG 694
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEddGGPITGYVVEYReKGSGDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|..
gi 665389652  695 VESPHPLELNVT 706
Cdd:cd00063    81 GESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 900-974 3.45e-08

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: 52.23  E-value: 3.45e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665389652    900 PLPISDLKAIQVAAREITLHWTAPAGE-YTDFELQYLSADEEAPQLLQNVTKN---TEITLQGLRPYHNYTFTVVVRSG 974
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDgITGYIVGYRVEYREEGSEWKEVNVTpssTSYTLTGLKPGTEYEFRVRAVNG 79
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
94-334 7.34e-08

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 57.32  E-value: 7.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   94 SPPFGFPEPNTTIPASDIGKDIKFSRALPGTEYNFWLYYTNSTHREQLTWTVNIT---TAPDPPANLSVQLRSSKSAFIT 170
Cdd:COG3401   173 DTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTtptTPPSAPTGLTATADTPGSVTLS 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  171 WRPPGSGRYSGFRIRVLGLTDLPFERSYSLEGNEtlqLSAKELTPGGSY--QVQAYSvYQGKES----VAYTSRNfTTKP 244
Cdd:COG3401   253 WDPVTESDATGYRVYRSNSGDGPFTKVATVTTTS---YTDTGLTNGTTYyyRVTAVD-AAGNESapsnVVSVTTD-LTPP 327

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  245 NTPGKFIVWFRNETTLLVLWQPPFPAGIyTHYRV--SITPDDAIQSVlyvereGEPPGPAQAAFKGLVPGREYNISVQTV 322
Cdd:COG3401   328 AAPSGLTATAVGSSSITLSWTASSDADV-TGYNVyrSTSGGGTYTKI------AETVTTTSYTDTGLTPGTTYYYKVTAV 400

                         250
                  ....*....|..
gi 665389652  323 SEDETSSVPTTA 334
Cdd:COG3401   401 DAAGNESAPSEE 412
fn3 pfam00041
Fibronectin type III domain;
622-698 1.46e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.49  E-value: 1.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   622 PPQNLTLQTVHTNLVVLHWQAPE--GSDFSEYVVRYRT----DASPWQRISGlHENEARIKDMHYGERYLVQVNTVSFGV 695
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgNGPITGYEVEYRPknsgEPWNEITVPG-TTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 665389652   696 ESP 698
Cdd:pfam00041   81 EGP 83
fn3 pfam00041
Fibronectin type III domain;
708-796 3.45e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 49.72  E-value: 3.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   708 PPQPVSnVVPlVDSRNLTLEWPRP---DGHVDFYTLKWWPTDEEDrvefknVTQLEDLSSPSVRIPIEDLSPGRQYRFEV 784
Cdd:pfam00041    2 APSNLT-VTD-VTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGE------PWNEITVPGTTTSVTLTGLKPGTEYEVRV 73

                           90
                   ....*....|..
gi 665389652   785 QASSNGIRSGTT 796
Cdd:pfam00041   74 QAVNGGGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 709-793 6.05e-07

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 49.03  E-value: 6.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  709 PQPVSNV-VPLVDSRNLTLEWPRPD---GHVDFYTLKWWPTDEEDRVEFKNvtqlEDLSSPSVRIPieDLSPGRQYRFEV 784
Cdd:cd00063     1 PSPPTNLrVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEV----TPGSETSYTLT--GLKPGTEYEFRV 74


                  ....*....
gi 665389652  785 QASSNGIRS 793
Cdd:cd00063    75 RAVNGGGES 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 151-242 7.43e-07

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 49.03  E-value: 7.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  151 PDPPANLSVQLRSSKSAFITWRPPGS--GRYSGFRIRVLGLTDLPFERSYSLEGNETlQLSAKELTPGGSYQVQAYSVYQ 228
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDdgGPITGYVVEYREKGSGDWKEVEVTPGSET-SYTLTGLKPGTEYEFRVRAVNG 79

                          90
                  ....*....|....
gi 665389652  229 GKESVAYTSRNFTT 242
Cdd:cd00063    80 GGESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
152-232 1.06e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 48.18  E-value: 1.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   152 DPPANLSVQLRSSKSAFITWRPP--GSGRYSGFRIRVLGLTDLPFERSYSLEGNETlQLSAKELTPGGSYQVQAYSVYQG 229
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdGNGPITGYEVEYRPKNSGEPWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVNGG 79


                   ...
gi 665389652   230 KES 232
Cdd:pfam00041   80 GEG 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 620-697 1.13e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.99  E-value: 1.13e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652    620 PKPPQNLTLQTVHTNLVVLHWQAPEGSDFSEYVVRYR----TDASPWQRISGLH-ENEARIKDMHYGERYLVQVNTVSFG 694
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRveyrEEGSEWKEVNVTPsSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 665389652    695 VES 697
Cdd:smart00060   81 GEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1007-1090 1.44e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.61  E-value: 1.44e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   1007 PGKVDYFQPSDVQPGEVTFEWS-LEPAEQHGPIDYFRItcQNADDAADVSSYEFPVNATQGKIDGLVPGNHYIFRIQAKS 1085
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEpPPDDGITGYIVGYRV--EYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 665389652   1086 ALGYG 1090
Cdd:smart00060   79 GAGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 244-338 2.69e-06

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.49  E-value: 2.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  244 PNTPGKFIVWFRNETTLLVLWQPP-FPAGIYTHYRVSITPDDAIQSVLYVEREGEPPgpaQAAFKGLVPGREYNISVQTV 322
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPeDDGGPITGYVVEYREKGSGDWKEVEVTPGSET---SYTLTGLKPGTEYEFRVRAV 77

                          90
                  ....*....|....*.
gi 665389652  323 SEDETSSVPTTARYLT 338
Cdd:cd00063    78 NGGGESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 151-232 3.79e-05

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 43.76  E-value: 3.79e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652    151 PDPPANLSVQLRSSKSAFITWRPPGSGRYSGFRI--RVLGLTDLPFERSYSLEGNETlQLSAKELTPGGSYQVQAYSVYQ 228
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVgyRVEYREEGSEWKEVNVTPSST-SYTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 665389652    229 GKES 232
Cdd:smart00060   80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 244-328 2.58e-04

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 41.45  E-value: 2.58e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652    244 PNTPGKFIVWFRNETTLLVLWQPPFPAGIyTHYRVSITPDDAIQSVLYVEREGEPPGPaQAAFKGLVPGREYNISVQTVS 323
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGI-TGYIVGYRVEYREEGSEWKEVNVTPSST-SYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 665389652    324 EDETS 328
Cdd:smart00060   79 GAGEG 83
UP_III cd09968
Uroplakin III; Uroplakin IIIa and IIIb, the dimerization partners of uroplakin Ib, are a ...
 1106-1248 7.44e-03

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


Pssm-ID: 197377  Cd Length: 187  Bit Score: 39.67  E-value: 7.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1106 VPEPSVTPLEVSRTSSTIEISFRQGYFSNAHG---------MVRSYTIIIAEDVGKNASGLEMPSWQDVQAYtvwlPYQA 1176
Cdd:cd09968     6 VPQLASTFLEGNPTSTTFTLEQPRCVFDSSASdtddvwlvvAVSNATNNFNAPQNSTDPISTYSQFSGGQYY----LTLR 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665389652 1177 IEPYNPfltsnGSRKSSLEAEHFTIG-TANCdkHQAGYCNGPLRAGTTYRIKIrAFTDEDKFTD-TVYSSPITT 1248
Cdd:cd09968    82 ASRDLY-----PCGNPSLNAYVLRVGaDGNC--TDNGNCNGPLPGPGPYRVKY-LVMNGSGVVAqTNWSDPIRL 147
 
Name Accession Description Interval E-value
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1358-1579 2.31e-134

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 416.37  E-value: 2.31e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1358 RFTNILPYDHSRFKLQPVDDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREK 1437
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1438 CDQYWPVDRVAMFYGDIKVQLIIDTHYHDWSISEFMVSRNCESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTD 1517
Cdd:cd14548    81 CDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIKQE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665389652 1518 MRPIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQ 1579
Cdd:cd14548   161 KGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1329-1582 2.79e-110

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 351.19  E-value: 2.79e-110
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   1329 FSEEFEELKHVGR-DQACSFANLPCNRPKNRFTNILPYDHSRFKLQPvDDDDGSDYINANYMPGHNSPREFIVTQGPLHS 1407
Cdd:smart00194    2 LEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKP-PPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   1408 TREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPVD-RVAMFYGDIKVQLIIDTHYHDWSISEFMVSRNC--ESRIMR 1484
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGcsETRTVT 160

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   1485 HFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDMRPIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKER 1564
Cdd:smart00194  161 HYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQR 240

                           250
                    ....*....|....*...
gi 665389652   1565 VFMVQTEQQYVCIHQCLL 1582
Cdd:smart00194  241 PGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1353-1582 6.18e-103

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 329.20  E-value: 6.18e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  1353 NRPKNRFTNILPYDHSRFKLQpvDDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFE 1432
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  1433 KGREKCDQYWPVDR-VAMFYGDIKVQLI-IDTHYHDWSISEFMVSRNC--ESRIMRHFHFTTWPDFGVPEPPQSLVRFVR 1508
Cdd:pfam00102   79 KGREKCAQYWPEEEgESLEYGDFTVTLKkEKEDEKDYTVRTLEVSNGGseETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665389652  1509 AFRDVIGTDMR-PIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLL 1582
Cdd:pfam00102  159 KVRKSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1357-1579 2.72e-96

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: 309.93  E-value: 2.72e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1357 NRFTNILPYDHSRFKLQPVDDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGRE 1436
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1437 KCDQYWPVDRVAMFYGDIKVQLIIDTHYHDWSISEFMVSrnCES-----RIMRHFHFTTWPDFGVPEPPQSLVRFVRAFR 1511
Cdd:cd14617    81 KCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKIC--SEEqldapRLVRHFHYTVWPDHGVPETTQSLIQFVRTVR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1512 DVIG--TDMRPIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQ 1579
Cdd:cd14617   159 DYINrtPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1348-1582 1.03e-95

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: 309.13  E-value: 1.03e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1348 ANLPCNRPKNRFTNILPYDHSRFKLQPVDDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVML 1427
Cdd:cd14614     7 ADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVML 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1428 TRCFEKGREKCDQYWPVDRVAMFYGDIKVQLIIDTHYHDWSISEFMVSRNCESRIMRHFHFTTWPDFGVP--EPPQSLVR 1505
Cdd:cd14614    87 TQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPtaNAAESILQ 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665389652 1506 FVRAFRDVIGTDMRPIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLL 1582
Cdd:cd14614   167 FVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQ 243
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1351-1582 1.18e-89

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 291.61  E-value: 1.18e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1351 PCNRPKNRFTNILPYDHSRFKLQPVDDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRC 1430
Cdd:cd14553     1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1431 FEKGREKCDQYWPvDRVAMFYGDIKVQLIIDTHYHDWSISEFMVSRN--CESRIMRHFHFTTWPDFGVPEPPQSLVRFVR 1508
Cdd:cd14553    81 EERSRVKCDQYWP-TRGTETYGLIQVTLLDTVELATYTVRTFALHKNgsSEKREVRQFQFTAWPDHGVPEHPTPFLAFLR 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665389652 1509 AFRDVIGTDMRPIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLL 1582
Cdd:cd14553   160 RVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALL 233
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1357-1582 4.16e-87

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: 283.63  E-value: 4.16e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1357 NRFTNILPYDHSRFKLQpVDDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGRE 1436
Cdd:cd14615     1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1437 KCDQYWPVDRvAMFYGDIKVQLIIDTHYHDWSISEFMVS--RNCESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVI 1514
Cdd:cd14615    80 KCEEYWPSKQ-KKDYGDITVTMTSEIVLPEWTIRDFTVKnaQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYM 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1515 GTDMR--PIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLL 1582
Cdd:cd14615   159 KQNPPnsPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCAL 228
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1357-1585 3.56e-86

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: 281.39  E-value: 3.56e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1357 NRFTNILPYDHSRFKLQPVDDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGRE 1436
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1437 KCDQYWPVDRVAMFYGDIKVQLIIDTHYHDWSISEFMV--SRNCESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVI 1514
Cdd:cd14619    81 KCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLkqVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQWL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665389652 1515 GTDMR--PIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLLAVL 1585
Cdd:cd14619   161 DQTMSggPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1383-1579 4.27e-84

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: 273.78  E-value: 4.27e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPVDR-VAMFYGDIKVQLIID 1461
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGgKPLEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1462 THYHDWSISEFMVSR--NCESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDMRPIIVHCSAGVGRSGTFIALD 1539
Cdd:cd00047    81 EELSDYTIRTLELSPkgCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAID 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 665389652 1540 RILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQ 1579
Cdd:cd00047   161 ILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1357-1579 2.65e-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: 261.38  E-value: 2.65e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1357 NRFTNILPYDHSRFKLQPVDDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGRE 1436
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1437 KCDQYWPVDRVAM-FYGDIKVQLIIDTHYHDWSISEFMVSRNCESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIG 1515
Cdd:cd14616    81 RCHQYWPEDNKPVtVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRASRA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665389652 1516 TDMRPIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQ 1579
Cdd:cd14616   161 HDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1357-1582 5.44e-79

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: 260.65  E-value: 5.44e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1357 NRFTNILPYDHSRFKLQPVDDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGRE 1436
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1437 KCDQYWPVDRVAMFYGDIKVQLIIDTHYHDWSISEFMVSRNCE--SRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVI 1514
Cdd:cd14618    81 LCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLrkERRVKHLHYTAWPDHGIPESTSSLMAFRELVREHV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1515 GT--DMRPIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLL 1582
Cdd:cd14618   161 QAtkGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1313-1582 1.43e-77

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: 258.43  E-value: 1.43e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1313 DFSEHYRIMSADSDFRFSEEFEELKHvGRDQACSFANLPCNRPKNRFTNILPYDHSRFKLQPVDDDDGSDYINANYMPGH 1392
Cdd:cd14626     2 DLADNIERLKANDGLKFSQEYESIDP-GQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1393 NSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPVdRVAMFYGDIKVQLIIDTHYHDWSISEF 1472
Cdd:cd14626    81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPI-RGTETYGMIQVTLLDTVELATYSVRTF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1473 MVSRN--CESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDMRPIIVHCSAGVGRSGTFIALDRILQHIHKSDY 1550
Cdd:cd14626   160 ALYKNgsSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKT 239

                         250       260       270
                  ....*....|....*....|....*....|..
gi 665389652 1551 VDIFGIVFAMRKERVFMVQTEQQYVCIHQCLL 1582
Cdd:cd14626   240 VDIYGHVTCMRSQRNYMVQTEDQYIFIHEALL 271
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1329-1582 1.31e-74

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


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 249.95  E-value: 1.31e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1329 FSEEFEELKHVGRDQACS--FANLPCNRPKNRFTNILPYDHSRFKLQPV--DDDDGSDYINANYMPGHNSPREFIVTQGP 1404
Cdd:cd17667     1 FSEDFEEVQRCTADMNITaeHSNHPDNKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1405 LHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPVDRvAMFYGDIKVQLIIDTHYHDWSISEFMVsRNCE----- 1479
Cdd:cd17667    81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTEN-SEEYGNIIVTLKSTKIHACYTVRRFSI-RNTKvkkgq 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1480 ---------SRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDMRPIIVHCSAGVGRSGTFIALDRILQHIHKSDY 1550
Cdd:cd17667   159 kgnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKST 238

                         250       260       270
                  ....*....|....*....|....*....|..
gi 665389652 1551 VDIFGIVFAMRKERVFMVQTEQQYVCIHQCLL 1582
Cdd:cd17667   239 VNVLGFLKHIRTQRNYLVQTEEQYIFIHDALL 270
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1331-1578 3.39e-74

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: 248.43  E-value: 3.39e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1331 EEFEELKHvgRDQACSF--ANLPCNRPKNRFTNILPYDHSRFKLQPVDDDDGSDYINANYMPGHNSPREFIVTQGPLHST 1408
Cdd:cd14543     7 EEYEDIRR--EPPAGTFlcSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1409 REEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPVDR-VAMFYGDIKVQLIIDTHYHDWSISEFMV--SRNCESRIMRH 1485
Cdd:cd14543    85 YSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEgSSLRYGDLTVTNLSVENKEHYKKTTLEIhnTETDESRQVTH 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1486 FHFTTWPDFGVPEPPQSLVRFVRAFRD-----VIGTDMR--------PIIVHCSAGVGRSGTFIALDRILQHIHKSDYVD 1552
Cdd:cd14543   165 FQFTSWPDFGVPSSAAALLDFLGEVRQqqalaVKAMGDRwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLN 244

                         250       260
                  ....*....|....*....|....*.
gi 665389652 1553 IFGIVFAMRKERVFMVQTEQQYVCIH 1578
Cdd:cd14543   245 VMQTVRRMRTQRAFSIQTPDQYYFCY 270
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1308-1582 4.05e-74

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: 248.85  E-value: 4.05e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1308 PVHVKDFSEHYRIMSADSDFRFSEEFEELKHvGRDQACSFANLPCNRPKNRFTNILPYDHSRFKLQPVDDDDGSDYINAN 1387
Cdd:cd14625     3 PIPISELAEHTERLKANDNLKLSQEYESIDP-GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1388 YMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPvDRVAMFYGDIKVQLIIDTHYHDW 1467
Cdd:cd14625    82 YIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWP-SRGTETYGMIQVTLLDTIELATF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1468 SISEFMVSRN--CESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDMRPIIVHCSAGVGRSGTFIALDRILQHI 1545
Cdd:cd14625   161 CVRTFSLHKNgsSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERI 240

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 665389652 1546 HKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLL 1582
Cdd:cd14625   241 KHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALL 277
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1383-1578 1.37e-72

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: 241.10  E-value: 1.37e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPvDRVAMFYGDIKVQLIIDT 1462
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWP-KEGTETYGNIQVTLLSTE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1463 HYHDWSISEFMVSRN--------CESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDMRPIIVHCSAGVGRSGT 1534
Cdd:cd14549    80 VLATYTVRTFSLKNLklkkvkgrSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTGT 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 665389652 1535 FIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIH 1578
Cdd:cd14549   160 YIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1348-1585 5.12e-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: 240.89  E-value: 5.12e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1348 ANLPCNRPKNRFTNILPYDHSRFKLQPVDDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVML 1427
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1428 TRCFEKGREKCDQYWPVDRVAMfYGDIKVQLIIDTHYHDWSISEFMVS--RNCESRIMRHFHFTTWPDFGVPEPPQSLVR 1505
Cdd:cd14554    81 TKLREMGREKCHQYWPAERSAR-YQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTVRQFQFTDWPEQGVPKSGEGFID 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1506 F---VRAFRDVIGTDmRPIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYvciHQCLL 1582
Cdd:cd14554   160 FigqVHKTKEQFGQE-GPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQY---QFCYR 235


                  ...
gi 665389652 1583 AVL 1585
Cdd:cd14554   236 AAL 238
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1308-1582 8.59e-70

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


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 236.55  E-value: 8.59e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1308 PVHVKDFSEHYRIMSADSDFRFSEEFEELKHvGRDQACSFANLPCNRPKNRFTNILPYDHSRFKLQPVDDDDGSDYINAN 1387
Cdd:cd14624     3 PIPILELADHIERLKANDNLKFSQEYESIDP-GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1388 YMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPvDRVAMFYGDIKVQLIIDTHYHDW 1467
Cdd:cd14624    82 YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWP-SRGTETYGLIQVTLLDTVELATY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1468 SISEFMVSRN--CESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDMRPIIVHCSAGVGRSGTFIALDRILQHI 1545
Cdd:cd14624   161 CVRTFALYKNgsSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERI 240

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 665389652 1546 HKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLL 1582
Cdd:cd14624   241 KHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALL 277
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1353-1582 1.06e-68

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: 231.45  E-value: 1.06e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1353 NRPKNRFTNILPYDHSRFKLQPVDDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFE 1432
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1433 KGREKCDQYWPVDrvAMFYGDIKVQLIIDTHYHDWSISEFMVSRNC--ESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAF 1510
Cdd:cd14630    83 VGRVKCVRYWPDD--TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGyhEIREIRQFHFTSWPDHGVPCYATGLLGFVRQV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665389652 1511 RDVIGTDMRPIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLL 1582
Cdd:cd14630   161 KFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAIL 232
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1308-1598 3.07e-67

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: 229.53  E-value: 3.07e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1308 PVHVKDFSEHYRIMSADSDFRFSEEFEELKHVGRDQACSFANLPCNRPKNRFTNILPYDHSRFKLQPVDDDDGSDYINAN 1387
Cdd:cd14621     7 PLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINAS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1388 YMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPvDRVAMFYGDIKVQLIIDTHYHDW 1467
Cdd:cd14621    87 FINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWP-DQGCWTYGNIRVSVEDVTVLVDY 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1468 SISEFM------VSRNCESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDMRPIIVHCSAGVGRSGTFIALDRI 1541
Cdd:cd14621   166 TVRKFCiqqvgdVTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAM 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 665389652 1542 LQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLLavlegkEHLLADSLEL 1598
Cdd:cd14621   246 LDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALL------EHYLYGDTEL 296
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1383-1579 8.02e-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: 222.12  E-value: 8.02e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANYM-PGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPVDRVAMFYGDIKVQLIID 1461
Cdd:cd18533     1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1462 THYHDWS--ISEFMVSR-NCESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGT--DMRPIIVHCSAGVGRSGTFI 1536
Cdd:cd18533    81 EENDDGGfiVREFELSKeDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSasLDPPIIVHCSAGVGRTGTFI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665389652 1537 ALDRILQHIHK--------SDYVD-IFGIVFAMRKERVFMVQTEQQYVCIHQ 1579
Cdd:cd18533   161 ALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1313-1582 2.76e-65

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: 223.00  E-value: 2.76e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1313 DFSEHYRIMSADSDFRFSEEFEELKHvGRDQACSFANLPCNRPKNRFTNILPYDHSRFKLQPVDDDDGSDYINANYMPGH 1392
Cdd:cd14633     1 DLLQHITQMKCAEGYGFKEEYESFFE-GQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1393 NSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPVDrvAMFYGDIKVQLIIDTHYHDWSISEF 1472
Cdd:cd14633    80 HRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD--TEIYKDIKVTLIETELLAEYVIRTF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1473 MVSRNC--ESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDMRPIIVHCSAGVGRSGTFIALDRILQHIHKSDY 1550
Cdd:cd14633   158 AVEKRGvhEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGV 237

                         250       260       270
                  ....*....|....*....|....*....|..
gi 665389652 1551 VDIFGIVFAMRKERVFMVQTEQQYVCIHQCLL 1582
Cdd:cd14633   238 VDIYNCVRELRSRRVNMVQTEEQYVFIHDAIL 269
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1359-1582 8.48e-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: 219.81  E-value: 8.48e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1359 FTNILPYDHSRFKLQPVDDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKC 1438
Cdd:cd14620     1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1439 DQYWPvDRVAMFYGDIKVQLIIDTHYHDWSISEFMVS----RNCE-SRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDV 1513
Cdd:cd14620    81 YQYWP-DQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQpqlpDGCKaPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665389652 1514 IGTDMRPIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLL 1582
Cdd:cd14620   160 NPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1357-1579 1.42e-64

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: 218.81  E-value: 1.42e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1357 NRFTNILPYDHSRFKLQPVDDDDGSDYINANYMPGHNSPRE-FIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKgR 1435
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKaYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1436 EKCDQYWPVDRVAMfYGDIKVQLIIDTHYHDWSISEFMVSRNCESRIMRHFHFTTWPDFGVPEPPQSLVRFVRafrDVIG 1515
Cdd:cd14547    80 EKCAQYWPEEENET-YGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQ---EVEE 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665389652 1516 TDMR-----PIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQ 1579
Cdd:cd14547   156 ARQTephrgPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1333-1595 5.49e-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: 219.51  E-value: 5.49e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1333 FEELKHVGRDQACSFANLPCNRPKNRFTNILPYDHSRFKLQPVDDDdgsdYINANYMPGHNSPREFIVTQGPLHSTREEF 1412
Cdd:cd14608     5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDND----YINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1413 WRMCWESNSRAIVMLTRCFEKGREKCDQYWPV-DRVAMFYGD--IKVQLIIDTHYHDWSISEFMVSR--NCESRIMRHFH 1487
Cdd:cd14608    81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQkEEKEMIFEDtnLKLTLISEDIKSYYTVRQLELENltTQETREILHFH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1488 FTTWPDFGVPEPPQSLVRFVRAFRD--VIGTDMRPIIVHCSAGVGRSGTFIALDRILQHIHKS---DYVDIFGIVFAMRK 1562
Cdd:cd14608   161 YTTWPDFGVPESPASFLNFLFKVREsgSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRkdpSSVDIKKVLLEMRK 240

                         250       260       270
                  ....*....|....*....|....*....|...
gi 665389652 1563 ERVFMVQTEQQyvcIHQCLLAVLEGKEHLLADS 1595
Cdd:cd14608   241 FRMGLIQTADQ---LRFSYLAVIEGAKFIMGDS 270
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1356-1573 7.31e-64

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: 217.26  E-value: 7.31e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1356 KNRFTNILPYDHSRFKLQPVDDDdgSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGR 1435
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1436 EKCDQYWPVDRVAMF---YGDIKVQLIIDTHYHDWSISEFMVSR--NCESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAF 1510
Cdd:cd14545    79 IKCAQYWPQGEGNAMifeDTGLKVTLLSEEDKSYYTVRTLELENlkTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665389652 1511 RD--VIGTDMRPIIVHCSAGVGRSGTFIALDRILQHIHKSDY--VDIFGIVFAMRKERVFMVQTEQQ 1573
Cdd:cd14545   159 REsgSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQ 225
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1353-1574 2.10e-63

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: 216.56  E-value: 2.10e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1353 NRPKNRFTNILPYDHSRFKLQPVDDD-DGSDYINANY-MPGHNSPRE------FIVTQGPLHSTREEFWRMCWESNSRAI 1424
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDPNvPGSDYINANYiRNENEGPTTdenaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1425 VMLTRCFEKGREKCDQYWPVDRVAMFYGDIKVQLIIDTHYHDWSISEFMVSR---NCESRIMRHFHFTTWPDFGVPEPPQ 1501
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKldqGDPIREIWHYQYLSWPDHGVPSDPG 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665389652 1502 SLVRF---VRAFRDVIgTDMRPIIVHCSAGVGRSGTFIALDRILQHIHKSDY---VDIFGIVFAMRKERVFMVQTEQQY 1574
Cdd:cd14544   161 GVLNFledVNQRQESL-PHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQY 238
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1348-1585 3.82e-63

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: 217.68  E-value: 3.82e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1348 ANLPCNRPKNRFTNILPYDHSRFKLQPVDDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVML 1427
Cdd:cd14627    48 ANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVML 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1428 TRCFEKGREKCDQYWPVDRVAMfYGDIKVQLIIDTHYHDWSISEFMVS--RNCESRIMRHFHFTTWPDFGVPEPPQSLVR 1505
Cdd:cd14627   128 TKLREMGREKCHQYWPAERSAR-YQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTVRQFQFTDWPEQGVPKSGEGFID 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1506 F---VRAFRDVIGTDmRPIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLL 1582
Cdd:cd14627   207 FigqVHKTKEQFGQD-GPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAAL 285


                  ...
gi 665389652 1583 AVL 1585
Cdd:cd14627   286 EYL 288
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1348-1590 6.51e-63

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: 216.91  E-value: 6.51e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1348 ANLPCNRPKNRFTNILPYDHSRFKLQPVDDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVML 1427
Cdd:cd14628    47 ANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1428 TRCFEKGREKCDQYWPVDRVAMfYGDIKVQLIIDTHYHDWSISEFMVS--RNCESRIMRHFHFTTWPDFGVPEPPQSLVR 1505
Cdd:cd14628   127 TKLREMGREKCHQYWPAERSAR-YQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTVRQFQFTDWPEQGVPKSGEGFID 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1506 F---VRAFRDVIGTDmRPIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLL 1582
Cdd:cd14628   206 FigqVHKTKEQFGQD-GPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAAL 284


                  ....*...
gi 665389652 1583 AVLEGKEH 1590
Cdd:cd14628   285 EYLGSFDH 292
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1348-1586 2.01e-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: 215.36  E-value: 2.01e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1348 ANLPCNRPKNRFTNILPYDHSRFKLQPVDDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVML 1427
Cdd:cd14629    48 ANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1428 TRCFEKGREKCDQYWPVDRVAMfYGDIKVQLIIDTHYHDWSISEFMVS--RNCESRIMRHFHFTTWPDFGVPEPPQSLVR 1505
Cdd:cd14629   128 TKLREMGREKCHQYWPAERSAR-YQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTIRQFQFTDWPEQGVPKTGEGFID 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1506 F---VRAFRDVIGTDmRPIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYvciHQCLL 1582
Cdd:cd14629   207 FigqVHKTKEQFGQD-GPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQY---QLCYR 282


                  ....
gi 665389652 1583 AVLE 1586
Cdd:cd14629   283 AALE 286
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1383-1579 1.30e-59

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


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 203.99  E-value: 1.30e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPvDRVAMFYGDIKVQLIIDT 1462
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP-DQGCWTYGNLRVRVEDTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1463 HYHDWSISEFMVSR-----NCES-RIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDMRPIIVHCSAGVGRSGTFI 1536
Cdd:cd14551    80 VLVDYTTRKFCIQKvnrgiGEKRvRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTFI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 665389652 1537 ALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQ 1579
Cdd:cd14551   160 VIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1383-1582 1.71e-59

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: 203.67  E-value: 1.71e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPVDRvAMFYGDIKVQLIIDT 1462
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADG-SEEYGNFLVTQKSVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1463 HYHDWSISEFMVsRNCE-----------SRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDMRPIIVHCSAGVGR 1531
Cdd:cd17668    80 VLAYYTVRNFTL-RNTKikkgsqkgrpsGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGR 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 665389652 1532 SGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLL 1582
Cdd:cd17668   159 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1330-1574 4.51e-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: 204.67  E-value: 4.51e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1330 SEEFEELKH----VGRDQACSF--ANLPCNRPKNRFTNILPYDHSRFKLQPVDDDDGSDYINANYMPGHNSPREFIVTQG 1403
Cdd:cd14603     1 AGEFSEIRAcsaaFKADYVCSTvaGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1404 PLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPVDRVAMFYGDIKVQLIIDTHYHDWSISEFMVSRNC-ESRI 1482
Cdd:cd14603    81 PLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTFQkESRS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1483 MRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDMRPIIVHCSAGVGRSGTFIALDRILQHIHKS---DYVDIFGIVFA 1559
Cdd:cd14603   161 VSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQripPDFSIFDVVLE 240

                         250
                  ....*....|....*
gi 665389652 1560 MRKERVFMVQTEQQY 1574
Cdd:cd14603   241 MRKQRPAAVQTEEQY 255
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1383-1579 8.77e-59

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: 201.59  E-value: 8.77e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWP-VDRVAMFYGDIKVQLIID 1461
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsMEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1462 THYHDWSISEFMVSRNCESRIMR---HFHFTTWPDFGVPEPPQSLV---RFVRAFRDVIGTdmrPIIVHCSAGVGRSGTF 1535
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKGSGRevtHIQFTSWPDHGVPEDPHLLLklrRRVNAFNNFFSG---PIVVHCSAGVGRTGTY 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 665389652 1536 IALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQ 1579
Cdd:cd14557   158 IGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1335-1573 4.60e-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: 201.73  E-value: 4.60e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1335 ELKHVGRDQACSFANLPCNRPKNRFTNILPYDHSRFKLQPVDDDdgsdYINANYMPGHNSPREFIVTQGPLHSTREEFWR 1414
Cdd:cd14607     6 EIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEND----YINASLVVIEEAQRSYILTQGPLPNTCCHFWL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1415 MCWESNSRAIVMLTRCFEKGREKCDQYWPV-DRVAMFYGD--IKVQLIID--THYHDWSISEFMVSRNCESRIMRHFHFT 1489
Cdd:cd14607    82 MVWQQKTKAVVMLNRIVEKDSVKCAQYWPTdEEEVLSFKEtgFSVKLLSEdvKSYYTVHLLQLENINSGETRTISHFHYT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1490 TWPDFGVPEPPQSLVRFVRAFRD--VIGTDMRPIIVHCSAGVGRSGTFIALDRILQHIHKSD--YVDIFGIVFAMRKERV 1565
Cdd:cd14607   162 TWPDFGVPESPASFLNFLFKVREsgSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRM 241


                  ....*...
gi 665389652 1566 FMVQTEQQ 1573
Cdd:cd14607   242 GLIQTPDQ 249
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1369-1582 6.61e-58

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: 199.48  E-value: 6.61e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1369 RFKLQPVDDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPVDrvA 1448
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD--T 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1449 MFYGDIKVQLIIDTHYHDWSISEFMVSRNC--ESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDMRPIIVHCS 1526
Cdd:cd14631    79 EVYGDFKVTCVEMEPLAEYVVRTFTLERRGynEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCS 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 665389652 1527 AGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLL 1582
Cdd:cd14631   159 AGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1383-1582 6.72e-58

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: 198.99  E-value: 6.72e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPVDrvAMFYGDIKVQLIIDT 1462
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDD--TEVYGDIKVTLVETE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1463 HYHDWSISEFMVSRN--CESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDMRPIIVHCSAGVGRSGTFIALDR 1540
Cdd:cd14555    79 PLAEYVVRTFALERRgyHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVIDI 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 665389652 1541 ILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLL 1582
Cdd:cd14555   159 MLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1383-1585 2.86e-56

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: 194.52  E-value: 2.86e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANYM--PGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWP--VDRVAMFYGDIKVQL 1458
Cdd:cd14538     1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdsLNKPLICGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1459 IIDTHYHDWSISEFMVSRN--CESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDmrPIIVHCSAGVGRSGTFI 1536
Cdd:cd14538    81 EKYQSLQDFVIRRISLRDKetGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHNSG--PIVVHCSAGIGRTGVLI 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 665389652 1537 ALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLLAVL 1585
Cdd:cd14538   159 TIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1353-1586 9.11e-56

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: 194.85  E-value: 9.11e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1353 NRPKNRFTNILPYDHSRFKLQPVD-DDDGSDYINANY-MPGHNS-------PREFIVTQGPLHSTREEFWRMCWESNSRA 1423
Cdd:cd14605     2 NKNKNRYKNILPFDHTRVVLHDGDpNEPVSDYINANIiMPEFETkcnnskpKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1424 IVMLTRCFEKGREKCDQYWPVDRVAMFYGDIKVQLIIDTHYHDWSISEFMVSR----NCEsRIMRHFHFTTWPDFGVPEP 1499
Cdd:cd14605    82 IVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLSKvgqgNTE-RTVWQYHFRTWPDHGVPSD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1500 PQSLVRF---VRAFRDVIgTDMRPIIVHCSAGVGRSGTFIALDRILQHIHKSDY---VDIFGIVFAMRKERVFMVQTEQQ 1573
Cdd:cd14605   161 PGGVLDFleeVHHKQESI-MDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEAQ 239

                         250
                  ....*....|...
gi 665389652 1574 YVCIHQCLLAVLE 1586
Cdd:cd14605   240 YRFIYMAVQHYIE 252
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1383-1574 1.08e-54

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: 189.79  E-value: 1.08e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPVDRvAMFYGDIKVQLIIDT 1462
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDG-SVSSGDITVELKDQT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1463 HYHDWSISEFMVSRNCE--SRIMRHFHFTTWPDFGVPEPPQSLVRFVRAF-RDVIGTDMRPIIVHCSAGVGRSGTFIALD 1539
Cdd:cd14552    80 DYEDYTLRDFLVTKGKGgsTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVqKQQQQSGNHPITVHCSAGAGRTGTFCALS 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 665389652 1540 RILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQY 1574
Cdd:cd14552   160 TVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQY 194
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1353-1585 7.80e-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: 188.50  E-value: 7.80e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1353 NRPKNRFTNILPYDHSRFKLqpvdDDDGsDYINANY--MPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRC 1430
Cdd:cd14597     3 NRKKNRYKNILPYDTTRVPL----GDEG-GYINASFikMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1431 FEKGREKCDQYWP--VDRVAMFYGDIKVQLIIDTHYHDWSIS--EFMVSRNCESRIMRHFHFTTWPDFGVPEPPQSLVRF 1506
Cdd:cd14597    78 VEGGKIKCQRYWPeiLGKTTMVDNRLQLTLVRMQQLKNFVIRvlELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLTF 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665389652 1507 VRAFRDVIGTDmrPIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLLAVL 1585
Cdd:cd14597   158 ISYMRHIHKSG--PIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVILYVL 234
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1349-1581 3.26e-53

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: 187.35  E-value: 3.26e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1349 NLPCNRPKNRFTNILPYDHSRFKLQ-PVDDDDGSDYINANYMPGHN-SPREFIVTQGPLHSTREEFWRMCWESNSRAIVM 1426
Cdd:cd14612    11 DIPGHASKDRYKTILPNPQSRVCLRrAGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVM 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1427 LTRCFEKgREKCDQYWPVDRVAmfYGDIKVQLIIDTHYHDWSISEFMVSRNCESRIMRHFHFTTWPDFGVPEPPQSLVRF 1506
Cdd:cd14612    91 ITKLKEK-KEKCVHYWPEKEGT--YGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPESAGPLLRL 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665389652 1507 VRAFRD--VIGTDMRPIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCL 1581
Cdd:cd14612   168 VAEVEEsrQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTL 244
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1358-1574 2.36e-52

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 184.09  E-value: 2.36e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1358 RFTNILPYDHSRFKLQPVDDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREK 1437
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1438 CDQYWPVDRVaMFYGDIKVQLIIDTHYHDWSISEFMVSRNCE--SRIMRHFHFTTWPDFGVPEPPQSLVRFVRAF-RDVI 1514
Cdd:cd14623    81 CAQYWPSDGS-VSYGDITIELKKEEECESYTVRDLLVTNTREnkSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVqKQQQ 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1515 GTDMRPIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQY 1574
Cdd:cd14623   160 QSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQY 219
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1351-1586 2.37e-52

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: 185.47  E-value: 2.37e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1351 PCNRPKNRFTNILPYDHSRFKLQPVDDD-DGSDYINANY-----MPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAI 1424
Cdd:cd14606    16 PENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYvknqlLGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1425 VMLTRCFEKGREKCDQYWPVDRVAMFYGDIKVQLIIDTHYHDWSISEFMVS---RNCESRIMRHFHFTTWPDFGVPEPPQ 1501
Cdd:cd14606    96 VMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSpldNGELIREIWHYQYLSWPDHGVPSEPG 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1502 SLVRFVRAFrDVIGTDMR---PIIVHCSAGVGRSGTFIALDRILQHIHKSDY---VDIFGIVFAMRKERVFMVQTEQQYV 1575
Cdd:cd14606   176 GVLSFLDQI-NQRQESLPhagPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQTEAQYK 254

                         250
                  ....*....|.
gi 665389652 1576 CIHQCLLAVLE 1586
Cdd:cd14606   255 FIYVAIAQFIE 265
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1383-1579 2.52e-52

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: 183.01  E-value: 2.52e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPVDRVAMF-YGDIKVQLIID 1461
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLqFGPFKISLEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1462 THY-HDWSISEFMVSRNCESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDMRPIIVHCSAGVGRSGTFIALD- 1539
Cdd:cd14542    81 KRVgPDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICAIDy 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 665389652 1540 --RILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQ 1579
Cdd:cd14542   161 vwNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1353-1586 2.90e-52

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: 186.29  E-value: 2.90e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1353 NRPKNRFTNILPYDHSRFKLQPVDDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFE 1432
Cdd:cd14604    57 NVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFE 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1433 KGREKCDQYWPV-DRVAMFYGDIKVQLIIDTHYHDWSISEFMVSRNCESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFR 1511
Cdd:cd14604   137 MGRKKCERYWPLyGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMR 216

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665389652 1512 DVIGTDMRPIIVHCSAGVGRSGTFIALD---RILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLLAVLE 1586
Cdd:cd14604   217 KYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFE 294
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1383-1582 3.74e-52

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: 182.56  E-value: 3.74e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPVDrvAMFYGDIKVQLIIDT 1462
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDD--SDTYGDIKITLLKTE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1463 HYHDWSISEFMVSRNCES--RIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDMRPIIVHCSAGVGRSGTFIALDR 1540
Cdd:cd14632    79 TLAEYSVRTFALERRGYSarHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLDV 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 665389652 1541 ILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLL 1582
Cdd:cd14632   159 MLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1332-1586 1.97e-51

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: 183.13  E-value: 1.97e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1332 EFEELKHVGRDQACSFANLPCNRPKNRFTNILPYDHSRFKLQpvdddDGSDYINANYM----PGHNSPREFIVTQGPLHS 1407
Cdd:cd14600    19 QFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQ-----GNEDYINASYVnmeiPSANIVNKYIATQGPLPH 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1408 TREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPVDRVAMFYGDIKVQliidTHYHDWSIS----EFMVS--RNCESR 1481
Cdd:cd14600    94 TCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQ----CHSEDCTIAyvfrEMLLTntQTGEER 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1482 IMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDvIGTDMRPIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMR 1561
Cdd:cd14600   170 TVTHLQYVAWPDHGVPDDSSDFLEFVNYVRS-KRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMR 248

                         250       260
                  ....*....|....*....|....*
gi 665389652 1562 KERVFMVQTEQQYVCIHQCLLAVLE 1586
Cdd:cd14600   249 DQRAMMVQTSSQYKFVCEAILRVYE 273
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1356-1574 2.56e-51

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: 181.19  E-value: 2.56e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1356 KNRFTNILPYDHSRFKLQPVDDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGR 1435
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1436 EKCDQYWP-VDRVAMFYGDIKVQLIIDTHYHDWSISEFMVSRNCESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVI 1514
Cdd:cd14602    81 KKCERYWAePGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665389652 1515 GTDMRPIIVHCSAGVGRSGTFIALD---RILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQY 1574
Cdd:cd14602   161 EDDSVPICIHCSAGCGRTGVICAIDytwMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQY 223
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1382-1574 1.41e-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: 177.89  E-value: 1.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1382 DYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPVDRvAMFYGDIKVQLIID 1461
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEG-SVTHGEITIEIKND 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1462 THYHDWSISEFMVSRNCE--SRIMRHFHFTTWPDFGVPEPPQSLVRFVRAF-RDVIGTDMRPIIVHCSAGVGRSGTFIAL 1538
Cdd:cd14622    80 TLLETISIRDFLVTYNQEkqTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVqKQQQQTGNHPIVVHCSAGAGRTGTFIAL 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 665389652 1539 DRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQY 1574
Cdd:cd14622   160 SNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQY 195
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1328-1574 1.95e-50

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: 180.64  E-value: 1.95e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1328 RFSEEFEEL-KHVGRDQACSFANLPCNRPKNRFTNILPYDHSRFKLQPVDDDDGSDYINANYMPGHNsPRE--FIVTQGP 1404
Cdd:cd14610    18 RLEKEWEALcAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHD-PRNpaYIATQGP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1405 LHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPvDRVAMFYGDIKVQLIIDthyHDWSiSEFMVS-------RN 1477
Cdd:cd14610    97 LPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWP-DEGSNLYHIYEVNLVSE---HIWC-EDFLVRsfylknlQT 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1478 CESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDMRPIIVHCSAGVGRSGTFIALDRILQHIHK-SDYVDIFGI 1556
Cdd:cd14610   172 NETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKgAKEIDIAAT 251

                         250
                  ....*....|....*...
gi 665389652 1557 VFAMRKERVFMVQTEQQY 1574
Cdd:cd14610   252 LEHLRDQRPGMVQTKEQF 269
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1356-1581 4.57e-50

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: 178.52  E-value: 4.57e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1356 KNRFTNILPYDHSRFKLQPVDDDDG-SDYINANYMPGHNSP-REFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEK 1433
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTSPDQDDPlSSYINANYIRGYGGEeKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1434 GrEKCDQYWPVDRVAmfYGDIKVQLIIDTHYHDWSISEFMVSRNCESRIMRHFHFTTWPDFGVPE--PPQ-SLVRFVRAF 1510
Cdd:cd14613   108 N-EKCTEYWPEEQVT--YEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYTSWPDQKTPDnaPPLlQLVQEVEEA 184

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665389652 1511 RDVIGTDMRPIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCL 1581
Cdd:cd14613   185 RQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1383-1586 7.70e-50

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: 176.09  E-value: 7.70e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANY--MPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPVD-RVAMFYGDIKVQLI 1459
Cdd:cd14596     1 YINASYitMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETlQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1460 IDTHYHDWSISEFMVSRN--CESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDmrPIIVHCSAGVGRSGTFIA 1537
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKetGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTG--PIVVHCSAGIGRAGVLIC 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 665389652 1538 LDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLLAVLE 1586
Cdd:cd14596   159 VDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1382-1587 9.09e-50

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: 175.98  E-value: 9.09e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1382 DYINANY----MPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPVDRVAMFYGDIKVQ 1457
Cdd:cd14541     1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1458 LIIDTHYHDWSISEFMV--SRNCESRIMRHFHFTTWPDFGVPEPPQ---SLVRFVRAFRDVIGTdmrPIIVHCSAGVGRS 1532
Cdd:cd14541    81 CVSEEVTPSFAFREFILtnTNTGEERHITQMQYLAWPDHGVPDDSSdflDFVKRVRQNRVGMVE---PTVVHCSAGIGRT 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 665389652 1533 GTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQY--VCihQCLLAVLEG 1587
Cdd:cd14541   158 GVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYrfVC--EAILRVYEE 212
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1356-1579 1.23e-48

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: 173.18  E-value: 1.23e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1356 KNRFTNILPYDHSRFKLQPVDDDDG-SDYINANYMPGH-NSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEK 1433
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYgGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1434 GrEKCDQYWPVDRvaMFYGDIKVQLIIDTHYHDWSISEFMVSRNCESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFR-D 1512
Cdd:cd14611    82 N-EKCVLYWPEKR--GIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEeD 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665389652 1513 VIGTDMR-PIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQ 1579
Cdd:cd14611   159 RLASPGRgPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1383-1574 8.38e-48

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


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 169.88  E-value: 8.38e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPVDRVAmfYGDIKVQLIIDT 1462
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT--YGDIEVELKDTE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1463 HYHDWSISEFMV--SRNCESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDM------RPIIVHCSAGVGRSGT 1534
Cdd:cd14558    79 KSPTYTVRVFEIthLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNskhgrsVPIVVHCSDGSSRTGI 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 665389652 1535 FIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQY 1574
Cdd:cd14558   159 FCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQY 198
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1328-1574 1.03e-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: 172.53  E-value: 1.03e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1328 RFSEEFEEL-KHVGRDQACSFANLPCNRPKNRFTNILPYDHSRFKLQPVDDDDGSDYINANYMPGHNsPR--EFIVTQGP 1404
Cdd:cd14609    16 RLAKEWQALcAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIEHD-PRmpAYIATQGP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1405 LHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPvDRVAMFYGDIKVQLIIDthyHDWSiSEFMVS-------RN 1477
Cdd:cd14609    95 LSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWP-DEGSSLYHIYEVNLVSE---HIWC-EDFLVRsfylknvQT 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1478 CESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDMRPIIVHCSAGVGRSGTFIALDRILQHIHKS-DYVDIFGI 1556
Cdd:cd14609   170 QETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAAT 249

                         250
                  ....*....|....*...
gi 665389652 1557 VFAMRKERVFMVQTEQQY 1574
Cdd:cd14609   250 LEHVRDQRPGMVRTKDQF 267
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1383-1585 3.47e-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: 157.23  E-value: 3.47e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANY--MPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWP---VDRVAMFYGDIKVQ 1457
Cdd:cd14540     1 YINASHitATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPtlgGEHDALTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1458 LIIDTHYHDWSISEFMVSR--NCESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDV-------IGTDMR--PIIVHCS 1526
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHtlSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVrrhtnqdVAGHNRnpPTLVHCS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 665389652 1527 AGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLLAVL 1585
Cdd:cd14540   161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1353-1586 2.49e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 157.86  E-value: 2.49e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1353 NRPKNRFTNILPYDHSRFKLQPvdDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFE 1432
Cdd:PHA02742   52 NMKKCRYPDAPCFDRNRVILKI--EDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1433 KGREKCDQYW-PVDRVAMFYGDIKVQLIIDTHYHDWSISEFMVSRNCESRIM--RHFHFTTWPDFGVPEPPQSLVRFVRA 1509
Cdd:PHA02742  130 DGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLdiKHFAYEDWPHGGLPRDPNKFLDFVLA 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1510 FRDVIGT-----------DMRPIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCih 1578
Cdd:PHA02742  210 VREADLKadvdikgenivKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF-- 287


                  ....*...
gi 665389652 1579 qCLLAVLE 1586
Cdd:PHA02742  288 -CYFIVLI 294
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1383-1574 1.31e-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: 152.60  E-value: 1.31e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANYMPGHNsPRE--FIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPvDRVAMFYGDIKVQLII 1460
Cdd:cd14546     1 YINASTIYDHD-PRNpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP-EEGSEVYHIYEVHLVS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1461 DthyHDWSiSEFMVS-------RNCESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDMRPIIVHCSAGVGRSG 1533
Cdd:cd14546    79 E---HIWC-DDYLVRsfylknlQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTG 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 665389652 1534 TFIALDRILQHIHKS-DYVDIFGIVFAMRKERVFMVQTEQQY 1574
Cdd:cd14546   155 TYILIDMVLNRMAKGaKEIDIAATLEHLRDQRPGMVKTKDQF 196
PHA02738 PHA02738
hypothetical protein; Provisional
 1316-1574 1.28e-40

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 153.54  E-value: 1.28e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1316 EHYRIMSADSDFRFSEEFEelkhvgrdqacsfanlpcNRPKNRFTNILPYDHSRFKLqPVDDDDGsDYINANYMPGHNSP 1395
Cdd:PHA02738   30 EHQKVISEKVDGTFNAEKK------------------NRKLNRYLDAVCFDHSRVIL-PAERNRG-DYINANYVDGFEYK 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1396 REFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWP-VDRVAMFYGDIKVQLI-IDTHYHDWSISEFM 1473
Cdd:PHA02738   90 KKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSdVEQGSIRFGKFKITTTqVETHPHYVKSTLLL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1474 VSRNCESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDV----------IGTDMR---PIIVHCSAGVGRSGTFIALDR 1540
Cdd:PHA02738  170 TDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCqkelaqeslqIGHNRLqppPIVVHCNAGLGRTPCYCVVDI 249

                         250       260       270
                  ....*....|....*....|....*....|....
gi 665389652 1541 ILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQY 1574
Cdd:PHA02738  250 SISRFDACATVSIPSIVSSIRNQRYYSLFIPFQY 283
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1382-1586 4.03e-39

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: 145.47  E-value: 4.03e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1382 DYINANYM----PGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPVDRVAMFYGDIKVQ 1457
Cdd:cd14601     1 DYINANYInmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1458 LIIDTHYHDWSISEFMVS--RNCESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDMRPIIVHCSAGVGRSGTF 1535
Cdd:cd14601    81 CHSEEGNPAYVFREMTLTnlEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGVL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 665389652 1536 IALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLLAVLE 1586
Cdd:cd14601   161 ITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYE 211
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1332-1586 5.18e-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: 147.84  E-value: 5.18e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1332 EFEELKHVGRDQACSFANLPCNRPKNRFTNILPYDHSRFKLQPVDDDDgSDYINANYMPGHNSPRE--FIVTQGPLHSTR 1409
Cdd:cd14599    17 EYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENN-TGYINASHIKVTVGGEEwhYIATQGPLPHTC 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1410 EEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWP---VDRVAMFYGDIKVQLIIDTHYHDWSISEFMVSR--NCESRIMR 1484
Cdd:cd14599    96 HDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPklgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHllSGQERTVW 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1485 HFHFTTWPDFGVPEPPQSLVRFVRAFRDV--------IGTDMR--PIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIF 1554
Cdd:cd14599   176 HLQYTDWPDHGCPEEVQGFLSYLEEIQSVrrhtnsmlDSTKNCnpPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVP 255

                         250       260       270
                  ....*....|....*....|....*....|..
gi 665389652 1555 GIVFAMRKERVFMVQTEQQYVCIHQCLLAVLE 1586
Cdd:cd14599   256 VMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1383-1574 6.45e-39

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: 144.45  E-value: 6.45e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANYMPGHN--SPReFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPVDR-VAMFYGDIKVQL- 1458
Cdd:cd14539     1 YINASLIEDLTpyCPR-FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERgQALVYGAITVSLq 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1459 -IIDTHYHdwsiSEFMVS-RNCESRIMR---HFHFTTWPDFGVPEPPQSLVRF---VRAFRDVIGTDMRPIIVHCSAGVG 1530
Cdd:cd14539    80 sVRTTPTH----VERIISiQHKDTRLSRsvvHLQFTTWPELGLPDSPNPLLRFieeVHSHYLQQRSLQTPIVVHCSSGVG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 665389652 1531 RSGTFIALDRILQHIHKSD-YVDIFGIVFAMRKERVFMVQTEQQY 1574
Cdd:cd14539   156 RTGAFCLLYAAVQEIEAGNgIPDLPQLVRKMRQQRKYMLQEKEHL 200
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1482-1582 2.26e-38

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 139.03  E-value: 2.26e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   1482 IMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDMR--PIIVHCSAGVGRSGTFIALDRILQHIHKSDY-VDIFGIVF 1558
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                            90       100
                    ....*....|....*....|....
gi 665389652   1559 AMRKERVFMVQTEQQYVCIHQCLL 1582
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALL 104
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1482-1582 2.26e-38

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: 139.03  E-value: 2.26e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   1482 IMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDMR--PIIVHCSAGVGRSGTFIALDRILQHIHKSDY-VDIFGIVF 1558
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                            90       100
                    ....*....|....*....|....
gi 665389652   1559 AMRKERVFMVQTEQQYVCIHQCLL 1582
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALL 104
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1351-1578 3.59e-37

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 143.22  E-value: 3.59e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1351 PCNRPKNRFTNILPYDHSRFKLQpVDDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRC 1430
Cdd:PHA02747   49 PENQPKNRYWDIPCWDHNRVILD-SGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPT 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1431 -FEKGREKCDQYW-PVDRVAMFYGDIKVQLIIDTHYHDWSISEFMVSRNC--ESRIMRHFHFTTWPDFGVPEPPQSLVRF 1506
Cdd:PHA02747  128 kGTNGEEKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKIlkDSRKISHFQCSEWFEDETPSDHPDFIKF 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1507 VRAF---RDVIGTD-------MRPIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVC 1576
Cdd:PHA02747  208 IKIIdinRKKSGKLfnpkdalLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLF 287


                  ..
gi 665389652 1577 IH 1578
Cdd:PHA02747  288 IQ 289
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1383-1579 4.75e-36

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: 136.00  E-value: 4.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRcFEKGREKCDQYWPVDRVAMfYGDIKVQLIIDT 1462
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQ-LDPKDQSCPQYWPDEGSGT-YGPIQVEFVSTT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1463 HYHDWSISEFMV---SRNCE-SRIMRHFHFTTWPDFG-VPEPPQSLVRFVRAF-RDVIGTDMRPIIVHCSAGVGRSGTFI 1536
Cdd:cd14556    79 IDEDVISRIFRLqntTRPQEgYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVeKWQEQSGEGPIVVHCLNGVGRSGVFC 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 665389652 1537 ALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQ 1579
Cdd:cd14556   159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1303-1577 3.00e-35

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 136.76  E-value: 3.00e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1303 ITPNRPVHVKDFSEHYRImsadsdfRFSEEFEELKHVGRDQacSFANLPCNRPKNRFTNILPYDHSRfklqpVDDDDGsd 1382
Cdd:COG5599     1 VSPKNPIAIKSEEEKINS-------RLSTLTNELAPSHNDP--QYLQNINGSPLNRFRDIQPYKETA-----LRANLG-- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANYMPGHNsPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFE--KGREKCDQYWPVD-RVAMFygDIKVQLI 1459
Cdd:COG5599    65 YLNANYIQVIG-NHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEisKPKVKMPVYFRQDgEYGKY--EVSSELT 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1460 ----IDTHYHdwsISEFMVSRNC---ESRIMRHFHFTTWPDFGVPEPPQ--SLVRFVRAFRDVIGTDMRPIIVHCSAGVG 1530
Cdd:COG5599   142 esiqLRDGIE---ARTYVLTIKGtgqKKIEIPVLHVKNWPDHGAISAEAlkNLADLIDKKEKIKDPDKLLPVVHCRAGVG 218

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 665389652 1531 RSGTFIALDRILQHI--HKSDYVDIFGIVFAMRKER-VFMVQTEQQYVCI 1577
Cdd:COG5599   219 RTGTLIACLALSKSInaLVQITLSVEEIVIDMRTSRnGGMVQTSEQLDVL 268
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1351-1584 3.58e-33

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 132.07  E-value: 3.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1351 PCNRPKNRFTNILPYDHSRF-------------------KLQPVDDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREE 1411
Cdd:PHA02746   49 KENLKKNRFHDIPCWDHSRVvinaheslkmfdvgdsdgkKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSED 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1412 FWRMCWESNSRAIVMLTRcFEKGREKCDQYWPVDR-VAMFYGDIKVQLIIDTHYHDWSISEFMVSRNCE--SRIMRHFHF 1488
Cdd:PHA02746  129 FFKLISEHESQVIVSLTD-IDDDDEKCFELWTKEEdSELAFGRFVAKILDIIEELSFTKTRLMITDKISdtSREIHHFWF 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1489 TTWPDFGVPEPPQSLVRFVRAFR----------DVIGTDMRPIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVF 1558
Cdd:PHA02746  208 PDWPDNGIPTGMAEFLELINKVNeeqaelikqaDNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVL 287

                         250       260
                  ....*....|....*....|....*.
gi 665389652 1559 AMRKERVFMVQTEQQYVCihqCLLAV 1584
Cdd:PHA02746  288 KIRKQRHSSVFLPEQYAF---CYKAL 310
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1383-1575 5.21e-33

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: 127.58  E-value: 5.21e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANYM--PGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGR-EKCDQYWPV-DRVAMFYGDIKVQL 1458
Cdd:cd17658     1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAeENESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1459 I-IDTHYHDWSISEFMVSRNcES----RIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRdVIGTDMRPIIVHCSAGVGRSG 1533
Cdd:cd17658    81 KkLKHSQHSITLRVLEVQYI-ESeeppLSVLHIQYPEWPDHGVPKDTRSVRELLKRLY-GIPPSAGPIVVHCSAGIGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 665389652 1534 TFIALDRILQHIHKSDY--VDIFGIVFAMRKERVFMVQTEQQYV 1575
Cdd:cd17658   159 AYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYI 202
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1383-1566 8.76e-31

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: 120.89  E-value: 8.76e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKgrEKCDQYWPVDRVAMFYGDIKVQLIIDT 1462
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELN--EDEPIYWPTKEKPLECETFKVTLSGED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1463 HYHDWS-----ISEFMVSRNCESRIM--RHFHFTTWPDfgVPEPPQSLVRFVRAFRDVIGTDMRPIIVHCSAGVGRSGTF 1535
Cdd:cd14550    79 HSCLSNeirliVRDFILESTQDDYVLevRQFQCPSWPN--PCSPIHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAATF 156

                         170       180       190
                  ....*....|....*....|....*....|...
gi 665389652 1536 IALDRILQHIHKSDYVDIFGIV--FAMRKERVF 1566
Cdd:cd14550   157 CALTTLHQQLEHESSVDVYQVAklYHLMRPGVF 189
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1383-1582 1.14e-30

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: 120.90  E-value: 1.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCfeKGREKCDQYWPvDRVAMFYGDIKVQLIidt 1462
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWP-EKTSCCYGPIQVEFV--- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1463 hyhDWSISEFMVS---RNCES-------RIMRHFHFTTWPDF-GVPEPPQSLVRFVRAF----RDVIGTDMRpIIVHCSA 1527
Cdd:cd14634    75 ---SADIDEDIISrifRICNMarpqdgyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLekwqEQYDGREGR-TVVHCLN 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 665389652 1528 GVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLL 1582
Cdd:cd14634   151 GGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVAL 205
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1383-1586 1.90e-30

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: 120.85  E-value: 1.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANYMPGHNSPRE--FIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWP---VDRVAMFYGDIKVQ 1457
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgSRHNTVTYGRFKIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1458 LIIDTHYHDWSISEFMVSR--NCESRIMRHFHFTTWPDFGVPE----------PPQSLVRFVRAFRDVIGTDMrPIIVHC 1525
Cdd:cd14598    81 TRFRTDSGCYATTGLKIKHllTGQERTVWHLQYTDWPEHGCPEdlkgflsyleEIQSVRRHTNSTIDPKSPNP-PVLVHC 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665389652 1526 SAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLLAVLE 1586
Cdd:cd14598   160 SAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1383-1582 5.35e-22

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: 95.83  E-value: 5.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCdQYWPVDRVAMFYGDIKVQLIIDT 1462
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKDEPINCETFKVTLIAEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1463 HY-----HDWSISEFMVSRNCESRIM--RHFHFTTWPDfgvPEPPQS-LVRFVRAFRDVIGTDMRPIIVHCSAGVGRSGT 1534
Cdd:cd17669    80 HKclsneEKLIIQDFILEATQDDYVLevRHFQCPKWPN---PDSPISkTFELISIIKEEAANRDGPMIVHDEHGGVTAGT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 665389652 1535 FIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLL 1582
Cdd:cd17669   157 FCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1383-1586 2.53e-21

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: 93.82  E-value: 2.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGRE-KCDQYWPvDRVAMFYGDIKVQLIID 1461
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP-EPGLQQYGPMEVEFVSG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1462 THYHDWSISEFMV---SRNCESRIM-RHFHFTTWPDF-GVPEPPQS---LVRFVRAFRDVIGtDMRpIIVHCSAGVGRSG 1533
Cdd:cd14637    80 SADEDIVTRLFRVqniTRLQEGHLMvRHFQFLRWSAYrDTPDSKKAflhLLASVEKWQRESG-EGR-TVVHCLNGGGRSG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 665389652 1534 TFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYvciHQCLLAVLE 1586
Cdd:cd14637   158 TYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQY---RFCYEIALE 207
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1383-1574 5.20e-21

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: 93.17  E-value: 5.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRC-FEKGrekCDQYWPvDRVAMFYGDIKVQLIID 1461
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWP-EEGMLRYGPIQVECMSC 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1462 THYHDWSISEFMV---SRNCESRIM-RHFHFTTWPDF-GVPEPPQSLVRF---VRAFRDVIGTDMRPIIVHCSAGVGRSG 1533
Cdd:cd14636    77 SMDCDVISRIFRIcnlTRPQEGYLMvQQFQYLGWASHrEVPGSKRSFLKLilqVEKWQEECDEGEGRTIIHCLNGGGRSG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 665389652 1534 TFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQY 1574
Cdd:cd14636   157 MFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQY 197
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1383-1574 1.33e-19

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: 88.98  E-value: 1.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCfeKGREKCDQYWPVDRVAMfYGDIKVQLIIDT 1462
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENGVHR-HGPIQVEFVSAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1463 HYHDWSISEFMVSRNCES----RIMRHFHFTTWPDF-GVPEPPQSLVRFVRAF----RDVIGTDMRpIIVHCSAGVGRSG 1533
Cdd:cd14635    78 LEEDIISRIFRIYNAARPqdgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVdkwqEEYNGGEGR-TVVHCLNGGGRSG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 665389652 1534 TFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQY 1574
Cdd:cd14635   157 TFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQY 197
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1383-1583 1.36e-19

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: 88.97  E-value: 1.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1383 YINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCdQYWPVDRVAMFYGDIKVQLIID- 1461
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEF-VYWPSREESMNCEAFTVTLISKd 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1462 ----THYHDWSISEFMVSRNCESRIM--RHFHFTTWPDfgvPEPP-QSLVRFVRAFRDVIGTDMRPIIVHCSAGVGRSGT 1534
Cdd:cd17670    80 rlclSNEEQIIIHDFILEATQDDYVLevRHFQCPKWPN---PDAPiSSTFELINVIKEEALTRDGPTIVHDEFGAVSAGT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 665389652 1535 FIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLLA 1583
Cdd:cd17670   157 LCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1320-1588 3.34e-15

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 78.47  E-value: 3.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1320 IMSADSDFRFSEEFEELKHVGRDQACSFANLPCNRPK--NRFTNILPYDHSRFKLQpvddDDGSdYINANYMPGHNSPRE 1397
Cdd:PHA02740   18 INKPDLLSCIIKEYRAIVPEHEDEANKACAQAENKAKdeNLALHITRLLHRRIKLF----NDEK-VLDARFVDGYDFEQK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1398 FIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKgreKC-DQYWPV-DRVAMFYGDIKV---QLIIDTHYHDWSISef 1472
Cdd:PHA02740   93 FICIINLCEDACDKFLQALSDNKVQIIVLISRHADK---KCfNQFWSLkEGCVITSDKFQIetlEIIIKPHFNLTLLS-- 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1473 MVSRNCESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIgTDMR---------PIIVHCSAGVGRSGTFIALDRILQ 1543
Cdd:PHA02740  168 LTDKFGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLC-ADLEkhkadgkiaPIIIDCIDGISSSAVFCVFDICAT 246

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 665389652 1544 HIHKSDYVDIFGIVFAMRKERVFMVQTEQQYVCIHQCLLAVLEGK 1588
Cdd:PHA02740  247 EFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLKEK 291
fn3 pfam00041
Fibronectin type III domain;
902-978 8.82e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.74  E-value: 8.82e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   902 PISDLKAIQVAAREITLHWTAPA---GEYTDFELQYLSADEEAPQLLQNVTKNT-EITLQGLRPYHNYTFTVVVRSGSIQ 977
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   .
gi 665389652   978 G 978
Cdd:pfam00041   82 G 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
319-749 1.01e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 66.56  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  319 VQTVSEDETSSVPTTARYLTVPERVLNVTFDEAYTTSSSFRVRWEP-PRTYSEFDAYQVMLS--TSRRIFNVPRAANGDS 395
Cdd:COG3401    26 LSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGrAGTTSGVAAVAVAAAppTATGLTTLTGSGSVGG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  396 VYFDYPDILEPGRTYEVVVKTIADNVNSWPASGEVTLRPRPVRSLGGFLDDRSNALHISWEPAETGRQDSYrisyheqtn 475
Cdd:COG3401   106 ATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSA--------- 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  476 asevPAPFPVAAESQITTNLTEYTLDsLLAGRRYLIAVQALSKGVASNASD----ITRYTRPAAPliQELRSIDQG---L 548
Cdd:COG3401   177 ----TAAVATTSLTVTSTTLVDGGGD-IEPGTTYYYRVAATDTGGESAPSNevsvTTPTTPPSAP--TGLTATADTpgsV 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  549 MLSWRSDVNSRQDRYEVhYQRNGTREERTM--ATNETSLTIHYLHPGSGYEVKVHAI-SHGVRSEPHSYFQAV----FPK 621
Cdd:COG3401   250 TLSWDPVTESDATGYRV-YRSNSGDGPFTKvaTVTTTSYTDTGLTNGTTYYYRVTAVdAAGNESAPSNVVSVTtdltPPA 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  622 PPQNLTLQTVHTNLVVLHWQAPEGSDFSEYVVrYRTDAS--PWQRI-SGLHENEARIKDMHYGERYLVQVNTV-SFGVES 697
Cdd:COG3401   329 APSGLTATAVGSSSITLSWTASSDADVTGYNV-YRSTSGggTYTKIaETVTTTSYTDTGLTPGTTYYYKVTAVdAAGNES 407

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665389652  698 PHPLELNVTMPPQPVSNVVPLVdsrnlTLEWPRPDGHVDFYTLKWWPTDEED 749
Cdd:COG3401   408 APSEEVSATTASAASGESLTAS-----VDAVPLTDVAGATAAASAASNPGVS 454
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 900-988 1.92e-10

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 59.05  E-value: 1.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  900 PLPISDLKAIQVAAREITLHWTAPA---GEYTDFELQYLSADEEAPQLLQ-NVTKNTEITLQGLRPYHNYTFTVVVRSGS 975
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEvTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|...
gi 665389652  976 IQGTDFADVSVST 988
Cdd:cd00063    81 GESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
247-328 7.26e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.04  E-value: 7.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   247 PGKFIVWFRNETTLLVLWQPPFPA-GIYTHYRVSITPDDAIQSVLYVEregEPPGPAQAAFKGLVPGREYNISVQTVSED 325
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPPDGnGPITGYEVEYRPKNSGEPWNEIT---VPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ...
gi 665389652   326 ETS 328
Cdd:pfam00041   80 GEG 82
fn3 pfam00041
Fibronectin type III domain;
1013-1092 1.25e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 56.65  E-value: 1.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  1013 FQPSDVQPGEVTFEWSlEPAEQHGPIDYFRITCQNADDAADVSSYEFPVNATQGKIDGLVPGNHYIFRIQAKSALGYGAE 1092
Cdd:pfam00041    6 LTVTDVTSTSLTVSWT-PPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
PTP_tm pfam18861
TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases ...
 1127-1247 1.70e-09

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.


Pssm-ID: 465889  Cd Length: 126  Bit Score: 57.23  E-value: 1.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  1127 FRQGYFSNAHGMVRSYTIIIAEDVGKNASGLEMPS--WQD-----VQAY-TVWLPyqaiepyNPFlTSNGSRKSSLEAEh 1198
Cdd:pfam18861    1 IQFSLFNSSNGPIKAYGVIVTTNDSLNRPLKEYLNktYYDwkykkTDSYlATVTP-------NPF-TSPRSSSRSLTVP- 71

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  1199 ftIGTANCDKhqaGYCNGPLRAGTTYRIKIRAFTD-----------EDKFTDTVYSSPIT 1247
Cdd:pfam18861   72 --VGTGSKWQ---GYCNGPLKPLGSYRFSVAAFTRlefddglidgeESYVSFTPFSEPIA 126
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1007-1098 4.52e-09

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 55.20  E-value: 4.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1007 PGKVDYFQPSDVQPGEVTFEWSlEPAEQHGPIDYFRITCQNADDAADVSSYEFPVNATQGKIDGLVPGNHYIFRIQAKSA 1086
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWT-PPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                          90
                  ....*....|....
gi 665389652 1087 LGYG--AEREHIQT 1098
Cdd:cd00063    80 GGESppSESVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
772-1171 5.28e-09

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 61.17  E-value: 5.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  772 EDLSPGRQYRFEVQASSNGIRSGT----THLSTRTMPLIQSDVFIANAGHEQgqdetITLSYTPTPA-DSTRFDIYRFSM 846
Cdd:COG3401   197 GDIEPGTTYYYRVAATDTGGESAPsnevSVTTPTTPPSAPTGLTATADTPGS-----VTLSWDPVTEsDATGYRVYRSNS 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  847 GDPTIkdkEKLANDTERKLSFSGLTPGKLYNVTVWTV-SGGVASLPVQRLY----RLHPLPISDLKAIQVAAREITLHWT 921
Cdd:COG3401   272 GDGPF---TKVATVTTTSYTDTGLTNGTTYYYRVTAVdAAGNESAPSNVVSvttdLTPPAAPSGLTATAVGSSSITLSWT 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  922 APAGEY-TDFELQYLSADEEAPQLLQNVTKNTEITLQGLRPYHNYTFTVV-VRSGSIQGTdfadvsvstlmrSSAPISAS 999
Cdd:COG3401   349 ASSDADvTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTaVDAAGNESA------------PSEEVSAT 416

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1000 yqTLTAPPGKVDYFQPSDVqPGEVTFEWSLEPAEQHGPIDYfriTCQNADDAADVSSYEFpVNATQGKIDGLVPGNHYIF 1079
Cdd:COG3401   417 --TASAASGESLTASVDAV-PLTDVAGATAAASAASNPGVS---AAVLADGGDTGNAVPF-TTTSSTVTATTTDTTTANL 489

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1080 RIQAKSA-LGYGAEREHIQTMPILAPPVPEPSVTPLEVSRTSSTIEISFRQGYFSNAHGMVRSYTIIIAEDVGKNASGLE 1158
Cdd:COG3401   490 SVTTGSLvGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSG 569

                         410
                  ....*....|...
gi 665389652 1159 MPSWQDVQAYTVW 1171
Cdd:COG3401   570 NLYLITTLGGSLL 582
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 620-706 2.83e-08

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 52.88  E-value: 2.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  620 PKPPQNLTLQTVHTNLVVLHWQAPE--GSDFSEYVVRYR-TDASPWQRISG--LHENEARIKDMHYGERYLVQVNTVSFG 694
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEddGGPITGYVVEYReKGSGDWKEVEVtpGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|..
gi 665389652  695 VESPHPLELNVT 706
Cdd:cd00063    81 GESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 900-974 3.45e-08

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: 52.23  E-value: 3.45e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665389652    900 PLPISDLKAIQVAAREITLHWTAPAGE-YTDFELQYLSADEEAPQLLQNVTKN---TEITLQGLRPYHNYTFTVVVRSG 974
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDgITGYIVGYRVEYREEGSEWKEVNVTpssTSYTLTGLKPGTEYEFRVRAVNG 79
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 1357-1577 3.48e-08

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: 56.25  E-value: 3.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1357 NRFTNIlpydHSRFKLQpvdddDGSDyINANYMPGHNSPReFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGRE 1436
Cdd:cd14559     1 NRFTNI----QTRVSTP-----VGKN-LNANRVQIGNKNV-AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRK 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1437 KCDQYWpvdRVAMFYGDIKV--------QLIIDTHYHDWSisefMVSRNCESRI-MRHFHFTTWPDFGV--PEPPQSLVR 1505
Cdd:cd14559    70 GLPPYF---RQSGTYGSVTVkskktgkdELVDGLKADMYN----LKITDGNKTItIPVVHVTNWPDHTAisSEGLKELAD 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1506 FVRAFRD-------------VIGTD-MRPIIvHCSAGVGRSGTFIALDRILQHIHKSDYVDifgIVFAMRKER-VFMVQT 1570
Cdd:cd14559   143 LVNKSAEekrnfykskgssaINDKNkLLPVI-HCRAGVGRTGQLAAAMELNKSPNNLSVED---IVSDMRTSRnGKMVQK 218


                  ....*..
gi 665389652 1571 EQQYVCI 1577
Cdd:cd14559   219 DEQLDTL 225
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
94-334 7.34e-08

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 57.32  E-value: 7.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   94 SPPFGFPEPNTTIPASDIGKDIKFSRALPGTEYNFWLYYTNSTHREQLTWTVNIT---TAPDPPANLSVQLRSSKSAFIT 170
Cdd:COG3401   173 DTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTtptTPPSAPTGLTATADTPGSVTLS 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  171 WRPPGSGRYSGFRIRVLGLTDLPFERSYSLEGNEtlqLSAKELTPGGSY--QVQAYSvYQGKES----VAYTSRNfTTKP 244
Cdd:COG3401   253 WDPVTESDATGYRVYRSNSGDGPFTKVATVTTTS---YTDTGLTNGTTYyyRVTAVD-AAGNESapsnVVSVTTD-LTPP 327

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  245 NTPGKFIVWFRNETTLLVLWQPPFPAGIyTHYRV--SITPDDAIQSVlyvereGEPPGPAQAAFKGLVPGREYNISVQTV 322
Cdd:COG3401   328 AAPSGLTATAVGSSSITLSWTASSDADV-TGYNVyrSTSGGGTYTKI------AETVTTTSYTDTGLTPGTTYYYKVTAV 400

                         250
                  ....*....|..
gi 665389652  323 SEDETSSVPTTA 334
Cdd:COG3401   401 DAAGNESAPSEE 412
fn3 pfam00041
Fibronectin type III domain;
622-698 1.46e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.49  E-value: 1.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   622 PPQNLTLQTVHTNLVVLHWQAPE--GSDFSEYVVRYRT----DASPWQRISGlHENEARIKDMHYGERYLVQVNTVSFGV 695
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgNGPITGYEVEYRPknsgEPWNEITVPG-TTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 665389652   696 ESP 698
Cdd:pfam00041   81 EGP 83
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1478-1537 2.74e-07

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 51.51  E-value: 2.74e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1478 CESRIMRHFHFTtWPDFGVPEPPQsLVRFVRAFRDVIGTDmRPIIVHCSAGVGRSGTFIA 1537
Cdd:COG2453    43 LEEAGLEYLHLP-IPDFGAPDDEQ-LQEAVDFIDEALREG-KKVLVHCRGGIGRTGTVAA 99
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1507-1579 3.15e-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: 50.43  E-value: 3.15e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665389652 1507 VRAFRDVIG---TDMRPIIVHCSAGVGRSGTFIALDRILQHIHksdyvDIFGIVFAMRKERVF-MVQTEQQYVCIHQ 1579
Cdd:cd14494    42 VDRFLEVLDqaeKPGEPVLVHCKAGVGRTGTLVACYLVLLGGM-----SAEEAVRIVRLIRPGgIPQTIEQLDFLIK 113
fn3 pfam00041
Fibronectin type III domain;
708-796 3.45e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 49.72  E-value: 3.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   708 PPQPVSnVVPlVDSRNLTLEWPRP---DGHVDFYTLKWWPTDEEDrvefknVTQLEDLSSPSVRIPIEDLSPGRQYRFEV 784
Cdd:pfam00041    2 APSNLT-VTD-VTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGE------PWNEITVPGTTTSVTLTGLKPGTEYEVRV 73

                           90
                   ....*....|..
gi 665389652   785 QASSNGIRSGTT 796
Cdd:pfam00041   74 QAVNGGGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 709-793 6.05e-07

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 49.03  E-value: 6.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  709 PQPVSNV-VPLVDSRNLTLEWPRPD---GHVDFYTLKWWPTDEEDRVEFKNvtqlEDLSSPSVRIPieDLSPGRQYRFEV 784
Cdd:cd00063     1 PSPPTNLrVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEV----TPGSETSYTLT--GLKPGTEYEFRV 74


                  ....*....
gi 665389652  785 QASSNGIRS 793
Cdd:cd00063    75 RAVNGGGES 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 151-242 7.43e-07

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 49.03  E-value: 7.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  151 PDPPANLSVQLRSSKSAFITWRPPGS--GRYSGFRIRVLGLTDLPFERSYSLEGNETlQLSAKELTPGGSYQVQAYSVYQ 228
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDdgGPITGYVVEYREKGSGDWKEVEVTPGSET-SYTLTGLKPGTEYEFRVRAVNG 79

                          90
                  ....*....|....
gi 665389652  229 GKESVAYTSRNFTT 242
Cdd:cd00063    80 GGESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
152-232 1.06e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 48.18  E-value: 1.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   152 DPPANLSVQLRSSKSAFITWRPP--GSGRYSGFRIRVLGLTDLPFERSYSLEGNETlQLSAKELTPGGSYQVQAYSVYQG 229
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdGNGPITGYEVEYRPKNSGEPWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVNGG 79


                   ...
gi 665389652   230 KES 232
Cdd:pfam00041   80 GEG 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 620-697 1.13e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.99  E-value: 1.13e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652    620 PKPPQNLTLQTVHTNLVVLHWQAPEGSDFSEYVVRYR----TDASPWQRISGLH-ENEARIKDMHYGERYLVQVNTVSFG 694
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRveyrEEGSEWKEVNVTPsSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 665389652    695 VES 697
Cdd:smart00060   81 GEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1007-1090 1.44e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.61  E-value: 1.44e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   1007 PGKVDYFQPSDVQPGEVTFEWS-LEPAEQHGPIDYFRItcQNADDAADVSSYEFPVNATQGKIDGLVPGNHYIFRIQAKS 1085
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEpPPDDGITGYIVGYRV--EYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 665389652   1086 ALGYG 1090
Cdd:smart00060   79 GAGEG 83
fn3 pfam00041
Fibronectin type III domain;
443-525 1.65e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.79  E-value: 1.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   443 FLDDRSNALHISWEPAETGRQ--DSYRISYhEQTNASEVPAPFPVAAesqittNLTEYTLDSLLAGRRYLIAVQALSKGV 520
Cdd:pfam00041    8 VTDVTSTSLTVSWTPPPDGNGpiTGYEVEY-RPKNSGEPWNEITVPG------TTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 665389652   521 ASNAS 525
Cdd:pfam00041   81 EGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 244-338 2.69e-06

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.49  E-value: 2.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  244 PNTPGKFIVWFRNETTLLVLWQPP-FPAGIYTHYRVSITPDDAIQSVLYVEREGEPPgpaQAAFKGLVPGREYNISVQTV 322
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPeDDGGPITGYVVEYREKGSGDWKEVEVTPGSET---SYTLTGLKPGTEYEFRVRAV 77

                          90
                  ....*....|....*.
gi 665389652  323 SEDETSSVPTTARYLT 338
Cdd:cd00063    78 NGGGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 548-611 4.26e-06

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 46.72  E-value: 4.26e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665389652  548 LMLSWR--SDVNSRQDRYEVHYQRNGTREERTMAT---NETSLTIHYLHPGSGYEVKVHAISHGVRSEP 611
Cdd:cd00063    17 VTLSWTppEDDGGPITGYVVEYREKGSGDWKEVEVtpgSETSYTLTGLKPGTEYEFRVRAVNGGGESPP 85
fn3 pfam00041
Fibronectin type III domain;
548-612 5.12e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.25  E-value: 5.12e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   548 LMLSWR--SDVNSRQDRYEVHYQ-RNGTRE--ERTMATNETSLTIHYLHPGSGYEVKVHAISHGVRSEPH 612
Cdd:pfam00041   16 LTVSWTppPDGNGPITGYEVEYRpKNSGEPwnEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 708-786 5.62e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 46.07  E-value: 5.62e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652    708 PPQPVSNVVPLVDSRNLTLEWPRP-DGHVDFYTLKWWPTDEEDRVEFKNVTqlEDLSSPSVRIpiEDLSPGRQYRFEVQA 786
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPpDDGITGYIVGYRVEYREEGSEWKEVN--VTPSSTSYTL--TGLKPGTEYEFRVRA 76
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
74-528 1.31e-05

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 50.00  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652   74 LVINVPNASSNANAFYRIDYSPPFGFPEPNTTIPASDIGKDIKFSRALPGTEYNFWLYYTNSTHREQLTWTVNITTAPDP 153
Cdd:COG3401    56 LVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGA 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  154 PANLSVQLRSSKSAFITWRPPGSGRYSGFRIRVLGLTDLPF----ERSYSLEGNETLQLSAKELTPGGSYQ--VQAY-SV 226
Cdd:COG3401   136 ATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSAtaavATTSLTVTSTTLVDGGGDIEPGTTYYyrVAATdTG 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  227 YQGKESVAYTSRNFTTKPNTPGKFIVWFRNETTLLVLWQPPFPAGIyTHYRvsitpddaiqsvlyVEREGEPPGP----- 301
Cdd:COG3401   216 GESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESDA-TGYR--------------VYRSNSGDGPftkva 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  302 --AQAAF--KGLVPGREYNISVQTVSEDETSSVP----TTARYLTVPERVLNVTFdeAYTTSSSFRVRWEPPrTYSEFDA 373
Cdd:COG3401   281 tvTTTSYtdTGLTNGTTYYYRVTAVDAAGNESAPsnvvSVTTDLTPPAAPSGLTA--TAVGSSSITLSWTAS-SDADVTG 357

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  374 YQVMLSTSRRIFNVPRAANGDSV-YFDypDILEPGRTYEVVVKTIADNVNSWPASGEV-----TLRPRPVRSLGGFLDDR 447
Cdd:COG3401   358 YNVYRSTSGGGTYTKIAETVTTTsYTD--TGLTPGTTYYYKVTAVDAAGNESAPSEEVsattaSAASGESLTASVDAVPL 435

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  448 SNALHISWEPAETGRQDSYRISYheqTNASEVPAPFPVAAESQITTNLTEYTLDSLLAGRRYLIAVQALSKGVASNASDI 527
Cdd:COG3401   436 TDVAGATAAASAASNPGVSAAVL---ADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVI 512


                  .
gi 665389652  528 T 528
Cdd:COG3401   513 G 513
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1492-1537 2.13e-05

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 46.12  E-value: 2.13e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 665389652 1492 PDFGVPEPPQsLVRFVRAFRDVIgTDMRPIIVHCSAGVGRSGTFIA 1537
Cdd:cd14504    58 EDYTPPTLEQ-IDEFLDIVEEAN-AKNEAVLVHCLAGKGRTGTMLA 101
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 151-232 3.79e-05

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 43.76  E-value: 3.79e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652    151 PDPPANLSVQLRSSKSAFITWRPPGSGRYSGFRI--RVLGLTDLPFERSYSLEGNETlQLSAKELTPGGSYQVQAYSVYQ 228
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVgyRVEYREEGSEWKEVNVTPSST-SYTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 665389652    229 GKES 232
Cdd:smart00060   80 AGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 434-531 3.94e-05

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: 44.02  E-value: 3.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  434 PRPVRSLGgFLDDRSNALHISWEPAET--GRQDSYRISYHEQTNASEVPAPFPVAAEsqittnlTEYTLDSLLAGRRYLI 511
Cdd:cd00063     1 PSPPTNLR-VTDVTSTSVTLSWTPPEDdgGPITGYVVEYREKGSGDWKEVEVTPGSE-------TSYTLTGLKPGTEYEF 72

                          90       100
                  ....*....|....*....|
gi 665389652  512 AVQALSKGVASNASDITRYT 531
Cdd:cd00063    73 RVRAVNGGGESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 434-519 6.95e-05

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 42.99  E-value: 6.95e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652    434 PRPVRSLGgFLDDRSNALHISWEPAETGRQDSYRISYHEQTNASEvpapfPVAAESQITTNLTEYTLDSLLAGRRYLIAV 513
Cdd:smart00060    1 PSPPSNLR-VTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEG-----SEWKEVNVTPSSTSYTLTGLKPGTEYEFRV 74


                    ....*.
gi 665389652    514 QALSKG 519
Cdd:smart00060   75 RAVNGA 80
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
451-603 1.36e-04

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


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 46.86  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  451 LHISWEPAETGrqDSYRIsYHEQTNASEVPAPfpvaaesqiTTNLTEYTLDSLLAGRrYLIAVQALS-KGVASNASDITR 529
Cdd:COG4733   554 LTVSWDAPAGA--VAYEV-EWRRDDGNWVSVP---------RTSGTSFEVPGIYAGD-YEVRVRAINaLGVSSAWAASSE 620

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  530 YT------RPAAPLIQELRSIDQGLMLSWRSDVNSRQDRYEVHYQRNGTREERTMATNE---TSLTIHYLHPGSGYEVKV 600
Cdd:COG4733   621 TTvtgktaPPPAPTGLTATGGLGGITLSWSFPVDADTLRTEIRYSTTGDWASATVAQALypgNTYTLAGLKAGQTYYYRA 700


                  ...
gi 665389652  601 HAI 603
Cdd:COG4733   701 RAV 703
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 533-609 2.00e-04

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 41.83  E-value: 2.00e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652    533 PAAPLIQELRSIDQG-LMLSWRSDVNSRQDRYEVHYQRNGTREER-----TMATNETSLTIHYLHPGSGYEVKVHAISHG 606
Cdd:smart00060    1 PSPPSNLRVTDVTSTsVTLSWEPPPDDGITGYIVGYRVEYREEGSewkevNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 665389652    607 VRS 609
Cdd:smart00060   81 GEG 83
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1483-1593 2.39e-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: 44.26  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1483 MRH---FHFTTWPDFGVPePPQSLVRFVRAFRDVIGTDMRpIIVHCSAGVGRSGTFIALDRI-LQHIHKSDYVDIFgivf 1558
Cdd:cd14506    73 MRAgiyFYNFGWKDYGVP-SLTTILDIVKVMAFALQEGGK-VAVHCHAGLGRTGVLIACYLVyALRMSADQAIRLV---- 146

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 665389652 1559 amRKERVFMVQTEQQYVCIHqcllavlEGKEHLLA 1593
Cdd:cd14506   147 --RSKRPNSIQTRGQVLCVR-------EFAQFLLP 172
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 244-328 2.58e-04

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 41.45  E-value: 2.58e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652    244 PNTPGKFIVWFRNETTLLVLWQPPFPAGIyTHYRVSITPDDAIQSVLYVEREGEPPGPaQAAFKGLVPGREYNISVQTVS 323
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGI-TGYIVGYRVEYREEGSEWKEVNVTPSST-SYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 665389652    324 EDETS 328
Cdd:smart00060   79 GAGEG 83
fn3 pfam00041
Fibronectin type III domain;
345-417 5.89e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 40.48  E-value: 5.89e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665389652   345 NVTFDEayTTSSSFRVRWEPPRTY-SEFDAYQVMLSTSRRI-----FNVPRAANgdSVYFDYpdiLEPGRTYEVVVKTI 417
Cdd:pfam00041    5 NLTVTD--VTSTSLTVSWTPPPDGnGPITGYEVEYRPKNSGepwneITVPGTTT--SVTLTG---LKPGTEYEVRVQAV 76
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
535-661 6.37e-04

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


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 44.55  E-value: 6.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  535 APLIQELRSIDQG-----LMLSWRSDVNSrqDRYEVHYQRNGTREERTMATNETSLTIHYLHPGSgYEVKVHAIS-HGVR 608
Cdd:COG4733   536 VTTSESLSVVAQGtavttLTVSWDAPAGA--VAYEVEWRRDDGNWVSVPRTSGTSFEVPGIYAGD-YEVRVRAINaLGVS 612

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 665389652  609 SEP--HSYFQAVF----PKPPQNLTLqTVHTNLVVLHWQAPEGSDFSEYVVRYRTDASP 661
Cdd:COG4733   613 SAWaaSSETTVTGktapPPAPTGLTA-TGGLGGITLSWSFPVDADTLRTEIRYSTTGDW 670
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
916-1088 1.17e-03

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


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 43.78  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  916 ITLHWTAPAGeYTDFELQYLSADEEapQLLQNVTKNTEITLQGLRPyHNYTFTVVvrsgsiqgtdfadvSVSTLMRSSAP 995
Cdd:COG4733   554 LTVSWDAPAG-AVAYEVEWRRDDGN--WVSVPRTSGTSFEVPGIYA-GDYEVRVR--------------AINALGVSSAW 615

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652  996 ISASYQTLT---APPGKVDYFQPSdVQPGEVTFEWSLEPAeqhGPIDYFRITCQNADDAADVSSYEFPVNATQGKIDGLV 1072
Cdd:COG4733   616 AASSETTVTgktAPPPAPTGLTAT-GGLGGITLSWSFPVD---ADTLRTEIRYSTTGDWASATVAQALYPGNTYTLAGLK 691

                         170
                  ....*....|....*.
gi 665389652 1073 PGNHYIFRIQAKSALG 1088
Cdd:COG4733   692 AGQTYYYRARAVDRSG 707
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1478-1579 5.38e-03

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: 39.55  E-value: 5.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1478 CESRIMRHFHFTTwPDFGVPEPPQSLVRFVRAFRDVIGtDMRPIIVHCSAGVGRSGTFIAldRILqhIHKSDYVDIFGIV 1557
Cdd:cd14505    68 YQQAGITWHHLPI-PDGGVPSDIAQWQELLEELLSALE-NGKKVLIHCKGGLGRTGLIAA--CLL--LELGDTLDPEQAI 141

                          90       100
                  ....*....|....*....|..
gi 665389652 1558 FAMRKERVFMVQTEQQYVCIHQ 1579
Cdd:cd14505   142 AAVRALRPGAIQTPKQENFLHQ 163
UP_III cd09968
Uroplakin III; Uroplakin IIIa and IIIb, the dimerization partners of uroplakin Ib, are a ...
 1106-1248 7.44e-03

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


Pssm-ID: 197377  Cd Length: 187  Bit Score: 39.67  E-value: 7.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389652 1106 VPEPSVTPLEVSRTSSTIEISFRQGYFSNAHG---------MVRSYTIIIAEDVGKNASGLEMPSWQDVQAYtvwlPYQA 1176
Cdd:cd09968     6 VPQLASTFLEGNPTSTTFTLEQPRCVFDSSASdtddvwlvvAVSNATNNFNAPQNSTDPISTYSQFSGGQYY----LTLR 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665389652 1177 IEPYNPfltsnGSRKSSLEAEHFTIG-TANCdkHQAGYCNGPLRAGTTYRIKIrAFTDEDKFTD-TVYSSPITT 1248
Cdd:cd09968    82 ASRDLY-----PCGNPSLNAYVLRVGaDGNC--TDNGNCNGPLPGPGPYRVKY-LVMNGSGVVAqTNWSDPIRL 147
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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