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Conserved domains on  [gi|1720354226|ref|XP_030108157|]
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tyrosine-protein phosphatase non-receptor type 14 isoform X1 [Mus musculus]

Protein Classification

FRMD7 family protein; protein-tyrosine phosphatase family protein( domain architecture ID 13902224)

FRMD7 family protein similar to Homo sapiens FERM domain-containing protein 7 (FRMD7) that plays a role in neurite development| protein-tyrosine phosphatase family protein, similar to Saccharomyces cerevisiae OCA6 that is required for replication of Brome mosaic virus, but may be inactive as a protein-tyrosine phosphatase as it lacks the CxxxxxR catalytic motif

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 898-1184 0e+00

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: 625.48  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  898 RLRALKKKLEDGMVFTEYEQIPNKKANGVFSTATLPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKVVVGGS 977
Cdd:cd14599      1 RCKTLERKLEEGMVFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  978 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTG 1057
Cdd:cd14599     81 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1058 LKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSVLEGIRTRHPPIVVHCSAGVGRTGVVILSE 1137
Cdd:cd14599    161 LKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDSTKNCNPPIVVHCSAGVGRTGVVILTE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1720354226 1138 LMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 1184
Cdd:cd14599    241 LMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 24-220 5.71e-54

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


:

Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 187.12  E-value: 5.71e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226    24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQAR-WVELEKPLKKHLDKFANEPLlFFGVMFY 102
Cdd:smart00295    3 KVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRhWLDPAKTLLDQDVKSEPLTL-YFRVKFY 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   103 VPNVSRLQQEATRY-QYYLQVKKDVLEGRLRCSLEQVIRLAGLAVQADFGDYNQFDS--QEFLREYVLFPMDLAMEEaAL 179
Cdd:smart00295   82 PPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdlRGELSLKRFLPKQLLDSR-KL 160

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 1720354226   180 EELTQKVAQEHKAHSGILPAEAELMYINEVERLDGFGQEIF 220
Cdd:smart00295  161 KEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 215-305 5.57e-29

FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and 21); This CD contains PTP members: pez/PTPN14 and PTPN21. A number of mutations in Pez have been shown to be associated with breast and colorectal cancer. The PTPN protein family belong to larger family of PTPs. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. The members are composed of a N-terminal FERM domain and a C-terminal PTP catalytic domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. Like most other ERM members they have a phosphoinositide-binding site in their FERM domain. The FERM C domain is the third structural domain within the FERM domain. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


:

Pssm-ID: 270009  Cd Length: 91  Bit Score: 111.23  E-value: 5.57e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  215 FGQEIFPVKDSHGNSVHLGIFFMGIFVRNRVGRQAVIYRWNDIGSVTHSKAAILLELIDKEETALFHTDDIENAKYISRL 294
Cdd:cd13188      1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRPPVFFRWEDIKNVINHKRTFSIECQNSEETVQFQFEDAETAKYVWKL 80

                           90
                   ....*....|.
gi 1720354226  295 FTTRHKFYKQN 305
Cdd:cd13188     81 CVLQHKFYRQN 91
 
Name Accession Description Interval E-value
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 898-1184 0e+00

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: 625.48  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  898 RLRALKKKLEDGMVFTEYEQIPNKKANGVFSTATLPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKVVVGGS 977
Cdd:cd14599      1 RCKTLERKLEEGMVFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  978 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTG 1057
Cdd:cd14599     81 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1058 LKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSVLEGIRTRHPPIVVHCSAGVGRTGVVILSE 1137
Cdd:cd14599    161 LKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDSTKNCNPPIVVHCSAGVGRTGVVILTE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1720354226 1138 LMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 1184
Cdd:cd14599    241 LMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
935-1181 5.71e-92

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 294.92  E-value: 5.71e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  935 NAERSRIREVVPYEENRVELIPTKENNtGYINASHIKVVVGgsEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEE 1014
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPS-DYINASYIDGYKK--PKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1015 EGGRTKSHRYWPKlgSKHSSATYGKFKVTTK-FRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLS 1093
Cdd:pfam00102   78 EKGREKCAQYWPE--EEGESLEYGDFTVTLKkEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLD 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1094 YLEEIQSVRRHTnsvlegirtRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYK 1173
Cdd:pfam00102  156 LLRKVRKSSLDG---------RSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYI 226


                   ....*...
gi 1720354226 1174 FVYQVLVQ 1181
Cdd:pfam00102  227 FLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
911-1181 1.77e-91

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 294.57  E-value: 1.77e-91
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   911 VFTEYEQIP-NKKANGVFSTATLPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKVVvgGSEWHYIATQGPLP 989
Cdd:smart00194    2 LEEEFEKLDrLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGP--NGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   990 HTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhsSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQER 1069
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGE--PLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETR 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  1070 TVWHLQYTDWPHHGCPEDVQGFLSYLEEIqsvrRHTNSVLEGirtrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKV 1149
Cdd:smart00194  158 TVTHYHYTNWPDHGVPESPESILDLIRAV----RKSQSTSTG------PIVVHCSAGVGRTGTFIAIDILLQQLEAGKEV 227

                           250       260       270
                    ....*....|....*....|....*....|..
gi 1720354226  1150 EVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1181
Cdd:smart00194  228 DIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 24-220 5.71e-54

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 187.12  E-value: 5.71e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226    24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQAR-WVELEKPLKKHLDKFANEPLlFFGVMFY 102
Cdd:smart00295    3 KVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRhWLDPAKTLLDQDVKSEPLTL-YFRVKFY 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   103 VPNVSRLQQEATRY-QYYLQVKKDVLEGRLRCSLEQVIRLAGLAVQADFGDYNQFDS--QEFLREYVLFPMDLAMEEaAL 179
Cdd:smart00295   82 PPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdlRGELSLKRFLPKQLLDSR-KL 160

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 1720354226   180 EELTQKVAQEHKAHSGILPAEAELMYINEVERLDGFGQEIF 220
Cdd:smart00295  161 KEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_F1_PTPN14 cd17191
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 18-104 8.24e-53

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 14 (PTPN14) and similar proteins; PTPN14, also termed protein-tyrosine phosphatase pez, or PTPD2, or PTP36, is a widely expressed non-transmembrane cytosolic protein tyrosine phosphatase (PTP). It belongs to the FERM family of PTPs characterized by a conserved N-terminal FERM domain and a C-terminal PTP catalytic domain with an intervening sequence containing an acidic region and a putative SH3 domain-binding sequence. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN14 plays a role in the nucleus during cell proliferation. It forms a complex with Kibra and LATS1 proteins and negatively regulates the key Hippo pathway protein Yes-associated protein (YAP) oncogenic function by controlling its localization. It specifically regulates p130 Crk-associated substrate (p130Cas) phosphorylation at tyrosine residue 128 (Y128) in colorectal cancer (CRC) cells. Moreover, PTPN14 may be a critical enzyme in regulating endothelial cell function. It plays a crucial role in organogenesis by inducing transforming growth factor beta (TGFbeta) and epithelial-mesenchymal transition (EMT). It also acts as a modifier of angiogenesis and hereditary haemorrhagic telangiectasia. It regulates the lymphatic function and choanal development through the interaction with the vascular endothelial growth factor receptor 3 (VEGFR3), a receptor tyrosine kinase essential for lymphangiogenesis. Furthermore, PTPN14 functions as a regulator of cell motility through its action on cell-cell adhesion. Beta-Catenin, a central component of adherens junctions, has been identified as a PTPN14 substrate. PTPN14 works as a novel sperm-motility biomarker and a potential mitochondrial protein.


Pssm-ID: 340711  Cd Length: 87  Bit Score: 179.08  E-value: 8.24e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   18 KNCFVTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKFANEPLLFF 97
Cdd:cd17191      1 KNCFVTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKQLDKFANEPLLFF 80


                   ....*..
gi 1720354226   98 GVMFYVP 104
Cdd:cd17191     81 GVMFYVP 87
PHA02738 PHA02738
hypothetical protein; Provisional
 914-1184 3.21e-46

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 168.95  E-value: 3.21e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  914 EYEQIPNKKANGVFSTATlpENAERSRIREVVPYEENRVELiPTKENNTGYINASHikvvVGGSEW--HYIATQGPLPHT 991
Cdd:PHA02738    30 EHQKVISEKVDGTFNAEK--KNRKLNRYLDAVCFDHSRVIL-PAERNRGDYINANY----VDGFEYkkKFICGQAPTRQT 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  992 CHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLlSGQERTV 1071
Cdd:PHA02738   103 CYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDV--EQGSIRFGKFKITTTQVETHPHYVKSTLLLTDG-TSATQTV 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1072 WHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRR--HTNSVLEG-IRTRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEK 1148
Cdd:PHA02738   180 THFNFTAWPDHDVPKNTSEFLNFVLEVRQCQKelAQESLQIGhNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACAT 259

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1720354226 1149 VEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 1184
Cdd:PHA02738   260 VSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVN 295
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 104-220 4.53e-34

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 126.61  E-value: 4.53e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  104 PNVSRLQQEATRYQYYLQVKKDVLEGRLRCSLEQVIRLAGLAVQADFGDYNQFDSQ-EFLREYVLFPMDLaMEEAALEEL 182
Cdd:pfam00373    1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTsEYLSLESFLPKQL-LRKMKSKEL 79

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1720354226  183 TQKVAQEHKAHSGILPAEAELMYINEVERLDGFGQEIF 220
Cdd:pfam00373   80 EKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
895-1185 1.08e-29

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 119.81  E-value: 1.08e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  895 IDERLRALKKKLEDGMVFTEYEQIPNkkangvfstatlpeNAERSRIREVVPYEENRVEliptkeNNTGYINASHIKVvv 974
Cdd:COG5599     16 INSRLSTLTNELAPSHNDPQYLQNIN--------------GSPLNRFRDIQPYKETALR------ANLGYLNANYIQV-- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  975 gGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGG--RTKSHRYWpklgskHSSATYGKFKVTTK------F 1046
Cdd:COG5599     74 -IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISkpKVKMPVYF------RQDGEYGKYEVSSEltesiqL 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1047 RTDSGCYAttgLKVKHLLSGQE-RTVWHLQYTDWPHHGCP--EDVQGFLSYLEEIQSVRRHTNSvlegirtrhpPIVVHC 1123
Cdd:COG5599    147 RDGIEART---YVLTIKGTGQKkIEIPVLHVKNWPDHGAIsaEALKNLADLIDKKEKIKDPDKL----------LPVVHC 213

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720354226 1124 SAGVGRTGVVILselmIYCLE------HNEKVEVPTMLRFLREQR-MFMIQTIAQykfvYQVLVQFLQN 1185
Cdd:COG5599    214 RAGVGRTGTLIA----CLALSksinalVQITLSVEEIVIDMRTSRnGGMVQTSEQ----LDVLVKLAEQ 274
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 215-305 5.57e-29

FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and 21); This CD contains PTP members: pez/PTPN14 and PTPN21. A number of mutations in Pez have been shown to be associated with breast and colorectal cancer. The PTPN protein family belong to larger family of PTPs. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. The members are composed of a N-terminal FERM domain and a C-terminal PTP catalytic domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. Like most other ERM members they have a phosphoinositide-binding site in their FERM domain. The FERM C domain is the third structural domain within the FERM domain. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270009  Cd Length: 91  Bit Score: 111.23  E-value: 5.57e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  215 FGQEIFPVKDSHGNSVHLGIFFMGIFVRNRVGRQAVIYRWNDIGSVTHSKAAILLELIDKEETALFHTDDIENAKYISRL 294
Cdd:cd13188      1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRPPVFFRWEDIKNVINHKRTFSIECQNSEETVQFQFEDAETAKYVWKL 80

                           90
                   ....*....|.
gi 1720354226  295 FTTRHKFYKQN 305
Cdd:cd13188     81 CVLQHKFYRQN 91
FERM_C pfam09380
FERM C-terminal PH-like domain;
224-306 2.28e-10

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 58.03  E-value: 2.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  224 DSHGNSVHLGIFFMGIFVRNRVGRQAVIYRWNDIGSVTHSKAAILLELIDK--EETALFHTDDIENAKYISRLFTTRHKF 301
Cdd:pfam09380    1 DKEGTDLWLGVSAKGILVYEDNNKILNLFPWREIRKISFKRKKFLIKLRDKssEETLGFYTESSRACKYLWKLCVEQHTF 80


                   ....*
gi 1720354226  302 YKQNK 306
Cdd:pfam09380   81 FRLRR 85
 
Name Accession Description Interval E-value
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 898-1184 0e+00

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: 625.48  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  898 RLRALKKKLEDGMVFTEYEQIPNKKANGVFSTATLPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKVVVGGS 977
Cdd:cd14599      1 RCKTLERKLEEGMVFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  978 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTG 1057
Cdd:cd14599     81 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1058 LKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSVLEGIRTRHPPIVVHCSAGVGRTGVVILSE 1137
Cdd:cd14599    161 LKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDSTKNCNPPIVVHCSAGVGRTGVVILTE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1720354226 1138 LMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 1184
Cdd:cd14599    241 LMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 964-1184 1.07e-142

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: 429.40  E-value: 1.07e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINASHIKVVVGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVT 1043
Cdd:cd14598      1 YINASHIKVTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVTYGRFKIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1044 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSVLEGiRTRHPPIVVHC 1123
Cdd:cd14598     81 TRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTIDP-KSPNPPVLVHC 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720354226 1124 SAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 1184
Cdd:cd14598    160 SAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 964-1183 3.22e-137

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: 414.93  E-value: 3.22e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINASHIKVVVGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVT 1043
Cdd:cd14540      1 YINASHITATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHDALTFGEYKVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1044 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSVLEGiRTRHPPIVVHC 1123
Cdd:cd14540     81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQDVAG-HNRNPPTLVHC 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1124 SAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFL 1183
Cdd:cd14540    160 SAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
935-1181 5.71e-92

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 294.92  E-value: 5.71e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  935 NAERSRIREVVPYEENRVELIPTKENNtGYINASHIKVVVGgsEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEE 1014
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPS-DYINASYIDGYKK--PKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1015 EGGRTKSHRYWPKlgSKHSSATYGKFKVTTK-FRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLS 1093
Cdd:pfam00102   78 EKGREKCAQYWPE--EEGESLEYGDFTVTLKkEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLD 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1094 YLEEIQSVRRHTnsvlegirtRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYK 1173
Cdd:pfam00102  156 LLRKVRKSSLDG---------RSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYI 226


                   ....*...
gi 1720354226 1174 FVYQVLVQ 1181
Cdd:pfam00102  227 FLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
911-1181 1.77e-91

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 294.57  E-value: 1.77e-91
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   911 VFTEYEQIP-NKKANGVFSTATLPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKVVvgGSEWHYIATQGPLP 989
Cdd:smart00194    2 LEEEFEKLDrLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGP--NGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   990 HTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhsSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQER 1069
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGE--PLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETR 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  1070 TVWHLQYTDWPHHGCPEDVQGFLSYLEEIqsvrRHTNSVLEGirtrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKV 1149
Cdd:smart00194  158 TVTHYHYTNWPDHGVPESPESILDLIRAV----RKSQSTSTG------PIVVHCSAGVGRTGTFIAIDILLQQLEAGKEV 227

                           250       260       270
                    ....*....|....*....|....*....|..
gi 1720354226  1150 EVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1181
Cdd:smart00194  228 DIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 964-1177 1.53e-77

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: 253.75  E-value: 1.53e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINASHIKVvvGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHssATYGKFKVT 1043
Cdd:cd00047      1 YINASYIDG--YRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKP--LEYGDITVT 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1044 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSvlegirtrhpPIVVHC 1123
Cdd:cd00047     77 LVSEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNG----------PIVVHC 146

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720354226 1124 SAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1177
Cdd:cd00047    147 SAGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 896-1175 7.97e-72

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: 240.91  E-value: 7.97e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  896 DERLRALKKKLEDGMVFTEYEQIPNKKANGVFSTATLPENAERSRIREVVPYEENRVELiptkENNTGYINASHIKVVVG 975
Cdd:cd14600      1 EESMAQLKKGLESGTVLIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVL----QGNEDYINASYVNMEIP 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  976 GSEW--HYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLgskHSSATYGKFKVTTKFRTDSGCY 1053
Cdd:cd14600     77 SANIvnKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDP---PDVMEYGGFRVQCHSEDCTIAY 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1054 ATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYleeIQSVRRhtnsvlegIRTRHPPIVVHCSAGVGRTGVV 1133
Cdd:cd14600    154 VFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEF---VNYVRS--------KRVENEPVLVHCSAGIGRTGVL 222

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1720354226 1134 ILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFV 1175
Cdd:cd14600    223 VTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFV 264
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 964-1183 3.86e-69

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: 230.34  E-value: 3.86e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINASHIKVVVGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlGSKHSSATYGKFKVT 1043
Cdd:cd14538      1 YINASHIRIPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPD-SLNKPLICGGRLEVS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1044 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYleeIQSVRRHTNSVlegirtrhpPIVVHC 1123
Cdd:cd14538     80 LEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRF---IRYMRRIHNSG---------PIVVHC 147

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1124 SAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFL 1183
Cdd:cd14538    148 SAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 911-1176 2.92e-64

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: 219.16  E-value: 2.92e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  911 VFTEYEQIPNKKANGVFSTATLPENAERSRIREVVPYEENRVEL-IPTKENNTGYINASHikvvVGGSEWH--YIATQGP 987
Cdd:cd14543      5 IYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLpKRNGDERTDYINANF----MDGYKQKnaYIATQGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  988 LPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQ 1067
Cdd:cd14543     81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPL--EEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDE 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1068 ERTVWHLQYTDWPHHGCPEDVQGFLSYLEEiqsVRRHTNSVLEGIRTR---H---PPIVVHCSAGVGRTGVVILSELMIY 1141
Cdd:cd14543    159 SRQVTHFQFTSWPDFGVPSSAAALLDFLGE---VRQQQALAVKAMGDRwkgHppgPPIVVHCSAGIGRTGTFCTLDICLS 235

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1720354226 1142 CLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVY 1176
Cdd:cd14543    236 QLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 964-1175 3.24e-63

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: 213.73  E-value: 3.24e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINASHIKVVVGGSEW--HYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGskhSSATYGKFK 1041
Cdd:cd14541      2 YINANYVNMEIPGSGIvnRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLG---ETMQFGNLQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1042 VTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYleeIQSVRRHTNSVLEgirtrhpPIVV 1121
Cdd:cd14541     79 ITCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDF---VKRVRQNRVGMVE-------PTVV 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720354226 1122 HCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFV 1175
Cdd:cd14541    149 HCSAGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFV 202
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 964-1177 4.44e-60

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: 204.79  E-value: 4.44e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINASHIKVVVGGSEwHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPklgSKHSSATYGKFKVT 1043
Cdd:cd18533      1 YINASYITLPGTSSK-RYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWP---SGEYEGEYGDLTVE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1044 ----TKFrtDSGCYATTGLKVKHlLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSvlegirtrHPPI 1119
Cdd:cd18533     77 lvseEEN--DDGGFIVREFELSK-EDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASL--------DPPI 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720354226 1120 VVHCSAGVGRTGVVILSELMIYCLE--HNEKVE-------VPTMLRFLREQRMFMIQTIAQYKFVYQ 1177
Cdd:cd18533    146 IVHCSAGVGRTGTFIALDSLLDELKrgLSDSQDledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 934-1183 5.97e-58

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: 199.67  E-value: 5.97e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  934 ENAERSRIREVVPYEENRVELiptkENNTGYINASHIKVVVGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAE 1013
Cdd:cd14597      2 ENRKKNRYKNILPYDTTRVPL----GDEGGYINASFIKMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1014 EEGGRTKSHRYWPKLGSKhSSATYGKFKVT-TKFRTDSGcYATTGLKVKHLLSGQERTVWHLQYTDWPHHGC---PEDVQ 1089
Cdd:cd14597     78 VEGGKIKCQRYWPEILGK-TTMVDNRLQLTlVRMQQLKN-FVIRVLELEDIQTREVRHITHLNFTAWPDHDTpsqPEQLL 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1090 GFLSYLEEIQsvrrhtnsvlegirtRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTI 1169
Cdd:cd14597    156 TFISYMRHIH---------------KSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTE 220

                          250
                   ....*....|....
gi 1720354226 1170 AQYKFVYQVLVQFL 1183
Cdd:cd14597    221 DQYIFCYQVILYVL 234
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 935-1185 1.41e-57

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: 199.23  E-value: 1.41e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  935 NAERSRIREVVPYEENRVELIPTKENNTG--YINASHIKVVVGGS-----EWHYIATQGPLPHTCHDFWQMVWEQGVNVI 1007
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRDPNVPGsdYINANYIRNENEGPttdenAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1008 AMVTAEEEGGRTKSHRYWPKLGSKHSsatYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQ-ERTVWHLQYTDWPHHGCPE 1086
Cdd:cd14544     81 VMTTKEVERGKNKCVRYWPDEGMQKQ---YGPYRVQNVSEHDTTDYTLRELQVSKLDQGDpIREIWHYQYLSWPDHGVPS 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1087 DVQGFLSYLEEIQSVRRHTNSvlEGirtrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNE---KVEVPTMLRFLREQRM 1163
Cdd:cd14544    158 DPGGVLNFLEDVNQRQESLPH--AG------PIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRS 229

                          250       260
                   ....*....|....*....|..
gi 1720354226 1164 FMIQTIAQYKFVYQVLVQFLQN 1185
Cdd:cd14544    230 GMVQTEAQYKFIYVAVAQYIET 251
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 964-1181 1.41e-56

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: 195.16  E-value: 1.41e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINASHIKVVVGGSEW--HYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGskhSSATYGKFK 1041
Cdd:cd14601      2 YINANYINMEIPSSSIinRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPS---GSSSYGGFQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1042 VTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHtnsvlegirtRHPPIVV 1121
Cdd:cd14601     79 VTCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAG----------KDEPVVV 148

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1122 HCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1181
Cdd:cd14601    149 HCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 964-1176 4.35e-54

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: 187.56  E-value: 4.35e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINASHIkvvvggSEWH----YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhssaTYGK 1039
Cdd:cd14549      1 YINANYV------DGYNkaraYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTE----TYGN 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1040 FKVTTKFRTDSGCYATTGLKVKHL------LSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSvlegir 1113
Cdd:cd14549     71 IQVTLLSTEVLATYTVRTFSLKNLklkkvkGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAG------ 144

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720354226 1114 trhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVY 1176
Cdd:cd14549    145 ----PIVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 24-220 5.71e-54

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 187.12  E-value: 5.71e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226    24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQAR-WVELEKPLKKHLDKFANEPLlFFGVMFY 102
Cdd:smart00295    3 KVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRhWLDPAKTLLDQDVKSEPLTL-YFRVKFY 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   103 VPNVSRLQQEATRY-QYYLQVKKDVLEGRLRCSLEQVIRLAGLAVQADFGDYNQFDS--QEFLREYVLFPMDLAMEEaAL 179
Cdd:smart00295   82 PPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdlRGELSLKRFLPKQLLDSR-KL 160

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 1720354226   180 EELTQKVAQEHKAHSGILPAEAELMYINEVERLDGFGQEIF 220
Cdd:smart00295  161 KEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_F1_PTPN14 cd17191
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 18-104 8.24e-53

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 14 (PTPN14) and similar proteins; PTPN14, also termed protein-tyrosine phosphatase pez, or PTPD2, or PTP36, is a widely expressed non-transmembrane cytosolic protein tyrosine phosphatase (PTP). It belongs to the FERM family of PTPs characterized by a conserved N-terminal FERM domain and a C-terminal PTP catalytic domain with an intervening sequence containing an acidic region and a putative SH3 domain-binding sequence. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN14 plays a role in the nucleus during cell proliferation. It forms a complex with Kibra and LATS1 proteins and negatively regulates the key Hippo pathway protein Yes-associated protein (YAP) oncogenic function by controlling its localization. It specifically regulates p130 Crk-associated substrate (p130Cas) phosphorylation at tyrosine residue 128 (Y128) in colorectal cancer (CRC) cells. Moreover, PTPN14 may be a critical enzyme in regulating endothelial cell function. It plays a crucial role in organogenesis by inducing transforming growth factor beta (TGFbeta) and epithelial-mesenchymal transition (EMT). It also acts as a modifier of angiogenesis and hereditary haemorrhagic telangiectasia. It regulates the lymphatic function and choanal development through the interaction with the vascular endothelial growth factor receptor 3 (VEGFR3), a receptor tyrosine kinase essential for lymphangiogenesis. Furthermore, PTPN14 functions as a regulator of cell motility through its action on cell-cell adhesion. Beta-Catenin, a central component of adherens junctions, has been identified as a PTPN14 substrate. PTPN14 works as a novel sperm-motility biomarker and a potential mitochondrial protein.


Pssm-ID: 340711  Cd Length: 87  Bit Score: 179.08  E-value: 8.24e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   18 KNCFVTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKFANEPLLFF 97
Cdd:cd17191      1 KNCFVTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKQLDKFANEPLLFF 80


                   ....*..
gi 1720354226   98 GVMFYVP 104
Cdd:cd17191     81 GVMFYVP 87
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 964-1184 8.27e-53

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 183.80  E-value: 8.27e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINASHIKVVVGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgSKHSSATYGKFKVT 1043
Cdd:cd14596      1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPE--TLQEPMELENYQLR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1044 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRhtnsvlEGirtrhpPIVVHC 1123
Cdd:cd14596     79 LENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHN------TG------PIVVHC 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720354226 1124 SAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 1184
Cdd:cd14596    147 SAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 940-1177 9.16e-53

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: 184.48  E-value: 9.16e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  940 RIREVVPYEENRVELIP-TKENNTGYINASHIKvvvgG--SEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEG 1016
Cdd:cd14548      1 RYTNILPYDHSRVKLIPiNEEEGSDYINANYIP----GynSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEK 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1017 GRTKSHRYWPKlgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHllSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLE 1096
Cdd:cd14548     77 GRVKCDHYWPF---DQDPVYYGDITVTMLSESVLPDWTIREFKLER--GDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVR 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1097 EIQSVRRHTNSvlegirtrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVY 1176
Cdd:cd14548    152 LVRDYIKQEKG----------PTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221


                   .
gi 1720354226 1177 Q 1177
Cdd:cd14548    222 Q 222
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 933-1184 6.59e-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: 183.54  E-value: 6.59e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  933 PENAERSRIREVVPYEENRVELIPTKENNTG--YINASHIK---VVVGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVI 1007
Cdd:cd14606     16 PENKSKNRYKNILPFDHSRVILQGRDSNIPGsdYINANYVKnqlLGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVI 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1008 AMVTAEEEGGRTKSHRYWPKLGSKHSsatYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQE-RTVWHLQYTDWPHHGCPE 1086
Cdd:cd14606     96 VMTTREVEKGRNKCVPYWPEVGMQRA---YGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELiREIWHYQYLSWPDHGVPS 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1087 DVQGFLSYLEEIqsvrrhtNSVLEGIRtRHPPIVVHCSAGVGRTGVVILSELMIYCLEH---NEKVEVPTMLRFLREQRM 1163
Cdd:cd14606    173 EPGGVLSFLDQI-------NQRQESLP-HAGPIIVHCSAGIGRTGTIIVIDMLMENISTkglDCDIDIQKTIQMVRAQRS 244

                          250       260
                   ....*....|....*....|.
gi 1720354226 1164 FMIQTIAQYKFVYQVLVQFLQ 1184
Cdd:cd14606    245 GMVQTEAQYKFIYVAIAQFIE 265
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 913-1181 6.65e-52

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: 183.49  E-value: 6.65e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  913 TEYEQIPNK----KANGVFST--ATLPENAERSRIREVVPYEENRVELIP-TKENNTGYINASHIKVVVGgsEWHYIATQ 985
Cdd:cd14603      2 GEFSEIRACsaafKADYVCSTvaGGRKENVKKNRYKDILPYDQTRVILSLlQEEGHSDYINANFIKGVDG--SRAYIATQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  986 GPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPklgSKHSSATYGKFKVTT--KFRTDSGCYATTgLKVKHl 1063
Cdd:cd14603     80 GPLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWA---QEQEPLQTGPFTITLvkEKRLNEEVILRT-LKVTF- 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1064 lSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEiqsVRRHTNSVLEgirtrhpPIVVHCSAGVGRTGVVILSElMIYCL 1143
Cdd:cd14603    155 -QKESRSVSHFQYMAWPDHGIPDSPDCMLAMIEL---ARRLQGSGPE-------PLCVHCSAGCGRTGVICTVD-YVRQL 222

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1720354226 1144 EHNEKVEvPTMLRF-----LREQRMFMIQTIAQYKFVYQVLVQ 1181
Cdd:cd14603    223 LLTQRIP-PDFSIFdvvleMRKQRPAAVQTEEQYEFLYHTVAQ 264
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 964-1177 7.91e-52

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: 181.04  E-value: 7.91e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINASHIKVVVGGSEwHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgSKHSSATYGKFKVT 1043
Cdd:cd14539      1 YINASLIEDLTPYCP-RFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPT--ERGQALVYGAITVS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1044 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHtnsvlegIRTRHPPIVVHC 1123
Cdd:cd14539     78 LQSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQ-------QRSLQTPIVVHC 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720354226 1124 SAGVGRTGV-VILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1177
Cdd:cd14539    151 SSGVGRTGAfCLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 935-1181 1.67e-51

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: 181.44  E-value: 1.67e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  935 NAERSRIREVVPYEENRVELIPTK-ENNTGYINASHIKvvvgGSEWH--YIATQGPLPHTCHDFWQMVWEQGVNVIAMVT 1011
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEgVPGSDYINANYCD----GYRKQnaYIATQGPLPETFGDFWRMVWEQRSATIVMMT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1012 AEEEGGRTKSHRYWPKLGskhsSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGF 1091
Cdd:cd14553     79 KLEERSRVKCDQYWPTRG----TETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPF 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1092 LSYLeeiqsvRRhtnsvlegIRTRHP----PIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQ 1167
Cdd:cd14553    155 LAFL------RR--------VKACNPpdagPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQ 220

                          250
                   ....*....|....
gi 1720354226 1168 TIAQYKFVYQVLVQ 1181
Cdd:cd14553    221 TEDQYIFIHDALLE 234
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 930-1177 2.81e-51

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: 180.80  E-value: 2.81e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  930 ATLPENAERSRIREVVPYEENRVELIPTK-ENNTGYINASHIKvvvgGSEWH--YIATQGPLPHTCHDFWQMVWEQGVNV 1006
Cdd:cd14554      1 ANLPCNKFKNRLVNILPYESTRVCLQPIRgVEGSDYINASFID----GYRQRgaYIATQGPLAETTEDFWRMLWEHNSTI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1007 IAMVTAEEEGGRTKSHRYWPklgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPE 1086
Cdd:cd14554     77 IVMLTKLREMGREKCHQYWP----AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPK 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1087 DVQGFLSYLEEIQSVRRHTNSvlEGirtrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMI 1166
Cdd:cd14554    153 SGEGFIDFIGQVHKTKEQFGQ--EG------PITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMV 224

                          250
                   ....*....|.
gi 1720354226 1167 QTIAQYKFVYQ 1177
Cdd:cd14554    225 QTEDQYQFCYR 235
FERM_F1_PTPN14_like cd17099
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 18-102 6.29e-51

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptors PTPN14, PTPN21, and similar proteins; This family includes tyrosine-protein phosphatase non-receptors PTPN14 and PTPN21, both of which are protein-tyrosine phosphatase (PTP). They belong to the FERM family of PTPs characterized by a conserved N-terminal FERM domain and a C-terminal PTP catalytic domain with an intervening sequence containing an acidic region and a putative SH3 domain-binding sequence. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN14 plays a role in the nucleus during cell proliferation. PTPN21 interacts with a Tec tyrosine kinase family member, the epithelial and endothelial tyrosine kinase (Etk, also known as Bmx), modulates Stat3 activation, and plays a role in the regulation of cell growth and differentiation.


Pssm-ID: 340619  Cd Length: 85  Bit Score: 173.57  E-value: 6.29e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   18 KNCFVTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKFANEPLLFF 97
Cdd:cd17099      1 KNSFVVRIQLLDNTVLECTLSPESTGQDCLEYVAQRLELREIEYFGLRYVNKKGQLRWVDLEKPLKKQLDKHAHEPLLYF 80


                   ....*
gi 1720354226   98 GVMFY 102
Cdd:cd17099     81 GVMFY 85
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 940-1177 7.14e-50

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: 176.05  E-value: 7.14e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  940 RIREVVPYEENRVeLIPTKENN--TGYINASHIKVVvGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGg 1017
Cdd:cd14547      2 RYKTILPNEHSRV-CLPSVDDDplSSYINANYIRGY-DGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1018 RTKSHRYWPKLgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHllSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEE 1097
Cdd:cd14547     79 KEKCAQYWPEE----ENETYGDFEVTVQSVKETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQE 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1098 IQSVRRHTNSvlegirtrHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1177
Cdd:cd14547    153 VEEARQTEPH--------RGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 914-1183 4.80e-49

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: 176.46  E-value: 4.80e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  914 EYEQIPNKKAN-GVFSTATLPENAERSRIREVVPYEENRVELIPTKE-NNTGYINASHIKVVvgGSEWHYIATQGPLPHT 991
Cdd:cd14627     31 EFKRLANSKAHtSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGvEGSDYINASFIDGY--RQQKAYIATQGPLAET 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  992 CHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPklgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTV 1071
Cdd:cd14627    109 TEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWP----AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTV 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1072 WHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNsvlegirtRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEV 1151
Cdd:cd14627    185 RQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFG--------QDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDI 256

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1720354226 1152 PTMLRFLREQRMFMIQTIAQYKFVYQVLVQFL 1183
Cdd:cd14627    257 FQTVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 939-1183 5.69e-49

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: 173.92  E-value: 5.69e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  939 SRIREVVPYEENRVELIPTKENNTG-YINASHIKVVvgGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGG 1017
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPGSdYINANYMPGY--WSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1018 RTKSHRYWPklgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEe 1097
Cdd:cd14619     79 RVKCEHYWP---LDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRR- 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1098 iqSVRRHTNSVLEGirtrhPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1177
Cdd:cd14619    155 --LLRQWLDQTMSG-----GPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQ 227


                   ....*.
gi 1720354226 1178 VLVQFL 1183
Cdd:cd14619    228 CILDFL 233
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 938-1181 8.83e-49

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: 173.49  E-value: 8.83e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  938 RSRIREVVPYEENRVEL-IPTKENNTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEG 1016
Cdd:cd14602      1 KNRYKDILPYDHSRVELsLITSDEDSDYINANFIKGVYGPRA--YIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1017 GRTKSHRYWPKLGSkhSSATYGKFKVTTKFRTDSGCYATTGLKVKhlLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLE 1096
Cdd:cd14602     79 GKKKCERYWAEPGE--MQLEFGPFSVTCEAEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPILELIW 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1097 EIQSVRRHTNsvlegirtrhPPIVVHCSAGVGRTGVVILSELMIYCLEHN---EKVEVPTMLRFLREQRMFMIQTIAQYK 1173
Cdd:cd14602    155 DVRCYQEDDS----------VPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIQEMRTQRPSLVQTKEQYE 224


                   ....*...
gi 1720354226 1174 FVYQVLVQ 1181
Cdd:cd14602    225 LVYNAVIE 232
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 934-1184 9.09e-49

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: 174.05  E-value: 9.09e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  934 ENAERSRIREVVPYEENRVELIPTKENNTG--YINASHI------KVVVGGSEWHYIATQGPLPHTCHDFWQMVWEQGVN 1005
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRVVLHDGDPNEPVsdYINANIImpefetKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1006 VIAMVTAEEEGGRTKSHRYWPklgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQ-ERTVWHLQYTDWPHHGC 1084
Cdd:cd14605     81 VIVMTTKEVERGKSKCVKYWP---DEYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGNtERTVWQYHFRTWPDHGV 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1085 PEDVQGFLSYLEEIqsvrrhtNSVLEGIrTRHPPIVVHCSAGVGRTGVVILSELMIYCLEhnEK-----VEVPTMLRFLR 1159
Cdd:cd14605    158 PSDPGGVLDFLEEV-------HHKQESI-MDAGPVVVHCSAGIGRTGTFIVIDILIDIIR--EKgvdcdIDVPKTIQMVR 227

                          250       260
                   ....*....|....*....|....*
gi 1720354226 1160 EQRMFMIQTIAQYKFVYQVLVQFLQ 1184
Cdd:cd14605    228 SQRSGMVQTEAQYRFIYMAVQHYIE 252
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 914-1183 4.86e-48

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: 173.38  E-value: 4.86e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  914 EYEQIPNKKAN-GVFSTATLPENAERSRIREVVPYEENRVELIPTKE-NNTGYINASHIKVVvgGSEWHYIATQGPLPHT 991
Cdd:cd14628     30 EFKRLASSKAHtSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGvEGSDYINASFIDGY--RQQKAYIATQGPLAET 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  992 CHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPklgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTV 1071
Cdd:cd14628    108 TEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWP----AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTV 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1072 WHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNsvlegirtRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEV 1151
Cdd:cd14628    184 RQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFG--------QDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDI 255

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1720354226 1152 PTMLRFLREQRMFMIQTIAQYKFVYQVLVQFL 1183
Cdd:cd14628    256 FQTVKMLRTQRPAMVQTEDQYQFCYRAALEYL 287
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 915-1181 3.61e-47

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: 170.59  E-value: 3.61e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  915 YEQIPNKKANGVFSTATLPENAERSRIREVVPYEENRVELipTKENNTgYINASHIKVvvGGSEWHYIATQGPLPHTCHD 994
Cdd:cd14608      5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKL--HQEDND-YINASLIKM--EEAQRSYILTQGPLPNTCGH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  995 FWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHL 1074
Cdd:cd14608     80 FWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHF 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1075 QYTDWPHHGCPEDVQGFLSYLEEIqsvrRHTNSvlegIRTRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNE---KVEV 1151
Cdd:cd14608    160 HYTTWPDFGVPESPASFLNFLFKV----RESGS----LSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKdpsSVDI 231

                          250       260       270
                   ....*....|....*....|....*....|
gi 1720354226 1152 PTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1181
Cdd:cd14608    232 KKVLLEMRKFRMGLIQTADQLRFSYLAVIE 261
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 939-1177 4.07e-47

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: 168.16  E-value: 4.07e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  939 SRIREVVPYEENRVELIPTKEN-NTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGG 1017
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVpGSDYINASYISGYLCPNE--FIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1018 RTKSHRYWPKlgSKHSSATYGKFKVTTKFRTDSGCYATTGLKV-KHllsGQERTVWHLQYTDWPHHGCPEDVQGFLSYLE 1096
Cdd:cd14616     79 RIRCHQYWPE--DNKPVTVFGDIVITKLMEDVQIDWTIRDLKIeRH---GDYMMVRQCNFTSWPEHGVPESSAPLIHFVK 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1097 EIQSVRRHTNSvlegirtrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVY 1176
Cdd:cd14616    154 LVRASRAHDNT----------PMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223


                   .
gi 1720354226 1177 Q 1177
Cdd:cd14616    224 Q 224
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 897-1181 2.31e-46

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: 167.91  E-value: 2.31e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  897 ERLRAlkkklEDGMVFT-EYEQI-PNKKANgvFSTATLPENAERSRIREVVPYEENRVELIPTKE-NNTGYINASHIKvv 973
Cdd:cd14626      8 ERLKA-----NDGLKFSqEYESIdPGQQFT--WENSNLEVNKPKNRYANVIAYDHSRVILTSVDGvPGSDYINANYID-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  974 vGGSEWH-YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhssaTYGKFKVTTKFRTDSGC 1052
Cdd:cd14626     79 -GYRKQNaYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTE----TYGMIQVTLLDTVELAT 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1053 YATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVrrhtNSVLEGirtrhpPIVVHCSAGVGRTGV 1132
Cdd:cd14626    154 YSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKAC----NPPDAG------PMVVHCSAGVGRTGC 223

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1720354226 1133 VILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1181
Cdd:cd14626    224 FIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
PHA02738 PHA02738
hypothetical protein; Provisional
 914-1184 3.21e-46

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 168.95  E-value: 3.21e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  914 EYEQIPNKKANGVFSTATlpENAERSRIREVVPYEENRVELiPTKENNTGYINASHikvvVGGSEW--HYIATQGPLPHT 991
Cdd:PHA02738    30 EHQKVISEKVDGTFNAEK--KNRKLNRYLDAVCFDHSRVIL-PAERNRGDYINANY----VDGFEYkkKFICGQAPTRQT 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  992 CHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLlSGQERTV 1071
Cdd:PHA02738   103 CYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDV--EQGSIRFGKFKITTTQVETHPHYVKSTLLLTDG-TSATQTV 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1072 WHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRR--HTNSVLEG-IRTRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEK 1148
Cdd:PHA02738   180 THFNFTAWPDHDVPKNTSEFLNFVLEVRQCQKelAQESLQIGhNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACAT 259

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1720354226 1149 VEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 1184
Cdd:PHA02738   260 VSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVN 295
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 938-1177 5.48e-46

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: 165.26  E-value: 5.48e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  938 RSRIREVVPYEENRVELiptKENNTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGG 1017
Cdd:cd14545      3 RYRDRDPYDHDRSRVKL---KQGDNDYINASLVEVEEAKRS--YILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1018 RTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLee 1097
Cdd:cd14545     78 QIKCAQYWPQGEGNAMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFL-- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1098 iQSVRRHtnSVLEgirTRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNE--KVEVPTMLRFLREQRMFMIQTIAQYKFV 1175
Cdd:cd14545    156 -QKVRES--GSLS---SDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQLRFS 229


                   ..
gi 1720354226 1176 YQ 1177
Cdd:cd14545    230 YL 231
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 939-1177 9.78e-46

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: 164.32  E-value: 9.78e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  939 SRIREVVPYEENRVELIPTKENN-TGYINASHIKvvvGGS-EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEG 1016
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYIP---GNNfRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1017 GRTKSHRYWPklgSKHSSATYGKFKVttKFRTDSGCYATTGLKVKhlLSGQE-----RTVWHLQYTDWPHHGCPEDVQGF 1091
Cdd:cd14617     78 GRVKCDHYWP---ADQDSLYYGDLIV--QMLSESVLPEWTIREFK--ICSEEqldapRLVRHFHYTVWPDHGVPETTQSL 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1092 LSYleeIQSVRRHTNsvlegiRTRHP-PIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIA 1170
Cdd:cd14617    151 IQF---VRTVRDYIN------RTPGSgPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTEC 221


                   ....*..
gi 1720354226 1171 QYKFVYQ 1177
Cdd:cd14617    222 QYVYLHQ 228
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 940-1177 1.49e-45

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: 163.83  E-value: 1.49e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  940 RIREVVPYEENRVELIPTKENNTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRT 1019
Cdd:cd14615      2 RYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKE--FIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1020 KSHRYWPKLGSKhssaTYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEeiq 1099
Cdd:cd14615     80 KCEEYWPSKQKK----DYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRH--- 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720354226 1100 SVRRHTNSVLegirtRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1177
Cdd:cd14615    153 LVREYMKQNP-----PNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 225
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 932-1182 3.46e-45

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: 163.47  E-value: 3.46e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  932 LPENAERSRIREVVPYEENRVEL--IPTKENNTGYINASHIKVVvGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAM 1009
Cdd:cd14612     12 IPGHASKDRYKTILPNPQSRVCLrrAGSQEEEGSYINANYIRGY-DGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVM 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1010 VTAEEEGgRTKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHllSGQERTVWHLQYTDWPHHGCPEDVQ 1089
Cdd:cd14612     91 ITKLKEK-KEKCVHYWPE-----KEGTYGRFEIRVQDMKECDGYTIRDLTIQL--EEESRSVKHYWFSSWPDHQTPESAG 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1090 GFLSYLEEIQSVRRHTNSVlegirtrhPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTI 1169
Cdd:cd14612    163 PLLRLVAEVEESRQTAASP--------GPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTS 234

                          250
                   ....*....|...
gi 1720354226 1170 AQYKFVYQVLVQF 1182
Cdd:cd14612    235 EQYQFLHHTLALY 247
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 915-1176 3.58e-45

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: 163.98  E-value: 3.58e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  915 YEQIPNKKANGVFSTATLPENAERSRIREVVPYEENRVELIPTkENNtgYINAShiKVVVGGSEWHYIATQGPLPHTCHD 994
Cdd:cd14607      4 YLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNT-END--YINAS--LVVIEEAQRSYILTQGPLPNTCCH 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  995 FWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHL 1074
Cdd:cd14607     79 FWLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHF 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1075 QYTDWPHHGCPEDVQGFLSYLEEIQSVRrhtnsvleGIRTRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNE--KVEVP 1152
Cdd:cd14607    159 HYTTWPDFGVPESPASFLNFLFKVRESG--------SLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIK 230

                          250       260
                   ....*....|....*....|....
gi 1720354226 1153 TMLRFLREQRMFMIQTIAQYKFVY 1176
Cdd:cd14607    231 QVLLDMRKYRMGLIQTPDQLRFSY 254
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 914-1183 5.82e-45

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: 164.51  E-value: 5.82e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  914 EYEQIPNKKAN-GVFSTATLPENAERSRIREVVPYEENRVELIPTKE-NNTGYINASHIKVVvgGSEWHYIATQGPLPHT 991
Cdd:cd14629     31 EFKLLANSKAHtSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGvEGSDYINASFIDGY--RQQKAYIATQGPLAET 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  992 CHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPklgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTV 1071
Cdd:cd14629    109 TEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWP----AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTI 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1072 WHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNsvlegirtRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEV 1151
Cdd:cd14629    185 RQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQFG--------QDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDM 256

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1720354226 1152 PTMLRFLREQRMFMIQTIAQYKFVYQVLVQFL 1183
Cdd:cd14629    257 FQTVKTLRTQRPAMVQTEDQYQLCYRAALEYL 288
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 964-1177 7.85e-44

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: 157.97  E-value: 7.85e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhsSATYGKFKVT 1043
Cdd:cd14542      1 YINANFIKGVSGSKA--YIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEE--QLQFGPFKIS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1044 ---TKFRTDSgcYATTGLKVKhlLSGQERTVWHLQYTDWPHHGCPEDVQgflSYLEEIQSVRRHTNSvlegirtRHPPIV 1120
Cdd:cd14542     77 lekEKRVGPD--FLIRTLKVT--FQKESRTVYQFHYTAWPDHGVPSSVD---PILDLVRLVRDYQGS-------EDVPIC 142

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720354226 1121 VHCSAGVGRTGVV--------ILSELMIyclehNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1177
Cdd:cd14542    143 VHCSAGCGRTGTIcaidyvwnLLKTGKI-----PEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 964-1177 8.81e-44

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: 157.68  E-value: 8.81e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINASHIKvvvGGSE-WHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLgsKHSSATYGkfKV 1042
Cdd:cd14557      1 YINASYID---GFKEpRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSM--EEGSRAFG--DV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1043 TTKFRTDSGC--YATTGLKVKHLL-SGQERTVWHLQYTDWPHHGCPEDVQGFLsyleeiqSVRRHTNSVLEGIRTrhpPI 1119
Cdd:cd14557     74 VVKINEEKICpdYIIRKLNINNKKeKGSGREVTHIQFTSWPDHGVPEDPHLLL-------KLRRRVNAFNNFFSG---PI 143

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720354226 1120 VVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1177
Cdd:cd14557    144 VVHCSAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 914-1181 4.52e-43

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: 158.72  E-value: 4.52e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  914 EYEQI-PNKKANgvFSTATLPENAERSRIREVVPYEENRVELIPTKE-NNTGYINASHIKVVvgGSEWHYIATQGPLPHT 991
Cdd:cd14625     27 EYESIdPGQQFT--WEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGiMGSDYINANYIDGY--RKQNAYIATQGPLPET 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  992 CHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhssaTYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTV 1071
Cdd:cd14625    103 FGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTE----TYGMIQVTLLDTIELATFCVRTFSLHKNGSSEKREV 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1072 WHLQYTDWPHHGCPEDVQGFLSYLEEIQSVrrhtNSVLEGirtrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEV 1151
Cdd:cd14625    179 RQFQFTAWPDHGVPEYPTPFLAFLRRVKTC----NPPDAG------PIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDI 248

                          250       260       270
                   ....*....|....*....|....*....|
gi 1720354226 1152 PTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1181
Cdd:cd14625    249 YGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 933-1181 6.05e-43

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: 158.28  E-value: 6.05e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  933 PENAERSRIREVVPYEENRVEL--IPTKEN-NTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAM 1009
Cdd:cd17667     25 PDNKHKNRYINILAYDHSRVKLrpLPGKDSkHSDYINANYVDGYNKAKA--YIATQGPLKSTFEDFWRMIWEQNTGIIVM 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1010 VTAEEEGGRTKSHRYWPklgsKHSSATYGKFKVTTKFRTDSGCYATTGL-----KVKHLLSGQ------ERTVWHLQYTD 1078
Cdd:cd17667    103 ITNLVEKGRRKCDQYWP----TENSEEYGNIIVTLKSTKIHACYTVRRFsirntKVKKGQKGNpkgrqnERTVIQYHYTQ 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1079 WPHHGCPEDVQGFLSYleeiqsVRRHTNSvlegiRTRH-PPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRF 1157
Cdd:cd17667    179 WPDMGVPEYALPVLTF------VRRSSAA-----RTPEmGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKH 247

                          250       260
                   ....*....|....*....|....
gi 1720354226 1158 LREQRMFMIQTIAQYKFVYQVLVQ 1181
Cdd:cd17667    248 IRTQRNYLVQTEEQYIFIHDALLE 271
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 897-1184 8.57e-43

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: 158.56  E-value: 8.57e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  897 ERLRALKKKLEDG-----MVFTEYEQIPNK-KANGVFSTAT--LPENAERSRIREVVPYEENRVEL-IPTKENNTGYINA 967
Cdd:cd14604     11 ERVQAMKSTDHNGednfaSDFMRLRRLSTKyRTEKIYPTATgeKEENVKKNRYKDILPFDHSRVKLtLKTSSQDSDYINA 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  968 SHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhsSATYGKFKVT---T 1044
Cdd:cd14604     91 NFIKGVYGPKA--YIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEE--PMTFGPFRISceaE 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1045 KFRTDsgcYATTGLKVKhlLSGQERTVWHLQYTDWPHHGCPedvQGFLSYLEEIQSVRRHTNSvlegirtRHPPIVVHCS 1124
Cdd:cd14604    167 QARTD---YFIRTLLLE--FQNETRRLYQFHYVNWPDHDVP---SSFDSILDMISLMRKYQEH-------EDVPICIHCS 231

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720354226 1125 AGVGRTGVVILSELMIYCLEHN---EKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 1184
Cdd:cd14604    232 AGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFE 294
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 939-1180 1.63e-42

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: 155.49  E-value: 1.63e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  939 SRIREVVPYEENRVELIP-TKENNTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGG 1017
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQlGGEPHSDYINANFIPGYTSPQE--FIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1018 RTKSHRYWPklgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEE 1097
Cdd:cd14618     79 RVLCDHYWP---SESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFREL 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1098 IQSVRRHTNSvlegirtrHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1177
Cdd:cd14618    156 VREHVQATKG--------KGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHS 227


                   ...
gi 1720354226 1178 VLV 1180
Cdd:cd14618    228 CIL 230
FERM_F1_PTPN21 cd17192
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 18-104 4.07e-42

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and similar proteins; PTPN21, also termed protein-tyrosine phosphatase D1 (PTPD1), is a cytosolic non-receptor protein-tyrosine phosphatase (PTP) that belongs to the FERM family of PTPs characterized by a conserved N-terminal FERM domain and a C-terminal PTP catalytic domain with an intervening sequence containing an acidic region and a putative SH3 domain-binding sequence. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN21 interacts with a Tec tyrosine kinase family member, the epithelial and endothelial tyrosine kinase (Etk, also known as Bmx), modulates Stat3 activation, and plays a role in the regulation of cell growth and differentiation. It also associates with and activates Src tyrosine kinase, and directs epidermal growth factor (EGF)/Src signaling to the nucleus through activating ERK1/2- and Elk1-dependent gene transcription. PTPD1-Src complex interacts a protein kinase A-anchoring protein AKAP121 to forms a PTPD1-Src-AKAP121 complex, which is required for efficient maintenance of mitochondrial membrane potential and ATP oxidative synthesis. As a novel component of the endocytic pathway, PTPN21 supports EGF receptor stability and mitogenic signaling in bladder cancer cells. Moreover, PTPD1 regulates focal adhesion kinase (FAK) autophosphorylation and cell migration through modulating Src-FAK signaling at adhesion sites.


Pssm-ID: 340712  Cd Length: 87  Bit Score: 148.63  E-value: 4.07e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   18 KNCFVTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKFANEPLLFF 97
Cdd:cd17192      1 KSCLVARIQLLNNEFVEFTLSVESTGQECLEAVAQRLELREITYFSLWYYNKQNQQRWVDLEKPLKKQLDKYALEPTVYF 80


                   ....*..
gi 1720354226   98 GVMFYVP 104
Cdd:cd17192     81 GVVFYVP 87
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 929-1183 4.97e-42

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: 154.28  E-value: 4.97e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  929 TATLPENAERSRIREVVPYEENRVELIPT-KENNTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVI 1007
Cdd:cd14614      6 AADLPVNRCKNRYTNILPYDFSRVKLVSMhEEEGSDYINANYIPGYNSPQE--YIATQGPLPETRNDFWKMVLQQKSQII 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1008 AMVTAEEEGGRTKSHRYWPklgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQErtVWHLQYTDWPHHGCPeD 1087
Cdd:cd14614     84 VMLTQCNEKRRVKCDHYWP---FTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQD--VMHFNYTAWPDHGVP-T 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1088 VQGFLSYLEEIQSVRRHTNSvlegirtRHPPIVVHCSAGVGRTGVVI-LSELMIYCLEHnEKVEVPTMLRFLREQRMFMI 1166
Cdd:cd14614    158 ANAAESILQFVQMVRQQAVK-------SKGPMIIHCSAGVGRTGTFIaLDRLLQHIRDH-EFVDILGLVSEMRSYRMSMV 229

                          250
                   ....*....|....*..
gi 1720354226 1167 QTIAQYKFVYQVlVQFL 1183
Cdd:cd14614    230 QTEEQYIFIHQC-VQLM 245
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 964-1176 5.72e-42

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: 152.98  E-value: 5.72e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINASHIKVvvggsewH------YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhssaTY 1037
Cdd:cd14546      1 YINASTIYD-------HdprnpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSE----VY 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1038 GKFKVTTkFRTDSGC--YATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYleeiqsvRRHTNSVLEGirtR 1115
Cdd:cd14546     70 HIYEVHL-VSEHIWCddYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEF-------RRKVNKSYRG---R 138

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720354226 1116 HPPIVVHCSAGVGRTGVVILSELMIYCLEHNEK-VEVPTMLRFLREQRMFMIQTIAQYKFVY 1176
Cdd:cd14546    139 SCPIVVHCSDGAGRTGTYILIDMVLNRMAKGAKeIDIAATLEHLRDQRPGMVKTKDQFEFVL 200
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 964-1180 7.00e-42

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: 152.83  E-value: 7.00e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINASHIKVVvgGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHssatYGKFKVT 1043
Cdd:cd17668      1 YINANYVDGY--NKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEE----YGNFLVT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1044 TKFRTDSGCYATTGLKVKH--LLSG------QERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSvlegirtr 1115
Cdd:cd17668     75 QKSVQVLAYYTVRNFTLRNtkIKKGsqkgrpSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVG-------- 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720354226 1116 hpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLV 1180
Cdd:cd17668    147 --PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 914-1182 5.38e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 153.62  E-value: 5.38e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  914 EYEQIpnKKANGVFSTATLPENAERSRIR--EVVPYEENRVeLIPTKENNTGYINASHikvvVGG--SEWHYIATQGPLP 989
Cdd:PHA02742    31 EHEHI--MQEIVAFSCNESLELKNMKKCRypDAPCFDRNRV-ILKIEDGGDDFINASY----VDGhnAKGRFICTQAPLE 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  990 HTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWpkLGSKHSSATYGKFKVTTK----FRTdsgcYATTGLKVKHLLS 1065
Cdd:PHA02742   104 ETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYW--MPHERGKATHGEFKIKTKkiksFRN----YAVTNLCLTDTNT 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1066 GQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSVLEG-IRTRHPPIVVHCSAGVGRTGVVILSELMIYclE 1144
Cdd:PHA02742   178 GASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVREADLKADVDIKGeNIVKEPPILVHCSAGLDRAGAFCAIDICIS--K 255

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1720354226 1145 HNEKVEVP--TMLRFLREQRMFMIQTIAQYKFVYQVLVQF 1182
Cdd:PHA02742   256 YNERAIIPllSIVRDLRKQRHNCLSLPQQYIFCYFIVLIF 295
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 944-1181 6.59e-41

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: 150.48  E-value: 6.59e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  944 VVPYEENRVELIPTKEN-NTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSH 1022
Cdd:cd14620      4 ILPYDHSRVILSQLDGIpCSDYINASYIDGYKEKNK--FIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCY 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1023 RYWPKLGSkhssATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQ---ERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQ 1099
Cdd:cd14620     82 QYWPDQGC----WTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGckaPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVK 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1100 SVrrhtNSVLEGirtrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVL 1179
Cdd:cd14620    158 SV----NPVHAG------PIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227


                   ..
gi 1720354226 1180 VQ 1181
Cdd:cd14620    228 LE 229
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 964-1177 1.71e-40

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: 148.52  E-value: 1.71e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINASHIKvvvGGSEWH-YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhssaTYGKFKV 1042
Cdd:cd14551      1 YINASYID---GYQEKNkFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCW----TYGNLRV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1043 TTKFRTDSGCYATTGLKVKHLLSG----QERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVrrhtNSVLEGirtrhpP 1118
Cdd:cd14551     74 RVEDTVVLVDYTTRKFCIQKVNRGigekRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSA----NPPRAG------P 143

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720354226 1119 IVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1177
Cdd:cd14551    144 IVVHCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 964-1176 1.82e-40

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: 148.38  E-value: 1.82e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINASHIKVVVGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRT-KSHRYWPKlgSKHSSATYGKFKV 1042
Cdd:cd17658      1 YINASLVETPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPA--EENESREFGRISV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1043 TTK-FRTDSGCYATTGLKVKHL-LSGQERTVWHLQYTDWPHHGCPEDVQgflsYLEEIqsVRRhtnsvLEGIRTRHPPIV 1120
Cdd:cd17658     79 TNKkLKHSQHSITLRVLEVQYIeSEEPPLSVLHIQYPEWPDHGVPKDTR----SVREL--LKR-----LYGIPPSAGPIV 147

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720354226 1121 VHCSAGVGRTGVvilselmiYCLEHN----------EKVEVPTMLRFLREQRMFMIQTIAQYKFVY 1176
Cdd:cd17658    148 VHCSAGIGRTGA--------YCTIHNtirrilegdmSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 897-1181 1.92e-40

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: 151.42  E-value: 1.92e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  897 ERLRAlkkklEDGMVFT-EYEQI-PNKKANgvFSTATLPENAERSRIREVVPYEENRVeLIPTKENNTG--YINASHIKV 972
Cdd:cd14624     14 ERLKA-----NDNLKFSqEYESIdPGQQFT--WEHSNLEVNKPKNRYANVIAYDHSRV-LLSAIEGIPGsdYINANYIDG 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  973 VvgGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhssaTYGKFKVTTKFRTDSGC 1052
Cdd:cd14624     86 Y--RKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTE----TYGLIQVTLLDTVELAT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1053 YATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVrrhtNSVLEGirtrhpPIVVHCSAGVGRTGV 1132
Cdd:cd14624    160 YCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTC----NPPDAG------PMVVHCSAGVGRTGC 229

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1720354226 1133 VILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1181
Cdd:cd14624    230 FIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 964-1180 2.65e-40

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: 147.80  E-value: 2.65e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINASHIKVVvgGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGskhsSATYGKFKVT 1043
Cdd:cd14552      1 YINASFIDGY--RQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDG----SVSSGDITVE 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1044 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNsvlegirtrHPPIVVHC 1123
Cdd:cd14552     75 LKDQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSG---------NHPITVHC 145

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720354226 1124 SAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLV 1180
Cdd:cd14552    146 SAGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 964-1176 3.37e-40

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: 147.54  E-value: 3.37e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINASHIKvvvggSEWH---YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgskhSSATYGKF 1040
Cdd:cd14558      1 YINASFID-----GYWGpksLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGD-----EKKTYGDI 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1041 KVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSvRRHTNSVLEGirtRHPPIV 1120
Cdd:cd14558     71 EVELKDTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQ-KLPYKNSKHG---RSVPIV 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720354226 1121 VHCSAGVGRTGvvilselmIYC-----LE--HNEK-VEVPTMLRFLREQRMFMIQTIAQYKFVY 1176
Cdd:cd14558    147 VHCSDGSSRTG--------IFCalwnlLEsaETEKvVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 940-1179 1.26e-39

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: 147.11  E-value: 1.26e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  940 RIREVVPYEENRVeLIPTK--ENNTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGG 1017
Cdd:cd14623      1 RVLQIIPYEFNRV-IIPVKrgEENTDYVNASFIDGYRQKDS--YIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1018 RTKSHRYWPKLGskhsSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEE 1097
Cdd:cd14623     78 QEKCAQYWPSDG----SVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAA 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1098 IQSVRRHTNSvlegirtrhPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1177
Cdd:cd14623    154 VQKQQQQSGN---------HPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYK 224


                   ..
gi 1720354226 1178 VL 1179
Cdd:cd14623    225 VV 226
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 938-1177 7.82e-39

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: 144.68  E-value: 7.82e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  938 RSRIREVVPYEENRVELIPTKENN--TGYINASHIKVVvGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEE 1015
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKNSNDslSTYINANYIRGY-GGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1016 GGRtKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHllSGQERTVWHLQYTDWPHHGCPEDVQGFLSYL 1095
Cdd:cd14611     81 KNE-KCVLYWPE-----KRGIYGKVEVLVNSVKECDNYTIRNLTLKQ--GSQSRSVKHYWYTSWPDHKTPDSAQPLLQLM 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1096 EEIQSVRRhtNSVLEGirtrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFV 1175
Cdd:cd14611    153 LDVEEDRL--ASPGRG------PVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFV 224


                   ..
gi 1720354226 1176 YQ 1177
Cdd:cd14611    225 HH 226
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 893-1181 1.81e-38

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: 145.94  E-value: 1.81e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  893 VPIDERLRALKKKL-EDGMVF-TEYEQIPNKKANGVFSTATLPENAERSRIREVVPYEENRVELIPTKE-NNTGYINASH 969
Cdd:cd14621      8 LPVDKLEEEINRRMaDDNKLFrEEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGvPDSDYINASF 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  970 IKvvvGGSEWH-YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSkhssATYGKFKVTTKFRT 1048
Cdd:cd14621     88 IN---GYQEKNkFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGC----WTYGNIRVSVEDVT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1049 DSGCYATTGLKVKHL--LSGQ--ERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVrrhtNSVLEGirtrhpPIVVHCS 1124
Cdd:cd14621    161 VLVDYTVRKFCIQQVgdVTNKkpQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNC----NPQYAG------AIVVHCS 230

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720354226 1125 AGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1181
Cdd:cd14621    231 AGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLE 287
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 895-1174 2.17e-38

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: 145.18  E-value: 2.17e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  895 IDERLRALKKKLEDGMVFTEYEQIPNKkangvFSTATLPENAERSRIREVVPYEENRVEL-IPTKENNTGYINASHIkVV 973
Cdd:cd14609      7 MEDHLRNRDRLAKEWQALCAYQAEPNT-----CSTAQGEANVKKNRNPDFVPYDHARIKLkAESNPSRSDYINASPI-IE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  974 VGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGskhsSATYGKFKVTTkFRTDSGC- 1052
Cdd:cd14609     81 HDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEG----SSLYHIYEVNL-VSEHIWCe 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1053 -YATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYleeiqsvRRHTNSVLEGirtRHPPIVVHCSAGVGRTG 1131
Cdd:cd14609    156 dFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDF-------RRKVNKCYRG---RSCPIIVHCSDGAGRTG 225

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1720354226 1132 VVILSELMIYCLEHNEK-VEVPTMLRFLREQRMFMIQTIAQYKF 1174
Cdd:cd14609    226 TYILIDMVLNRMAKGVKeIDIAATLEHVRDQRPGMVRTKDQFEF 269
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 909-1183 2.41e-38

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 145.91  E-value: 2.41e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  909 GMVFTEYEQIPNKKANGVFSTATLPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKvvvgGSE--WHYIATQG 986
Cdd:PHA02747    25 GIIRDEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWID----GFEddKKFIATQG 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  987 PLPHTCHDFWQMVWEQGVNVIAMVT-AEEEGGRTKSHRYWPKlgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLS 1065
Cdd:PHA02747   101 PFAETCADFWKAVWQEHCSIIVMLTpTKGTNGEEKCYQYWCL--NEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKIL 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1066 GQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSVLEGIRTRHPPIVVHCSAGVGRTGVVILSELMIYCLEH 1145
Cdd:PHA02747   179 KDSRKISHFQCSEWFEDETPSDHPDFIKFIKIIDINRKKSGKLFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVK 258

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1720354226 1146 NEKVEVPTMLRFLREQRMFMIQTIAQYKFV---YQVLVQFL 1183
Cdd:PHA02747   259 RKAICLAKTAEKIREQRHAGIMNFDDYLFIqpgYEVLHYFL 299
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 915-1174 3.06e-38

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: 144.81  E-value: 3.06e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  915 YEQIPNkkangVFSTATLPENAERSRIREVVPYEENRVEL-IPTKENNTGYINASHIkVVVGGSEWHYIATQGPLPHTCH 993
Cdd:cd14610     29 YQAEPN-----ATNVAQREENVQKNRSLAVLPYDHSRIILkAENSHSHSDYINASPI-MDHDPRNPAYIATQGPLPATVA 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  994 DFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSK--HssaTYGKFKVTTKFRTDSgcYATTGLKVKHLLSGQERTV 1071
Cdd:cd14610    103 DFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNlyH---IYEVNLVSEHIWCED--FLVRSFYLKNLQTNETRTV 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1072 WHLQYTDWPHHGCPEDVQGFLSYleeiqsvRRHTNSVLEGirtRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEK-VE 1150
Cdd:cd14610    178 TQFHFLSWNDQGVPASTRSLLDF-------RRKVNKCYRG---RSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAKeID 247

                          250       260
                   ....*....|....*....|....
gi 1720354226 1151 VPTMLRFLREQRMFMIQTIAQYKF 1174
Cdd:cd14610    248 IAATLEHLRDQRPGMVQTKEQFEF 271
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 932-1179 4.94e-38

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: 143.46  E-value: 4.94e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  932 LPENAERSRIREVVPYEENRVELIPTKENN--TGYINASHIKVVvGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAM 1009
Cdd:cd14613     22 IPGLVRKNRYKTILPNPHSRVCLTSPDQDDplSSYINANYIRGY-GGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVM 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1010 VTAEEEGGRtKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHllSGQERTVWHLQYTDWPHHGCPEDVQ 1089
Cdd:cd14613    101 ITNIEEMNE-KCTEYWPE-----EQVTYEGIEITVKQVIHADDYRLRLITLKS--GGEERGLKHYWYTSWPDQKTPDNAP 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1090 GFLSYLEEIQSVRRHTnsvlegiRTRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTI 1169
Cdd:cd14613    173 PLLQLVQEVEEARQQA-------EPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTC 245

                          250
                   ....*....|
gi 1720354226 1170 AQYKFVYQVL 1179
Cdd:cd14613    246 EQYQFVHHVL 255
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 964-1181 1.78e-37

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: 140.05  E-value: 1.78e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINASHIKVVVGGSewHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgskhSSATYGKFKVT 1043
Cdd:cd14555      1 YINANYIDGYHRPN--HYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPD-----DTEVYGDIKVT 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1044 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSvrrhTNSVLEGirtrhpPIVVHC 1123
Cdd:cd14555     74 LVETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKA----SNPPSAG------PIVVHC 143

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720354226 1124 SAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1181
Cdd:cd14555    144 SAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 934-1181 3.35e-37

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: 140.16  E-value: 3.35e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  934 ENAERSRIREVVPYEENRVELIPTKEN-NTGYINASHIKVVvgGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTA 1012
Cdd:cd14630      2 ENRNKNRYGNIISYDHSRVRLQLLDGDpHSDYINANYIDGY--HRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1013 EEEGGRTKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFL 1092
Cdd:cd14630     80 LVEVGRVKCVRYWPD-----DTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1093 SYLEEIqsvrRHTNSVLEGirtrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQY 1172
Cdd:cd14630    155 GFVRQV----KFLNPPDAG------PIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQY 224


                   ....*....
gi 1720354226 1173 KFVYQVLVQ 1181
Cdd:cd14630    225 VFVHDAILE 233
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 951-1181 2.53e-36

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: 137.07  E-value: 2.53e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  951 RVELIPTKENNTG-YINASHIKVVVGGSewHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlg 1029
Cdd:cd14631      1 RVILQPVEDDPSSdYINANYIDGYQRPS--HYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD-- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1030 skhSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIqsvrRHTNSVL 1109
Cdd:cd14631     77 ---DTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRV----KLSNPPS 149

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720354226 1110 EGirtrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1181
Cdd:cd14631    150 AG------PIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 964-1182 6.93e-36

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: 135.52  E-value: 6.93e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINASHIKvvvGGSEWHY-IATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGskhsSATYGKFKV 1042
Cdd:cd14622      2 YINASFID---GYRQKDYfIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEG----SVTHGEITI 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1043 TTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSvlegirtrhPPIVVH 1122
Cdd:cd14622     75 EIKNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGN---------HPIVVH 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1123 CSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQF 1182
Cdd:cd14622    146 CSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 964-1181 2.10e-35

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: 134.02  E-value: 2.10e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINASHIKVVVGGSewHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgskhSSATYGKFKVT 1043
Cdd:cd14632      1 YINANYIDGYHRSN--HFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPD-----DSDTYGDIKIT 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1044 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYleeiqsVRRhtnsvlegIRTRHP----PI 1119
Cdd:cd14632     74 LLKTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAF------IRR--------VKASTPpdagPV 139

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720354226 1120 VVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1181
Cdd:cd14632    140 VVHCSAGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 905-1181 5.31e-35

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


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 135.17  E-value: 5.31e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  905 KLEDGMVFTEYEQIPNKKANGVFSTATLPENAERSRIREVVPYEENRVELIPTK-ENNTGYINASHIKVVVGGSewHYIA 983
Cdd:cd14633     10 KCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEgETSSDYINGNYIDGYHRPN--HYIA 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  984 TQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHL 1063
Cdd:cd14633     88 TQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPD-----DTEIYKDIKVTLIETELLAEYVIRTFAVEKR 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1064 LSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSvlegirtrhpPIVVHCSAGVGRTGVVILSELMIYCL 1143
Cdd:cd14633    163 GVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAG----------PLVVHCSAGAGRTGCFIVIDIMLDMA 232

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1720354226 1144 EHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1181
Cdd:cd14633    233 EREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 104-220 4.53e-34

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 126.61  E-value: 4.53e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  104 PNVSRLQQEATRYQYYLQVKKDVLEGRLRCSLEQVIRLAGLAVQADFGDYNQFDSQ-EFLREYVLFPMDLaMEEAALEEL 182
Cdd:pfam00373    1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTsEYLSLESFLPKQL-LRKMKSKEL 79

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1720354226  183 TQKVAQEHKAHSGILPAEAELMYINEVERLDGFGQEIF 220
Cdd:pfam00373   80 EKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1070-1179 2.08e-30

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 115.92  E-value: 2.08e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  1070 TVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRhtnsvlegIRTRHPPIVVHCSAGVGRTGVVILSELMIYCLEH-NEK 1148
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLN--------QSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGE 72

                            90       100       110
                    ....*....|....*....|....*....|.
gi 1720354226  1149 VEVPTMLRFLREQRMFMIQTIAQYKFVYQVL 1179
Cdd:smart00404   73 VDIFDTVKELRSQRPGMVQTEEQYLFLYRAL 103
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1070-1179 2.08e-30

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: 115.92  E-value: 2.08e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  1070 TVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRhtnsvlegIRTRHPPIVVHCSAGVGRTGVVILSELMIYCLEH-NEK 1148
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLN--------QSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGE 72

                            90       100       110
                    ....*....|....*....|....*....|.
gi 1720354226  1149 VEVPTMLRFLREQRMFMIQTIAQYKFVYQVL 1179
Cdd:smart00012   73 VDIFDTVKELRSQRPGMVQTEEQYLFLYRAL 103
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 910-1179 6.46e-30

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 121.67  E-value: 6.46e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  910 MVFTEYEQIPNKKANGVFSTATLPENAERSRIREVVPYEENRVEL--------------------IPTKENNTGYINASH 969
Cdd:PHA02746    26 FVLLEHAEVMDIPIRGTTNHFLKKENLKKNRFHDIPCWDHSRVVInaheslkmfdvgdsdgkkieVTSEDNAENYIHANF 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  970 IKvvvGGSEWH-YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTaEEEGGRTKSHRYWPKlgSKHSSATYGKFKVTTKFRT 1048
Cdd:PHA02746   106 VD---GFKEANkFICAQGPKEDTSEDFFKLISEHESQVIVSLT-DIDDDDEKCFELWTK--EEDSELAFGRFVAKILDII 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1049 DSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSVLEGIRTRHPPIVVHCSAGVG 1128
Cdd:PHA02746   180 EELSFTKTRLMITDKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAELIKQADNDPQTLGPIVVHCSAGIG 259

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720354226 1129 RTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVL 1179
Cdd:PHA02746   260 RAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
895-1185 1.08e-29

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 119.81  E-value: 1.08e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  895 IDERLRALKKKLEDGMVFTEYEQIPNkkangvfstatlpeNAERSRIREVVPYEENRVEliptkeNNTGYINASHIKVvv 974
Cdd:COG5599     16 INSRLSTLTNELAPSHNDPQYLQNIN--------------GSPLNRFRDIQPYKETALR------ANLGYLNANYIQV-- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  975 gGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGG--RTKSHRYWpklgskHSSATYGKFKVTTK------F 1046
Cdd:COG5599     74 -IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISkpKVKMPVYF------RQDGEYGKYEVSSEltesiqL 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1047 RTDSGCYAttgLKVKHLLSGQE-RTVWHLQYTDWPHHGCP--EDVQGFLSYLEEIQSVRRHTNSvlegirtrhpPIVVHC 1123
Cdd:COG5599    147 RDGIEART---YVLTIKGTGQKkIEIPVLHVKNWPDHGAIsaEALKNLADLIDKKEKIKDPDKL----------LPVVHC 213

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720354226 1124 SAGVGRTGVVILselmIYCLE------HNEKVEVPTMLRFLREQR-MFMIQTIAQykfvYQVLVQFLQN 1185
Cdd:COG5599    214 RAGVGRTGTLIA----CLALSksinalVQITLSVEEIVIDMRTSRnGGMVQTSEQ----LDVLVKLAEQ 274
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 215-305 5.57e-29

FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and 21); This CD contains PTP members: pez/PTPN14 and PTPN21. A number of mutations in Pez have been shown to be associated with breast and colorectal cancer. The PTPN protein family belong to larger family of PTPs. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. The members are composed of a N-terminal FERM domain and a C-terminal PTP catalytic domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. Like most other ERM members they have a phosphoinositide-binding site in their FERM domain. The FERM C domain is the third structural domain within the FERM domain. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270009  Cd Length: 91  Bit Score: 111.23  E-value: 5.57e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  215 FGQEIFPVKDSHGNSVHLGIFFMGIFVRNRVGRQAVIYRWNDIGSVTHSKAAILLELIDKEETALFHTDDIENAKYISRL 294
Cdd:cd13188      1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRPPVFFRWEDIKNVINHKRTFSIECQNSEETVQFQFEDAETAKYVWKL 80

                           90
                   ....*....|.
gi 1720354226  295 FTTRHKFYKQN 305
Cdd:cd13188     81 CVLQHKFYRQN 91
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 114-212 2.14e-27

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 106.95  E-value: 2.14e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  114 TRYQYYLQVKKDVLEGRLRCSLEQVIRLAGLAVQADFGDYNQ-FDSQEFLREYVLFPMDLaMEEAALEELTQKVAQEHKA 192
Cdd:cd14473      1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPsEHKPKYLSLKRFLPKQL-LKQRKPEEWEKRIVELHKK 79

                           90       100
                   ....*....|....*....|
gi 1720354226  193 HSGILPAEAELMYINEVERL 212
Cdd:cd14473     80 LRGLSPAEAKLKYLKIARKL 99
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 981-1177 5.32e-26

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: 106.72  E-value: 5.32e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  981 YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTkSHRYWPklgsKHSSATYGKFKVTTKFRTDSGCYATTGLKV 1060
Cdd:cd14556     16 FIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQS-CPQYWP----DEGSGTYGPIQVEFVSTTIDEDVISRIFRL 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1061 KHLLSGQE--RTVWHLQYTDWPHHG-CPEDVQGFLSYLEEIQSVRRHTNsvlEGirtrhpPIVVHCSAGVGRTGVVILSE 1137
Cdd:cd14556     91 QNTTRPQEgyRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSG---EG------PIVVHCLNGVGRSGVFCAIS 161

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1720354226 1138 LMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1177
Cdd:cd14556    162 SVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
FERM_N pfam09379
FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the ...
 25-87 2.12e-22

FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the FERM domain.


Pssm-ID: 430570  Cd Length: 63  Bit Score: 91.50  E-value: 2.12e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720354226   25 IRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLD 87
Cdd:pfam09379    1 VRLLDGTVLEFDVQPKATGQVLLDQVCNHLNLKEKDYFGLQFLDDNGEHRWLDLSKRLSKQAP 63
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
 21-101 2.79e-20

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found in FERM (Four.1/Ezrin/Radixin/Moesin) family proteins; FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain is present at the N-terminus of a large and diverse group of proteins that mediate linkage of the cytoskeleton to the plasma membrane. FERM-containing proteins are ubiquitous components of the cytocortex and are involved in cell transport, cell structure and signaling functions. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N), which is structurally similar to ubiquitin.


Pssm-ID: 340464  Cd Length: 80  Bit Score: 86.10  E-value: 2.79e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   21 FVTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKfANEPLLFFGVM 100
Cdd:cd01765      1 ISCRVRLLDGTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFYEDNDGQKHWLDLDKKISKQLKR-SGPYQFYFRVK 79


                   .
gi 1720354226  101 F 101
Cdd:cd01765     80 F 80
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 964-1177 1.74e-18

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: 85.07  E-value: 1.74e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKShrYWPKLGSKHSSATYGKFKVT 1043
Cdd:cd14550      1 YINASYLQGYRRSNE--FIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTKEKPLECETFKVTLSG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1044 TKFRTDSGcyaTTGLKVKHLL--SGQER---TVWHLQYTDWPHHGCPedvqgFLSYLEEIQSVRRHTNSvlegirtRHPP 1118
Cdd:cd14550     77 EDHSCLSN---EIRLIVRDFIleSTQDDyvlEVRQFQCPSWPNPCSP-----IHTVFELINTVQEWAQQ-------RDGP 141

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720354226 1119 IVVH-----CSAGVgrtgVVILSELMIYcLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1177
Cdd:cd14550    142 IVVHdryggVQAAT----FCALTTLHQQ-LEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 964-1180 6.23e-18

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: 83.57  E-value: 6.23e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVtAEEEGGRTKSHRYWPklgSKHSSATYGKFKVT 1043
Cdd:cd17670      1 YINASYIMGYYRSNE--FIITQHPLPHTTKDFWRMIWDHNAQIIVML-PDNQGLAEDEFVYWP---SREESMNCEAFTVT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1044 TkFRTDSGCYATTGLKVKH---LLSGQERTVW---HLQYTDWPHHGCPedvqgflsyleeIQSVRRHTNSVLEGIRTRHP 1117
Cdd:cd17670     75 L-ISKDRLCLSNEEQIIIHdfiLEATQDDYVLevrHFQCPKWPNPDAP------------ISSTFELINVIKEEALTRDG 141

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720354226 1118 PIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLV 1180
Cdd:cd17670    142 PTIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 964-1181 2.69e-15

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 75.83  E-value: 2.69e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINA----SHIKVVVggsewhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTaeEEGGRTKSHRYWPklgsKHSSATYGK 1039
Cdd:cd14634      1 YINAalmdSHKQPAA------FIVTQHPLPNTVADFWRLVFDYNCSSVVMLN--EMDAAQLCMQYWP----EKTSCCYGP 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1040 FKVTTKFRTDSGCYATTGLKVKHLLSGQE--RTVWHLQYTDWP-HHGCPEDVQGFLsyleeiQSVRRhTNSVLEGIRTRH 1116
Cdd:cd14634     69 IQVEFVSADIDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPaYRDTPPSKRSIL------KVVRR-LEKWQEQYDGRE 141

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720354226 1117 PPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1181
Cdd:cd14634    142 GRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 964-1181 1.01e-14

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: 74.17  E-value: 1.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRT-KSHRYWPKLGSKHssatYGKFKV 1042
Cdd:cd14637      1 YINAALTDSYTRSAA--FIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQ----YGPMEV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1043 TTKFRTDSGCYATTGLKVKHLLSGQER--TVWHLQYTDW-PHHGCPEDVQGFLSYLEEIQSVRRHTNsvlEGiRTrhppi 1119
Cdd:cd14637     75 EFVSGSADEDIVTRLFRVQNITRLQEGhlMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESG---EG-RT----- 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720354226 1120 VVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1181
Cdd:cd14637    146 VVHCLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 964-1180 2.42e-14

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: 73.10  E-value: 2.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVT-----AEEEggrtksHRYWPklgSKHSSATYG 1038
Cdd:cd17669      1 YINASYIMGYYQSNE--FIITQHPLLHTIKDFWRMIWDHNAQLIVMLPdgqnmAEDE------FVYWP---NKDEPINCE 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1039 KFKVTTkFRTDSGCYAT-TGLKVKHLL--SGQERTVW---HLQYTDWPHHGCPedvqgflsyleeIQSVRRHTNSVLEGI 1112
Cdd:cd17669     70 TFKVTL-IAEEHKCLSNeEKLIIQDFIleATQDDYVLevrHFQCPKWPNPDSP------------ISKTFELISIIKEEA 136

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720354226 1113 RTRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLV 1180
Cdd:cd17669    137 ANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
FERM_F1_EPB41L4A cd17107
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 21-103 2.81e-14

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band 4.1-like protein 4A (EPB41L4A) and similar proteins; EPB41L4A, also termed protein NBL4, is a member of the band 4.1/Nbl4 (novel band 4.1-like protein 4) group of the FERM protein superfamily. It contains a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). EPB41L4A is an important component of the beta-catenin/Tcf pathway. It may be related to determination of cell polarity or proliferation.


Pssm-ID: 340627  Cd Length: 91  Bit Score: 69.29  E-value: 2.81e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   21 FVTRIRLLDSNviECTLSVE------STGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKFANEPL 94
Cdd:cd17107      3 FYCEIVLLDES--ELILTIQqdgiksSKGSVVLDVVFQHLNLLETDYFGLRYIDRQHQTHWLDPAKTLSEQLKLIGPPYT 80


                   ....*....
gi 1720354226   95 LFFGVMFYV 103
Cdd:cd17107     81 LYFGVKFYA 89
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 889-1184 1.04e-13

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 73.46  E-value: 1.04e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  889 DATRVPIDERLRALKKKLEDGMVFTEYEQIPNKKANGVFSTATLPENAERSRIR--EVVPYEENRVELIptkeNNTGYIN 966
Cdd:PHA02740     5 DAVDINGMDFINFINKPDLLSCIIKEYRAIVPEHEDEANKACAQAENKAKDENLalHITRLLHRRIKLF----NDEKVLD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  967 ASHIKVVvgGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEggRTKSHRYWpklgskhsSATYGKFKVTTKF 1046
Cdd:PHA02740    81 ARFVDGY--DFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHAD--KKCFNQFW--------SLKEGCVITSDKF 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1047 RTDSGCYATTGLKVKHLLS-----GQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQS----VRRHTNSVLEGirtrhp 1117
Cdd:PHA02740   149 QIETLEIIIKPHFNLTLLSltdkfGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDlcadLEKHKADGKIA------ 222

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720354226 1118 PIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 1184
Cdd:PHA02740   223 PIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLK 289
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 964-1181 1.75e-12

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: 67.79  E-value: 1.75e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  964 YINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKshRYWPKLGSKHSSATYGKFkVT 1043
Cdd:cd14635      1 YINAALMDSYKQPSA--FIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQLCP--QYWPENGVHRHGPIQVEF-VS 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1044 TKFRTDsgcYATTGLKVKHLLSGQE--RTVWHLQYTDWP-HHGCPEDVQGFLSYLEEIQSVRRHTNSVlEGiRTrhppiV 1120
Cdd:cd14635     76 ADLEED---IISRIFRIYNAARPQDgyRMVQQFQFLGWPmYRDTPVSKRSFLKLIRQVDKWQEEYNGG-EG-RT-----V 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720354226 1121 VHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1181
Cdd:cd14635    146 VHCLNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 981-1181 2.25e-12

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: 67.36  E-value: 2.25e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  981 YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTaeEEGGRTKSHRYWPKLGskhsSATYGKFKVTTkFRTDSGCYATTGL-K 1059
Cdd:cd14636     16 FIVTQHPLPNTVKDFWRLVYDYGCTSIVMLN--EVDLAQGCPQYWPEEG----MLRYGPIQVEC-MSCSMDCDVISRIfR 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1060 VKHLLSGQE--RTVWHLQYTDWP-HHGCPEDVQGFLSYLEEIQSVRRHTNSVlEGiRTrhppiVVHCSAGVGRTGVVILS 1136
Cdd:cd14636     89 ICNLTRPQEgyLMVQQFQYLGWAsHREVPGSKRSFLKLILQVEKWQEECDEG-EG-RT-----IIHCLNGGGRSGMFCAI 161

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1720354226 1137 ELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 1181
Cdd:cd14636    162 SIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
FERM_F1_FRMD3 cd17102
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 21-102 1.27e-11

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 3 (FRMD3) and similar proteins; FRMD3, also termed band 4.1-like protein 4O, or ovary type protein 4.1 (4.1O), belongs to the 4.1 protein superfamily, which share the highly conserved membrane-association FERM domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). FRMD3 is involved in maintaining cell shape and integrity. It also functions as a tumour suppressor in non-small cell lung carcinoma (NSCLC). Some single nucleotide polymorphisms (SNPs) located in FRMD3 have been associated with diabetic kidney disease (DKD) in different ethnicities.


Pssm-ID: 340622  Cd Length: 82  Bit Score: 61.49  E-value: 1.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   21 FVTRIRLL-DSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLdKFANEPLLFFGV 99
Cdd:cd17102      1 YKCTIRLLdDSEVICCEFKKDTKGQFLLDYVCNYLNLLEKDYFGLRYVDTEKQRHWLDPNKSIYKQL-KGVPPYVLCFRV 79


                   ...
gi 1720354226  100 MFY 102
Cdd:cd17102     80 KFY 82
FERM_F1_PTPN3_like cd17100
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 19-103 3.64e-11

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and similar proteins; This family includes two tyrosine-protein phosphatase non-receptors, PTPN3 and PTPN4, both of which belong to the non-transmembrane FERM-containing protein-tyrosine phosphatase (PTP) subfamily characterized by a conserved N-terminal FERM domain, a PDZ domain, and a C-terminal PTP catalytic domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340620  Cd Length: 86  Bit Score: 60.40  E-value: 3.64e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   19 NCFVTrirLLDSnvIECTLSVE--STGQECLEAVAQRLELRETHYFGLWFLSKS---QQARWVELEKPLKKHLdKFANEP 93
Cdd:cd17100      3 RCIVH---FLDD--TEQTFEVEkrDKGQVLLDKVFNHLELVEKDYFGLQFSDDSpatDSMRWLDPLKPIRKQI-KGGPPY 76

                           90
                   ....*....|
gi 1720354226   94 LLFFGVMFYV 103
Cdd:cd17100     77 YLNFRVKFYV 86
FERM_F1_FARP1_like cd17098
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, RhoGEF and ...
 24-105 8.75e-11

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, RhoGEF and pleckstrin domain-containing protein 1 (FARP1) and similar proteins; This family includes the F1 sub-domain of FERM, RhoGEF and pleckstrin domain-containing proteins FARP1, FARP2, and FERM domain-containing protein 7 (FRMD7). FARP1, also termed chondrocyte-derived ezrin-like protein (CDEP), or pleckstrin homology (PH) domain-containing family C member 2 (PLEKHC2), is a neuronal activator of the RhoA GTPase. It promotes outgrowth of developing motor neuron dendrites. It also regulates excitatory synapse formation and morphology, as well as activates the GTPase Rac1 to promote F-actin assembly. FARP2, also termed FERM domain including RhoGEF (FIR), or Pleckstrin homology (PH) domain-containing family C member 3, is a Dbl-family guanine nucleotide exchange factor (GEF) that activates Rac1 or Cdc42 in response to upstream signals, suggesting roles in regulating processes such as neuronal axon guidance and bone homeostasis. It is also a key molecule involved in the response of neuronal growth cones to class-3 semaphorins. FRMD7 plays an important role in neuronal development and is involved in the regulation of F-actin, neurofilament, and microtubule dynamics. All family members contain a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340618  Cd Length: 85  Bit Score: 59.15  E-value: 8.75e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLdKFANEPLLFFGVMFYV 103
Cdd:cd17098      4 KVQMLDDTVHIFQVQQKALGEVLFDQVCKHLNLLESDYFGLEFTDPEGNKCWLDPEKPILRQV-KRPKDVVFKFVVKFYT 82


                   ..
gi 1720354226  104 PN 105
Cdd:cd17098     83 PD 84
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 965-1173 1.84e-10

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 62.42  E-value: 1.84e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  965 INASHIKVvvgGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWpklgskHSSATYGKFKVTT 1044
Cdd:cd14559     18 LNANRVQI---GNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYF------RQSGTYGSVTVKS 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1045 KfRTDSGcYATTGLKVKHL---LSGQERT----VWHLqyTDWPHHGcPEDVQGFLSYLEEIQSVRRHTNSVLEGIRTR-- 1115
Cdd:cd14559     89 K-KTGKD-ELVDGLKADMYnlkITDGNKTitipVVHV--TNWPDHT-AISSEGLKELADLVNKSAEEKRNFYKSKGSSai 163

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720354226 1116 -----HPPiVVHCSAGVGRTGVVILSELMIyclEHNEKVEVPTMLRFLREQR-MFMIQTIAQYK 1173
Cdd:cd14559    164 ndknkLLP-VIHCRAGVGRTGQLAAAMELN---KSPNNLSVEDIVSDMRTSRnGKMVQKDEQLD 223
FERM_F1_MYLIP cd17104
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in E3 ...
 20-87 1.92e-10

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in E3 ubiquitin-protein ligase MYLIP and similar proteins; MYLIP, also termed inducible degrader of the LDL-receptor (Idol), or myosin regulatory light chain interacting protein (MIR), is an E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC), LDLR, VLDLR and LRP8. Its activity depends on E2 ubiquitin-conjugating enzymes of the UBE2D family, including UBE2D1, UBE2D2, UBE2D3, and UBE2D4. MYLIP stimulates clathrin-independent endocytosis and acts as a sterol-dependent inhibitor of cellular cholesterol uptake by binding directly to the cytoplasmic tail of the LDLR and promoting its ubiquitination via the UBE2D1/E1 complex. The ubiquitinated LDLR then enters the multivesicular body (MVB) protein-sorting pathway and is shuttled to the lysosome for degradation. Moreover, MYLIP has been identified as a novel ERM-like protein that affects cytoskeleton interactions regulating cell motility, such as neurite outgrowth. The ERM proteins includes ezrin, radixin, and moesin, which are cytoskeletal effector proteins linking actin to membrane-bound proteins at the cell surface. MYLIP contains a FERM-domain and a C-terminal C3HC4-type RING-HC finger. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340624  Cd Length: 81  Bit Score: 58.05  E-value: 1.92e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720354226   20 CFVTRirlLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLD 87
Cdd:cd17104      3 CLVSQ---PDSVVIEVEVDPKANGQECLDKVCQKLGIIEKDYFGLQYTGPKGERLWLNLRNRISRQLP 67
FERM_C pfam09380
FERM C-terminal PH-like domain;
224-306 2.28e-10

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 58.03  E-value: 2.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  224 DSHGNSVHLGIFFMGIFVRNRVGRQAVIYRWNDIGSVTHSKAAILLELIDK--EETALFHTDDIENAKYISRLFTTRHKF 301
Cdd:pfam09380    1 DKEGTDLWLGVSAKGILVYEDNNKILNLFPWREIRKISFKRKKFLIKLRDKssEETLGFYTESSRACKYLWKLCVEQHTF 80


                   ....*
gi 1720354226  302 YKQNK 306
Cdd:pfam09380   81 FRLRR 85
FERM_F1_EPB41L2 cd17202
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 24-105 2.83e-09

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like protein 2 (EPB41L2) and similar proteins; EPB41L2, also termed generally expressed protein 4.1 (4.1G), belongs to the skeletal protein 4.1 family that is involved in cellular processes such as cell adhesion, migration and signaling. EPB41L2 contains a FERM domain, a spectrin and actin binding (SAB) domain, and a C-terminal domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340722  Cd Length: 84  Bit Score: 54.98  E-value: 2.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLdkfANEPLLF-FGVMFY 102
Cdd:cd17202      5 KVTLLDGTEYSCDLEKRAKGQVLFDKVCEHLNLLEKDYFGLLYQVSANQKNWLDSTKEIKRQI---RRLPWLFtFNVKFY 81


                   ...
gi 1720354226  103 VPN 105
Cdd:cd17202     82 PPD 84
FERM_F1_ERM_like cd17097
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 21-102 6.04e-09

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family proteins; The ezrin-radixin-moesin (ERM) family includes a group of closely related cytoskeletal proteins that play an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif. They exist in two states, a dormant state in which the FERM domain binds to its own C-terminal tail and thereby precludes binding of some partner proteins, and an activated state, in which the FERM domain binds to one of many membrane binding proteins and the C-terminal tail binds to F-actin. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Merlin, which is highly related to the members of the ezrin, radixin, and moesin (ERM) protein family that are directly attached to and functionally linked with NHE1, is included in this family.


Pssm-ID: 340617  Cd Length: 83  Bit Score: 53.82  E-value: 6.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   21 FVTRIRLLDSNViECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKFANEPLLFFGVM 100
Cdd:cd17097      1 INVRVTTMDAEL-EFSIKPKAKGRELFDLVCRTIGLRETWYFGLQYENKKGRVAWLKPDKKVLTQDVSKNNTLKFFFLVK 79


                   ..
gi 1720354226  101 FY 102
Cdd:cd17097     80 FY 81
FERM_F1_EPB41L4B cd17204
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 24-102 6.95e-09

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band 4.1-like protein 4B (EPB41L4B); EPB41L4B, also termed FERM-containing protein CG1, or expressed in high metastatic cells (Ehm2), or Lulu2, is a member of the band 4.1/Nbl4 (novel band 4.1-like protein 4) group of the FERM protein superfamily. It contains a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). EPB41L4B is a positive regulator of keratinocyte adhesion and motility, suggesting a role in wound healing. It also promotes cancer metastasis in melanoma, prostate cancer and breast cancer.


Pssm-ID: 340724  Cd Length: 84  Bit Score: 54.05  E-value: 6.95e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720354226   24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLdKFANEPLLFFGVMFY 102
Cdd:cd17204      4 RVLLLDGTDVSVELPKHAKGQDLFDQIVYHLDLVETDYFGLQFMDAAQVAHWLDHTKPIKKQI-KIGPPYTLHFRIKYY 81
FERM_F1_EPB41L cd17106
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 24-105 1.14e-08

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like proteins; The family includes erythrocyte membrane protein band 4.1-like proteins EPB41L1/4.1N, EPB41L2/4.1G, and EPB41L3/4.1B. They belong to the skeletal protein 4.1 family that is involved in cellular processes such as cell adhesion, migration and signaling. EPB41L1 is a cytoskeleton-associated protein that may serve as a tumor suppressor in solid tumors. EPB41L2 is involved in cellular processes such as cell adhesion, migration and signaling. EPB41L3 also acts as a tumor suppressor implicated in a variety of meningiomas and carcinomas. Members in this family contain a FERM domain, a spectrin and actin binding (SAB) domain, and a C-terminal domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340626  Cd Length: 84  Bit Score: 53.21  E-value: 1.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLdkfANEPLLF-FGVMFY 102
Cdd:cd17106      5 KVLLLDGTEYTCEVEKRAKGQVLFDKVCEHLNLLEKDYFGLTYRDAQDQKNWLDPAKEIKKQI---RSGPWLFsFNVKFY 81


                   ...
gi 1720354226  103 VPN 105
Cdd:cd17106     82 PPD 84
FERM_F1_EPB41L1 cd17201
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 24-105 2.51e-08

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like protein 1 (EPB41L1) and similar proteins; EPB41L1, also termed neuronal protein 4.1 (4.1N), belongs to the skeletal protein 4.1 family that is involved in cellular processes such as cell adhesion, migration and signaling. It is a cytoskeleton-associated protein that may serve as a tumor suppressor in solid tumors. It suppresses hypoxia-induced epithelial-mesenchymal transition in epithelial ovarian cancer (EOC) cells. The down-regulation of EPB41L1 expression is a critical step for non-small cell lung cancer (NSCLC) development. Moreover, EPB41L1 functions as a linker protein between inositol 1,4,5-trisphosphate receptor type1 (IP3R1) and actin filaments in neurons. EPB41L1 contains a FERM domain, a spectrin and actin binding (SAB) domain, and a C-terminal domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340721  Cd Length: 84  Bit Score: 52.19  E-value: 2.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLdkfANEPLLF-FGVMFY 102
Cdd:cd17201      5 KVTLLDGSEYECEVEKHARGQVLFDTVCEHLNLLEKDYFGLTFCDTESQKNWLDPSKEIKKQI---RSGPWHFaFTVKFY 81


                   ...
gi 1720354226  103 VPN 105
Cdd:cd17201     82 PPD 84
FERM_F1_EPB41L5_like cd17108
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 24-102 3.42e-08

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like 5 (EPB41L5) and similar proteins; This family includes FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like proteins, EPB41L5 and EPB41L4B. EPB41L5 is a mesenchymal-specific protein that is an integral component of the ARF6-based pathway. EPB41L4B is a positive regulator of keratinocyte adhesion and motility, suggesting a role in wound healing. It also promotes cancer metastasis in melanoma, prostate cancer and breast cancer. Both EPB41L5 and EPB41L4B contain a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340628  Cd Length: 81  Bit Score: 51.97  E-value: 3.42e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720354226   24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLdKFANEPLLFFGVMFY 102
Cdd:cd17108      4 KVILLDGTDLSIELPKKAKGQELYEQVFYHLDLIEKDYFGLQFMDAAQVQHWLDPTKKIKKQV-KIGPPYTLRFRVKFY 81
FERM_F1_EPB41L5 cd17205
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 24-102 3.68e-08

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like 5 (EPB41L5); EPB41L5 is a mesenchymal-specific protein that is an integral component of the ARF6-based pathway. It is normally induced during epithelial-mesenchymal transition (EMT) by an EMT-related transcriptional factor, ZEB1, which drives ARF6-based invasion, metastasis and drug resistance. EPB41L5 also binds to paxillin to enhance integrin/paxillin association, and thus promotes focal adhesion dynamics. Moreover, EPB41L5 acts as a substrate for the E3 ubiquitin ligase Mind bomb 1 (Mib1), which is essential for activation of Notch signaling. EPB41L5 is a member of the band 4.1/Nbl4 (novel band 4.1-like protein 4) group of the FERM protein superfamily. It contains a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340725  Cd Length: 86  Bit Score: 51.96  E-value: 3.68e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720354226   24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLdKFANEPLLFFGVMFY 102
Cdd:cd17205      6 RVSLLDGTDVSVDLPKKAKGQELFEQIMYHLDLIEKDYFGLRFMDSAQVAHWLDVTKSIKKQV-KIGPPYCLHLRVKFY 83
FERM_F1_EPB41 cd17105
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 24-105 4.35e-08

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1 (EPB41) and similar proteins; EPB41, also termed protein 4.1 (P4.1), or 4.1R, or Band 4.1, or EPB4.1, belongs to the skeletal protein 4.1 family that is involved in cellular processes such as cell adhesion, migration and signaling. EPB41 is a widely expressed cytoskeletal phosphoprotein that stabilizes the spectrin-actin cytoskeleton and anchors the cytoskeleton to the cell membrane. EPB41 contains a FERM domain, a spectrin and actin binding (SAB) domain, and a C-terminal domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340625  Cd Length: 83  Bit Score: 51.74  E-value: 4.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKFANEplLFFGVMFYV 103
Cdd:cd17105      4 KVSLLDDTVYECEVEKHAKGQDLFKKVCEHLNLLEEDYFGLAIWDSPTSKTWLDPAKEIKKQVHGGPWE--FTFNVKFYP 81


                   ..
gi 1720354226  104 PN 105
Cdd:cd17105     82 PD 83
FERM_F1_FRMD4B cd17200
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 24-106 1.41e-07

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 4B (FRMD4B); FRMD4B, also termed GRP1-binding protein GRSP1, interacts with the coil-coil domain of ARF exchange factor GRP1 to form the Grsp1-Grp1 complex that co-localizes with cortical actin rich regions in response to stimulation of CHO-T cells with insulin or epidermal growth factor (EGF). FRMD4B contains a FERM protein interaction domain as well as two coiled coil domains and may therefore function as a scaffolding protein. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340720  Cd Length: 89  Bit Score: 50.27  E-value: 1.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKH-LDKFANEPLLFFGVMFY 102
Cdd:cd17200      6 QVHLLDDRKLELLVQPKLLSRELLDLVASHFNLKEKEYFGITFIDDTGQSNWLQLDHRVLDHdLPKKSGPVTLYFAVRFY 85


                   ....
gi 1720354226  103 VPNV 106
Cdd:cd17200     86 IESI 89
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1084-1177 2.03e-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: 2.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1084 CPEDVQGFLSYLEEIQSvrrhtnsvlegirtRHPPIVVHCSAGVGRTGVVILSELMIYcleHNEKVEVptMLRFLREQRM 1163
Cdd:cd14494     38 TLAMVDRFLEVLDQAEK--------------PGEPVLVHCKAGVGRTGTLVACYLVLL---GGMSAEE--AVRIVRLIRP 98

                           90
                   ....*....|....*
gi 1720354226 1164 FMI-QTIAQYKFVYQ 1177
Cdd:cd14494     99 GGIpQTIEQLDFLIK 113
FERM_F1_FRMD4 cd17103
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 23-106 1.11e-06

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing proteins FRMD4A, FRMD4B, and similar proteins; This family includes FERM domain-containing proteins FRMD4A and FRMD4B, both of which contain a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). FRMD4A is a cytohesin adaptor involved in cell structure, transport and signaling. It promotes the growth of cancer cells in tongue, head and neck squamous cell carcinomas. FRMD4B, also termed GRP1-binding protein GRSP1, interacts with the coil-coil domain of ARF exchange factor GRP1 to form the Grsp1-Grp1 complex that co-localizes with cortical actin rich regions in response to stimulation of CHO-T cells with insulin or epidermal growth factor (EGF).


Pssm-ID: 340623  Cd Length: 91  Bit Score: 47.66  E-value: 1.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   23 TRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHL--DKFANEPL-LFFGV 99
Cdd:cd17103      5 CQVVLLDDRRLEILVQPKLLAGDLLDLVASHFNLKEKEYFGLAYEDETGHYNWLQLDKRVLDHEfpKKWSSGPLvLHFAV 84


                   ....*..
gi 1720354226  100 MFYVPNV 106
Cdd:cd17103     85 KFYVESI 91
FERM_F1_EPB41L3 cd17203
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 24-105 1.36e-06

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like protein 3 (EPB41L3) and similar proteins; EPB41L3, also termed 4.1B, or differentially expressed in adenocarcinoma of the lung protein 1 (DAL-1), belongs to the skeletal protein 4.1 family that is involved in cellular processes such as cell adhesion, migration and signaling. EPB41L3 is a tumor suppressor that has been implicated in a variety of meningiomas and carcinomas. EPB41L3 contains a FERM domain, a spectrin and actin binding (SAB) domain, and a C-terminal domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340723  Cd Length: 84  Bit Score: 47.24  E-value: 1.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKFANEplLFFGVMFYV 103
Cdd:cd17203      5 KVTLLDGSEYTCEVEKRSKGQVLFDKVCEHLNLLEKDYFGLTYRDSENQKNWLDPAKEIKKQIRSGAWQ--FSFNVKFYP 82


                   ..
gi 1720354226  104 PN 105
Cdd:cd17203     83 PD 84
FERM_F1_PTPN4 cd17194
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 22-103 1.77e-06

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 4 (PTPN4); PTPN4, also termed protein-tyrosine phosphatase MEG1 (MEG) or PTPase-MEG1, belongs to the non-transmembrane FERM-containing protein-tyrosine phosphatase (PTP) subfamily characterized by a conserved N-terminal FERM domain, a PDZ domain, and a C-terminal PTP catalytic domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN4 protects cells against apoptosis. It associates with the mitogen-activated protein kinase p38gamma (also known as MAPK12) to form a PTPN4-p38gamma complex that promotes cellular signaling, preventing cell death induction. It also inhibits tyrosine phosphorylation and subsequent cytoplasm translocation of TRIF-related adaptor molecule (TRAM, also known as TICAM2), resulting in the disturbance of TRAM-TRIF interaction. Moreover, PTPN4 negatively regulates cell proliferation and motility through dephosphorylation of CrkI.


Pssm-ID: 340714  Cd Length: 84  Bit Score: 47.22  E-value: 1.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   22 VTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQA-RWVELEKPLKKHLdKFANEPLLFFGVM 100
Cdd:cd17194      3 VCNILLLDNTVQAFKVNKHDQGQVLLDLVFKHLDLTERDYFGLQLADDSTDNpRWLDPNKPIRKQL-KRGSPHNLNFRVK 81


                   ...
gi 1720354226  101 FYV 103
Cdd:cd17194     82 FFV 84
FERM_C_FRMD3_FRMD5 cd13192
FERM domain C-lobe of FERM domain-containing protein 3 and 5 (FRMD3 and 5); FRMD3 (also called ...
 201-303 2.75e-06

FERM domain C-lobe of FERM domain-containing protein 3 and 5 (FRMD3 and 5); FRMD3 (also called Band 4.1-like protein 4O/4.1O though it is not a true member of that family) is a novel putative tumor suppressor gene that is implicated in the origin and progression of lung cancer. In humans there are 5 isoforms that are produced by alternative splicing. Less is known about FRMD5, though there are 2 isoforms of the human protein are produced by alternative splicing. Both FRMD3 and FRMD5 contain a N-terminal FERM domain, followed by a FERM adjacent (FA) domain, and 4.1 protein C-terminal domain (CTD). The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270013  Cd Length: 105  Bit Score: 47.00  E-value: 2.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  201 AELMYINEVERLDGFGQEIFPVKDSHGNSVHLGIFFMGIFVRnRVGRQAVIYRWNDIGSVTHSKAAILLELIDKEE---T 277
Cdd:cd13192      1 AEDNFLRKAATLETYGVDPHPVKDHRGNQLYLGFTHTGIVTF-QGGKRVHHFRWNDITKFNYEGKMFILHVMQKEEkkhT 79

                           90       100
                   ....*....|....*....|....*.
gi 1720354226  278 ALFHTDDIENAKYISRLFTTRHKFYK 303
Cdd:cd13192     80 LGFKCPTPAACKHLWKCAVEQQAFYT 105
FERM_F1_Merlin cd17186
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in merlin and ...
 20-102 5.76e-06

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in merlin and similar proteins; Merlin, also termed moesin-ezrin-radixin-like protein, or neurofibromin-2 (NF2), or Schwannomerlin, or Schwannomin, is a member of the ezrin/radixin/moesin (ERM) family of cytoskeletal proteins that plays an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif, merlin however lacks the typical actin-binding motif in the C-tail. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Merlin plays vital roles in controlling proper development of organ sizes by specifically binding to a large number of target proteins localized both in cytoplasm and nuclei. Merlin may function as a tumor suppressor that functions upstream of the core Hippo pathway kinases Lats1/2 (Wts in Drosophila) and Mst1/2 (Hpo in Drosophila), as well as the nuclear E3 ubiquitin ligase DDB1-and-Cullin 4-associated Factor 1 (DCAF1)-associated cullin 4-Roc1 ligase, CRL4(DCAF1). Merlin may also has a tumor suppressor function in melanoma cells, the inhibition of the proto-oncogenic Na(+)/H(+) exchanger isoform 1 (NHE1) activity.


Pssm-ID: 340706  Cd Length: 85  Bit Score: 45.45  E-value: 5.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   20 CFVTRIRLLDSNvIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHlDKFANEPLLF-FG 98
Cdd:cd17186      2 TFTVRIVTMDAE-MEFNCEMKWKGKDLFDLVCRTIGLRETWYFGLQYTDSKGTVAWLKMDKKVLDQ-DVPKEEPVTFhFL 79


                   ....
gi 1720354226   99 VMFY 102
Cdd:cd17186     80 AKFY 83
FERM_F1_PTPN13_like cd17101
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 25-105 5.92e-06

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 13 (PTPN13) and similar proteins; This family includes tyrosine-protein phosphatase non-receptor type 13 (PTPN13), FERM and PDZ domain-containing protein 2 (FRMPD2), and FERM domain-containing proteins FRMD1 and FRMD6. All family members contain a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340621  Cd Length: 97  Bit Score: 46.01  E-value: 5.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   25 IRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLsKSQQARWVELEKPL--------KKHLDKFANEP--- 93
Cdd:cd17101      6 VVLLNGQRLQVAVDVKTTVQDLFDQVCDHLGLQETELFGLAVL-KDGEYFFLDPDTKLskyapkgwKSEAKKGLKGGkpv 84

                           90
                   ....*....|...
gi 1720354226   94 -LLFFGVMFYVPN 105
Cdd:cd17101     85 fTLYFRVKFYVDN 97
FERM_F1_FARP2 cd17190
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 24-105 7.34e-06

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF and pleckstrin domain-containing protein 2 (FARP2) and similar proteins; FARP2, also termed FERM domain including RhoGEF (FIR), or Pleckstrin homology (PH) domain-containing family C member 3, is a Dbl-family guanine nucleotide exchange factor (GEF) that activates Rac1 or Cdc42 in response to upstream signals, suggesting roles in regulating processes such as neuronal axon guidance and bone homeostasis. It is also a key molecule involved in the response of neuronal growth cones to class-3 semaphorins. FARP2 contains a FERM domain, a Dbl-homology (DH) domain and two pleckstrin homology (PH) domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340710  Cd Length: 85  Bit Score: 45.17  E-value: 7.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKFANEpLLFFGVMFYV 103
Cdd:cd17190      4 RVKLLDNTTEPLEIEPKADGQALLSQVFKRLNLVESDYFGLEFQNSQSNWIWLEPMKLIVKQVRRPKNT-KLRLAVKFFP 82


                   ..
gi 1720354226  104 PN 105
Cdd:cd17190     83 PD 84
FERM_F1_FRMD1 cd17197
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 33-105 1.13e-05

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 1 (FRMD1); FRMD1 is an uncharacterized FERM domain-containing protein. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340717  Cd Length: 98  Bit Score: 45.18  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   33 IECTLSVESTGQECLEAVAQRLELRETHYFGLwFLSKSQQARWVELEKPLKKHL------------DKFANEPLLFFGVM 100
Cdd:cd17197     14 LSLTVGVKATGQELFQQVCELLKIKEAHFFGL-SVVKNNEHIFMDLEQKLSKYFpkewkketgkgtEKFSIPFVACFRVQ 92


                   ....*
gi 1720354226  101 FYVPN 105
Cdd:cd17197     93 YYVEN 97
FERM_F1_PTPN3 cd17193
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 22-103 3.16e-05

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 3 (PTPN3); PTPN3, also termed protein-tyrosine phosphatase H1 (PTP-H1), belongs to the non-transmembrane FERM-containing protein-tyrosine phosphatase (PTP) subfamily characterized by a conserved N-terminal FERM domain, a PDZ domain, and a C-terminal PTP catalytic domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN3 associates with the mitogen-activated protein kinase p38gamma (also known as MAPK12) to form a PTPN3-p38gamma complex that promotes Ras-induced oncogenesis. It may also act as a tumor suppressor in lung cancer through its modulation of epidermal growth factor receptor (EGFR) signaling. Moreover, PTPN3 shows sensitizing effect to anti-estrogens. It dephosphorylates the tyrosine kinase EGFR, disrupts its interaction with the nuclear estrogen receptor, and increases breast cancer sensitivity to small molecule tyrosine kinase inhibitors (TKIs). It also cooperates with vitamin D receptor to stimulate breast cancer growth through their mutual stabilization.


Pssm-ID: 340713  Cd Length: 84  Bit Score: 43.69  E-value: 3.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   22 VTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQA-RWVELEKPLKKHLdKFANEPLLFFGVM 100
Cdd:cd17193      3 ICNVHFLDGSVQSFKVNKQDTGQVLLDMAYNHLGLTEREYFGLQHNEDSVDSpRWLEPSKPIRKQL-KGGFPCSLHFRVR 81


                   ...
gi 1720354226  101 FYV 103
Cdd:cd17193     82 FFI 84
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1119-1175 3.83e-05

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: 46.19  E-value: 3.83e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720354226 1119 IVVHCSAGVGRTGVVILSELMIYClehneKVEVPTMLRFLREQRMFMIQTIAQYKFV 1175
Cdd:cd14506    112 VAVHCHAGLGRTGVLIACYLVYAL-----RMSADQAIRLVRSKRPNSIQTRGQVLCV 163
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1079-1177 5.72e-05

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 44.95  E-value: 5.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1079 WPHH-----GCPEDVQGFLSYLEEIQSVrrhtnsvLEGIRTrhppIVVHCSAGVGRTGVVILSELmiycLEHNEKVEVPT 1153
Cdd:cd14505     75 WHHLpipdgGVPSDIAQWQELLEELLSA-------LENGKK----VLIHCKGGLGRTGLIAACLL----LELGDTLDPEQ 139

                           90       100
                   ....*....|....*....|....
gi 1720354226 1154 MLRFLREQRMFMIQTIAQYKFVYQ 1177
Cdd:cd14505    140 AIAAVRALRPGAIQTPKQENFLHQ 163
FERM_F1_FRMD4A cd17199
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 24-106 5.84e-05

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 4A (FRMD4A); FRMD4A is a cytohesin adaptor involved in cell structure, transport and signaling. It promotes the growth of cancer cells in tongue, head and neck squamous cell carcinomas. It also regulates tau secretion by activating cytohesin-Arf6 signaling through connecting cytohesin family Arf6-specific guanine-nucleotide exchange factors (GEFs) and Par-3 at primordial adherens junctions during epithelial polarization. As a genetic risk factor for late-onset Alzheimer's disease (AD), FRMD4A may play a role in amyloidogenic and tau-related pathways in AD. FRMD4A contains a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340719  Cd Length: 89  Bit Score: 43.03  E-value: 5.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKH-LDKFANEPLLFFGVMFY 102
Cdd:cd17199      6 QVHLLDDRKLELLVQPKLLAKELLDLVASHFNLKEKEYFGIAFTDETGHLNWLQLDRRVLEHdFPKKSGPVVLYFCVRFY 85


                   ....
gi 1720354226  103 VPNV 106
Cdd:cd17199     86 IESI 89
FERM_F1_FARP1 cd17189
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 24-105 3.12e-04

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF and pleckstrin domain-containing protein 1 (FARP1); FARP1, also termed chondrocyte-derived ezrin-like protein (CDEP), or pleckstrin homology (PH) domain-containing family C member 2 (PLEKHC2), is a neuronal activator of the RhoA GTPase. It promotes outgrowth of developing motor neuron dendrites. It also regulates excitatory synapse formation and morphology, as well as activates the GTPase Rac1 to promote F-actin assembly. As a novel downstream signaling partner of Rif, FARP1 is involved in the regulation of semaphorin signaling in neurons. FARP1 contains a FERM domain, a Dbl-homology (DH) domain and two pleckstrin homology (PH) domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340709  Cd Length: 85  Bit Score: 40.56  E-value: 3.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKfANEPLLFFGVMFYV 103
Cdd:cd17189      4 KVQMLDDTQEVFEVPQRAPGKVLLDAVCSHLNLVEGDYFGLEFQDHRKVMVWLDLLKPIVKQIRR-PKHVVLRFVVKFFP 82


                   ..
gi 1720354226  104 PN 105
Cdd:cd17189     83 PD 84
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1109-1177 3.48e-04

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 41.88  E-value: 3.48e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720354226 1109 LEGIRTRHPPIVVHCSAGVGRTGVVILSeLMIYclehnEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1177
Cdd:COG2453     73 IDEALREGKKVLVHCRGGIGRTGTVAAA-YLVL-----LGLSAEEALARVRAARPGAVETPAQRAFLER 135
FERM_F1_FRMD7 cd17188
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 24-105 3.76e-04

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 7 (FRMD7); FRMD7 plays an important role in neuronal development and is involved in the regulation of F-actin, neurofilament, and microtubule dynamics. It interacts with the Rho GTPase regulator, RhoGDIalpha, and activates the Rho subfamily member Rac1, which regulates reorganization of actin filaments and controls neuronal outgrowth. Mutations in the FRMD7 gene are responsible for the X-linked idiopathic congenital nystagmus (ICN), a disease which affects ocular motor control. FRMD7 contains a FERM domain, and a pleckstrin homology (PH) domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340708  Cd Length: 86  Bit Score: 40.56  E-value: 3.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   24 RIRLLDSNviECTLSVE--STGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLdKFANEPLLFFGVMF 101
Cdd:cd17188      5 KVQFLDDS--QKVFVVDqkSTGKDLFNMSCSHLNLVEKEYFGLEFRNHAGNNVWLELLKPITKQI-KNPKELIFKFTVKF 81


                   ....
gi 1720354226  102 YVPN 105
Cdd:cd17188     82 FPVD 85
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 1088-1162 8.17e-04

Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region.


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 40.71  E-value: 8.17e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720354226 1088 VQGFLSYLEEIQSVRRHTNSVLEGIRTRHPPIVVHCSAGVGRTGVVILSELMIYclehnEKVEVPTMLRFLREQR 1162
Cdd:pfam00782   41 IPVEDNHETNISKYLEEAVEFIDDARQKGGKVLVHCQAGISRSATLIIAYLMKT-----RNLSLNEAYSFVKERR 110
FERM_F1_Moesin cd17237
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in moesin and ...
 24-102 1.41e-03

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in moesin and similar proteins; Moesin, also termed membrane-organizing extension spike protein, is a member of the ezrin/radixin/moesin (ERM) family of cytoskeletal proteins that plays an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif. The C-terminal domain can fold back to bind to the FERM domain forming an autoinhibited conformation. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Moesin is involved in mitotic spindle function through stabilizing cell shape and microtubules at the cell cortex. It is required for the formation of F-actin networks that mediate endosome biogenesis or maturation and transport through the degradative pathway.


Pssm-ID: 340757  Cd Length: 84  Bit Score: 38.96  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   24 RIRLLDSNvIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHlDKFANEPLLF-FGVMFY 102
Cdd:cd17237      5 RVTTMDAE-LEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQ-DVRKESPLLFkFRAKFY 82
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
1055-1162 1.85e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 39.96  E-value: 1.85e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226  1055 TTGLKVKHLLSGQERTVW----HLQYTDWPHHGcpEDVQGFLSYLEEiqsvrrhTNSVLEGIRTRHPPIVVHCSAGVGRT 1130
Cdd:smart00195   22 LKKLGITHVINVTNEVPNyngsDFTYLGVPIDD--NTETKISPYFPE-------AVEFIEDAESKGGKVLVHCQAGVSRS 92

                            90       100       110
                    ....*....|....*....|....*....|..
gi 1720354226  1131 GVVILSELMIYclehnEKVEVPTMLRFLREQR 1162
Cdd:smart00195   93 ATLIIAYLMKT-----RNMSLNDAYDFVKDRR 119
FERM_F1_ERM cd17187
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 24-102 2.32e-03

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family proteins, Ezrin, Radixin, and Moesin; The ezrin-radixin-moesin (ERM) family includes a group of closely related cytoskeletal proteins that plays an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif. They exist in two states, a dormant state in which the FERM domain binds to its own C-terminal tail and thereby precludes binding of some partner proteins, and an activated state, in which the FERM domain binds to one of many membrane binding proteins and the C-terminal tail binds to F-actin. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340707 [Multi-domain]  Cd Length: 83  Bit Score: 38.22  E-value: 2.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226   24 RIRLLDSNvIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHlDKFANEPLLF-FGVMFY 102
Cdd:cd17187      4 RVTTMDAE-LEFAIQPNTTGKQLFDQVVKTIGLREIWFFGLQYVDSKGYSTWLKLNKKVLSQ-DVKKENPLQFkFRAKFY 81
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1118-1177 5.73e-03

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: 38.41  E-value: 5.73e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354226 1118 PIVVHCSAGVGRTGvVILSELMIYClehnEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 1177
Cdd:cd14504     84 AVLVHCLAGKGRTG-TMLACYLVKT----GKISAVDAINEIRRIRPGSIETSEQEKFVIQ 138
Y_phosphatase3 pfam13350
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
 1108-1138 7.67e-03

Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 families.


Pssm-ID: 463853 [Multi-domain]  Cd Length: 243  Bit Score: 39.53  E-value: 7.67e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1720354226 1108 VLEGIRTRHPPIVVHCSAGVGRTGVV---ILSEL 1138
Cdd:pfam13350  121 LFEALADNDGPVLFHCTAGKDRTGVAaalLLSLL 154
 
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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