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Conserved domains on  [gi|34328899|ref|NP_005392|]
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tyrosine-protein phosphatase non-receptor type 14 [Homo sapiens]

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 ...
 896-1182 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: 641.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  896 RFRTLKKKLEEGMVFTEYEQIPKKKANGIFSTAALPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKVVVGGA 975
Cdd:cd14599    1 RCKTLERKLEEGMVFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  976 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSVCYATTG 1055
Cdd:cd14599   81 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1056 LKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVRRHTNSMLEGTKNRHPPIVVHCSAGVGRTGVLILSE 1135
Cdd:cd14599  161 LKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDSTKNCNPPIVVHCSAGVGRTGVVILTE 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 34328899 1136 LMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQFLQ 1182
Cdd:cd14599  241 LMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 24-220 7.05e-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: 186.73  E-value: 7.05e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899      24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQAR-WVELEKPLKKHLDKFANEPLlFFGVMFY 102
Cdd:smart00295    3 KVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRhWLDPAKTLLDQDVKSEPLTL-YFRVKFY 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899     103 VPNVSWLQQEATRY-QYYLQVKKDVLEGRLRCTLDQVIRLAGLAVQADFGDYNQFDS--QDFLREYVLFPMDLaLEEAVL 179
Cdd:smart00295   82 PPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdlRGELSLKRFLPKQL-LDSRKL 160

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 34328899     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 1.07e-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: 113.15  E-value: 1.07e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  215 FGQEIFPVKDNHGNCVHLGIFFMGIFVRNRIGRQAVIYRWNDMGNITHNKSTILVELINKEETALFHTDDIENAKYISRL 294
Cdd:cd13188    1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRPPVFFRWEDIKNVINHKRTFSIECQNSEETVQFQFEDAETAKYVWKL 80

                         90
                 ....*....|.
gi 34328899  295 FATRHKFYKQN 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 ...
 896-1182 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: 641.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  896 RFRTLKKKLEEGMVFTEYEQIPKKKANGIFSTAALPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKVVVGGA 975
Cdd:cd14599    1 RCKTLERKLEEGMVFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  976 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSVCYATTG 1055
Cdd:cd14599   81 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1056 LKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVRRHTNSMLEGTKNRHPPIVVHCSAGVGRTGVLILSE 1135
Cdd:cd14599  161 LKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDSTKNCNPPIVVHCSAGVGRTGVVILTE 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 34328899 1136 LMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQFLQ 1182
Cdd:cd14599  241 LMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
909-1179 2.79e-92

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 296.88  E-value: 2.79e-92
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899     909 VFTEYEQIPKKKANGI-FSTAALPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKVVVGGAEwhYIATQGPLP 987
Cdd:smart00194    2 LEEEFEKLDRLKPDDEsCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKA--YIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899     988 HTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhsSATYGKFKVTTKFRTDSVCYATTGLKVKHLLSGQER 1067
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGE--PLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETR 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899    1068 TVWHLQYTDWPDHGCPEDVQGFLSYLEEIqsvrRHTNSMLEGtknrhpPIVVHCSAGVGRTGVLILSELMIYCLEHNEKV 1147
Cdd:smart00194  158 TVTHYHYTNWPDHGVPESPESILDLIRAV----RKSQSTSTG------PIVVHCSAGVGRTGTFIAIDILLQQLEAGKEV 227

                           250       260       270
                    ....*....|....*....|....*....|..
gi 34328899    1148 EVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQ 1179
Cdd:smart00194  228 DIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
933-1179 3.20e-92

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 295.69  E-value: 3.20e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899    933 NAERSRIREVVPYEENRVELIPTKENNtGYINASHIKVVVGgaEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEE 1012
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPS-DYINASYIDGYKK--PKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   1013 EGGRTKSHRYWPKlgSKHSSATYGKFKVTTK-FRTDSVCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLS 1091
Cdd:pfam00102   78 EKGREKCAQYWPE--EEGESLEYGDFTVTLKkEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLD 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   1092 YLEEIQSVRRHtnsmlegtkNRHPPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYK 1171
Cdd:pfam00102  156 LLRKVRKSSLD---------GRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYI 226


                   ....*...
gi 34328899   1172 FVYQVLIQ 1179
Cdd:pfam00102  227 FLYDAILE 234
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 24-220 7.05e-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: 186.73  E-value: 7.05e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899      24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQAR-WVELEKPLKKHLDKFANEPLlFFGVMFY 102
Cdd:smart00295    3 KVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRhWLDPAKTLLDQDVKSEPLTL-YFRVKFY 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899     103 VPNVSWLQQEATRY-QYYLQVKKDVLEGRLRCTLDQVIRLAGLAVQADFGDYNQFDS--QDFLREYVLFPMDLaLEEAVL 179
Cdd:smart00295   82 PPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdlRGELSLKRFLPKQL-LDSRKL 160

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 34328899     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 1.02e-52

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: 1.02e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   18 KNCFVTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKFANEPLLFF 97
Cdd:cd17191    1 KNCFVTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKQLDKFANEPLLFF 80


                 ....*..
gi 34328899   98 GVMFYVP 104
Cdd:cd17191   81 GVMFYVP 87
PHA02738 PHA02738
hypothetical protein; Provisional
 906-1182 1.48e-47

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 173.19  E-value: 1.48e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   906 EGMVFTEYEQIPKKKANGIFStaALPENAERSRIREVVPYEENRVELiPTKENNTGYINASHikvvVGGAEW--HYIATQ 983
Cdd:PHA02738   24 EEVITREHQKVISEKVDGTFN--AEKKNRKLNRYLDAVCFDHSRVIL-PAERNRGDYINANY----VDGFEYkkKFICGQ 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   984 GPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLgsKHSSATYGKFKVTTKFRTDSVCYATTGLKVKHLlS 1063
Cdd:PHA02738   97 APTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDV--EQGSIRFGKFKITTTQVETHPHYVKSTLLLTDG-T 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  1064 GQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVRR--HTNSMLEGTKNRHPP-IVVHCSAGVGRTGVLILSELMIYC 1140
Cdd:PHA02738  174 SATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCQKelAQESLQIGHNRLQPPpIVVHCNAGLGRTPCYCVVDISISR 253

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 34328899  1141 LEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQFLQ 1182
Cdd:PHA02738  254 FDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVN 295
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 104-220 8.09e-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: 126.23  E-value: 8.09e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899    104 PNVSWLQQEATRYQYYLQVKKDVLEGRLRCTLDQVIRLAGLAVQADFGDYNQFDSQ-DFLREYVLFPMDLaLEEAVLEEL 182
Cdd:pfam00373    1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTsEYLSLESFLPKQL-LRKMKSKEL 79

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 34328899    183 TQKVAQEHKAHSGILPAEAELMYINEVERLDGFGQEIF 220
Cdd:pfam00373   80 EKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
929-1183 7.27e-32

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 126.36  E-value: 7.27e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  929 ALPENAERSRIREVVPYEENRVEliptkeNNTGYINASHIKVvvgGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMV 1008
Cdd:COG5599   38 QNINGSPLNRFRDIQPYKETALR------ANLGYLNANYIQV---IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVL 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1009 TAEEEGG--RTKSHRYWpklgskHSSATYGKFKVTTK------FRTDSVCYAttgLKVKHLLSGQE-RTVWHLQYTDWPD 1079
Cdd:COG5599  109 ASDDEISkpKVKMPVYF------RQDGEYGKYEVSSEltesiqLRDGIEART---YVLTIKGTGQKkIEIPVLHVKNWPD 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1080 HGCPEDVQgflsyLEEIQSVRRHTNSMLEGTKNrhpPIVVHCSAGVGRTGVLILselmIYCLE------HNEKVEVPMML 1153
Cdd:COG5599  180 HGAISAEA-----LKNLADLIDKKEKIKDPDKL---LPVVHCRAGVGRTGTLIA----CLALSksinalVQITLSVEEIV 247

                        250       260       270
                 ....*....|....*....|....*....|.
gi 34328899 1154 RLLREQR-MFMIQTIAQykfvYQVLIQFLQN 1183
Cdd:COG5599  248 IDMRTSRnGGMVQTSEQ----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 1.07e-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: 113.15  E-value: 1.07e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  215 FGQEIFPVKDNHGNCVHLGIFFMGIFVRNRIGRQAVIYRWNDMGNITHNKSTILVELINKEETALFHTDDIENAKYISRL 294
Cdd:cd13188    1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRPPVFFRWEDIKNVINHKRTFSIECQNSEETVQFQFEDAETAKYVWKL 80

                         90
                 ....*....|.
gi 34328899  295 FATRHKFYKQN 305
Cdd:cd13188   81 CVLQHKFYRQN 91
FERM_C pfam09380
FERM C-terminal PH-like domain;
224-306 1.25e-10

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 58.80  E-value: 1.25e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899    224 DNHGNCVHLGIFFMGIFVRNRIGRQAVIYRWNDMGNITHNKSTILVELINK--EETALFHTDDIENAKYISRLFATRHKF 301
Cdd:pfam09380    1 DKEGTDLWLGVSAKGILVYEDNNKILNLFPWREIRKISFKRKKFLIKLRDKssEETLGFYTESSRACKYLWKLCVEQHTF 80


                   ....*
gi 34328899    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 ...
 896-1182 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: 641.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  896 RFRTLKKKLEEGMVFTEYEQIPKKKANGIFSTAALPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKVVVGGA 975
Cdd:cd14599    1 RCKTLERKLEEGMVFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  976 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSVCYATTG 1055
Cdd:cd14599   81 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1056 LKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVRRHTNSMLEGTKNRHPPIVVHCSAGVGRTGVLILSE 1135
Cdd:cd14599  161 LKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDSTKNCNPPIVVHCSAGVGRTGVVILTE 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 34328899 1136 LMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQFLQ 1182
Cdd:cd14599  241 LMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 962-1182 4.51e-144

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: 432.86  E-value: 4.51e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  962 YINASHIKVVVGGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVT 1041
Cdd:cd14598    1 YINASHIKVTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVTYGRFKIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1042 TKFRTDSVCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVRRHTNSMLEgTKNRHPPIVVHC 1121
Cdd:cd14598   81 TRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTID-PKSPNPPVLVHC 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34328899 1122 SAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQFLQ 1182
Cdd:cd14598  160 SAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 962-1181 3.97e-141

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: 425.33  E-value: 3.97e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  962 YINASHIKVVVGGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVT 1041
Cdd:cd14540    1 YINASHITATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHDALTFGEYKVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1042 TKFRTDSVCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVRRHTNSMLeGTKNRHPPIVVHC 1121
Cdd:cd14540   81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQDV-AGHNRNPPTLVHC 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1122 SAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQFL 1181
Cdd:cd14540  160 SAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
909-1179 2.79e-92

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 296.88  E-value: 2.79e-92
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899     909 VFTEYEQIPKKKANGI-FSTAALPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKVVVGGAEwhYIATQGPLP 987
Cdd:smart00194    2 LEEEFEKLDRLKPDDEsCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKA--YIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899     988 HTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhsSATYGKFKVTTKFRTDSVCYATTGLKVKHLLSGQER 1067
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGE--PLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETR 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899    1068 TVWHLQYTDWPDHGCPEDVQGFLSYLEEIqsvrRHTNSMLEGtknrhpPIVVHCSAGVGRTGVLILSELMIYCLEHNEKV 1147
Cdd:smart00194  158 TVTHYHYTNWPDHGVPESPESILDLIRAV----RKSQSTSTG------PIVVHCSAGVGRTGTFIAIDILLQQLEAGKEV 227

                           250       260       270
                    ....*....|....*....|....*....|..
gi 34328899    1148 EVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQ 1179
Cdd:smart00194  228 DIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
933-1179 3.20e-92

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 295.69  E-value: 3.20e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899    933 NAERSRIREVVPYEENRVELIPTKENNtGYINASHIKVVVGgaEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEE 1012
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPS-DYINASYIDGYKK--PKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   1013 EGGRTKSHRYWPKlgSKHSSATYGKFKVTTK-FRTDSVCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLS 1091
Cdd:pfam00102   78 EKGREKCAQYWPE--EEGESLEYGDFTVTLKkEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLD 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   1092 YLEEIQSVRRHtnsmlegtkNRHPPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYK 1171
Cdd:pfam00102  156 LLRKVRKSSLD---------GRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYI 226


                   ....*...
gi 34328899   1172 FVYQVLIQ 1179
Cdd:pfam00102  227 FLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 962-1175 8.57e-79

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: 257.21  E-value: 8.57e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  962 YINASHIKVvvGGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHssATYGKFKVT 1041
Cdd:cd00047    1 YINASYIDG--YRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKP--LEYGDITVT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1042 TKFRTDSVCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVRRHTNSmlegtknrhpPIVVHC 1121
Cdd:cd00047   77 LVSEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNG----------PIVVHC 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 34328899 1122 SAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQ 1175
Cdd:cd00047  147 SAGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 894-1179 3.74e-75

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: 250.15  E-value: 3.74e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  894 DERFRTLKKKLEEGMVFTEYEQIPKKKANGIFSTAALPENAERSRIREVVPYEENRVELiptkENNTGYINASHIKVVVG 973
Cdd:cd14600    1 EESMAQLKKGLESGTVLIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVL----QGNEDYINASYVNMEIP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  974 GAEW--HYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLgskHSSATYGKFKVTTKFRTDSVCY 1051
Cdd:cd14600   77 SANIvnKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDP---PDVMEYGGFRVQCHSEDCTIAY 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1052 ATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVRRHTNsmlegtknrhpPIVVHCSAGVGRTGVL 1131
Cdd:cd14600  154 VFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVENE-----------PVLVHCSAGIGRTGVL 222

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 34328899 1132 ILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQ 1179
Cdd:cd14600  223 VTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAILR 270
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 962-1181 7.88e-71

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: 235.35  E-value: 7.88e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  962 YINASHIKVVVGGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlGSKHSSATYGKFKVT 1041
Cdd:cd14538    1 YINASHIRIPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPD-SLNKPLICGGRLEVS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1042 TKFRTDSVCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYleeIQSVRRHTNSMlegtknrhpPIVVHC 1121
Cdd:cd14538   80 LEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRF---IRYMRRIHNSG---------PIVVHC 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1122 SAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQFL 1181
Cdd:cd14538  148 SAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 909-1174 4.48e-66

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: 224.17  E-value: 4.48e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  909 VFTEYEQIPKKKANGIFSTAALPENAERSRIREVVPYEENRVEL-IPTKENNTGYINASHikvvVGGAEWH--YIATQGP 985
Cdd:cd14543    5 IYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLpKRNGDERTDYINANF----MDGYKQKnaYIATQGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  986 LPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgSKHSSATYGKFKVTTKFRTDSVCYATTGLKVKHLLSGQ 1065
Cdd:cd14543   81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPL--EEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1066 ERTVWHLQYTDWPDHGCPEDVQGFLSYLEEiqsVRRHTNSMLEGTKNR---H---PPIVVHCSAGVGRTGVLILSELMIY 1139
Cdd:cd14543  159 SRQVTHFQFTSWPDFGVPSSAAALLDFLGE---VRQQQALAVKAMGDRwkgHppgPPIVVHCSAGIGRTGTFCTLDICLS 235

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 34328899 1140 CLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVY 1174
Cdd:cd14543  236 QLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 962-1173 1.34e-65

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: 220.66  E-value: 1.34e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  962 YINASHIKVVVGGAEW--HYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGskhSSATYGKFK 1039
Cdd:cd14541    2 YINANYVNMEIPGSGIvnRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLG---ETMQFGNLQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1040 VTTKFRTDSVCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYleeIQSVRRHTNSMLEgtknrhpPIVV 1119
Cdd:cd14541   79 ITCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDF---VKRVRQNRVGMVE-------PTVV 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 34328899 1120 HCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFV 1173
Cdd:cd14541  149 HCSAGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFV 202
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 962-1175 3.56e-62

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: 210.95  E-value: 3.56e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  962 YINASHIKVVvGGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPklgSKHSSATYGKFKVT 1041
Cdd:cd18533    1 YINASYITLP-GTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWP---SGEYEGEYGDLTVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1042 ----TKFrtDSVCYATTGLKVKHlLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVRRHTNSMlegtknrhPPI 1117
Cdd:cd18533   77 lvseEEN--DDGGFIVREFELSK-EDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLD--------PPI 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34328899 1118 VVHCSAGVGRTGVLILSELMIYCLE--HNEKVEVPMMLRL-------LREQRMFMIQTIAQYKFVYQ 1175
Cdd:cd18533  146 IVHCSAGVGRTGTFIALDSLLDELKrgLSDSQDLEDSEDPvyeivnqLRKQRMSMVQTLRQYIFLYD 212
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 932-1181 2.92e-59

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: 203.52  E-value: 2.92e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  932 ENAERSRIREVVPYEENRVELiptkENNTGYINASHIKVVVGGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAE 1011
Cdd:cd14597    2 ENRKKNRYKNILPYDTTRVPL----GDEGGYINASFIKMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1012 EEGGRTKSHRYWPKLGSKhSSATYGKFKVTTKFRTDSVCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGC---PEDVQG 1088
Cdd:cd14597   78 VEGGKIKCQRYWPEILGK-TTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTpsqPEQLLT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1089 FLSYLEEIqsvrrhtnsmlegtkNRHPPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIA 1168
Cdd:cd14597  157 FISYMRHI---------------HKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTED 221

                        250
                 ....*....|...
gi 34328899 1169 QYKFVYQVLIQFL 1181
Cdd:cd14597  222 QYIFCYQVILYVL 234
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 933-1183 8.50e-59

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: 202.69  E-value: 8.50e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  933 NAERSRIREVVPYEENRVELIPTKENNTG--YINASHIKVVVGGA-----EWHYIATQGPLPHTCHDFWQMVWEQGVNVI 1005
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDRDPNVPGsdYINANYIRNENEGPttdenAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1006 AMVTAEEEGGRTKSHRYWPKLGSKHSsatYGKFKVTTKFRTDSVCYATTGLKVKHLLSGQ-ERTVWHLQYTDWPDHGCPE 1084
Cdd:cd14544   81 VMTTKEVERGKNKCVRYWPDEGMQKQ---YGPYRVQNVSEHDTTDYTLRELQVSKLDQGDpIREIWHYQYLSWPDHGVPS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1085 DVQGFLSYLEEIQsvRRHTNSMLEGtknrhpPIVVHCSAGVGRTGVLILSELMIYCLEHNE---KVEVPMMLRLLREQRM 1161
Cdd:cd14544  158 DPGGVLNFLEDVN--QRQESLPHAG------PIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRS 229

                        250       260
                 ....*....|....*....|..
gi 34328899 1162 FMIQTIAQYKFVYQVLIQFLQN 1183
Cdd:cd14544  230 GMVQTEAQYKFIYVAVAQYIET 251
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 962-1179 6.31e-58

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: 199.02  E-value: 6.31e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  962 YINASHIKVVVGGAEW--HYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGskhSSATYGKFK 1039
Cdd:cd14601    2 YINANYINMEIPSSSIinRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPS---GSSSYGGFQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1040 VTTKFRTDSVCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVRRHtnsmlegtknRHPPIVV 1119
Cdd:cd14601   79 VTCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAG----------KDEPVVV 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1120 HCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQ 1179
Cdd:cd14601  149 HCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 938-1175 3.80e-55

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: 191.41  E-value: 3.80e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  938 RIREVVPYEENRVELIP-TKENNTGYINASHIKvvvggAEWH---YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEE 1013
Cdd:cd14548    1 RYTNILPYDHSRVKLIPiNEEEGSDYINANYIP-----GYNSpreFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCME 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1014 GGRTKSHRYWPKlgsKHSSATYGKFKVTtkFRTDSVCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYL 1093
Cdd:cd14548   76 KGRVKCDHYWPF---DQDPVYYGDITVT--MLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1094 EEIQSVRRHTNSmlegtknrhpPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFV 1173
Cdd:cd14548  151 RLVRDYIKQEKG----------PTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFL 220


                 ..
gi 34328899 1174 YQ 1175
Cdd:cd14548  221 HQ 222
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 962-1174 4.13e-55

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: 190.25  E-value: 4.13e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  962 YINASHIKvvvggaEWH----YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhssaTYGK 1037
Cdd:cd14549    1 YINANYVD------GYNkaraYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTE----TYGN 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1038 FKVTTKFRTDSVCYATTGLKVKHL------LSGQERTVWHLQYTDWPDHGCPEDVQGFLSYleeiqsVRRHTNSMLEGTK 1111
Cdd:cd14549   71 IQVTLLSTEVLATYTVRTFSLKNLklkkvkGRSSERVVYQYHYTQWPDHGVPDYTLPVLSF------VRKSSAANPPGAG 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34328899 1112 nrhpPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVY 1174
Cdd:cd14549  145 ----PIVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 911-1179 1.54e-54

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: 191.19  E-value: 1.54e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  911 TEYEQIPKK----KANGIFSTAA--LPENAERSRIREVVPYEENRVELIP-TKENNTGYINASHIKVVVGgaEWHYIATQ 983
Cdd:cd14603    2 GEFSEIRACsaafKADYVCSTVAggRKENVKKNRYKDILPYDQTRVILSLlQEEGHSDYINANFIKGVDG--SRAYIATQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  984 GPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPklgSKHSSATYGKFKVTT---KFRTDSVCYATtgLKVKH 1060
Cdd:cd14603   80 GPLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWA---QEQEPLQTGPFTITLvkeKRLNEEVILRT--LKVTF 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1061 llSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEiqsVRRHTNSMLEgtknrhpPIVVHCSAGVGRTGVLILSElMIYC 1140
Cdd:cd14603  155 --QKESRSVSHFQYMAWPDHGIPDSPDCMLAMIEL---ARRLQGSGPE-------PLCVHCSAGCGRTGVICTVD-YVRQ 221

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 34328899 1141 LEHNEKVE-----VPMMLRlLREQRMFMIQTIAQYKFVYQVLIQ 1179
Cdd:cd14603  222 LLLTQRIPpdfsiFDVVLE-MRKQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 962-1182 4.57e-54

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: 187.65  E-value: 4.57e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  962 YINASHIKVVVGGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPK-----LGSKHSSATYG 1036
Cdd:cd14596    1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPEtlqepMELENYQLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1037 KFKVTTKFRTDSvcyattgLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVRRhtnsmlEGtknrhpP 1116
Cdd:cd14596   81 NYQALQYFIIRI-------IKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHN------TG------P 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34328899 1117 IVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQFLQ 1182
Cdd:cd14596  142 IVVHCSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 24-220 7.05e-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: 186.73  E-value: 7.05e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899      24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQAR-WVELEKPLKKHLDKFANEPLlFFGVMFY 102
Cdd:smart00295    3 KVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRhWLDPAKTLLDQDVKSEPLTL-YFRVKFY 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899     103 VPNVSWLQQEATRY-QYYLQVKKDVLEGRLRCTLDQVIRLAGLAVQADFGDYNQFDS--QDFLREYVLFPMDLaLEEAVL 179
Cdd:smart00295   82 PPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdlRGELSLKRFLPKQL-LDSRKL 160

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 34328899     180 EELTQKVAQEHKAHSGILPAEAELMYINEVERLDGFGQEIF 220
Cdd:smart00295  161 KEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 931-1182 3.79e-53

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: 187.39  E-value: 3.79e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  931 PENAERSRIREVVPYEENRVELIPTKENNTG--YINASHIK---VVVGGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVI 1005
Cdd:cd14606   16 PENKSKNRYKNILPFDHSRVILQGRDSNIPGsdYINANYVKnqlLGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1006 AMVTAEEEGGRTKSHRYWPKLGSKHSsatYGKFKVTTKFRTDSVCYATTGLKVKHLLSGQE-RTVWHLQYTDWPDHGCPE 1084
Cdd:cd14606   96 VMTTREVEKGRNKCVPYWPEVGMQRA---YGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELiREIWHYQYLSWPDHGVPS 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1085 DVQGFLSYLEEIqsvrrhtNSMLEGTKNRhPPIVVHCSAGVGRTGVLILSELMIYCLEH---NEKVEVPMMLRLLREQRM 1161
Cdd:cd14606  173 EPGGVLSFLDQI-------NQRQESLPHA-GPIIVHCSAGIGRTGTIIVIDMLMENISTkglDCDIDIQKTIQMVRAQRS 244

                        250       260
                 ....*....|....*....|.
gi 34328899 1162 FMIQTIAQYKFVYQVLIQFLQ 1182
Cdd:cd14606  245 GMVQTEAQYKFIYVAIAQFIE 265
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 933-1179 7.90e-53

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: 185.29  E-value: 7.90e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  933 NAERSRIREVVPYEENRVELIPTK-ENNTGYINASHIKvvvgGAEWH--YIATQGPLPHTCHDFWQMVWEQGVNVIAMVT 1009
Cdd:cd14553    3 NKPKNRYANVIAYDHSRVILQPIEgVPGSDYINANYCD----GYRKQnaYIATQGPLPETFGDFWRMVWEQRSATIVMMT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1010 AEEEGGRTKSHRYWPKLGskhsSATYGKFKVTTkfrTDSVCYATTGLKVKHLL---SGQERTVWHLQYTDWPDHGCPEDV 1086
Cdd:cd14553   79 KLEERSRVKCDQYWPTRG----TETYGLIQVTL---LDTVELATYTVRTFALHkngSSEKREVRQFQFTAWPDHGVPEHP 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1087 QGFLSYLeeiqsvRRhtnsmlegTKNRHP----PIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMF 1162
Cdd:cd14553  152 TPFLAFL------RR--------VKACNPpdagPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNY 217

                        250
                 ....*....|....*..
gi 34328899 1163 MIQTIAQYKFVYQVLIQ 1179
Cdd:cd14553  218 MVQTEDQYIFIHDALLE 234
FERM_F1_PTPN14 cd17191
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 18-104 1.02e-52

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: 1.02e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   18 KNCFVTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKFANEPLLFF 97
Cdd:cd17191    1 KNCFVTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKQLDKFANEPLLFF 80


                 ....*..
gi 34328899   98 GVMFYVP 104
Cdd:cd17191   81 GVMFYVP 87
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 962-1175 2.94e-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: 182.20  E-value: 2.94e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  962 YINASHIKVVVGGAEwHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgSKHSSATYGKFKVT 1041
Cdd:cd14539    1 YINASLIEDLTPYCP-RFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPT--ERGQALVYGAITVS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1042 TKFRTDSVCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVRRHTNSMlegtknrHPPIVVHC 1121
Cdd:cd14539   78 LQSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSL-------QTPIVVHC 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 34328899 1122 SAGVGRTGVL-ILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQ 1175
Cdd:cd14539  151 SSGVGRTGAFcLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 938-1175 6.21e-52

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: 182.21  E-value: 6.21e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  938 RIREVVPYEENRVeLIPTKENN--TGYINASHIKVVvGGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGg 1015
Cdd:cd14547    2 RYKTILPNEHSRV-CLPSVDDDplSSYINANYIRGY-DGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1016 RTKSHRYWPKLgskhSSATYGKFKVTTKFRTDSVCYATTGLKVKHllSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEE 1095
Cdd:cd14547   79 KEKCAQYWPEE----ENETYGDFEVTVQSVKETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQE 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1096 IQSVRRhtnsmlegTKNRHPPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQ 1175
Cdd:cd14547  153 VEEARQ--------TEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 928-1175 1.05e-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: 181.95  E-value: 1.05e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  928 AALPENAERSRIREVVPYEENRVELIPTKE-NNTGYINASHIKvvvgGAEWH--YIATQGPLPHTCHDFWQMVWEQGVNV 1004
Cdd:cd14554    1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGvEGSDYINASFID----GYRQRgaYIATQGPLAETTEDFWRMLWEHNSTI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1005 IAMVTAEEEGGRTKSHRYWPklgsKHSSATYGKFKVTTKFRTDSVCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPE 1084
Cdd:cd14554   77 IVMLTKLREMGREKCHQYWP----AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPK 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1085 DVQGFLSYLEEIQSVRRHTNSmlEGtknrhpPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMI 1164
Cdd:cd14554  153 SGEGFIDFIGQVHKTKEQFGQ--EG------PITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMV 224

                        250
                 ....*....|.
gi 34328899 1165 QTIAQYKFVYQ 1175
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 6.28e-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: 6.28e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   18 KNCFVTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKFANEPLLFF 97
Cdd:cd17099    1 KNSFVVRIQLLDNTVLECTLSPESTGQDCLEYVAQRLELREIEYFGLRYVNKKGQLRWVDLEKPLKKQLDKHAHEPLLYF 80


                 ....*
gi 34328899   98 GVMFY 102
Cdd:cd17099   81 GVMFY 85
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 937-1181 4.71e-50

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: 177.00  E-value: 4.71e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  937 SRIREVVPYEENRVELIPTKENNTG-YINASHIKVVvgGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGG 1015
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHEEPGSdYINANYMPGY--WSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1016 RTKSHRYWPklgSKHSSATYGKFKVTTKFRTDSVCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEe 1095
Cdd:cd14619   79 RVKCEHYWP---LDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRR- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1096 iqSVRRHTNSMLEGTknrhpPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQ 1175
Cdd:cd14619  155 --LLRQWLDQTMSGG-----PTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQ 227


                 ....*.
gi 34328899 1176 VLIQFL 1181
Cdd:cd14619  228 CILDFL 233
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 932-1182 1.94e-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: 175.98  E-value: 1.94e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  932 ENAERSRIREVVPYEENRVELIPTKENNTG--YINASHI------KVVVGGAEWHYIATQGPLPHTCHDFWQMVWEQGVN 1003
Cdd:cd14605    1 ENKNKNRYKNILPFDHTRVVLHDGDPNEPVsdYINANIImpefetKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1004 VIAMVTAEEEGGRTKSHRYWPklgSKHSSATYGKFKVTTKFRTDSVCYATTGLKVKHLLSGQ-ERTVWHLQYTDWPDHGC 1082
Cdd:cd14605   81 VIVMTTKEVERGKSKCVKYWP---DEYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGNtERTVWQYHFRTWPDHGV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1083 PEDVQGFLSYLEEiqsVRRHTNSMLEGTknrhpPIVVHCSAGVGRTGVLILSELMIYCLEhnEK-----VEVPMMLRLLR 1157
Cdd:cd14605  158 PSDPGGVLDFLEE---VHHKQESIMDAG-----PVVVHCSAGIGRTGTFIVIDILIDIIR--EKgvdcdIDVPKTIQMVR 227

                        250       260
                 ....*....|....*....|....*
gi 34328899 1158 EQRMFMIQTIAQYKFVYQVLIQFLQ 1182
Cdd:cd14605  228 SQRSGMVQTEAQYRFIYMAVQHYIE 252
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 889-1181 4.03e-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: 4.03e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  889 TRVPMDERFRTLKK--KLEEGMVFT----EYEQIPKKKAN-GIFSTAALPENAERSRIREVVPYEENRVELIPTKE-NNT 960
Cdd:cd14627    2 TEVPARNLYSYIQKlaQVEVGEHVTgmelEFKRLANSKAHtSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGvEGS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  961 GYINASHIKVVvgGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPklgsKHSSATYGKFKV 1040
Cdd:cd14627   82 DYINASFIDGY--RQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWP----AERSARYQYFVV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1041 TTKFRTDSVCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVRRHTnsmlegtkNRHPPIVVH 1120
Cdd:cd14627  156 DPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQF--------GQDGPISVH 227

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34328899 1121 CSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQFL 1181
Cdd:cd14627  228 CSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 936-1179 5.88e-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: 173.87  E-value: 5.88e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  936 RSRIREVVPYEENRVEL-IPTKENNTGYINASHIKVVVGGAEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEG 1014
Cdd:cd14602    1 KNRYKDILPYDHSRVELsLITSDEDSDYINANFIKGVYGPRA--YIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1015 GRTKSHRYWPKLGSkhSSATYGKFKVTTKFRTDSVCYATTGLKVKhlLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLE 1094
Cdd:cd14602   79 GKKKCERYWAEPGE--MQLEFGPFSVTCEAEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPILELIW 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1095 EIQSVRRHTNsmlegtknrhPPIVVHCSAGVGRTGVLILSELMIYCLEHN---EKVEVPMMLRLLREQRMFMIQTIAQYK 1171
Cdd:cd14602  155 DVRCYQEDDS----------VPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIQEMRTQRPSLVQTKEQYE 224


                 ....*...
gi 34328899 1172 FVYQVLIQ 1179
Cdd:cd14602  225 LVYNAVIE 232
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 889-1181 5.97e-49

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: 176.08  E-value: 5.97e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  889 TRVPMDERFRTLKK--KLEEGMVFT----EYEQIPKKKAN-GIFSTAALPENAERSRIREVVPYEENRVELIPTKE-NNT 960
Cdd:cd14628    1 TEVPARNLYAYIQKltQIETGENVTgmelEFKRLASSKAHtSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGvEGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  961 GYINASHIKVVvgGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPklgsKHSSATYGKFKV 1040
Cdd:cd14628   81 DYINASFIDGY--RQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWP----AERSARYQYFVV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1041 TTKFRTDSVCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVRRHTnsmlegtkNRHPPIVVH 1120
Cdd:cd14628  155 DPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQF--------GQDGPISVH 226

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34328899 1121 CSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQFL 1181
Cdd:cd14628  227 CSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYL 287
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 913-1179 1.49e-48

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: 174.44  E-value: 1.49e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  913 YEQIPKKKANGIFSTAALPENAERSRIREVVPYEENRVELipTKENNTgYINASHIKVvvGGAEWHYIATQGPLPHTCHD 992
Cdd:cd14608    5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKL--HQEDND-YINASLIKM--EEAQRSYILTQGPLPNTCGH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  993 FWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSVCYATTGLKVKHLLSGQERTVWHL 1072
Cdd:cd14608   80 FWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1073 QYTDWPDHGCPEDVQGFLSYLEEIqsvrRHTNSMlegtKNRHPPIVVHCSAGVGRTGVLILSELMIYCLEHNE---KVEV 1149
Cdd:cd14608  160 HYTTWPDFGVPESPASFLNFLFKV----RESGSL----SPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKdpsSVDI 231

                        250       260       270
                 ....*....|....*....|....*....|
gi 34328899 1150 PMMLRLLREQRMFMIQTIAQYKFVYQVLIQ 1179
Cdd:cd14608  232 KKVLLEMRKFRMGLIQTADQLRFSYLAVIE 261
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 936-1175 5.55e-48

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: 171.04  E-value: 5.55e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  936 RSRIREVVPYEENRVELiptKENNTGYINAShiKVVVGGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGG 1015
Cdd:cd14545    3 RYRDRDPYDHDRSRVKL---KQGDNDYINAS--LVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1016 RTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSVCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEE 1095
Cdd:cd14545   78 QIKCAQYWPQGEGNAMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1096 IqsvrRHTNSMLEGtknrHPPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLL--REQRMFMIQTIAQYKFV 1173
Cdd:cd14545  158 V----RESGSLSSD----VGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPSSVDVKKVLLemRKYRMGLIQTPDQLRFS 229


                 ..
gi 34328899 1174 YQ 1175
Cdd:cd14545  230 YL 231
PHA02738 PHA02738
hypothetical protein; Provisional
 906-1182 1.48e-47

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 173.19  E-value: 1.48e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   906 EGMVFTEYEQIPKKKANGIFStaALPENAERSRIREVVPYEENRVELiPTKENNTGYINASHikvvVGGAEW--HYIATQ 983
Cdd:PHA02738   24 EEVITREHQKVISEKVDGTFN--AEKKNRKLNRYLDAVCFDHSRVIL-PAERNRGDYINANY----VDGFEYkkKFICGQ 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   984 GPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLgsKHSSATYGKFKVTTKFRTDSVCYATTGLKVKHLlS 1063
Cdd:PHA02738   97 APTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDV--EQGSIRFGKFKITTTQVETHPHYVKSTLLLTDG-T 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  1064 GQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVRR--HTNSMLEGTKNRHPP-IVVHCSAGVGRTGVLILSELMIYC 1140
Cdd:PHA02738  174 SATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCQKelAQESLQIGHNRLQPPpIVVHCNAGLGRTPCYCVVDISISR 253

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 34328899  1141 LEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQFLQ 1182
Cdd:PHA02738  254 FDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVN 295
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 937-1175 1.50e-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: 169.70  E-value: 1.50e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  937 SRIREVVPYEENRVELIPTKEN-NTGYINASHIKVVVGGAEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGG 1015
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVpGSDYINASYISGYLCPNE--FIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1016 RTKSHRYWPKlgSKHSSATYGKFKVTTKFRTDSVCYATTGLKV-KHllsGQERTVWHLQYTDWPDHGCPEDVQGFLSYLE 1094
Cdd:cd14616   79 RIRCHQYWPE--DNKPVTVFGDIVITKLMEDVQIDWTIRDLKIeRH---GDYMMVRQCNFTSWPEHGVPESSAPLIHFVK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1095 EIQSVRRHTNSmlegtknrhpPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVY 1174
Cdd:cd14616  154 LVRASRAHDNT----------PMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223


                 .
gi 34328899 1175 Q 1175
Cdd:cd14616  224 Q 224
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 937-1175 2.57e-47

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: 168.94  E-value: 2.57e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  937 SRIREVVPYEENRVELIPTKENN-TGYINASHIKVVvgGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGG 1015
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYIPGN--NFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1016 RTKSHRYWPklgSKHSSATYGKFKVttKFRTDSVCYATTGLKVKhlLSGQE-----RTVWHLQYTDWPDHGCPEDVQGFL 1090
Cdd:cd14617   79 RVKCDHYWP---ADQDSLYYGDLIV--QMLSESVLPEWTIREFK--ICSEEqldapRLVRHFHYTVWPDHGVPETTQSLI 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1091 SYleeIQSVRRHTnsmlegtkNRHP---PIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTI 1167
Cdd:cd14617  152 QF---VRTVRDYI--------NRTPgsgPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTE 220


                 ....*...
gi 34328899 1168 AQYKFVYQ 1175
Cdd:cd14617  221 CQYVYLHQ 228
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 930-1180 9.22e-47

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: 168.09  E-value: 9.22e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  930 LPENAERSRIREVVPYEENRVEL--IPTKENNTGYINASHIKVVvGGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAM 1007
Cdd:cd14612   12 IPGHASKDRYKTILPNPQSRVCLrrAGSQEEEGSYINANYIRGY-DGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVM 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1008 VTAEEEGgRTKSHRYWPKlgskhSSATYGKFKVTTKFRTDSVCYATTGLKVKHllSGQERTVWHLQYTDWPDHGCPEDVQ 1087
Cdd:cd14612   91 ITKLKEK-KEKCVHYWPE-----KEGTYGRFEIRVQDMKECDGYTIRDLTIQL--EEESRSVKHYWFSSWPDHQTPESAG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1088 GFLSYLEEIQSVRRHTNSMlegtknrhPPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTI 1167
Cdd:cd14612  163 PLLRLVAEVEESRQTAASP--------GPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTS 234

                        250
                 ....*....|...
gi 34328899 1168 AQYKFVYQVLIQF 1180
Cdd:cd14612  235 EQYQFLHHTLALY 247
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 938-1175 9.32e-47

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: 167.30  E-value: 9.32e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  938 RIREVVPYEENRVELIPTKENNTGYINASHIKVVVGGAEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRT 1017
Cdd:cd14615    2 RYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKE--FIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1018 KSHRYWPKLGSKhssaTYGKFKVTTKFRTDSVCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEeiq 1097
Cdd:cd14615   80 KCEEYWPSKQKK----DYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRH--- 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34328899 1098 SVRRHTNSMLegtknRHPPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQ 1175
Cdd:cd14615  153 LVREYMKQNP-----PNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 225
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 903-1179 4.52e-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: 167.13  E-value: 4.52e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  903 KLEEGMVFT-EYEQI-PKKKANgiFSTAALPENAERSRIREVVPYEENRVELIPTKE-NNTGYINASHIKvvvGGAEWH- 978
Cdd:cd14626   11 KANDGLKFSqEYESIdPGQQFT--WENSNLEVNKPKNRYANVIAYDHSRVILTSVDGvPGSDYINANYID---GYRKQNa 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  979 YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhssaTYGKFKVTTKFRTDSVCYATTGLKV 1058
Cdd:cd14626   86 YIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTE----TYGMIQVTLLDTVELATYSVRTFAL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1059 KHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVrrhtNSMLEGtknrhpPIVVHCSAGVGRTGVLILSELMI 1138
Cdd:cd14626  162 YKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKAC----NPPDAG------PMVVHCSAGVGRTGCFIVIDAML 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 34328899 1139 YCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQ 1179
Cdd:cd14626  232 ERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 913-1174 1.43e-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: 165.14  E-value: 1.43e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  913 YEQIPKKKANGIFSTAALPENAERSRIREVVPYEENRVELIPTkENNtgYINAShiKVVVGGAEWHYIATQGPLPHTCHD 992
Cdd:cd14607    4 YLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNT-END--YINAS--LVVIEEAQRSYILTQGPLPNTCCH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  993 FWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSVCYATTGLKVKHLLSGQERTVWHL 1072
Cdd:cd14607   79 FWLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1073 QYTDWPDHGCPEDVQGFLSYLEEIqsvrRHTNSMlegtKNRHPPIVVHCSAGVGRTGVLILSELMIYCLEHNE--KVEVP 1150
Cdd:cd14607  159 HYTTWPDFGVPESPASFLNFLFKV----RESGSL----SPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIK 230

                        250       260
                 ....*....|....*....|....
gi 34328899 1151 MMLRLLREQRMFMIQTIAQYKFVY 1174
Cdd:cd14607  231 QVLLDMRKYRMGLIQTPDQLRFSY 254
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 912-1181 2.72e-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: 165.67  E-value: 2.72e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  912 EYEQIPKKKAN-GIFSTAALPENAERSRIREVVPYEENRVELIPTKE-NNTGYINASHIKVVvgGAEWHYIATQGPLPHT 989
Cdd:cd14629   31 EFKLLANSKAHtSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGvEGSDYINASFIDGY--RQQKAYIATQGPLAET 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  990 CHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPklgsKHSSATYGKFKVTTKFRTDSVCYATTGLKVKHLLSGQERTV 1069
Cdd:cd14629  109 TEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWP----AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTI 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1070 WHLQYTDWPDHGCPEDVQGFLSYLEEIQSVRRHTnsmlegtkNRHPPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEV 1149
Cdd:cd14629  185 RQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQF--------GQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDM 256

                        250       260       270
                 ....*....|....*....|....*....|..
gi 34328899 1150 PMMLRLLREQRMFMIQTIAQYKFVYQVLIQFL 1181
Cdd:cd14629  257 FQTVKTLRTQRPAMVQTEDQYQLCYRAALEYL 288
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 962-1175 3.85e-45

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: 161.92  E-value: 3.85e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  962 YINASHIKvvvGGAE-WHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLgsKHSSATYGkfKV 1040
Cdd:cd14557    1 YINASYID---GFKEpRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSM--EEGSRAFG--DV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1041 TTKFRTDSVC--YATTGLKVKHLL-SGQERTVWHLQYTDWPDHGCPEDVQGFLsyleeiqSVRRHTNSMlegtKNRHP-P 1116
Cdd:cd14557   74 VVKINEEKICpdYIIRKLNINNKKeKGSGREVTHIQFTSWPDHGVPEDPHLLL-------KLRRRVNAF----NNFFSgP 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 34328899 1117 IVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQ 1175
Cdd:cd14557  143 IVVHCSAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 962-1175 3.85e-45

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: 161.82  E-value: 3.85e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  962 YINASHIKVVVGGAEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhsSATYGKFKVT 1041
Cdd:cd14542    1 YINANFIKGVSGSKA--YIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEE--QLQFGPFKIS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1042 ---TKFRTDSvcYATTGLKVKhlLSGQERTVWHLQYTDWPDHGCPEDVQgflSYLEEIQSVRRHTNSmlegtknRHPPIV 1118
Cdd:cd14542   77 lekEKRVGPD--FLIRTLKVT--FQKESRTVYQFHYTAWPDHGVPSSVD---PILDLVRLVRDYQGS-------EDVPIC 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34328899 1119 VHCSAGVGRTGVL--------ILSELMIyclehNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQ 1175
Cdd:cd14542  143 VHCSAGCGRTGTIcaidyvwnLLKTGKI-----PEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 937-1178 3.41e-44

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: 160.11  E-value: 3.41e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  937 SRIREVVPYEENRVELIP-TKENNTGYINASHIKVVVGGAEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGG 1015
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQlGGEPHSDYINANFIPGYTSPQE--FIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1016 RTKSHRYWPklgSKHSSATYGKFKVTTKFRTDSVCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEe 1095
Cdd:cd14618   79 RVLCDHYWP---SESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRE- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1096 iqSVRRHtnsmLEGTKNRHpPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQ 1175
Cdd:cd14618  155 --LVREH----VQATKGKG-PTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHS 227


                 ...
gi 34328899 1176 VLI 1178
Cdd:cd14618  228 CIL 230
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 912-1179 3.58e-44

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: 161.80  E-value: 3.58e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  912 EYEQI-PKKKANgiFSTAALPENAERSRIREVVPYEENRVELIPTKE-NNTGYINASHIKVVvgGAEWHYIATQGPLPHT 989
Cdd:cd14625   27 EYESIdPGQQFT--WEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGiMGSDYINANYIDGY--RKQNAYIATQGPLPET 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  990 CHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhssaTYGKFKVTTKFRTDSVCYATTGLKVKHLLSGQERTV 1069
Cdd:cd14625  103 FGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTE----TYGMIQVTLLDTIELATFCVRTFSLHKNGSSEKREV 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1070 WHLQYTDWPDHGCPEDVQGFLSYLEEIQSVrrhtNSMLEGtknrhpPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEV 1149
Cdd:cd14625  179 RQFQFTAWPDHGVPEYPTPFLAFLRRVKTC----NPPDAG------PIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDI 248

                        250       260       270
                 ....*....|....*....|....*....|
gi 34328899 1150 PMMLRLLREQRMFMIQTIAQYKFVYQVLIQ 1179
Cdd:cd14625  249 YGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 931-1179 1.73e-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: 159.82  E-value: 1.73e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  931 PENAERSRIREVVPYEENRVEL--IPTKEN-NTGYINASHIKVVVGGAEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAM 1007
Cdd:cd17667   25 PDNKHKNRYINILAYDHSRVKLrpLPGKDSkHSDYINANYVDGYNKAKA--YIATQGPLKSTFEDFWRMIWEQNTGIIVM 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1008 VTAEEEGGRTKSHRYWPklgsKHSSATYGKFKVTTKFRTDSVCYATTGL-----KVKHLLSGQ------ERTVWHLQYTD 1076
Cdd:cd17667  103 ITNLVEKGRRKCDQYWP----TENSEEYGNIIVTLKSTKIHACYTVRRFsirntKVKKGQKGNpkgrqnERTVIQYHYTQ 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1077 WPDHGCPEDVQGFLSYleeiqsVRRHTNSMLEGTKnrhpPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLL 1156
Cdd:cd17667  179 WPDMGVPEYALPVLTF------VRRSSAARTPEMG----PVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHI 248

                        250       260
                 ....*....|....*....|...
gi 34328899 1157 REQRMFMIQTIAQYKFVYQVLIQ 1179
Cdd:cd17667  249 RTQRNYLVQTEEQYIFIHDALLE 271
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 927-1175 4.34e-43

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: 157.36  E-value: 4.34e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  927 TAALPENAERSRIREVVPYEENRVELIPT-KENNTGYINASHIKVVVGGAEwhYIATQGPLPHTCHDFWQMVWEQGVNVI 1005
Cdd:cd14614    6 AADLPVNRCKNRYTNILPYDFSRVKLVSMhEEEGSDYINANYIPGYNSPQE--YIATQGPLPETRNDFWKMVLQQKSQII 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1006 AMVTAEEEGGRTKSHRYWPklgSKHSSATYGKFKVTTKFRTDSVCYATTGLKVKHLLSGQErtVWHLQYTDWPDHGCPeD 1085
Cdd:cd14614   84 VMLTQCNEKRRVKCDHYWP---FTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQD--VMHFNYTAWPDHGVP-T 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1086 VQGFLSYLEEIQSVRRHTNsmlegtkNRHPPIVVHCSAGVGRTGVLI-LSELMIYCLEHnEKVEVPMMLRLLREQRMFMI 1164
Cdd:cd14614  158 ANAAESILQFVQMVRQQAV-------KSKGPMIIHCSAGVGRTGTFIaLDRLLQHIRDH-EFVDILGLVSEMRSYRMSMV 229

                        250
                 ....*....|.
gi 34328899 1165 QTIAQYKFVYQ 1175
Cdd:cd14614  230 QTEEQYIFIHQ 240
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 932-1182 9.23e-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: 158.17  E-value: 9.23e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  932 ENAERSRIREVVPYEENRVEL-IPTKENNTGYINASHIKVVVGGAEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTA 1010
Cdd:cd14604   56 ENVKKNRYKDILPFDHSRVKLtLKTSSQDSDYINANFIKGVYGPKA--YIATQGPLANTVIDFWRMIWEYNVAIIVMACR 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1011 EEEGGRTKSHRYWPKLGSKhsSATYGKFKVT---TKFRTDsvcYATTGLKVKhlLSGQERTVWHLQYTDWPDHGCPedvQ 1087
Cdd:cd14604  134 EFEMGRKKCERYWPLYGEE--PMTFGPFRISceaEQARTD---YFIRTLLLE--FQNETRRLYQFHYVNWPDHDVP---S 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1088 GFLSYLEEIQSVRRHtnsmlegTKNRHPPIVVHCSAGVGRTGVLILSELMIYCLEHN---EKVEVPMMLRLLREQRMFMI 1164
Cdd:cd14604  204 SFDSILDMISLMRKY-------QEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHSAV 276

                        250
                 ....*....|....*...
gi 34328899 1165 QTIAQYKFVYQVLIQFLQ 1182
Cdd:cd14604  277 QTKEQYELVHRAIAQLFE 294
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 962-1175 2.17e-42

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: 153.91  E-value: 2.17e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  962 YINASHIKvvvGGAEWH-YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhssaTYGKFKV 1040
Cdd:cd14551    1 YINASYID---GYQEKNkFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCW----TYGNLRV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1041 TTKFRTDSVCYATTGLKVKHLLSG----QERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVrrhtNSMLEGtknrhpP 1116
Cdd:cd14551   74 RVEDTVVLVDYTTRKFCIQKVNRGigekRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSA----NPPRAG------P 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 34328899 1117 IVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQ 1175
Cdd:cd14551  144 IVVHCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 942-1179 2.28e-42

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: 154.71  E-value: 2.28e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  942 VVPYEENRVELIPTKEN-NTGYINASHIKVVVGGAEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSH 1020
Cdd:cd14620    4 ILPYDHSRVILSQLDGIpCSDYINASYIDGYKEKNK--FIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1021 RYWPKLGSkhssATYGKFKVTTKFRTDSVCYATTGLKVKHLLSGQ---ERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQ 1097
Cdd:cd14620   82 QYWPDQGC----WTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGckaPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1098 SVrrhtNSMLEGtknrhpPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVL 1177
Cdd:cd14620  158 SV----NPVHAG------PIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227


                 ..
gi 34328899 1178 IQ 1179
Cdd:cd14620  228 LE 229
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 962-1178 3.23e-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: 153.60  E-value: 3.23e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  962 YINASHIKVVvgGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHssatYGKFKVT 1041
Cdd:cd17668    1 YINANYVDGY--NKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEE----YGNFLVT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1042 TKFRTDSVCYATTGLKVKH--LLSG------QERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVRRHTNSmlegtknr 1113
Cdd:cd17668   75 QKSVQVLAYYTVRNFTLRNtkIKKGsqkgrpSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVG-------- 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34328899 1114 hpPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLI 1178
Cdd:cd17668  147 --PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
FERM_F1_PTPN21 cd17192
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 18-104 4.06e-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: 4.06e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   18 KNCFVTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKFANEPLLFF 97
Cdd:cd17192    1 KSCLVARIQLLNNEFVEFTLSVESTGQECLEAVAQRLELREITYFSLWYYNKQNQQRWVDLEKPLKKQLDKYALEPTVYF 80


                 ....*..
gi 34328899   98 GVMFYVP 104
Cdd:cd17192   81 GVVFYVP 87
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 962-1174 6.17e-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: 6.17e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  962 YINASHIKVvvggaewH------YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhssaTY 1035
Cdd:cd14546    1 YINASTIYD-------HdprnpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSE----VY 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1036 GKFKVTTkFRTDSVC--YATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYleeiqsvRRHTNSMLEGtknR 1113
Cdd:cd14546   70 HIYEVHL-VSEHIWCddYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEF-------RRKVNKSYRG---R 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34328899 1114 HPPIVVHCSAGVGRTGVLILSELMIYCLEHNEK-VEVPMMLRLLREQRMFMIQTIAQYKFVY 1174
Cdd:cd14546  139 SCPIVVHCSDGAGRTGTYILIDMVLNRMAKGAKeIDIAATLEHLRDQRPGMVKTKDQFEFVL 200
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 962-1174 6.40e-41

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


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 149.92  E-value: 6.40e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  962 YINASHIKVVVGGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRT-KSHRYWPKlgSKHSSATYGKFKV 1040
Cdd:cd17658    1 YINASLVETPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPA--EENESREFGRISV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1041 TTK-FRTDSVCYATTGLKVKHL-LSGQERTVWHLQYTDWPDHGCPEDVqgflsyleeiQSVRRHTNSMLEGTKNRHpPIV 1118
Cdd:cd17658   79 TNKkLKHSQHSITLRVLEVQYIeSEEPPLSVLHIQYPEWPDHGVPKDT----------RSVRELLKRLYGIPPSAG-PIV 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34328899 1119 VHCSAGVGRTGVlilselmiYCLEHN----------EKVEVPMMLRLLREQRMFMIQTIAQYKFVY 1174
Cdd:cd17658  148 VHCSAGIGRTGA--------YCTIHNtirrilegdmSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 912-1179 1.27e-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: 151.81  E-value: 1.27e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  912 EYEQI-PKKKANgiFSTAALPENAERSRIREVVPYEENRVeLIPTKENNTG--YINASHIKVVvgGAEWHYIATQGPLPH 988
Cdd:cd14624   27 EYESIdPGQQFT--WEHSNLEVNKPKNRYANVIAYDHSRV-LLSAIEGIPGsdYINANYIDGY--RKQNAYIATQGALPE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  989 TCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhssaTYGKFKVTTKFRTDSVCYATTGLKVKHLLSGQERT 1068
Cdd:cd14624  102 TFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTE----TYGLIQVTLLDTVELATYCVRTFALYKNGSSEKRE 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1069 VWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVrrhtNSMLEGtknrhpPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVE 1148
Cdd:cd14624  178 VRQFQFTAWPDHGVPEHPTPFLAFLRRVKTC----NPPDAG------PMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVD 247

                        250       260       270
                 ....*....|....*....|....*....|.
gi 34328899 1149 VPMMLRLLREQRMFMIQTIAQYKFVYQVLIQ 1179
Cdd:cd14624  248 IYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 962-1177 1.89e-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: 148.19  E-value: 1.89e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  962 YINASHIKVVvgGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGskhsSATYGKFKVT 1041
Cdd:cd14552    1 YINASFIDGY--RQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDG----SVSSGDITVE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1042 TKFRTDSVCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVRRHTNSMlegtknrhpPIVVHC 1121
Cdd:cd14552   75 LKDQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNH---------PITVHC 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 34328899 1122 SAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVL 1177
Cdd:cd14552  146 SAGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 962-1174 2.80e-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: 147.92  E-value: 2.80e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  962 YINASHIKvvvggAEWH---YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgskhSSATYGKF 1038
Cdd:cd14558    1 YINASFID-----GYWGpksLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGD-----EKKTYGDI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1039 KVTTKFRTDSVCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIqsvrRHTNSMLEGTKNRHPPIV 1118
Cdd:cd14558   71 EVELKDTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSI----KQKLPYKNSKHGRSVPIV 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34328899 1119 VHCSAGVGRTGvlilselmIYC-----LE--HNEK-VEVPMMLRLLREQRMFMIQTIAQYKFVY 1174
Cdd:cd14558  147 VHCSDGSSRTG--------IFCalwnlLEsaETEKvVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 938-1177 3.50e-40

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: 148.65  E-value: 3.50e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  938 RIREVVPYEENRVeLIPTK--ENNTGYINASHIKvvvGGAEWH-YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEG 1014
Cdd:cd14623    1 RVLQIIPYEFNRV-IIPVKrgEENTDYVNASFID---GYRQKDsYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEER 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1015 GRTKSHRYWPKLGskhsSATYGKFKVTTKFRTDSVCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLE 1094
Cdd:cd14623   77 GQEKCAQYWPSDG----SVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1095 EIQSVRRHTNSMlegtknrhpPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVY 1174
Cdd:cd14623  153 AVQKQQQQSGNH---------PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCY 223


                 ...
gi 34328899 1175 QVL 1177
Cdd:cd14623  224 KVV 226
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 932-1180 4.36e-40

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 150.92  E-value: 4.36e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   932 ENAERSRIREVVPYEENRVeLIPTKENNTGYINASHikvvVGG--AEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVT 1009
Cdd:PHA02742   51 KNMKKCRYPDAPCFDRNRV-ILKIEDGGDDFINASY----VDGhnAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMIT 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  1010 AEEEGGRTKSHRYWpkLGSKHSSATYGKFKVTTK----FRTdsvcYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPED 1085
Cdd:PHA02742  126 KIMEDGKEACYPYW--MPHERGKATHGEFKIKTKkiksFRN----YAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRD 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  1086 VQGFLSYLEEIqsvrRHTNSMLE---GTKNR--HPPIVVHCSAGVGRTGVLILSELMIYclEHNEKVEVPMM--LRLLRE 1158
Cdd:PHA02742  200 PNKFLDFVLAV----READLKADvdiKGENIvkEPPILVHCSAGLDRAGAFCAIDICIS--KYNERAIIPLLsiVRDLRK 273

                         250       260
                  ....*....|....*....|..
gi 34328899  1159 QRMFMIQTIAQYKFVYQVLIQF 1180
Cdd:PHA02742  274 QRHNCLSLPQQYIFCYFIVLIF 295
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 912-1179 1.01e-39

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: 149.40  E-value: 1.01e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  912 EYEQIPKKKANGIFSTAALPENAERSRIREVVPYEENRVELIPTKE-NNTGYINASHIKvvvGGAEWH-YIATQGPLPHT 989
Cdd:cd14621   31 EFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGvPDSDYINASFIN---GYQEKNkFIAAQGPKEET 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  990 CHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSkhssATYGKFKVTTKFRTDSVCYATTGLKVKHL--LSGQ-- 1065
Cdd:cd14621  108 VNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGC----WTYGNIRVSVEDVTVLVDYTVRKFCIQQVgdVTNKkp 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1066 ERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVrrhtNSMLEGtknrhpPIVVHCSAGVGRTGVLILSELMIYCLEHNE 1145
Cdd:cd14621  184 QRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNC----NPQYAG------AIVVHCSAGVGRTGTFIVIDAMLDMMHAER 253

                        250       260       270
                 ....*....|....*....|....*....|....
gi 34328899 1146 KVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQ 1179
Cdd:cd14621  254 KVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLE 287
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 936-1175 1.08e-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: 146.99  E-value: 1.08e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  936 RSRIREVVPYEENRVELIPTKENN--TGYINASHIKVVvGGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEE 1013
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKPKNSNDslSTYINANYIRGY-GGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1014 GGRtKSHRYWPKlgskhSSATYGKFKVTTKFRTDSVCYATTGLKVKHllSGQERTVWHLQYTDWPDHGCPEDVQGFLSYL 1093
Cdd:cd14611   81 KNE-KCVLYWPE-----KRGIYGKVEVLVNSVKECDNYTIRNLTLKQ--GSQSRSVKHYWYTSWPDHKTPDSAQPLLQLM 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1094 EEIQSVRRhtNSMLEGtknrhpPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFV 1173
Cdd:cd14611  153 LDVEEDRL--ASPGRG------PVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFV 224


                 ..
gi 34328899 1174 YQ 1175
Cdd:cd14611  225 HH 226
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 930-1177 2.87e-39

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: 146.93  E-value: 2.87e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  930 LPENAERSRIREVVPYEENRVELIPTKENN--TGYINASHIKVVvGGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAM 1007
Cdd:cd14613   22 IPGLVRKNRYKTILPNPHSRVCLTSPDQDDplSSYINANYIRGY-GGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVM 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1008 VTAEEEGGRtKSHRYWPKlgskhSSATYGKFKVTTKfrtDSVCYATTGLKVKHLLSG-QERTVWHLQYTDWPDHGCPEDV 1086
Cdd:cd14613  101 ITNIEEMNE-KCTEYWPE-----EQVTYEGIEITVK---QVIHADDYRLRLITLKSGgEERGLKHYWYTSWPDQKTPDNA 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1087 QGFLSYLEEIQSVRRHTnsmlegtKNRHPPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQT 1166
Cdd:cd14613  172 PPLLQLVQEVEEARQQA-------EPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQT 244

                        250
                 ....*....|.
gi 34328899 1167 IAQYKFVYQVL 1177
Cdd:cd14613  245 CEQYQFVHHVL 255
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 901-1172 4.54e-39

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: 147.13  E-value: 4.54e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  901 KKKLEEgmvftEYEQIPKKKANGIFSTAALPE-NAERSRIREVVPYEENRVEL-IPTKENNTGYINASHIKVvvggaewH 978
Cdd:cd14610   16 KNRLEK-----EWEALCAYQAEPNATNVAQREeNVQKNRSLAVLPYDHSRIILkAENSHSHSDYINASPIMD-------H 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  979 ------YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhssaTYGKFKVTtkFRTDSV-C- 1050
Cdd:cd14610   84 dprnpaYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSN----LYHIYEVN--LVSEHIwCe 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1051 -YATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYleeiqsvRRHTNSMLEGtknRHPPIVVHCSAGVGRTG 1129
Cdd:cd14610  158 dFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDF-------RRKVNKCYRG---RSCPIIVHCSDGAGRSG 227

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 34328899 1130 VLILSELMIYCLEHNEK-VEVPMMLRLLREQRMFMIQTIAQYKF 1172
Cdd:cd14610  228 TYILIDMVLNKMAKGAKeIDIAATLEHLRDQRPGMVQTKEQFEF 271
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 907-1181 5.27e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 147.84  E-value: 5.27e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   907 GMVFTEYEQIPKKKANGIFSTAALPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKvvvgGAE--WHYIATQG 984
Cdd:PHA02747   25 GIIRDEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWID----GFEddKKFIATQG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   985 PLPHTCHDFWQMVWEQGVNVIAMVT-AEEEGGRTKSHRYWPKlgSKHSSATYGKFKVTTKFRTDSVCYATTGLKVKHLLS 1063
Cdd:PHA02747  101 PFAETCADFWKAVWQEHCSIIVMLTpTKGTNGEEKCYQYWCL--NEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKIL 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  1064 GQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVRRHTNSMLEGTKNRHPPIVVHCSAGVGRTGVLILSELMIYCLEH 1143
Cdd:PHA02747  179 KDSRKISHFQCSEWFEDETPSDHPDFIKFIKIIDINRKKSGKLFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVK 258

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 34328899  1144 NEKVEVPMMLRLLREQRMFMIQTIAQYKFV---YQVLIQFL 1181
Cdd:PHA02747  259 RKAICLAKTAEKIREQRHAGIMNFDDYLFIqpgYEVLHYFL 299
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 962-1179 2.87e-38

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: 141.98  E-value: 2.87e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  962 YINASHIKvvvgGAEW--HYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgskhSSATYGKFK 1039
Cdd:cd14555    1 YINANYID----GYHRpnHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPD-----DTEVYGDIK 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1040 VTTkFRTDSVC-YATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVrrhtnsmlegTKNRHPPIV 1118
Cdd:cd14555   72 VTL-VETEPLAeYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKAS----------NPPSAGPIV 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34328899 1119 VHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQ 1179
Cdd:cd14555  141 VHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 893-1172 4.23e-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: 144.41  E-value: 4.23e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  893 MDERFRTLKKKLEEGMVFTEYEQIPKKkangiFSTAALPENAERSRIREVVPYEENRVEL-IPTKENNTGYINASHIkVV 971
Cdd:cd14609    7 MEDHLRNRDRLAKEWQALCAYQAEPNT-----CSTAQGEANVKKNRNPDFVPYDHARIKLkAESNPSRSDYINASPI-IE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  972 VGGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGskhsSATYGKFKVTtkFRTDSV-C 1050
Cdd:cd14609   81 HDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEG----SSLYHIYEVN--LVSEHIwC 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1051 --YATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYleeiqsvRRHTNSMLEGtknRHPPIVVHCSAGVGRT 1128
Cdd:cd14609  155 edFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDF-------RRKVNKCYRG---RSCPIIVHCSDGAGRT 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 34328899 1129 GVLILSELMIYCLEHNEK-VEVPMMLRLLREQRMFMIQTIAQYKF 1172
Cdd:cd14609  225 GTYILIDMVLNRMAKGVKeIDIAATLEHVRDQRPGMVRTKDQFEF 269
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 932-1179 4.31e-38

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: 142.86  E-value: 4.31e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  932 ENAERSRIREVVPYEENRVELIPTKEN-NTGYINASHIKVVvgGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTA 1010
Cdd:cd14630    2 ENRNKNRYGNIISYDHSRVRLQLLDGDpHSDYINANYIDGY--HRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1011 EEEGGRTKSHRYWPKlgskhSSATYGKFKVTTKFRTDSVCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFL 1090
Cdd:cd14630   80 LVEVGRVKCVRYWPD-----DTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1091 SYLEEIqsvrRHTNSMLEGtknrhpPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQY 1170
Cdd:cd14630  155 GFVRQV----KFLNPPDAG------PIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQY 224


                 ....*....
gi 34328899 1171 KFVYQVLIQ 1179
Cdd:cd14630  225 VFVHDAILE 233
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 949-1179 6.37e-37

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: 138.61  E-value: 6.37e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  949 RVELIPTKENNTG-YINASHIKVVVGGAewHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlg 1027
Cdd:cd14631    1 RVILQPVEDDPSSdYINANYIDGYQRPS--HYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1028 skhSSATYGKFKVTTKFRTDSVCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIqsvrRHTNSML 1107
Cdd:cd14631   77 ---DTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRV----KLSNPPS 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34328899 1108 EGtknrhpPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQ 1179
Cdd:cd14631  150 AG------PIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 903-1179 1.25e-36

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: 139.79  E-value: 1.25e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  903 KLEEGMVFTEYEQIPKKKANGIFSTAALPENAERSRIREVVPYEENRVELIPTK-ENNTGYINASHIKVVvgGAEWHYIA 981
Cdd:cd14633   10 KCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEgETSSDYINGNYIDGY--HRPNHYIA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  982 TQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgskhSSATYGKFKVTTKFRTDSVCYATTGLKVKHL 1061
Cdd:cd14633   88 TQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPD-----DTEIYKDIKVTLIETELLAEYVIRTFAVEKR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1062 LSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSvrrhtnsmleGTKNRHPPIVVHCSAGVGRTGVLILSELMIYCL 1141
Cdd:cd14633  163 GVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS----------KSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMA 232

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 34328899 1142 EHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQ 1179
Cdd:cd14633  233 EREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 959-1179 1.39e-36

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: 137.49  E-value: 1.39e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  959 NTGYINASHikvvvggAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgskhSSATYGKF 1038
Cdd:cd14632    3 NANYIDGYH-------RSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPD-----DSDTYGDI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1039 KVTTkFRTDSVC-YATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSvrrhtnsmleGTKNRHPPI 1117
Cdd:cd14632   71 KITL-LKTETLAeYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKA----------STPPDAGPV 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34328899 1118 VVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQ 1179
Cdd:cd14632  140 VVHCSAGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 962-1180 2.85e-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: 136.29  E-value: 2.85e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  962 YINASHIKvvvGGAEWHY-IATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGskhsSATYGkfKV 1040
Cdd:cd14622    2 YINASFID---GYRQKDYfIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEG----SVTHG--EI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1041 TTKFRTDSVCYATT--GLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVRRHTNSMlegtknrhpPIV 1118
Cdd:cd14622   73 TIEIKNDTLLETISirDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNH---------PIV 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34328899 1119 VHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQF 1180
Cdd:cd14622  144 VHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 104-220 8.09e-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: 126.23  E-value: 8.09e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899    104 PNVSWLQQEATRYQYYLQVKKDVLEGRLRCTLDQVIRLAGLAVQADFGDYNQFDSQ-DFLREYVLFPMDLaLEEAVLEEL 182
Cdd:pfam00373    1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTsEYLSLESFLPKQL-LRKMKSKEL 79

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 34328899    183 TQKVAQEHKAHSGILPAEAELMYINEVERLDGFGQEIF 220
Cdd:pfam00373   80 EKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1068-1179 8.36e-33

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 122.85  E-value: 8.36e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899    1068 TVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVRRHtnsmlegtKNRHPPIVVHCSAGVGRTGVLILSELMIYCLEH-NEK 1146
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQ--------SESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGE 72

                            90       100       110
                    ....*....|....*....|....*....|...
gi 34328899    1147 VEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQ 1179
Cdd:smart00404   73 VDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1068-1179 8.36e-33

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: 122.85  E-value: 8.36e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899    1068 TVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVRRHtnsmlegtKNRHPPIVVHCSAGVGRTGVLILSELMIYCLEH-NEK 1146
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQ--------SESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGE 72

                            90       100       110
                    ....*....|....*....|....*....|...
gi 34328899    1147 VEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQ 1179
Cdd:smart00012   73 VDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
929-1183 7.27e-32

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 126.36  E-value: 7.27e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  929 ALPENAERSRIREVVPYEENRVEliptkeNNTGYINASHIKVvvgGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMV 1008
Cdd:COG5599   38 QNINGSPLNRFRDIQPYKETALR------ANLGYLNANYIQV---IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVL 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1009 TAEEEGG--RTKSHRYWpklgskHSSATYGKFKVTTK------FRTDSVCYAttgLKVKHLLSGQE-RTVWHLQYTDWPD 1079
Cdd:COG5599  109 ASDDEISkpKVKMPVYF------RQDGEYGKYEVSSEltesiqLRDGIEART---YVLTIKGTGQKkIEIPVLHVKNWPD 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1080 HGCPEDVQgflsyLEEIQSVRRHTNSMLEGTKNrhpPIVVHCSAGVGRTGVLILselmIYCLE------HNEKVEVPMML 1153
Cdd:COG5599  180 HGAISAEA-----LKNLADLIDKKEKIKDPDKL---LPVVHCRAGVGRTGTLIA----CLALSksinalVQITLSVEEIV 247

                        250       260       270
                 ....*....|....*....|....*....|.
gi 34328899 1154 RLLREQR-MFMIQTIAQykfvYQVLIQFLQN 1183
Cdd:COG5599  248 IDMRTSRnGGMVQTSEQ----LDVLVKLAEQ 274
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 908-1177 1.39e-31

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 126.68  E-value: 1.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   908 MVFTEYEQIPKKKANGIFSTAALPENAERSRIREVVPYEENRVEL--------------------IPTKENNTGYINASH 967
Cdd:PHA02746   26 FVLLEHAEVMDIPIRGTTNHFLKKENLKKNRFHDIPCWDHSRVVInaheslkmfdvgdsdgkkieVTSEDNAENYIHANF 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   968 IKvvvGGAEWH-YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTaEEEGGRTKSHRYWPKlgSKHSSATYGKFKVTTKFRT 1046
Cdd:PHA02746  106 VD---GFKEANkFICAQGPKEDTSEDFFKLISEHESQVIVSLT-DIDDDDEKCFELWTK--EEDSELAFGRFVAKILDII 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  1047 DSVCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQSVRRHTNSMLEGTKNRHPPIVVHCSAGVG 1126
Cdd:PHA02746  180 EELSFTKTRLMITDKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAELIKQADNDPQTLGPIVVHCSAGIG 259

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 34328899  1127 RTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVL 1177
Cdd:PHA02746  260 RAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 215-305 1.07e-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: 113.15  E-value: 1.07e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  215 FGQEIFPVKDNHGNCVHLGIFFMGIFVRNRIGRQAVIYRWNDMGNITHNKSTILVELINKEETALFHTDDIENAKYISRL 294
Cdd:cd13188    1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRPPVFFRWEDIKNVINHKRTFSIECQNSEETVQFQFEDAETAKYVWKL 80

                         90
                 ....*....|.
gi 34328899  295 FATRHKFYKQN 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 2.55e-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: 2.55e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  114 TRYQYYLQVKKDVLEGRLRCTLDQVIRLAGLAVQADFGDYNQ-FDSQDFLREYVLFPMDLaLEEAVLEELTQKVAQEHKA 192
Cdd:cd14473    1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPsEHKPKYLSLKRFLPKQL-LKQRKPEEWEKRIVELHKK 79

                         90       100
                 ....*....|....*....|
gi 34328899  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 ...
 979-1175 5.22e-27

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: 109.80  E-value: 5.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  979 YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTkSHRYWPKlgskHSSATYGKFKVTTKFRTDSVCYATTGLKV 1058
Cdd:cd14556   16 FIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQS-CPQYWPD----EGSGTYGPIQVEFVSTTIDEDVISRIFRL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1059 KHLLSGQE--RTVWHLQYTDWPDHG-CPEDVQGFLSYLEEIQSVRRHTNsmlEGtknrhpPIVVHCSAGVGRTGVLILSE 1135
Cdd:cd14556   91 QNTTRPQEgyRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSG---EG------PIVVHCLNGVGRSGVFCAIS 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 34328899 1136 LMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQ 1175
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 2.02e-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: 2.02e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34328899     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 3.01e-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: 3.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   21 FVTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKfANEPLLFFGVM 100
Cdd:cd01765    1 ISCRVRLLDGTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFYEDNDGQKHWLDLDKKISKQLKR-SGPYQFYFRVK 79


                 .
gi 34328899  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 ...
 962-1175 2.50e-19

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: 87.38  E-value: 2.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  962 YINASHIKVVVGGAEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKShrYWPklgSKHSSATYGKFKVT 1041
Cdd:cd14550    1 YINASYLQGYRRSNE--FIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWP---TKEKPLECETFKVT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1042 TKFRTDSVCYATTGLKVKHLL--SGQER---TVWHLQYTDWPDHGCPedvqgFLSYLEEIQSVRRHTNSmlegtknRHPP 1116
Cdd:cd14550   74 LSGEDHSCLSNEIRLIVRDFIleSTQDDyvlEVRQFQCPSWPNPCSP-----IHTVFELINTVQEWAQQ-------RDGP 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34328899 1117 IVVH-----CSAGvgrTGVLiLSELMIYcLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQ 1175
Cdd:cd14550  142 IVVHdryggVQAA---TFCA-LTTLHQQ-LEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 962-1178 6.14e-19

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


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 86.66  E-value: 6.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  962 YINASHIKVVVGGAEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVtAEEEGGRTKSHRYWPklgSKHSSATYGKFKVT 1041
Cdd:cd17670    1 YINASYIMGYYRSNE--FIITQHPLPHTTKDFWRMIWDHNAQIIVML-PDNQGLAEDEFVYWP---SREESMNCEAFTVT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1042 TkFRTDSVCYATTGLKVKH---LLSGQERTVW---HLQYTDWPDHGCPedvqgflsyleeIQSVRRHTNSMLEGTKNRHP 1115
Cdd:cd17670   75 L-ISKDRLCLSNEEQIIIHdfiLEATQDDYVLevrHFQCPKWPNPDAP------------ISSTFELINVIKEEALTRDG 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34328899 1116 PIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLI 1178
Cdd:cd17670  142 PTIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 962-1179 2.12e-16

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: 79.29  E-value: 2.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  962 YINA----SHIKVVVggaewhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTaeEEGGRTKSHRYWPklgsKHSSATYGK 1037
Cdd:cd14634    1 YINAalmdSHKQPAA------FIVTQHPLPNTVADFWRLVFDYNCSSVVMLN--EMDAAQLCMQYWP----EKTSCCYGP 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1038 FKV---TTKFRTDSVcyaTTGLKVKHLLSGQE--RTVWHLQYTDWPDH-GCPEDVQGFLsyleeiQSVRRhTNSMLEGTK 1111
Cdd:cd14634   69 IQVefvSADIDEDII---SRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSIL------KVVRR-LEKWQEQYD 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34328899 1112 NRHPPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQ 1179
Cdd:cd14634  139 GREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 962-1178 5.64e-16

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: 77.73  E-value: 5.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  962 YINASHIKVVVGGAEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVT-----AEEEggrtksHRYWPklgSKHSSATYG 1036
Cdd:cd17669    1 YINASYIMGYYQSNE--FIITQHPLLHTIKDFWRMIWDHNAQLIVMLPdgqnmAEDE------FVYWP---NKDEPINCE 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1037 KFKVTTkFRTDSVCYAT-TGLKVKHLL--SGQERTVW---HLQYTDWPDHGCPedvqgflsyleeIQSVRRHTNSMLEGT 1110
Cdd:cd17669   70 TFKVTL-IAEEHKCLSNeEKLIIQDFIleATQDDYVLevrHFQCPKWPNPDSP------------ISKTFELISIIKEEA 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34328899 1111 KNRHPPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLI 1178
Cdd:cd17669  137 ANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 962-1179 7.83e-15

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: 74.56  E-value: 7.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  962 YINASHIKVVVGGAEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRT-KSHRYWPKLGSKHS--------S 1032
Cdd:cd14637    1 YINAALTDSYTRSAA--FIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYgpmevefvS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1033 ATYGKFKVTTKFRTDSVcyatTGLKVKHLLsgqertVWHLQYTDW-PDHGCPEDVQGFLSYLEEIQSVRRhtnsmlegtK 1111
Cdd:cd14637   79 GSADEDIVTRLFRVQNI----TRLQEGHLM------VRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQR---------E 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34328899 1112 NRHPPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQ 1179
Cdd:cd14637  140 SGEGRTVVHCLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 976-1182 1.20e-14

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 76.16  E-value: 1.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   976 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEggRTKSHRYWpklgskhsSATYGKFKVTTKFRTDSVCYATTG 1055
Cdd:PHA02740   90 EQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHAD--KKCFNQFW--------SLKEGCVITSDKFQIETLEIIIKP 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  1056 LKVKHLLS-----GQERTVWHLQYTDWPDHGCPEDVQGFLSYLEEIQS----VRRHTnsmlegTKNRHPPIVVHCSAGVG 1126
Cdd:PHA02740  160 HFNLTLLSltdkfGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDlcadLEKHK------ADGKIAPIIIDCIDGIS 233

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 34328899  1127 RTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQFLQ 1182
Cdd:PHA02740  234 SSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLK 289
FERM_F1_EPB41L4A cd17107
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 21-103 2.54e-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: 69.68  E-value: 2.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   21 FVTRIRLLDSNviECTLSVE------STGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKFANEPL 94
Cdd:cd17107    3 FYCEIVLLDES--ELILTIQqdgiksSKGSVVLDVVFQHLNLLETDYFGLRYIDRQHQTHWLDPAKTLSEQLKLIGPPYT 80


                 ....*....
gi 34328899   95 LFFGVMFYV 103
Cdd:cd17107   81 LYFGVKFYA 89
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 963-1171 2.16e-13

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: 70.89  E-value: 2.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  963 INASHIKVvvgGAEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWpklgskHSSATYGKFKVTT 1042
Cdd:cd14559   18 LNANRVQI---GNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYF------RQSGTYGSVTVKS 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1043 KfRTDSVcYATTGLKVKHL---LSGQERT----VWHLqyTDWPDHGcPEDVQGFLSYLEEIQSVRRHTNSMLEGT----- 1110
Cdd:cd14559   89 K-KTGKD-ELVDGLKADMYnlkITDGNKTitipVVHV--TNWPDHT-AISSEGLKELADLVNKSAEEKRNFYKSKgssai 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34328899 1111 --KNRHPPiVVHCSAGVGRTGVLILSELMIyclEHNEKVEVPMMLRLLREQR-MFMIQTIAQYK 1171
Cdd:cd14559  164 ndKNKLLP-VIHCRAGVGRTGQLAAAMELN---KSPNNLSVEDIVSDMRTSRnGKMVQKDEQLD 223
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 979-1179 3.35e-13

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: 69.72  E-value: 3.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  979 YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKshRYWPKLGSKHSSATYGKFkVTTKFRTDSVcyaTTGLKV 1058
Cdd:cd14635   16 FIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQLCP--QYWPENGVHRHGPIQVEF-VSADLEEDII---SRIFRI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1059 KHLLSGQE--RTVWHLQYTDWPDH-GCPEDVQGFLSYLEEIQSVRRHtnsmLEGTKNRhppIVVHCSAGVGRTGVLILSE 1135
Cdd:cd14635   90 YNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEE----YNGGEGR---TVVHCLNGGGRSGTFCAIS 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 34328899 1136 LMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQ 1179
Cdd:cd14635  163 IVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 962-1179 5.83e-13

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: 69.28  E-value: 5.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  962 YINASHIKVVVGGAEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTaeEEGGRTKSHRYWPKLGSkhssATYGKFKVT 1041
Cdd:cd14636    1 YINAALMDSYRQPAA--FIVTQHPLPNTVKDFWRLVYDYGCTSIVMLN--EVDLAQGCPQYWPEEGM----LRYGPIQVE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1042 TKFRTDSVCYATTGLKVKHLLSGQE--RTVWHLQYTDWPDH-GCPEDVQGFLSYLEEIQSVRRHTNsmlEGTKNrhppIV 1118
Cdd:cd14636   73 CMSCSMDCDVISRIFRICNLTRPQEgyLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECD---EGEGR----TI 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34328899 1119 VHCSAGVGRTGVLILSELMIYCLEHNEKVEVPMMLRLLREQRMFMIQTIAQYKFVYQVLIQ 1179
Cdd:cd14636  146 IHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
FERM_F1_FRMD3 cd17102
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 21-102 1.36e-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: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   21 FVTRIRLL-DSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLdKFANEPLLFFGV 99
Cdd:cd17102    1 YKCTIRLLdDSEVICCEFKKDTKGQFLLDYVCNYLNLLEKDYFGLRYVDTEKQRHWLDPNKSIYKQL-KGVPPYVLCFRV 79


                 ...
gi 34328899  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 3.63e-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: 3.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   19 NCFVTrirLLDSnvIECTLSVE--STGQECLEAVAQRLELRETHYFGLWFLSKS---QQARWVELEKPLKKHLdKFANEP 93
Cdd:cd17100    3 RCIVH---FLDD--TEQTFEVEkrDKGQVLLDKVFNHLELVEKDYFGLQFSDDSpatDSMRWLDPLKPIRKQI-KGGPPY 76

                         90
                 ....*....|
gi 34328899   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 1.02e-10

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: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLdKFANEPLLFFGVMFYV 103
Cdd:cd17098    4 KVQMLDDTVHIFQVQQKALGEVLFDQVCKHLNLLESDYFGLEFTDPEGNKCWLDPEKPILRQV-KRPKDVVFKFVVKFYT 82


                 ..
gi 34328899  104 PN 105
Cdd:cd17098   83 PD 84
FERM_C pfam09380
FERM C-terminal PH-like domain;
224-306 1.25e-10

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 58.80  E-value: 1.25e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899    224 DNHGNCVHLGIFFMGIFVRNRIGRQAVIYRWNDMGNITHNKSTILVELINK--EETALFHTDDIENAKYISRLFATRHKF 301
Cdd:pfam09380    1 DKEGTDLWLGVSAKGILVYEDNNKILNLFPWREIRKISFKRKKFLIKLRDKssEETLGFYTESSRACKYLWKLCVEQHTF 80


                   ....*
gi 34328899    302 YKQNK 306
Cdd:pfam09380   81 FRLRR 85
FERM_F1_MYLIP cd17104
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in E3 ...
 20-87 2.10e-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: 2.10e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34328899   20 CFVTRirlLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLD 87
Cdd:cd17104    3 CLVSQ---PDSVVIEVEVDPKANGQECLDKVCQKLGIIEKDYFGLQYTGPKGERLWLNLRNRISRQLP 67
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 34328899   24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLdkfANEPLLF-FGVMFY 102
Cdd:cd17202    5 KVTLLDGTEYSCDLEKRAKGQVLFDKVCEHLNLLEKDYFGLLYQVSANQKNWLDSTKEIKRQI---RRLPWLFtFNVKFY 81


                 ...
gi 34328899  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 6.03e-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: 6.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   21 FVTRIRLLDSNViECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKFANEPLLFFGVM 100
Cdd:cd17097    1 INVRVTTMDAEL-EFSIKPKAKGRELFDLVCRTIGLRETWYFGLQYENKKGRVAWLKPDKKVLTQDVSKNNTLKFFFLVK 79


                 ..
gi 34328899  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 6.93e-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: 6.93e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34328899   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 1.17e-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: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLdkfANEPLLF-FGVMFY 102
Cdd:cd17106    5 KVLLLDGTEYTCEVEKRAKGQVLFDKVCEHLNLLEKDYFGLTYRDAQDQKNWLDPAKEIKKQI---RSGPWLFsFNVKFY 81


                 ...
gi 34328899  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 2.50e-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: 2.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLdkfANEPLLF-FGVMFY 102
Cdd:cd17201    5 KVTLLDGSEYECEVEKHARGQVLFDTVCEHLNLLEKDYFGLTFCDTESQKNWLDPSKEIKKQI---RSGPWHFaFTVKFY 81


                 ...
gi 34328899  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 3.52e-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: 51.58  E-value: 3.52e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34328899   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 3.67e-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: 3.67e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34328899   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 4.34e-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: 4.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKFANEplLFFGVMFYV 103
Cdd:cd17105    4 KVSLLDDTVYECEVEKHAKGQDLFKKVCEHLNLLEEDYFGLAIWDSPTSKTWLDPAKEIKKQVHGGPWE--FTFNVKFYP 81


                 ..
gi 34328899  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 34328899   24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKH-LDKFANEPLLFFGVMFY 102
Cdd:cd17200    6 QVHLLDDRKLELLVQPKLLSRELLDLVASHFNLKEKEYFGITFIDDTGQSNWLQLDHRVLDHdLPKKSGPVTLYFAVRFY 85


                 ....
gi 34328899  103 VPNV 106
Cdd:cd17200   86 IESI 89
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1082-1175 2.66e-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: 2.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1082 CPEDVQGFLSYLEEiqsvrrhtnsmlegTKNRHPPIVVHCSAGVGRTGVLILSELMIYcleHNEKVEVpmMLRLLREQRM 1161
Cdd:cd14494   38 TLAMVDRFLEVLDQ--------------AEKPGEPVLVHCKAGVGRTGTLVACYLVLL---GGMSAEE--AVRIVRLIRP 98

                         90
                 ....*....|....*
gi 34328899 1162 FMI-QTIAQYKFVYQ 1175
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 34328899   23 TRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHL--DKFANEPL-LFFGV 99
Cdd:cd17103    5 CQVVLLDDRRLEILVQPKLLAGDLLDLVASHFNLKEKEYFGLAYEDETGHYNWLQLDKRVLDHEfpKKWSSGPLvLHFAV 84


                 ....*..
gi 34328899  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 34328899   24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKFANEplLFFGVMFYV 103
Cdd:cd17203    5 KVTLLDGSEYTCEVEKRSKGQVLFDKVCEHLNLLEKDYFGLTYRDSENQKNWLDPAKEIKKQIRSGAWQ--FSFNVKFYP 82


                 ..
gi 34328899  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 34328899   22 VTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQA-RWVELEKPLKKHLdKFANEPLLFFGVM 100
Cdd:cd17194    3 VCNILLLDNTVQAFKVNKHDQGQVLLDLVFKHLDLTERDYFGLQLADDSTDNpRWLDPNKPIRKQL-KRGSPHNLNFRVK 81


                 ...
gi 34328899  101 FYV 103
Cdd:cd17194   82 FFV 84
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1078-1175 2.00e-06

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: 49.18  E-value: 2.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1078 PDHGCPEDVQGFLSYLEEIQSVrrhtnsmLEGTKNrhppIVVHCSAGVGRTGvLILSELMiycLEHNEKVEVPMMLRLLR 1157
Cdd:cd14505   81 PDGGVPSDIAQWQELLEELLSA-------LENGKK----VLIHCKGGLGRTG-LIAACLL---LELGDTLDPEQAIAAVR 145

                         90
                 ....*....|....*...
gi 34328899 1158 EQRMFMIQTIAQYKFVYQ 1175
Cdd:cd14505  146 ALRPGAIQTPKQENFLHQ 163
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 4.97e-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: 46.23  E-value: 4.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899  201 AELMYINEVERLDGFGQEIFPVKDNHGNCVHLGIFFMGIFVRnRIGRQAVIYRWNDMGNITHNKSTILVELINKEE---T 277
Cdd:cd13192    1 AEDNFLRKAATLETYGVDPHPVKDHRGNQLYLGFTHTGIVTF-QGGKRVHHFRWNDITKFNYEGKMFILHVMQKEEkkhT 79

                         90       100
                 ....*....|....*....|....*.
gi 34328899  278 ALFHTDDIENAKYISRLFATRHKFYK 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 5.75e-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: 5.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   20 CFVTRIRLLDSNvIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHlDKFANEPLLF-FG 98
Cdd:cd17186    2 TFTVRIVTMDAE-MEFNCEMKWKGKDLFDLVCRTIGLRETWYFGLQYTDSKGTVAWLKMDKKVLDQ-DVPKEEPVTFhFL 79


                 ....
gi 34328899   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 5.91e-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: 5.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   25 IRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLsKSQQARWVELEKPL--------KKHLDKFANEP--- 93
Cdd:cd17101    6 VVLLNGQRLQVAVDVKTTVQDLFDQVCDHLGLQETELFGLAVL-KDGEYFFLDPDTKLskyapkgwKSEAKKGLKGGkpv 84

                         90
                 ....*....|...
gi 34328899   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 9.82e-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: 44.78  E-value: 9.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKFANEpLLFFGVMFYV 103
Cdd:cd17190    4 RVKLLDNTTEPLEIEPKADGQALLSQVFKRLNLVESDYFGLEFQNSQSNWIWLEPMKLIVKQVRRPKNT-KLRLAVKFFP 82


                 ..
gi 34328899  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 1.27e-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: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   33 IECTLSVESTGQECLEAVAQRLELRETHYFGLwFLSKSQQARWVELEKPLKKHL------------DKFANEPLLFFGVM 100
Cdd:cd17197   14 LSLTVGVKATGQELFQQVCELLKIKEAHFFGL-SVVKNNEHIFMDLEQKLSKYFpkewkketgkgtEKFSIPFVACFRVQ 92


                 ....*
gi 34328899  101 FYVPN 105
Cdd:cd17197   93 YYVEN 97
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1077-1175 2.77e-05

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 45.35  E-value: 2.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1077 WPDHGCPEDvqgflsylEEIQSVRRHTNSMLEGTKnrhpPIVVHCSAGVGRTGVLILSELMIYCLEHNEKVEvpmmlrLL 1156
Cdd:COG2453   55 IPDFGAPDD--------EQLQEAVDFIDEALREGK----KVLVHCRGGIGRTGTVAAAYLVLLGLSAEEALA------RV 116

                         90
                 ....*....|....*....
gi 34328899 1157 REQRMFMIQTIAQYKFVYQ 1175
Cdd:COG2453  117 RAARPGAVETPAQRAFLER 135
FERM_F1_PTPN3 cd17193
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 22-103 3.21e-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: 43.30  E-value: 3.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   22 VTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQA-RWVELEKPLKKHLdKFANEPLLFFGVM 100
Cdd:cd17193    3 ICNVHFLDGSVQSFKVNKQDTGQVLLDMAYNHLGLTEREYFGLQHNEDSVDSpRWLEPSKPIRKQL-KGGFPCSLHFRVR 81


                 ...
gi 34328899  101 FYV 103
Cdd:cd17193   82 FFI 84
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1077-1173 5.29e-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: 45.80  E-value: 5.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1077 WPDHGCPedvqgflSYLEEIQSVRRHTNSMLEGTKnrhppIVVHCSAGVGRTGVLILSELMIYClehneKVEVPMMLRLL 1156
Cdd:cd14506   84 WKDYGVP-------SLTTILDIVKVMAFALQEGGK-----VAVHCHAGLGRTGVLIACYLVYAL-----RMSADQAIRLV 146

                         90
                 ....*....|....*..
gi 34328899 1157 REQRMFMIQTIAQYKFV 1173
Cdd:cd14506  147 RSKRPNSIQTRGQVLCV 163
FERM_F1_FRMD4A cd17199
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 24-106 5.60e-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: 5.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKH-LDKFANEPLLFFGVMFY 102
Cdd:cd17199    6 QVHLLDDRKLELLVQPKLLAKELLDLVASHFNLKEKEYFGIAFTDETGHLNWLQLDRRVLEHdFPKKSGPVVLYFCVRFY 85


                 ....
gi 34328899  103 VPNV 106
Cdd:cd17199   86 IESI 89
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 1086-1160 2.10e-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: 42.25  E-value: 2.10e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34328899   1086 VQGFLSYLEEIQSVRRHTNSMLEGTKNRHPPIVVHCSAGVGRTGVLILSELMIYclehnEKVEVPMMLRLLREQR 1160
Cdd:pfam00782   41 IPVEDNHETNISKYLEEAVEFIDDARQKGGKVLVHCQAGISRSATLIIAYLMKT-----RNLSLNEAYSFVKERR 110
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1078-1175 3.60e-04

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 41.88  E-value: 3.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1078 PDHGCP--EDVQGFLSYLEEiqsvrrhtnsmlEGTKNRhpPIVVHCSAGVGRTGvLILSELMIYClEHNEKVEVpmmLRL 1155
Cdd:cd14504   58 EDYTPPtlEQIDEFLDIVEE------------ANAKNE--AVLVHCLAGKGRTG-TMLACYLVKT-GKISAVDA---INE 118

                         90       100
                 ....*....|....*....|
gi 34328899 1156 LREQRMFMIQTIAQYKFVYQ 1175
Cdd:cd14504  119 IRRIRPGSIETSEQEKFVIQ 138
FERM_F1_FARP1 cd17189
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 24-105 3.75e-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: 3.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   24 RIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKfANEPLLFFGVMFYV 103
Cdd:cd17189    4 KVQMLDDTQEVFEVPQRAPGKVLLDAVCSHLNLVEGDYFGLEFQDHRKVMVWLDLLKPIVKQIRR-PKHVVLRFVVKFFP 82


                 ..
gi 34328899  104 PN 105
Cdd:cd17189   83 PD 84
FERM_F1_FRMD7 cd17188
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 24-105 4.31e-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: 40.18  E-value: 4.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   24 RIRLLDSNviECTLSVE--STGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLdKFANEPLLFFGVMF 101
Cdd:cd17188    5 KVQFLDDS--QKVFVVDqkSTGKDLFNMSCSHLNLVEKEYFGLEFRNHAGNNVWLELLKPITKQI-KNPKELIFKFTVKF 81


                 ....
gi 34328899  102 YVPN 105
Cdd:cd17188   82 FPVD 85
FERM_F1_Moesin cd17237
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in moesin and ...
 24-102 1.48e-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: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   24 RIRLLDSNvIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHlDKFANEPLLF-FGVMFY 102
Cdd:cd17237    5 RVTTMDAE-LEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQ-DVRKESPLLFkFRAKFY 82
FERM_F1_ERM cd17187
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 24-102 2.31e-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: 2.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899   24 RIRLLDSNvIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHlDKFANEPLLF-FGVMFY 102
Cdd:cd17187    4 RVTTMDAE-LEFAIQPNTTGKQLFDQVVKTIGLREIWFFGLQYVDSKGYSTWLKLNKKVLSQ-DVKKENPLQFkFRAKFY 81
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 1078-1132 2.47e-03

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


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 40.13  E-value: 2.47e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 34328899 1078 PDHGCPED--VQGFLSYLEEIQSVrrhtnsmlegtknrhppIVVHCSAGVGRTGVLI 1132
Cdd:cd14499   88 PDGSTPSDdiVKKFLDICENEKGA-----------------IAVHCKAGLGRTGTLI 127
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
1084-1160 3.93e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 38.80  E-value: 3.93e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34328899    1084 EDVQGFLSYLEEiqsvrrhTNSMLEGTKNRHPPIVVHCSAGVGRTGVLILSELMIYclehnEKVEVPMMLRLLREQR 1160
Cdd:smart00195   55 NTETKISPYFPE-------AVEFIEDAESKGGKVLVHCQAGVSRSATLIIAYLMKT-----RNMSLNDAYDFVKDRR 119
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 1077-1161 4.29e-03

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins; Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity.


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 39.10  E-value: 4.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328899 1077 WPDHGCPEdvqgfLSYLEEIqsVRRHTNSMLEGTKNrhpPIVVHCSAGVGRTGVLILSeLMIYCLEHNEKVEVpmmLRLL 1156
Cdd:cd14497   68 FPDHHPPP-----LGLLLEI--VDDIDSWLSEDPNN---VAVVHCKAGKGRTGTVICA-YLLYYGQYSTADEA---LEYF 133


                 ....*
gi 34328899 1157 REQRM 1161
Cdd:cd14497  134 AKKRF 138
 
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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