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Conserved domains on  [gi|767979565|ref|XP_011534669|]
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tyrosine-protein phosphatase non-receptor type 21 isoform X1 [Homo sapiens]

Protein Classification

FERM_F1_PTPN21 and FERM_B-lobe domain-containing protein( domain architecture ID 13020114)

protein containing domains FERM_F1_PTPN21, FERM_B-lobe, FERM_C_PTPN14_PTPN21, and PTP_DSP_cys

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 883-1169 0e+00

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.


The actual alignment was detected with superfamily member cd14599:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 287  Bit Score: 540.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  883 RCKILEQRLEQGMVFTEYERILKKRlVDGECSTARLPENAERNRFQDVLPYDDVRVELVPTKENNTGYINASHIKVSVSG 962
Cdd:cd14599     1 RCKTLERKLEEGMVFTEYEQIPKKK-ADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  963 IEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVTYGRFKITTRFRTDSGCYATT 1042
Cdd:cd14599    80 EEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1043 GLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTSD-PQSPNPPLLVHCSAGVGRTGVVILS 1121
Cdd:cd14599   160 GLKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDsTKNCNPPIVVHCSAGVGRTGVVILT 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 767979565 1122 EIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQFLK 1169
Cdd:cd14599   240 ELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
FERM_F1_PTPN21 cd17192
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 20-106 8.63e-60

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: 199.09  E-value: 8.63e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   20 KSCLVARIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQLDKYALEPTVYF 99
Cdd:cd17192     1 KSCLVARIQLLNNEFVEFTLSVESTGQECLEAVAQRLELREITYFSLWYYNKQNQQRWVDLEKPLKKQLDKYALEPTVYF 80


                  ....*..
gi 767979565  100 GVVFYVP 106
Cdd:cd17192    81 GVVFYVP 87
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 24-222 1.37e-53

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: 185.96  E-value: 1.37e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565     24 VARIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQ-RRWVDLEKPLKKQLDKYaLEPTVYFGVV 102
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDlRHWLDPAKTLLDQDVKS-EPLTLYFRVK 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565    103 FYVPSVSQLQQEITRY-QYYLQLKKDILEGSIPCTLEQAIQLAGLAVQADFGDFDQYES--QDFLQKFALFPVGWLQDEK 179
Cdd:smart00295   80 FYPPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdlRGELSLKRFLPKQLLDSRK 159

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|...
gi 767979565    180 vLEEATQKVALLHQKYRGLTAPDAEMLYMQEVERMDGYGEESY 222
Cdd:smart00295  160 -LKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 217-307 7.65e-53

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: 179.41  E-value: 7.65e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  217 YGEESYPAKDSQGSDISIGACLEGIFVKHKNGRHPVVFRWHDIANMSHNKSFFALELANKEETIQFQTEDMETAKYIWRL 296
Cdd:cd13188     1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRPPVFFRWEDIKNVINHKRTFSIECQNSEETVQFQFEDAETAKYVWKL 80

                          90
                  ....*....|.
gi 767979565  297 CVARHKFYRLN 307
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 ...
 883-1169 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: 540.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  883 RCKILEQRLEQGMVFTEYERILKKRlVDGECSTARLPENAERNRFQDVLPYDDVRVELVPTKENNTGYINASHIKVSVSG 962
Cdd:cd14599     1 RCKTLERKLEEGMVFTEYEQIPKKK-ADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  963 IEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVTYGRFKITTRFRTDSGCYATT 1042
Cdd:cd14599    80 EEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1043 GLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTSD-PQSPNPPLLVHCSAGVGRTGVVILS 1121
Cdd:cd14599   160 GLKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDsTKNCNPPIVVHCSAGVGRTGVVILT 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 767979565 1122 EIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQFLK 1169
Cdd:cd14599   240 ELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
896-1166 4.08e-99

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 314.98  E-value: 4.08e-99
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565    896 VFTEYERILKKRLVDGECSTARLPENAERNRFQDVLPYDDVRVELVPTKENNTGYINASHIKVSVSgiEWDYIATQGPLQ 975
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNG--PKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565    976 NTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRhnTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQER 1055
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGE--PLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETR 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   1056 TVWHLQYTDWPEHGCPEDLKGFLSYLEEIqsvrRHTNSTSDPqspnpPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLD 1135
Cdd:smart00194  158 TVTHYHYTNWPDHGVPESPESILDLIRAV----RKSQSTSTG-----PIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVD 228

                           250       260       270
                    ....*....|....*....|....*....|.
gi 767979565   1136 IPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1166
Cdd:smart00194  229 IFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
921-1166 6.51e-91

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 291.84  E-value: 6.51e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   921 NAERNRFQDVLPYDDVRVELVPTKENNtGYINASHIKVSvsGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEE 1000
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPS-DYINASYIDGY--KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  1001 EGGREKSFRYWPRlgSRHNTVTYGRFKITTR-FRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLS 1079
Cdd:pfam00102   78 EKGREKCAQYWPE--EEGESLEYGDFTVTLKkEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLD 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  1080 YLEEIQSVRrhtnstsdPQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTF 1159
Cdd:pfam00102  156 LLRKVRKSS--------LDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIF 227


                   ....*..
gi 767979565  1160 VYRVLIQ 1166
Cdd:pfam00102  228 LYDAILE 234
FERM_F1_PTPN21 cd17192
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 20-106 8.63e-60

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: 199.09  E-value: 8.63e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   20 KSCLVARIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQLDKYALEPTVYF 99
Cdd:cd17192     1 KSCLVARIQLLNNEFVEFTLSVESTGQECLEAVAQRLELREITYFSLWYYNKQNQQRWVDLEKPLKKQLDKYALEPTVYF 80


                  ....*..
gi 767979565  100 GVVFYVP 106
Cdd:cd17192    81 GVVFYVP 87
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 24-222 1.37e-53

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: 185.96  E-value: 1.37e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565     24 VARIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQ-RRWVDLEKPLKKQLDKYaLEPTVYFGVV 102
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDlRHWLDPAKTLLDQDVKS-EPLTLYFRVK 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565    103 FYVPSVSQLQQEITRY-QYYLQLKKDILEGSIPCTLEQAIQLAGLAVQADFGDFDQYES--QDFLQKFALFPVGWLQDEK 179
Cdd:smart00295   80 FYPPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdlRGELSLKRFLPKQLLDSRK 159

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|...
gi 767979565    180 vLEEATQKVALLHQKYRGLTAPDAEMLYMQEVERMDGYGEESY 222
Cdd:smart00295  160 -LKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 217-307 7.65e-53

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: 179.41  E-value: 7.65e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  217 YGEESYPAKDSQGSDISIGACLEGIFVKHKNGRHPVVFRWHDIANMSHNKSFFALELANKEETIQFQTEDMETAKYIWRL 296
Cdd:cd13188     1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRPPVFFRWEDIKNVINHKRTFSIECQNSEETVQFQFEDAETAKYVWKL 80

                          90
                  ....*....|.
gi 767979565  297 CVARHKFYRLN 307
Cdd:cd13188    81 CVLQHKFYRQN 91
PHA02738 PHA02738
hypothetical protein; Provisional
 899-1171 4.97e-50

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 180.12  E-value: 4.97e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  899 EYERILKKRlVDGECSTARlpENAERNRFQDVLPYDDVRVELvPTKENNTGYINASHikvsVSGIEWD--YIATQGPLQN 976
Cdd:PHA02738   30 EHQKVISEK-VDGTFNAEK--KNRKLNRYLDAVCFDHSRVIL-PAERNRGDYINANY----VDGFEYKkkFICGQAPTRQ 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  977 TCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLgsRHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLlTGQERT 1056
Cdd:PHA02738  102 TCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDV--EQGSIRFGKFKITTTQVETHPHYVKSTLLLTDG-TSATQT 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1057 VWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRR--HTNS--TSDPQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNE 1132
Cdd:PHA02738  179 VTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCQKelAQESlqIGHNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACA 258

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767979565 1133 VLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQFLKSS 1171
Cdd:PHA02738  259 TVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVNLT 297
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
919-1166 8.57e-31

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 123.28  E-value: 8.57e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  919 PENAERNRFQDVLPYDDVRVElvptkeNNTGYINASHIKVsvsGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTA 998
Cdd:COG5599    40 INGSPLNRFRDIQPYKETALR------ANLGYLNANYIQV---IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLAS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  999 EEEGG--REKSFRYWPRLGSrhntvtYGRFKI------TTRFRTDSGCYATTgLKMKHllTGQE-RTVWHLQYTDWPEHG 1069
Cdd:COG5599   111 DDEISkpKVKMPVYFRQDGE------YGKYEVsselteSIQLRDGIEARTYV-LTIKG--TGQKkIEIPVLHVKNWPDHG 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1070 CPEDlkgflSYLEEIQSVRRHTNSTSDPqsPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDI---PRVLDMLRQQ 1146
Cdd:COG5599   182 AISA-----EALKNLADLIDKKEKIKDP--DKLLPVVHCRAGVGRTGTLIACLALSKSINALVQITLsveEIVIDMRTSR 254

                         250       260
                  ....*....|....*....|
gi 767979565 1147 RMMLVQTLCQYTFVYRVLIQ 1166
Cdd:COG5599   255 NGGMVQTSEQLDVLVKLAEQ 274
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 106-220 1.09e-29

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 114.29  E-value: 1.09e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   106 PSVSQLQQEITRYQYYLQLKKDILEGSIPCTLEQAIQLAGLAVQADFGDFDQYESQ-DFLQKFALFPVgWLQDEKVLEEA 184
Cdd:pfam00373    1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTsEYLSLESFLPK-QLLRKMKSKEL 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 767979565   185 TQKVALLHQKYRGLTAPDAEMLYMQEVERMDGYGEE 220
Cdd:pfam00373   80 EKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVE 115
FERM_C pfam09380
FERM C-terminal PH-like domain;
226-308 2.44e-27

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 106.18  E-value: 2.44e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   226 DSQGSDISIGACLEGIFVKHKNGRHPVVFRWHDIANMSHNKSFFALELANK--EETIQFQTEDMETAKYIWRLCVARHKF 303
Cdd:pfam09380    1 DKEGTDLWLGVSAKGILVYEDNNKILNLFPWREIRKISFKRKKFLIKLRDKssEETLGFYTESSRACKYLWKLCVEQHTF 80


                   ....*
gi 767979565   304 YRLNQ 308
Cdd:pfam09380   81 FRLRR 85
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 116-214 6.47e-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: 105.79  E-value: 6.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  116 TRYQYYLQLKKDILEGSIPCTLEQAIQLAGLAVQADFGDFDQYESQD-FLQKFALFPVgWLQDEKVLEEATQKVALLHQK 194
Cdd:cd14473     1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPkYLSLKRFLPK-QLLKQRKPEEWEKRIVELHKK 79

                          90       100
                  ....*....|....*....|
gi 767979565  195 YRGLTAPDAEMLYMQEVERM 214
Cdd:cd14473    80 LRGLSPAEAKLKYLKIARKL 99
FERM_N pfam09379
FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the ...
 27-89 6.63e-18

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: 78.79  E-value: 6.63e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767979565    27 IQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQLD 89
Cdd:pfam09379    1 VRLLDGTVLEFDVQPKATGQVLLDQVCNHLNLKEKDYFGLQFLDDNGEHRWLDLSKRLSKQAP 63
 
Name Accession Description Interval E-value
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 883-1169 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: 540.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  883 RCKILEQRLEQGMVFTEYERILKKRlVDGECSTARLPENAERNRFQDVLPYDDVRVELVPTKENNTGYINASHIKVSVSG 962
Cdd:cd14599     1 RCKTLERKLEEGMVFTEYEQIPKKK-ADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  963 IEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVTYGRFKITTRFRTDSGCYATT 1042
Cdd:cd14599    80 EEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1043 GLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTSD-PQSPNPPLLVHCSAGVGRTGVVILS 1121
Cdd:cd14599   160 GLKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDsTKNCNPPIVVHCSAGVGRTGVVILT 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 767979565 1122 EIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQFLK 1169
Cdd:cd14599   240 ELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 950-1169 3.64e-177

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: 518.76  E-value: 3.64e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  950 YINASHIKVSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVTYGRFKIT 1029
Cdd:cd14598     1 YINASHIKVTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVTYGRFKIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1030 TRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTSDPQSPNPPLLVHCS 1109
Cdd:cd14598    81 TRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTIDPKSPNPPVLVHCS 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1110 AGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQFLK 1169
Cdd:cd14598   161 AGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 950-1168 1.24e-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: 426.10  E-value: 1.24e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  950 YINASHIKVSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVTYGRFKIT 1029
Cdd:cd14540     1 YINASHITATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHDALTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1030 TRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTSDPQSPNPPLLVHCS 1109
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQDVAGHNRNPPTLVHCS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767979565 1110 AGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQFL 1168
Cdd:cd14540   161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
896-1166 4.08e-99

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 314.98  E-value: 4.08e-99
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565    896 VFTEYERILKKRLVDGECSTARLPENAERNRFQDVLPYDDVRVELVPTKENNTGYINASHIKVSVSgiEWDYIATQGPLQ 975
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNG--PKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565    976 NTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRhnTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQER 1055
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGE--PLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETR 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   1056 TVWHLQYTDWPEHGCPEDLKGFLSYLEEIqsvrRHTNSTSDPqspnpPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLD 1135
Cdd:smart00194  158 TVTHYHYTNWPDHGVPESPESILDLIRAV----RKSQSTSTG-----PIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVD 228

                           250       260       270
                    ....*....|....*....|....*....|.
gi 767979565   1136 IPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1166
Cdd:smart00194  229 IFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
921-1166 6.51e-91

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 291.84  E-value: 6.51e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   921 NAERNRFQDVLPYDDVRVELVPTKENNtGYINASHIKVSvsGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEE 1000
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPS-DYINASYIDGY--KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  1001 EGGREKSFRYWPRlgSRHNTVTYGRFKITTR-FRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLS 1079
Cdd:pfam00102   78 EKGREKCAQYWPE--EEGESLEYGDFTVTLKkEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLD 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  1080 YLEEIQSVRrhtnstsdPQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTF 1159
Cdd:pfam00102  156 LLRKVRKSS--------LDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIF 227


                   ....*..
gi 767979565  1160 VYRVLIQ 1166
Cdd:pfam00102  228 LYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 950-1162 1.80e-75

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: 247.97  E-value: 1.80e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  950 YINASHIKVSvsGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSrhNTVTYGRFKIT 1029
Cdd:cd00047     1 YINASYIDGY--RGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGG--KPLEYGDITVT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1030 TRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHtnstsdpqsPNPPLLVHCS 1109
Cdd:cd00047    77 LVSEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARK---------PNGPIVVHCS 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767979565 1110 AGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYR 1162
Cdd:cd00047   148 AGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 881-1160 1.32e-68

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: 231.66  E-value: 1.32e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  881 DERCKILEQRLEQGMVFTEYERILKKRlvDGECST-ARLPENAERNRFQDVLPYDDVRVELvptkENNTGYINASHIKVS 959
Cdd:cd14600     1 EESMAQLKKGLESGTVLIQFEQLYRKK--PGLAITcAKLPQNMDKNRYKDVLPYDATRVVL----QGNEDYINASYVNME 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  960 VSG--IEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLgsrHNTVTYGRFKITTRFRTDSG 1037
Cdd:cd14600    75 IPSanIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDP---PDVMEYGGFRVQCHSEDCTI 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1038 CYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHtnstsdpqspNPPLLVHCSAGVGRTGV 1117
Cdd:cd14600   152 AYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVE----------NEPVLVHCSAGIGRTGV 221

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767979565 1118 VILSEIMIACLEHNE---VLDIPRvldMLRQQRMMLVQTLCQYTFV 1160
Cdd:cd14600   222 LVTMETAMCLTERNQpvyPLDIVR---KMRDQRAMMVQTSSQYKFV 264
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 921-1170 5.94e-64

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: 217.33  E-value: 5.94e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  921 NAERNRFQDVLPYDDVRVEL--VPTKENNTGYINASHIKVSVSGIEWD-----YIATQGPLQNTCQDFWQMVWEQGIAII 993
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILkdRDPNVPGSDYINANYIRNENEGPTTDenaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  994 AMVTAEEEGGREKSFRYWPRLGsrhNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQ-ERTVWHLQYTDWPEHGCPE 1072
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEG---MQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDpIREIWHYQYLSWPDHGVPS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1073 DLKGFLSYLEEIqsvrrHTNSTSDPQSpnPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVL---DIPRVLDMLRQQRMM 1149
Cdd:cd14544   158 DPGGVLNFLEDV-----NQRQESLPHA--GPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDcdiDIQKTIQMVRSQRSG 230

                         250       260
                  ....*....|....*....|.
gi 767979565 1150 LVQTLCQYTFVYRVLIQFLKS 1170
Cdd:cd14544   231 MVQTEAQYKFIYVAVAQYIET 251
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 950-1160 2.59e-61

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 208.34  E-value: 2.59e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  950 YINASHIKVSVSGIEW--DYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGsrhNTVTYGRFK 1027
Cdd:cd14541     2 YINANYVNMEIPGSGIvnRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLG---ETMQFGNLQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1028 ITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeIQSVRRHTnstsdpQSPNPPLLVH 1107
Cdd:cd14541    79 ITCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDF---VKRVRQNR------VGMVEPTVVH 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767979565 1108 CSAGVGRTGVVILSEIMIACLEHNE---VLDIPRvlDMlRQQRMMLVQTLCQYTFV 1160
Cdd:cd14541   150 CSAGIGRTGVLITMETAMCLIEANEpvyPLDIVR--TM-RDQRAMLIQTPSQYRFV 202
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 950-1161 5.05e-61

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: 207.49  E-value: 5.05e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  950 YINASHIKVSVSGIEwDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRlgsrhNTVTYGRFKIT 1029
Cdd:cd18533     1 YINASYITLPGTSSK-RYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPS-----GEYEGEYGDLT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1030 TRFRT----DSGCYATTGLKMKHlLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNStsdpqspNPPLL 1105
Cdd:cd18533    75 VELVSeeenDDGGFIVREFELSK-EDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASL-------DPPII 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767979565 1106 VHCSAGVGRTGVVILSEIMIACLE--HNEVLD-------IPRVLDMLRQQRMMLVQTLCQYTFVY 1161
Cdd:cd18533   147 VHCSAGVGRTGTFIALDSLLDELKrgLSDSQDledsedpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 950-1168 2.12e-60

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: 205.69  E-value: 2.12e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  950 YINASHIKVSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRlGSRHNTVTYGRFKIT 1029
Cdd:cd14538     1 YINASHIRIPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPD-SLNKPLICGGRLEVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1030 TRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeIQSVRRHTNSTsdpqspnpPLLVHCS 1109
Cdd:cd14538    80 LEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRF---IRYMRRIHNSG--------PIVVHCS 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767979565 1110 AGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQFL 1168
Cdd:cd14538   149 AGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
FERM_F1_PTPN21 cd17192
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 20-106 8.63e-60

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: 199.09  E-value: 8.63e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   20 KSCLVARIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQLDKYALEPTVYF 99
Cdd:cd17192     1 KSCLVARIQLLNNEFVEFTLSVESTGQECLEAVAQRLELREITYFSLWYYNKQNQQRWVDLEKPLKKQLDKYALEPTVYF 80


                  ....*..
gi 767979565  100 GVVFYVP 106
Cdd:cd17192    81 GVVFYVP 87
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 896-1161 8.60e-59

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: 203.36  E-value: 8.60e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  896 VFTEYERIlKKRLVDGECSTARLPENAERNRFQDVLPYDDVRVELVPTKEN-NTGYINASHikvsVSGIEWD--YIATQG 972
Cdd:cd14543     5 IYEEYEDI-RREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDeRTDYINANF----MDGYKQKnaYIATQG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  973 PLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGsrHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTG 1052
Cdd:cd14543    80 PLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEE--GSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1053 QERTVWHLQYTDWPEHGCPEDLKGFLSYLEEiqsVRRHTNS-------TSDPQSPNPPLLVHCSAGVGRTGVVILSEIMI 1125
Cdd:cd14543   158 ESRQVTHFQFTSWPDFGVPSSAAALLDFLGE---VRQQQALavkamgdRWKGHPPGPPIVVHCSAGIGRTGTFCTLDICL 234

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767979565 1126 ACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVY 1161
Cdd:cd14543   235 SQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 920-1168 1.58e-57

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: 198.52  E-value: 1.58e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  920 ENAERNRFQDVLPYDDVRVELvptkENNTGYINASHIKVSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAE 999
Cdd:cd14597     2 ENRKKNRYKNILPYDTTRVPL----GDEGGYINASFIKMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1000 EEGGREKSFRYWPRLGSRhNTVTYGRFKIT-TRFRTDSGcYATTGLKMKHLLTGQERTVWHLQYTDWPEHGC---PEDLK 1075
Cdd:cd14597    78 VEGGKIKCQRYWPEILGK-TTMVDNRLQLTlVRMQQLKN-FVIRVLELEDIQTREVRHITHLNFTAWPDHDTpsqPEQLL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1076 GFLSYLeeiqsvrRHTNSTSdpqspnpPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLC 1155
Cdd:cd14597   156 TFISYM-------RHIHKSG-------PIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTED 221

                         250
                  ....*....|...
gi 767979565 1156 QYTFVYRVLIQFL 1168
Cdd:cd14597   222 QYIFCYQVILYVL 234
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 24-222 1.37e-53

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: 185.96  E-value: 1.37e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565     24 VARIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQ-RRWVDLEKPLKKQLDKYaLEPTVYFGVV 102
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDlRHWLDPAKTLLDQDVKS-EPLTLYFRVK 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565    103 FYVPSVSQLQQEITRY-QYYLQLKKDILEGSIPCTLEQAIQLAGLAVQADFGDFDQYES--QDFLQKFALFPVGWLQDEK 179
Cdd:smart00295   80 FYPPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdlRGELSLKRFLPKQLLDSRK 159

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|...
gi 767979565    180 vLEEATQKVALLHQKYRGLTAPDAEMLYMQEVERMDGYGEESY 222
Cdd:smart00295  160 -LKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 920-1170 3.07e-53

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: 187.15  E-value: 3.07e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  920 ENAERNRFQDVLPYDDVRVELVPTKENNTG--YINASHI------KVSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIA 991
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVLHDGDPNEPVsdYINANIImpefetKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  992 IIAMVTAEEEGGREKSFRYWPRLGSRHNtvtYGRFKITTRFRTDSGCYATTGLKMKHLLTGQ-ERTVWHLQYTDWPEHGC 1070
Cdd:cd14605    81 VIVMTTKEVERGKSKCVKYWPDEYALKE---YGVMRVRNVKESAAHDYILRELKLSKVGQGNtERTVWQYHFRTWPDHGV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1071 PEDLKGFLSYLEEIqsvrrhtNSTSDPQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEV---LDIPRVLDMLRQQR 1147
Cdd:cd14605   158 PSDPGGVLDFLEEV-------HHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQR 230

                         250       260
                  ....*....|....*....|...
gi 767979565 1148 MMLVQTLCQYTFVYRVLIQFLKS 1170
Cdd:cd14605   231 SGMVQTEAQYRFIYMAVQHYIET 253
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 919-1170 4.80e-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: 187.01  E-value: 4.80e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  919 PENAERNRFQDVLPYDDVRVELVPTKENNTG--YINASHIKVSVSGIEWD---YIATQGPLQNTCQDFWQMVWEQGIAII 993
Cdd:cd14606    16 PENKSKNRYKNILPFDHSRVILQGRDSNIPGsdYINANYVKNQLLGPDENaktYIASQGCLEATVNDFWQMAWQENSRVI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  994 AMVTAEEEGGREKSFRYWPRLGSrhnTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQE-RTVWHLQYTDWPEHGCPE 1072
Cdd:cd14606    96 VMTTREVEKGRNKCVPYWPEVGM---QRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELiREIWHYQYLSWPDHGVPS 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1073 DLKGFLSYLEEIqsvrrhtNSTSDPQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEV---LDIPRVLDMLRQQRMM 1149
Cdd:cd14606   173 EPGGVLSFLDQI-------NQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSG 245

                         250       260
                  ....*....|....*....|.
gi 767979565 1150 LVQTLCQYTFVYRVLIQFLKS 1170
Cdd:cd14606   246 MVQTEAQYKFIYVAIAQFIET 266
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 217-307 7.65e-53

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: 179.41  E-value: 7.65e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  217 YGEESYPAKDSQGSDISIGACLEGIFVKHKNGRHPVVFRWHDIANMSHNKSFFALELANKEETIQFQTEDMETAKYIWRL 296
Cdd:cd13188     1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRPPVFFRWEDIKNVINHKRTFSIECQNSEETVQFQFEDAETAKYVWKL 80

                          90
                  ....*....|.
gi 767979565  297 CVARHKFYRLN 307
Cdd:cd13188    81 CVLQHKFYRQN 91
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 910-1166 1.26e-52

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 185.80  E-value: 1.26e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  910 DGECST--ARLPENAERNRFQDVLPYDDVRVELVP-TKENNTGYINASHIKVSVsgIEWDYIATQGPLQNTCQDFWQMVW 986
Cdd:cd14603    17 DYVCSTvaGGRKENVKKNRYKDILPYDQTRVILSLlQEEGHSDYINANFIKGVD--GSRAYIATQGPLSHTVLDFWRMIW 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  987 EQGIAIIAMVTAEEEGGREKSFRYWPrlgSRHNTVTYGRFKITTrfRTDSGCYATTGLKMKHLLTGQE-RTVWHLQYTDW 1065
Cdd:cd14603    95 QYGVKVILMACREIEMGKKKCERYWA---QEQEPLQTGPFTITL--VKEKRLNEEVILRTLKVTFQKEsRSVSHFQYMAW 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1066 PEHGCPEDLKGFLSYLEEiqsVRRHTNSTSDpqspnpPLLVHCSAGVGRTGVVILSEIMIACL------EHNEVLDIprV 1139
Cdd:cd14603   170 PDHGIPDSPDCMLAMIEL---ARRLQGSGPE------PLCVHCSAGCGRTGVICTVDYVRQLLltqripPDFSIFDV--V 238

                         250       260
                  ....*....|....*....|....*..
gi 767979565 1140 LDMlRQQRMMLVQTLCQYTFVYRVLIQ 1166
Cdd:cd14603   239 LEM-RKQRPAAVQTEEQYEFLYHTVAQ 264
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 916-1162 3.77e-51

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


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 180.41  E-value: 3.77e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  916 ARLPENAERNRFQDVLPYDDVRVELVPTK-ENNTGYINASHIkvsvSGIEWD--YIATQGPLQNTCQDFWQMVWEQGIAI 992
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQPIRgVEGSDYINASFI----DGYRQRgaYIATQGPLAETTEDFWRMLWEHNSTI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  993 IAMVTAEEEGGREKSFRYWPrlgsRHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPE 1072
Cdd:cd14554    77 IVMLTKLREMGREKCHQYWP----AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1073 DLKGFLSYLEEIQsvrrhtnSTSDPQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQ 1152
Cdd:cd14554   153 SGEGFIDFIGQVH-------KTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQ 225

                         250
                  ....*....|
gi 767979565 1153 TLCQYTFVYR 1162
Cdd:cd14554   226 TEDQYQFCYR 235
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 950-1160 6.43e-51

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: 178.60  E-value: 6.43e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  950 YINASHIKVSV--SGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSrhnTVTYGRFK 1027
Cdd:cd14601     2 YINANYINMEIpsSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSG---SSSYGGFQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1028 ITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNStsdpqspnpPLLVH 1107
Cdd:cd14601    79 VTCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDE---------PVVVH 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767979565 1108 CSAGVGRTGVVILSEIMIACLEHNEV---LDIPRVldmLRQQRMMLVQTLCQYTFV 1160
Cdd:cd14601   150 CSAGIGRTGVLITMETAMCLIECNQPvypLDIVRT---MRDQRAMMIQTPSQYRFV 202
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 950-1161 2.19e-50

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: 176.77  E-value: 2.19e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  950 YINASHikvsVSGIEWD--YIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRhntvTYGRFK 1027
Cdd:cd14549     1 YINANY----VDGYNKAraYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTE----TYGNIQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1028 ITTRFRTDSGCYATTGLKMKHL------LTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsVRRhtNSTSDPQSPN 1101
Cdd:cd14549    73 VTLLSTEVLATYTVRTFSLKNLklkkvkGRSSERVVYQYHYTQWPDHGVPDYTLPVLSF------VRK--SSAANPPGAG 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1102 pPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVY 1161
Cdd:cd14549   145 -PIVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 921-1166 2.60e-50

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: 177.97  E-value: 2.60e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  921 NAERNRFQDVLPYDDVRVELVPTK-ENNTGYINASHIkvsvSGI--EWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVT 997
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEgVPGSDYINANYC----DGYrkQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  998 AEEEGGREKSFRYWPRLGsrhnTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGF 1077
Cdd:cd14553    79 KLEERSRVKCDQYWPTRG----TETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPF 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1078 LSYLeeiQSVRRHTNSTSDpqspnpPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQY 1157
Cdd:cd14553   155 LAFL---RRVKACNPPDAG------PIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQY 225


                  ....*....
gi 767979565 1158 TFVYRVLIQ 1166
Cdd:cd14553   226 IFIHDALLE 234
PHA02738 PHA02738
hypothetical protein; Provisional
 899-1171 4.97e-50

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 180.12  E-value: 4.97e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  899 EYERILKKRlVDGECSTARlpENAERNRFQDVLPYDDVRVELvPTKENNTGYINASHikvsVSGIEWD--YIATQGPLQN 976
Cdd:PHA02738   30 EHQKVISEK-VDGTFNAEK--KNRKLNRYLDAVCFDHSRVIL-PAERNRGDYINANY----VDGFEYKkkFICGQAPTRQ 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  977 TCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLgsRHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLlTGQERT 1056
Cdd:PHA02738  102 TCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDV--EQGSIRFGKFKITTTQVETHPHYVKSTLLLTDG-TSATQT 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1057 VWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRR--HTNS--TSDPQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNE 1132
Cdd:PHA02738  179 VTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCQKelAQESlqIGHNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACA 258

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767979565 1133 VLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQFLKSS 1171
Cdd:PHA02738  259 TVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVNLT 297
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 925-1162 9.12e-50

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 176.05  E-value: 9.12e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  925 NRFQDVLPYDDVRVELvPTKENN--TGYINASHIKvSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEG 1002
Cdd:cd14547     1 NRYKTILPNEHSRVCL-PSVDDDplSSYINANYIR-GYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1003 gREKSFRYWPRLgsrhNTVTYGRFKITTRFRTDSGCYATTGLKMKHllTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLE 1082
Cdd:cd14547    79 -KEKCAQYWPEE----ENETYGDFEVTVQSVKETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1083 EIQSVRRHTNSTsdpqspnPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYR 1162
Cdd:cd14547   152 EVEEARQTEPHR-------GPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 899-1170 2.03e-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: 177.62  E-value: 2.03e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  899 EYERILKKRLVDGECSTARLPENAERNRFQDVLPYDDVRVELVPTKE-NNTGYINASHIKVSVSgiEWDYIATQGPLQNT 977
Cdd:cd14628    30 EFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGvEGSDYINASFIDGYRQ--QKAYIATQGPLAET 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  978 CQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRlgsrHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTV 1057
Cdd:cd14628   108 TEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPA----ERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTV 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1058 WHLQYTDWPEHGCPEDLKGFLSYLEEIqsvrrhtNSTSDPQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIP 1137
Cdd:cd14628   184 RQFQFTDWPEQGVPKSGEGFIDFIGQV-------HKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIF 256

                         250       260       270
                  ....*....|....*....|....*....|...
gi 767979565 1138 RVLDMLRQQRMMLVQTLCQYTFVYRVLIQFLKS 1170
Cdd:cd14628   257 QTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGS 289
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 926-1161 5.32e-49

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: 173.69  E-value: 5.32e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  926 RFQDVLPYDDVRVELVP-TKENNTGYINASHIKVSVSGIEwdYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGR 1004
Cdd:cd14548     1 RYTNILPYDHSRVKLIPiNEEEGSDYINANYIPGYNSPRE--FIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1005 EKSFRYWPrlgSRHNTVTYGrfKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeI 1084
Cdd:cd14548    79 VKCDHYWP---FDQDPVYYG--DITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRF---V 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767979565 1085 QSVRRHTNstsdpqSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVY 1161
Cdd:cd14548   151 RLVRDYIK------QEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 900-1169 8.03e-49

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: 175.21  E-value: 8.03e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  900 YERIlKKRLVDGECSTARLPENAERNRFQDVLPYDDVRVELvpTKENNTgYINASHIKVSVSgiEWDYIATQGPLQNTCQ 979
Cdd:cd14608     5 YQDI-RHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKL--HQEDND-YINASLIKMEEA--QRSYILTQGPLPNTCG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  980 DFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWH 1059
Cdd:cd14608    79 HFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILH 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1060 LQYTDWPEHGCPEDLKGFLSYLEEIqsvrRHTNSTSdPQspNPPLLVHCSAGVGRTGVVILSEIMIACLEHNE---VLDI 1136
Cdd:cd14608   159 FHYTTWPDFGVPESPASFLNFLFKV----RESGSLS-PE--HGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKdpsSVDI 231

                         250       260       270
                  ....*....|....*....|....*....|...
gi 767979565 1137 PRVLDMLRQQRMMLVQTLCQYTFVYRVLIQFLK 1169
Cdd:cd14608   232 KKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAK 264
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 906-1170 2.03e-48

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: 174.54  E-value: 2.03e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  906 KRLVDGECSTAR-----LPENAERNRFQDVLPYDDVRVELVPTKE-NNTGYINASHIKVSVSgiEWDYIATQGPLQNTCQ 979
Cdd:cd14627    33 KRLANSKAHTSRfisanLPCNKFKNRLVNIMPYETTRVCLQPIRGvEGSDYINASFIDGYRQ--QKAYIATQGPLAETTE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  980 DFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPrlgsRHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWH 1059
Cdd:cd14627   111 DFWRMLWENNSTIVVMLTKLREMGREKCHQYWP----AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQ 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1060 LQYTDWPEHGCPEDLKGFLSYLEEIqsvrrhtNSTSDPQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRV 1139
Cdd:cd14627   187 FQFTDWPEQGVPKSGEGFIDFIGQV-------HKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQT 259

                         250       260       270
                  ....*....|....*....|....*....|.
gi 767979565 1140 LDMLRQQRMMLVQTLCQYTFVYRVLIQFLKS 1170
Cdd:cd14627   260 VKMLRTQRPAMVQTEDEYQFCYQAALEYLGS 290
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 950-1169 1.11e-47

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: 169.16  E-value: 1.11e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  950 YINASHIKVSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRlgSRHNTVTYGRFKIT 1029
Cdd:cd14596     1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPE--TLQEPMELENYQLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1030 TRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCP---EDLKGFLSYLeeiqsvrRHTNSTSdpqspnpPLLV 1106
Cdd:cd14596    79 LENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPqssDQLVKFICYM-------RKVHNTG-------PIVV 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767979565 1107 HCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQFLK 1169
Cdd:cd14596   145 HCSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 925-1165 2.08e-47

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: 169.35  E-value: 2.08e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  925 NRFQDVLPYDDVRVELVP-TKENNTGYINASHIKVSVSGIEwdYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGG 1003
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQlGGEPHSDYINANFIPGYTSPQE--FIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1004 REKSFRYWPrlgSRHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEe 1083
Cdd:cd14618    79 RVLCDHYWP---SESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRE- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1084 iqSVRRHTNSTSDpqspNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRV 1163
Cdd:cd14618   155 --LVREHVQATKG----KGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSC 228


                  ..
gi 767979565 1164 LI 1165
Cdd:cd14618   229 IL 230
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 924-1166 3.43e-47

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: 168.87  E-value: 3.43e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  924 RNRFQDVLPYDDVRVEL-VPTKENNTGYINASHIKvSVSGIEwDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEG 1002
Cdd:cd14602     1 KNRYKDILPYDHSRVELsLITSDEDSDYINANFIK-GVYGPR-AYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1003 GREKSFRYWPRLGSrhNTVTYGRFKITTRFRTDSGCYATTGLKMKhlLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLE 1082
Cdd:cd14602    79 GKKKCERYWAEPGE--MQLEFGPFSVTCEAEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPILELIW 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1083 EIQSVRRHTnstsdpqspNPPLLVHCSAGVGRTGVVILSEIMIACLEHN---EVLDIPRVLDMLRQQRMMLVQTLCQYTF 1159
Cdd:cd14602   155 DVRCYQEDD---------SVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIQEMRTQRPSLVQTKEQYEL 225


                  ....*..
gi 767979565 1160 VYRVLIQ 1166
Cdd:cd14602   226 VYNAVIE 232
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 925-1162 4.62e-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: 168.17  E-value: 4.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  925 NRFQDVLPYDDVRVELVPTKENN-TGYINASHIkvSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGG 1003
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYI--PGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1004 REKSFRYWPrlgSRHNTVTYGrfKITTRFRTDSGCYATTGLKMKHLLTGQ---ERTVWHLQYTDWPEHGCPEDLKGFLSY 1080
Cdd:cd14617    79 RVKCDHYWP---ADQDSLYYG--DLIVQMLSESVLPEWTIREFKICSEEQldaPRLVRHFHYTVWPDHGVPETTQSLIQF 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1081 leeIQSVRRHTNSTSDPQspnpPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFV 1160
Cdd:cd14617   154 ---VRTVRDYINRTPGSG----PTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYL 226


                  ..
gi 767979565 1161 YR 1162
Cdd:cd14617   227 HQ 228
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 925-1162 4.68e-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: 168.46  E-value: 4.68e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  925 NRFQDVLPYDDVRVELVPTKENNTGYINASHIKVSVSGIEwdYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGR 1004
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKE--FIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1005 EKSFRYWPRLGSRhntvTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEei 1084
Cdd:cd14615    79 TKCEEYWPSKQKK----DYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRH-- 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767979565 1085 qSVRRHtnstSDPQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYR 1162
Cdd:cd14615   153 -LVREY----MKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 225
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 924-1161 7.63e-47

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: 167.57  E-value: 7.63e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  924 RNRFQDVLPYDDVRVELvptKENNTGYINASHIKVSVSGIEwdYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGG 1003
Cdd:cd14545     3 RYRDRDPYDHDRSRVKL---KQGDNDYINASLVEVEEAKRS--YILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1004 REKSFRYWPRLGSRHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLee 1083
Cdd:cd14545    78 QIKCAQYWPQGEGNAMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFL-- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1084 iQSVRRHTNSTSDPQspnpPLLVHCSAGVGRTGVVILSEIMIACLEHNEV--LDIPRVLDMLRQQRMMLVQTLCQYTFVY 1161
Cdd:cd14545   156 -QKVRESGSLSSDVG----PPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 950-1161 1.21e-46

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: 166.02  E-value: 1.21e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  950 YINASHIKvSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRlgSRHNTVTYGRFKIT 1029
Cdd:cd14539     1 YINASLIE-DLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPT--ERGQALVYGAITVS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1030 TRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTsdpqspNPPLLVHCS 1109
Cdd:cd14539    78 LQSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSL------QTPIVVHCS 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767979565 1110 AGVGRTGV-VILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVY 1161
Cdd:cd14539   152 SGVGRTGAfCLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
FERM_F1_PTPN14_like cd17099
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 20-104 1.33e-46

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: 161.25  E-value: 1.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   20 KSCLVARIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQLDKYALEPTVYF 99
Cdd:cd17099     1 KNSFVVRIQLLDNTVLECTLSPESTGQDCLEYVAQRLELREIEYFGLRYVNKKGQLRWVDLEKPLKKQLDKHAHEPLLYF 80


                  ....*
gi 767979565  100 GVVFY 104
Cdd:cd17099    81 GVMFY 85
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 925-1168 2.17e-46

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: 166.60  E-value: 2.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  925 NRFQDVLPYDDVRVELVPTKENNTG-YINASHIKVSVSGIEwdYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGG 1003
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSdYINANYMPGYWSSQE--FIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1004 REKSFRYWPRlgsRHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEe 1083
Cdd:cd14619    79 RVKCEHYWPL---DYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRR- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1084 iqSVRRHTNSTsdpQSPNPPlLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRV 1163
Cdd:cd14619   155 --LLRQWLDQT---MSGGPT-VVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQC 228


                  ....*
gi 767979565 1164 LIQFL 1168
Cdd:cd14619   229 ILDFL 233
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 918-1167 1.21e-45

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 165.01  E-value: 1.21e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  918 LPENAERNRFQDVLPYDDVRVEL--VPTKENNTGYINASHIKvSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAM 995
Cdd:cd14612    12 IPGHASKDRYKTILPNPQSRVCLrrAGSQEEEGSYINANYIR-GYDGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVM 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  996 VTAEEEgGREKSFRYWPRLGSrhntvTYGRFKITTRFRTDSGCYATTGLKMKHllTGQERTVWHLQYTDWPEHGCPEDLK 1075
Cdd:cd14612    91 ITKLKE-KKEKCVHYWPEKEG-----TYGRFEIRVQDMKECDGYTIRDLTIQL--EEESRSVKHYWFSSWPDHQTPESAG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1076 GFLSYLEEIQSVRRhtnstsdpQSPNP-PLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTL 1154
Cdd:cd14612   163 PLLRLVAEVEESRQ--------TAASPgPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTS 234

                         250
                  ....*....|...
gi 767979565 1155 CQYTFVYRVLIQF 1167
Cdd:cd14612   235 EQYQFLHHTLALY 247
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 896-1166 1.82e-45

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: 165.21  E-value: 1.82e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  896 VFTEYERILKKRLVDGECSTArlPENAERNRFQDVLPYDDVRVELVP---TKENNTGYINASHikvsVSGIEWD--YIAT 970
Cdd:cd17667     4 DFEEVQRCTADMNITAEHSNH--PDNKHKNRYINILAYDHSRVKLRPlpgKDSKHSDYINANY----VDGYNKAkaYIAT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  971 QGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPrlgsRHNTVTYGRFKITTRFRTDSGCYATTGL-----K 1045
Cdd:cd17667    78 QGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWP----TENSEEYGNIIVTLKSTKIHACYTVRRFsirntK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1046 MKHLLTGQ------ERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsVRRhtnsTSDPQSPN-PPLLVHCSAGVGRTGVV 1118
Cdd:cd17667   154 VKKGQKGNpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTF------VRR----SSAARTPEmGPVLVHCSAGVGRTGTY 223

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 767979565 1119 ILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1166
Cdd:cd17667   224 IVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 271
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 915-1170 3.90e-45

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


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 164.90  E-value: 3.90e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  915 TARLPENAERNRFQDVLPYDDVRVELVPTKE-NNTGYINASHIKVSVSgiEWDYIATQGPLQNTCQDFWQMVWEQGIAII 993
Cdd:cd14629    47 SANLPCNKFKNRLVNIMPYELTRVCLQPIRGvEGSDYINASFIDGYRQ--QKAYIATQGPLAETTEDFWRMLWEHNSTIV 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  994 AMVTAEEEGGREKSFRYWPrlgsRHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPED 1073
Cdd:cd14629   125 VMLTKLREMGREKCHQYWP----AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKT 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1074 LKGFLSYLEEIqsvrrhtNSTSDPQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQT 1153
Cdd:cd14629   201 GEGFIDFIGQV-------HKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQT 273

                         250
                  ....*....|....*..
gi 767979565 1154 LCQYTFVYRVLIQFLKS 1170
Cdd:cd14629   274 EDQYQLCYRAALEYLGS 290
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 916-1161 3.96e-45

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 163.98  E-value: 3.96e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  916 ARLPENAERNRFQDVLPYDDVRVELVPTkENNtgYINAShiKVSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAM 995
Cdd:cd14607    19 AKYPENRNRNRYRDVSPYDHSRVKLQNT-END--YINAS--LVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVM 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  996 VTAEEEGGREKSFRYWPRLGSRHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLK 1075
Cdd:cd14607    94 LNRIVEKDSVKCAQYWPTDEEEVLSFKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWPDFGVPESPA 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1076 GFLSYLEEIqsvrRHTNSTSdPQspNPPLLVHCSAGVGRTGVVILSEIMIACLEHNE--VLDIPRVLDMLRQQRMMLVQT 1153
Cdd:cd14607   174 SFLNFLFKV----RESGSLS-PE--HGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLIQT 246


                  ....*...
gi 767979565 1154 LCQYTFVY 1161
Cdd:cd14607   247 PDQLRFSY 254
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 920-1169 7.85e-45

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: 164.34  E-value: 7.85e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  920 ENAERNRFQDVLPYDDVRVEL-VPTKENNTGYINASHIKvSVSGIEwDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTA 998
Cdd:cd14604    56 ENVKKNRYKDILPFDHSRVKLtLKTSSQDSDYINANFIK-GVYGPK-AYIATQGPLANTVIDFWRMIWEYNVAIIVMACR 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  999 EEEGGREKSFRYWPRLGSrhNTVTYGRFKIT---TRFRTDSgCYATTGLKMKHlltgQERTVWHLQYTDWPEHGCPEDlk 1075
Cdd:cd14604   134 EFEMGRKKCERYWPLYGE--EPMTFGPFRISceaEQARTDY-FIRTLLLEFQN----ETRRLYQFHYVNWPDHDVPSS-- 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1076 gFLSYLEEIQSVRRHTnstsdpQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHN---EVLDIPRVLDMLRQQRMMLVQ 1152
Cdd:cd14604   205 -FDSILDMISLMRKYQ------EHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHSAVQ 277

                         250
                  ....*....|....*..
gi 767979565 1153 TLCQYTFVYRVLIQFLK 1169
Cdd:cd14604   278 TKEQYELVHRAIAQLFE 294
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 925-1162 6.43e-44

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: 158.92  E-value: 6.43e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  925 NRFQDVLPYDDVRVELVPTKEN-NTGYINASHIKVSVSGIEwdYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGG 1003
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVpGSDYINASYISGYLCPNE--FIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1004 REKSFRYWPRlgSRHNTVTYGRFKITTRFRTDSGCYATTGLKM-KHlltGQERTVWHLQYTDWPEHGCPEDLKGFLSYLE 1082
Cdd:cd14616    79 RIRCHQYWPE--DNKPVTVFGDIVITKLMEDVQIDWTIRDLKIeRH---GDYMMVRQCNFTSWPEHGVPESSAPLIHFVK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1083 EIQSVRRHTNStsdpqspnpPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYR 1162
Cdd:cd14616   154 LVRASRAHDNT---------PMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 878-1166 2.09e-43

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: 159.43  E-value: 2.09e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  878 ATNDERCKIleqrlEQGMVFT-EYERILKKRLVDGECSTarLPENAERNRFQDVLPYDDVRVELVPTKE-NNTGYINASH 955
Cdd:cd14626     4 ADNIERLKA-----NDGLKFSqEYESIDPGQQFTWENSN--LEVNKPKNRYANVIAYDHSRVILTSVDGvPGSDYINANY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  956 IKVSVSgiEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRhntvTYGRFKITTRFRTD 1035
Cdd:cd14626    77 IDGYRK--QNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTE----TYGMIQVTLLDTVE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1036 SGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVrrhtnstsdpqspNP----PLLVHCSAG 1111
Cdd:cd14626   151 LATYSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKAC-------------NPpdagPMVVHCSAG 217

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767979565 1112 VGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1166
Cdd:cd14626   218 VGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 950-1162 2.61e-43

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: 156.53  E-value: 2.61e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  950 YINASHIKVSVSGIEwdYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLgsRHNTVTYGRFKIT 1029
Cdd:cd14557     1 YINASYIDGFKEPRK--YIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSM--EEGSRAFGDVVVK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1030 TRFRTDSGCYATTGLKMKHLL-TGQERTVWHLQYTDWPEHGCPEDLKGFLsyleeiqSVRRHTNSTSDPQSpnPPLLVHC 1108
Cdd:cd14557    77 INEEKICPDYIIRKLNINNKKeKGSGREVTHIQFTSWPDHGVPEDPHLLL-------KLRRRVNAFNNFFS--GPIVVHC 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767979565 1109 SAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYR 1162
Cdd:cd14557   148 SAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 866-1166 1.97e-42

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: 156.79  E-value: 1.97e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  866 PLPdegkeVATRATNDERCKILEQ-RLEQgmvftEYERILKKRLVDGECSTarLPENAERNRFQDVLPYDDVRVELVPTK 944
Cdd:cd14625     3 PIP-----ISELAEHTERLKANDNlKLSQ-----EYESIDPGQQFTWEHSN--LEVNKPKNRYANVIAYDHSRVILQPIE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  945 E-NNTGYINASHIKVSVSgiEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGsrhnTVTY 1023
Cdd:cd14625    71 GiMGSDYINANYIDGYRK--QNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRG----TETY 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1024 GRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQsvrrhtnsTSDPQSPNpP 1103
Cdd:cd14625   145 GMIQVTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVK--------TCNPPDAG-P 215

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767979565 1104 LLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1166
Cdd:cd14625   216 IVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 950-1164 2.24e-42

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: 153.96  E-value: 2.24e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  950 YINASHIkvsvSGIEWD--YIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSrhntVTYGRFK 1027
Cdd:cd14552     1 YINASFI----DGYRQKdaYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGS----VSSGDIT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1028 ITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNstsdpqspNPPLLVH 1107
Cdd:cd14552    73 VELKDQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSG--------NHPITVH 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767979565 1108 CSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVL 1164
Cdd:cd14552   145 CSAGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 880-1169 2.45e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 157.47  E-value: 2.45e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  880 NDERCKILEQRLEQGMVF----TEYERILKKrLVDGECSTARLPENAERNRFQDVLPYDDVRVeLVPTKENNTGYINASH 955
Cdd:PHA02742    8 KNSFAKNCEQLIEESNLAeilkEEHEHIMQE-IVAFSCNESLELKNMKKCRYPDAPCFDRNRV-ILKIEDGGDDFINASY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  956 ikVSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWprLGSRHNTVTYGRFKITTR---- 1031
Cdd:PHA02742   86 --VDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYW--MPHERGKATHGEFKIKTKkiks 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1032 FRTdsgcYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIqsvrRHTNSTSD-PQS-----PNPPLL 1105
Cdd:PHA02742  162 FRN----YAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAV----READLKADvDIKgenivKEPPIL 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767979565 1106 VHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQFLK 1169
Cdd:PHA02742  234 VHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLIFAK 297
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 894-1168 4.46e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 156.70  E-value: 4.46e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  894 GMVFTEYERILKKRlVDGECSTARLPENAERNRFQDVLPYDDVRVELVPTKENNTGYINASHIkvsvSGIEWD--YIATQ 971
Cdd:PHA02747   25 GIIRDEHHQIILKP-FDGLIANFEKPENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWI----DGFEDDkkFIATQ 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  972 GPLQNTCQDFWQMVWEQGIAIIAMVT-AEEEGGREKSFRYWPrLGSRHNTVTYGrFKITTRFRTDSGCYATTGLKMKHLL 1050
Cdd:PHA02747  100 GPFAETCADFWKAVWQEHCSIIVMLTpTKGTNGEEKCYQYWC-LNEDGNIDMED-FRIETLKTSVRAKYILTLIEITDKI 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1051 TGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTSDPQSP-NPPLLVHCSAGVGRTGVVILSEIMIACLE 1129
Cdd:PHA02747  178 LKDSRKISHFQCSEWFEDETPSDHPDFIKFIKIIDINRKKSGKLFNPKDAlLCPIVVHCSDGVGKTGIFCAVDICLNQLV 257

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767979565 1130 HNEVLDIPRVLDMLRQQRMMLVQTLCQYTFV---YRVLIQFL 1168
Cdd:PHA02747  258 KRKAICLAKTAEKIREQRHAGIMNFDDYLFIqpgYEVLHYFL 299
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 950-1162 6.45e-42

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: 152.58  E-value: 6.45e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  950 YINASHIKvSVSGiEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSrhNTVTYGRFKIT 1029
Cdd:cd14542     1 YINANFIK-GVSG-SKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGE--EQLQFGPFKIS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1030 ---TRFRTDSgcYATTGLKMKhlLTGQERTVWHLQYTDWPEHGCPEDLKgflSYLEEIQSVRRHTNSTSdpqspnPPLLV 1106
Cdd:cd14542    77 lekEKRVGPD--FLIRTLKVT--FQKESRTVYQFHYTAWPDHGVPSSVD---PILDLVRLVRDYQGSED------VPICV 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767979565 1107 HCSAGVGRTGVV--------ILSEIMIAclEHNEVLDIprVLDMlRQQRMMLVQTLCQYTFVYR 1162
Cdd:cd14542   144 HCSAGCGRTGTIcaidyvwnLLKTGKIP--EEFSLFDL--VREM-RKQRPAMVQTKEQYELVYR 202
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 915-1162 1.24e-41

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: 153.12  E-value: 1.24e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  915 TARLPENAERNRFQDVLPYDDVRVELVPT-KENNTGYINASHIKVSVSGIEwdYIATQGPLQNTCQDFWQMVWEQGIAII 993
Cdd:cd14614     6 AADLPVNRCKNRYTNILPYDFSRVKLVSMhEEEGSDYINANYIPGYNSPQE--YIATQGPLPETRNDFWKMVLQQKSQII 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  994 AMVTAEEEGGREKSFRYWPrlgSRHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQErtVWHLQYTDWPEHGCPeD 1073
Cdd:cd14614    84 VMLTQCNEKRRVKCDHYWP---FTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQD--VMHFNYTAWPDHGVP-T 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1074 LKGFLSYLEEIQSVRRHTNSTSDpqspnpPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQT 1153
Cdd:cd14614   158 ANAAESILQFVQMVRQQAVKSKG------PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQT 231


                  ....*....
gi 767979565 1154 LCQYTFVYR 1162
Cdd:cd14614   232 EEQYIFIHQ 240
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 926-1164 2.52e-41

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: 151.74  E-value: 2.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  926 RFQDVLPYDDVRVeLVPTK--ENNTGYINASHIKVSVSgiEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGG 1003
Cdd:cd14623     1 RVLQIIPYEFNRV-IIPVKrgEENTDYVNASFIDGYRQ--KDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1004 REKSFRYWPRLGSrhntVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEE 1083
Cdd:cd14623    78 QEKCAQYWPSDGS----VSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1084 IQSVRRhtnstsdpQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRV 1163
Cdd:cd14623   154 VQKQQQ--------QSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKV 225


                  .
gi 767979565 1164 L 1164
Cdd:cd14623   226 V 226
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 918-1164 1.10e-40

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: 151.17  E-value: 1.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  918 LPENAERNRFQDVLPYDDVRVELVPTKENN--TGYINASHIKvSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAM 995
Cdd:cd14613    22 IPGLVRKNRYKTILPNPHSRVCLTSPDQDDplSSYINANYIR-GYGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVM 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  996 VTAEEEGGrEKSFRYWPRlgsrhNTVTYGRFKITTRFRTDSGCYATTGLKMKHllTGQERTVWHLQYTDWPEHGCPEDLK 1075
Cdd:cd14613   101 ITNIEEMN-EKCTEYWPE-----EQVTYEGIEITVKQVIHADDYRLRLITLKS--GGEERGLKHYWYTSWPDQKTPDNAP 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1076 GFLSYLEEIQSVRRHTnstsdpQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLC 1155
Cdd:cd14613   173 PLLQLVQEVEEARQQA------EPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCE 246


                  ....*....
gi 767979565 1156 QYTFVYRVL 1164
Cdd:cd14613   247 QYQFVHHVL 255
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 927-1166 4.17e-40

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: 148.17  E-value: 4.17e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  927 FQDVLPYDDVRVELVPTKEN-NTGYINASHIKVSVSgiEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGRE 1005
Cdd:cd14620     1 YPNILPYDHSRVILSQLDGIpCSDYINASYIDGYKE--KNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1006 KSFRYWPRLGSRhntvTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQ---ERTVWHLQYTDWPEHGCPEDLKGFLSYLE 1082
Cdd:cd14620    79 KCYQYWPDQGCW----TYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGckaPRLVTQLHFTSWPDFGVPFTPIGMLKFLK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1083 EIQSVrrhtnstsdpqspNP----PLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYT 1158
Cdd:cd14620   155 KVKSV-------------NPvhagPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYS 221


                  ....*...
gi 767979565 1159 FVYRVLIQ 1166
Cdd:cd14620   222 FIYQALLE 229
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 924-1161 5.04e-40

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: 148.14  E-value: 5.04e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  924 RNRFQDVLPYDDVRVELVPTKENN--TGYINASHIKvSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEE 1001
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNSNDslSTYINANYIR-GYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1002 GGrEKSFRYWPrlgsrHNTVTYGRFKITTRFRTDSGCYATTGLKMKHllTGQERTVWHLQYTDWPEHGCPEDLKGFLSYL 1081
Cdd:cd14611    81 KN-EKCVLYWP-----EKRGIYGKVEVLVNSVKECDNYTIRNLTLKQ--GSQSRSVKHYWYTSWPDHKTPDSAQPLLQLM 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1082 EEIQSVRRHTNSTSdpqspnpPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVY 1161
Cdd:cd14611   153 LDVEEDRLASPGRG-------PVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 899-1166 1.81e-39

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: 148.34  E-value: 1.81e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  899 EYERILKKRLVDGECSTarLPENAERNRFQDVLPYDDVRVeLVPTKENNTG--YINASHIKVSVSgiEWDYIATQGPLQN 976
Cdd:cd14624    27 EYESIDPGQQFTWEHSN--LEVNKPKNRYANVIAYDHSRV-LLSAIEGIPGsdYINANYIDGYRK--QNAYIATQGALPE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  977 TCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGsrhnTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERT 1056
Cdd:cd14624   102 TFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRG----TETYGLIQVTLLDTVELATYCVRTFALYKNGSSEKRE 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1057 VWHLQYTDWPEHGCPEDLKGFLSYLEEIQsvrrhtnsTSDPQSPNPpLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDI 1136
Cdd:cd14624   178 VRQFQFTAWPDHGVPEHPTPFLAFLRRVK--------TCNPPDAGP-MVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDI 248

                         250       260       270
                  ....*....|....*....|....*....|
gi 767979565 1137 PRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1166
Cdd:cd14624   249 YGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 950-1165 2.61e-39

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: 145.51  E-value: 2.61e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  950 YINASHikvsVSGI--EWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRHntvtYGRFK 1027
Cdd:cd17668     1 YINANY----VDGYnkPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEE----YGNFL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1028 ITTRFRTDSGCYA--TTGLKMKHLLTG------QERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNStsdpqs 1099
Cdd:cd17668    73 VTQKSVQVLAYYTvrNFTLRNTKIKKGsqkgrpSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVG------ 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767979565 1100 pnpPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLI 1165
Cdd:cd17668   147 ---PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 920-1166 2.72e-39

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: 146.32  E-value: 2.72e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  920 ENAERNRFQDVLPYDDVRVELVPTKEN-NTGYINASHIkvsvSGIEWD--YIATQGPLQNTCQDFWQMVWEQGIAIIAMV 996
Cdd:cd14630     2 ENRNKNRYGNIISYDHSRVRLQLLDGDpHSDYINANYI----DGYHRPrhYIATQGPMQETVKDFWRMIWQENSASVVMV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  997 TAEEEGGREKSFRYWPrlgsrHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKG 1076
Cdd:cd14630    78 TNLVEVGRVKCVRYWP-----DDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1077 FLSYLEEIQSVrrhtnstsdpqspNP----PLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQ 1152
Cdd:cd14630   153 LLGFVRQVKFL-------------NPpdagPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQ 219

                         250
                  ....*....|....
gi 767979565 1153 TLCQYTFVYRVLIQ 1166
Cdd:cd14630   220 TEEQYVFVHDAILE 233
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 950-1161 4.87e-39

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: 144.46  E-value: 4.87e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  950 YINASHIkvsvSGIeW---DYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSrhntvTYGRF 1026
Cdd:cd14558     1 YINASFI----DGY-WgpkSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKK-----TYGDI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1027 KITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeIQSVRRHTNSTSDPQSPNPPLLV 1106
Cdd:cd14558    71 EVELKDTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDM---IKSIKQKLPYKNSKHGRSVPIVV 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767979565 1107 HCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVY 1161
Cdd:cd14558   148 HCSDGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 950-1161 4.89e-39

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: 144.51  E-value: 4.89e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  950 YINASHIkvsvsgIEWD-----YIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRhntvTYG 1024
Cdd:cd14546     1 YINASTI------YDHDprnpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSE----VYH 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1025 RFKITTrFRTDSGC--YATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsvRRHTNSTSDPQSpnP 1102
Cdd:cd14546    71 IYEVHL-VSEHIWCddYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEF-------RRKVNKSYRGRS--C 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1103 PLLVHCSAGVGRTGVVILSEIMIACLEHN-EVLDIPRVLDMLRQQRMMLVQTLCQYTFVY 1161
Cdd:cd14546   141 PIVVHCSDGAGRTGTYILIDMVLNRMAKGaKEIDIAATLEHLRDQRPGMVKTKDQFEFVL 200
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 909-1166 5.56e-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: 147.48  E-value: 5.56e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  909 VDGECSTARLPENAERNRFQDVLPYDDVRVELVPTKE-NNTGYINASHIkvsvSGIEWD--YIATQGPLQNTCQDFWQMV 985
Cdd:cd14621    40 IQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGvPDSDYINASFI----NGYQEKnkFIAAQGPKEETVNDFWRMI 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  986 WEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRhntvTYGRFKITTRFRTDSGCYATTGLKMKHL--LTGQ--ERTVWHLQ 1061
Cdd:cd14621   116 WEQNTATIVMVTNLKERKECKCAQYWPDQGCW----TYGNIRVSVEDVTVLVDYTVRKFCIQQVgdVTNKkpQRLITQFH 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1062 YTDWPEHGCPEDLKGFLSYLEEIQsvrrhtnsTSDPQSPNPpLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLD 1141
Cdd:cd14621   192 FTSWPDFGVPFTPIGMLKFLKKVK--------NCNPQYAGA-IVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVS 262

                         250       260
                  ....*....|....*....|....*
gi 767979565 1142 MLRQQRMMLVQTLCQYTFVYRVLIQ 1166
Cdd:cd14621   263 RIRAQRCQMVQTDMQYVFIYQALLE 287
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 913-1159 7.96e-39

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: 146.34  E-value: 7.96e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  913 CSTARLPENAERNRFQDVLPYDDVRVEL-VPTKENNTGYINASHIkvsvsgIEWD-----YIATQGPLQNTCQDFWQMVW 986
Cdd:cd14609    34 CSTAQGEANVKKNRNPDFVPYDHARIKLkAESNPSRSDYINASPI------IEHDprmpaYIATQGPLSHTIADFWQMVW 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  987 EQGIAIIAMVTAEEEGGREKSFRYWPRLGSRhntvTYGRFKITTrFRTDSGC--YATTGLKMKHLLTGQERTVWHLQYTD 1064
Cdd:cd14609   108 ENGCTVIVMLTPLVEDGVKQCDRYWPDEGSS----LYHIYEVNL-VSEHIWCedFLVRSFYLKNVQTQETRTLTQFHFLS 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1065 WPEHGCPEDLKGFLSYleeiqsvRRHTNSTSDPQSpnPPLLVHCSAGVGRTGVVILSEIMIACLEHN-EVLDIPRVLDML 1143
Cdd:cd14609   183 WPAEGIPSSTRPLLDF-------RRKVNKCYRGRS--CPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHV 253

                         250
                  ....*....|....*.
gi 767979565 1144 RQQRMMLVQTLCQYTF 1159
Cdd:cd14609   254 RDQRPGMVRTKDQFEF 269
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 950-1167 3.59e-38

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: 142.07  E-value: 3.59e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  950 YINASHIKvsvSGIEWDY-IATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSrhntVTYGrfKI 1028
Cdd:cd14622     2 YINASFID---GYRQKDYfIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGS----VTHG--EI 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1029 TTRFRTDSGCYATTGLKMkhLLT----GQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRhtnstsdpQSPNPPL 1104
Cdd:cd14622    73 TIEIKNDTLLETISIRDF--LVTynqeKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQ--------QTGNHPI 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767979565 1105 LVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQF 1167
Cdd:cd14622   143 VVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 888-1159 4.22e-38

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain.


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 144.43  E-value: 4.22e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  888 EQRLEQgmvftEYERILKKRLVDGECSTARLPENAERNRFQDVLPYDDVRVEL-VPTKENNTGYINASHIkvsvsgIEWD 966
Cdd:cd14610    16 KNRLEK-----EWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILkAENSHSHSDYINASPI------MDHD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  967 -----YIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVtYGRFKITTRFRTDSgcYAT 1041
Cdd:cd14610    85 prnpaYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHI-YEVNLVSEHIWCED--FLV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1042 TGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsvRRHTNSTSDPQSpnPPLLVHCSAGVGRTGVVILS 1121
Cdd:cd14610   162 RSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDF-------RRKVNKCYRGRS--CPIIVHCSDGAGRSGTYILI 232

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767979565 1122 EIMIACLEHN-EVLDIPRVLDMLRQQRMMLVQTLCQYTF 1159
Cdd:cd14610   233 DMVLNKMAKGaKEIDIAATLEHLRDQRPGMVQTKEQFEF 271
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 886-1166 4.85e-38

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: 144.03  E-value: 4.85e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  886 ILEQRLEQGMVFTE-YERILKKRlvDGECSTARLPENAERNRFQDVLPYDDVRVELVPTK-ENNTGYINASHIkvsvSGI 963
Cdd:cd14633     6 ITQMKCAEGYGFKEeYESFFEGQ--SAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEgETSSDYINGNYI----DGY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  964 EW--DYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPrlgsrHNTVTYGRFKITTRFRTDSGCYAT 1041
Cdd:cd14633    80 HRpnHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP-----DDTEIYKDIKVTLIETELLAEYVI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1042 TGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSvrrhtnstSDPQSPNpPLLVHCSAGVGRTGVVILS 1121
Cdd:cd14633   155 RTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS--------KSPPNAG-PLVVHCSAGAGRTGCFIVI 225

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 767979565 1122 EIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1166
Cdd:cd14633   226 DIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 950-1166 4.91e-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: 141.59  E-value: 4.91e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  950 YINASHIkvsvSGIEWD--YIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPrlgsrHNTVTYGRFK 1027
Cdd:cd14555     1 YINANYI----DGYHRPnhYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP-----DDTEVYGDIK 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1028 ITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSvrrhtnstSDPQSPNpPLLVH 1107
Cdd:cd14555    72 VTLVETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKA--------SNPPSAG-PIVVH 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767979565 1108 CSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1166
Cdd:cd14555   143 CSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 950-1162 1.03e-37

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: 140.43  E-value: 1.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  950 YINASHIkvsvSGIEWD--YIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGSRhntvTYGRFK 1027
Cdd:cd14551     1 YINASYI----DGYQEKnkFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCW----TYGNLR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1028 ITTRFRTDSGCYATTGLKMKHLLTG----QERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVrrhtnstsDPQSPNpP 1103
Cdd:cd14551    73 VRVEDTVVLVDYTTRKFCIQKVNRGigekRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSA--------NPPRAG-P 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767979565 1104 LLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYR 1162
Cdd:cd14551   144 IVVHCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 937-1166 1.12e-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: 140.93  E-value: 1.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  937 RVELVPTKENNTG-YINASHIkvsvSGIEW--DYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPr 1013
Cdd:cd14631     1 RVILQPVEDDPSSdYINANYI----DGYQRpsHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1014 lgsrHNTVTYGRFKITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQsvrrhtns 1093
Cdd:cd14631    76 ----DDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVK-------- 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767979565 1094 TSDPQSPNpPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1166
Cdd:cd14631   144 LSNPPSAG-PIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 950-1161 9.37e-36

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: 134.90  E-value: 9.37e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  950 YINASHIKVSVSGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGR-EKSFRYWPRlgSRHNTVTYGRFKI 1028
Cdd:cd17658     1 YINASLVETPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPA--EENESREFGRISV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1029 TTR-FRTDSGCYATTGLKMKHL-LTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVrrhtnstsdPQSPNpPLLV 1106
Cdd:cd17658    79 TNKkLKHSQHSITLRVLEVQYIeSEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGI---------PPSAG-PIVV 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1107 HCSAGVGRTGVVI-----LSEIMIACLehnEVLDIPRVLDMLRQQRMMLVQTLCQYTFVY 1161
Cdd:cd17658   149 HCSAGIGRTGAYCtihntIRRILEGDM---SAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
FERM_F1_PTPN14 cd17191
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 20-106 5.93e-34

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: 125.54  E-value: 5.93e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   20 KSCLVARIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQLDKYALEPTVYF 99
Cdd:cd17191     1 KNCFVTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKQLDKFANEPLLFF 80


                  ....*..
gi 767979565  100 GVVFYVP 106
Cdd:cd17191    81 GVMFYVP 87
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 950-1166 6.15e-34

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: 129.79  E-value: 6.15e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  950 YINASHIkvsvSGIEWD--YIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPrlgsrHNTVTYGRFK 1027
Cdd:cd14632     1 YINANYI----DGYHRSnhFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP-----DDSDTYGDIK 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1028 ITTRFRTDSGCYATTGLKMKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLeeiqsvrRHTNSTSDPQSpnPPLLVH 1107
Cdd:cd14632    72 ITLLKTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFI-------RRVKASTPPDA--GPVVVH 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767979565 1108 CSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1166
Cdd:cd14632   143 CSAGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 909-1164 8.10e-34

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 133.23  E-value: 8.10e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  909 VDGECSTARLPENAERNRFQDVLPYDDVRVEL--------------------VPTKENNTGYINASHikvsVSGIEW--D 966
Cdd:PHA02746   39 IRGTTNHFLKKENLKKNRFHDIPCWDHSRVVInaheslkmfdvgdsdgkkieVTSEDNAENYIHANF----VDGFKEanK 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  967 YIATQGPLQNTCQDFWQMVWEQGIAIIAMVTaEEEGGREKSFRYWPRlgSRHNTVTYGRFKITTRFRTDSGCYATTGLKM 1046
Cdd:PHA02746  115 FICAQGPKEDTSEDFFKLISEHESQVIVSLT-DIDDDDEKCFELWTK--EEDSELAFGRFVAKILDIIEELSFTKTRLMI 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1047 KHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTSDPQSPNP-PLLVHCSAGVGRTGVVILSEIMI 1125
Cdd:PHA02746  192 TDKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAELIKQADNDPQTLgPIVVHCSAGIGRAGTFCAIDNAL 271

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767979565 1126 ACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVL 1164
Cdd:PHA02746  272 EQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1056-1166 4.93e-32

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 120.54  E-value: 4.93e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   1056 TVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHtnstsdpQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEH-NEVL 1134
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQ-------SESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEV 73

                            90       100       110
                    ....*....|....*....|....*....|..
gi 767979565   1135 DIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1166
Cdd:smart00404   74 DIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1056-1166 4.93e-32

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: 120.54  E-value: 4.93e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   1056 TVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHtnstsdpQSPNPPLLVHCSAGVGRTGVVILSEIMIACLEH-NEVL 1134
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQ-------SESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEV 73

                            90       100       110
                    ....*....|....*....|....*....|..
gi 767979565   1135 DIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1166
Cdd:smart00012   74 DIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
919-1166 8.57e-31

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 123.28  E-value: 8.57e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  919 PENAERNRFQDVLPYDDVRVElvptkeNNTGYINASHIKVsvsGIEWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTA 998
Cdd:COG5599    40 INGSPLNRFRDIQPYKETALR------ANLGYLNANYIQV---IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLAS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  999 EEEGG--REKSFRYWPRLGSrhntvtYGRFKI------TTRFRTDSGCYATTgLKMKHllTGQE-RTVWHLQYTDWPEHG 1069
Cdd:COG5599   111 DDEISkpKVKMPVYFRQDGE------YGKYEVsselteSIQLRDGIEARTYV-LTIKG--TGQKkIEIPVLHVKNWPDHG 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1070 CPEDlkgflSYLEEIQSVRRHTNSTSDPqsPNPPLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDI---PRVLDMLRQQ 1146
Cdd:COG5599   182 AISA-----EALKNLADLIDKKEKIKDP--DKLLPVVHCRAGVGRTGTLIACLALSKSINALVQITLsveEIVIDMRTSR 254

                         250       260
                  ....*....|....*....|
gi 767979565 1147 RMMLVQTLCQYTFVYRVLIQ 1166
Cdd:COG5599   255 NGGMVQTSEQLDVLVKLAEQ 274
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 106-220 1.09e-29

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 114.29  E-value: 1.09e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   106 PSVSQLQQEITRYQYYLQLKKDILEGSIPCTLEQAIQLAGLAVQADFGDFDQYESQ-DFLQKFALFPVgWLQDEKVLEEA 184
Cdd:pfam00373    1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTsEYLSLESFLPK-QLLRKMKSKEL 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 767979565   185 TQKVALLHQKYRGLTAPDAEMLYMQEVERMDGYGEE 220
Cdd:pfam00373   80 EKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVE 115
FERM_C pfam09380
FERM C-terminal PH-like domain;
226-308 2.44e-27

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 106.18  E-value: 2.44e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   226 DSQGSDISIGACLEGIFVKHKNGRHPVVFRWHDIANMSHNKSFFALELANK--EETIQFQTEDMETAKYIWRLCVARHKF 303
Cdd:pfam09380    1 DKEGTDLWLGVSAKGILVYEDNNKILNLFPWREIRKISFKRKKFLIKLRDKssEETLGFYTESSRACKYLWKLCVEQHTF 80


                   ....*
gi 767979565   304 YRLNQ 308
Cdd:pfam09380   81 FRLRR 85
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 116-214 6.47e-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: 105.79  E-value: 6.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  116 TRYQYYLQLKKDILEGSIPCTLEQAIQLAGLAVQADFGDFDQYESQD-FLQKFALFPVgWLQDEKVLEEATQKVALLHQK 194
Cdd:cd14473     1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPkYLSLKRFLPK-QLLKQRKPEEWEKRIVELHKK 79

                          90       100
                  ....*....|....*....|
gi 767979565  195 YRGLTAPDAEMLYMQEVERM 214
Cdd:cd14473    80 LRGLSPAEAKLKYLKIARKL 99
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 950-1161 5.18e-25

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: 104.03  E-value: 5.18e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  950 YINA----SHIKVSVsgiewdYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTaEEEGGREKSFRYWPRLGSRhntvTYGR 1025
Cdd:cd14556     1 YINAalldSYKQPAA------FIVTQHPLPNTVTDFWRLVYDYGCTSIVMLN-QLDPKDQSCPQYWPDEGSG----TYGP 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1026 FKITTRFRTDSGCYATTGLKMKHLLTGQE--RTVWHLQYTDWPEHG-CPEDLKGFLSYLEEIQSVRRhtnstsdpQSPNP 1102
Cdd:cd14556    70 IQVEFVSTTIDEDVISRIFRLQNTTRPQEgyRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQE--------QSGEG 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767979565 1103 PLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVY 1161
Cdd:cd14556   142 PIVVHCLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
 23-103 4.73e-19

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: 82.64  E-value: 4.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   23 LVARIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQLDKYAlEPTVYFGVV 102
Cdd:cd01765     1 ISCRVRLLDGTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFYEDNDGQKHWLDLDKKISKQLKRSG-PYQFYFRVK 79


                  .
gi 767979565  103 F 103
Cdd:cd01765    80 F 80
FERM_N pfam09379
FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the ...
 27-89 6.63e-18

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: 78.79  E-value: 6.63e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767979565    27 IQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQLD 89
Cdd:pfam09379    1 VRLLDGTVLEFDVQPKATGQVLLDQVCNHLNLKEKDYFGLQFLDDNGEHRWLDLSKRLSKQAP 63
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 218-305 1.12e-17

FERM domain C-lobe; 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: 275389  Cd Length: 93  Bit Score: 78.96  E-value: 1.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  218 GEESYPAKDSQ--GSDISIGACLEGI-FVKHKNGRHPVVFRWHDIANMSHNK-SFFALELAN--KEETIQFQTEDMEtAK 291
Cdd:cd00836     1 GVEFFPVKDKSkkGSPIILGVNPEGIsVYDELTGQPLVLFPWPNIKKISFSGaKKFTIVVADedKQSKLLFQTPSRQ-AK 79

                          90
                  ....*....|....
gi 767979565  292 YIWRLCVARHKFYR 305
Cdd:cd00836    80 EIWKLIVGYHRFLL 93
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 964-1169 4.24e-17

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 83.48  E-value: 4.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  964 EWDYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEggrEKSF-RYWprlGSRHNTV-TYGRFKITTRFRTDSGCYAT 1041
Cdd:PHA02740   90 EQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHAD---KKCFnQFW---SLKEGCViTSDKFQIETLEIIIKPHFNL 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1042 TGLKMKHLLtGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQS----VRRHTNSTSdpqspNPPLLVHCSAGVGRTGV 1117
Cdd:PHA02740  164 TLLSLTDKF-GQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDlcadLEKHKADGK-----IAPIIIDCIDGISSSAV 237

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767979565 1118 VILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQFLK 1169
Cdd:PHA02740  238 FCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLK 289
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 950-1161 1.08e-15

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: 76.98  E-value: 1.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  950 YINASHIKVSVSGIEwdYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEggREKSFRYWPrlgSRHNTVTYGRFKIT 1029
Cdd:cd14550     1 YINASYLQGYRRSNE--FIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNEL--NEDEPIYWP---TKEKPLECETFKVT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1030 TRFRTDSGCYATTGLKMKHLL--TGQER---TVWHLQYTDWPeHGCPEDLKGFlsylEEIQSVRRHTNSTsdpqspNPPL 1104
Cdd:cd14550    74 LSGEDHSCLSNEIRLIVRDFIleSTQDDyvlEVRQFQCPSWP-NPCSPIHTVF----ELINTVQEWAQQR------DGPI 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767979565 1105 LVH-----CSAGVgrtgVVILSEIMIAcLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVY 1161
Cdd:cd14550   143 VVHdryggVQAAT----FCALTTLHQQ-LEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 950-1165 3.20e-15

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: 75.87  E-value: 3.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  950 YINASHIKVSVSGIEwdYIATQGPLQNTCQDFWQMVWEQGIAIIAMVtAEEEGGREKSFRYWPrlgSRHNTVTYGRFKIT 1029
Cdd:cd17670     1 YINASYIMGYYRSNE--FIITQHPLPHTTKDFWRMIWDHNAQIIVML-PDNQGLAEDEFVYWP---SREESMNCEAFTVT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1030 TrFRTDSGCYATTGLKMKH---LLTGQERTVW---HLQYTDWPEHGCPedlkgfLSYLEEIQSVRRHTNSTSDpqspnPP 1103
Cdd:cd17670    75 L-ISKDRLCLSNEEQIIIHdfiLEATQDDYVLevrHFQCPKWPNPDAP------ISSTFELINVIKEEALTRD-----GP 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767979565 1104 LLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLI 1165
Cdd:cd17670   143 TIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 967-1166 3.64e-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: 75.72  E-value: 3.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  967 YIATQGPLQNTCQDFWQMVWEQGIAIIAMVTA-EEEGGREKSFRYWPRLGSRHntvtYGRFK------------ITTRFR 1033
Cdd:cd14637    16 FIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQlNQSNSAWPCLQYWPEPGLQQ----YGPMEvefvsgsadediVTRLFR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1034 TDSgcyaTTGLKMKHLLtgqertVWHLQYTDW-PEHGCPEDLKGFLSYLEEIQSVRRhtnstsdpQSPNPPLLVHCSAGV 1112
Cdd:cd14637    92 VQN----ITRLQEGHLM------VRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQR--------ESGEGRTVVHCLNGG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767979565 1113 GRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1166
Cdd:cd14637   154 GRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
FERM_F1_EPB41L4A cd17107
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 26-105 5.48e-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: 68.52  E-value: 5.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   26 RIQLLNNEfvEFTLSVE------STGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQLDKYALEPTVYF 99
Cdd:cd17107     6 EIVLLDES--ELILTIQqdgiksSKGSVVLDVVFQHLNLLETDYFGLRYIDRQHQTHWLDPAKTLSEQLKLIGPPYTLYF 83


                  ....*.
gi 767979565  100 GVVFYV 105
Cdd:cd17107    84 GVKFYA 89
FERM_C_4_1_family cd13184
FERM domain C-lobe of Protein 4.1 family; The protein 4.1 family includes four well-defined ...
 217-306 1.09e-13

FERM domain C-lobe of Protein 4.1 family; The protein 4.1 family includes four well-defined members: erythroid protein 4.1 (4.1R), the best known and characterized member, 4.1G (general), 4.1N (neuronal), and 4.1 B (brain). The less well understood 4.1O/FRMD3 is not a true member of this family and is not included in this hierarchy. Besides three highly conserved domains, FERM, SAB (spectrin and actin binding domain) and CTD (C-terminal domain), the proteins from this family contain several unique domains: U1, U2 and U3. FERM domains like other members of the FERM domain superfamily have a cloverleaf architecture with three distinct lobes: (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 brain is a particularly rich source of protein 4.1 isoforms. The various 4.1R, 4.1G, 4.1N, and 4.1B mRNAs are all expressed in distinct patterns within the brain. It is likely that 4.1 proteins play important functional roles in the brain including motor coordination and spatial learning, postmitotic differentiation, and synaptic architecture and function. In addition they are found in nonerythroid, nonneuronal cells where they may play a general structural role in nuclear architecture and/or may interact with splicing factors. 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: 270005  Cd Length: 94  Bit Score: 67.73  E-value: 1.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  217 YGEESYPAKDSQGSDISIGACLEGIFVkHKNGRHPVVFRWHDIANMSHNKSFFAL-----ELANKEETIQFQTEDMETAK 291
Cdd:cd13184     1 YGVDLHPAKDSEGVDIMLGVCSSGLLV-YRDRLRINRFAWPKVLKISYKRNNFYIkirpgEFEQYETTIGFKLPNHRAAK 79

                          90
                  ....*....|....*
gi 767979565  292 YIWRLCVARHKFYRL 306
Cdd:cd13184    80 RLWKVCVEHHTFFRL 94
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 950-1165 1.97e-13

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: 70.41  E-value: 1.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  950 YINASHIKVSVSGIEwdYIATQGPLQNTCQDFWQMVWEQGIAIIAMVtAEEEGGREKSFRYWPrlgSRHNTVTYGRFKIT 1029
Cdd:cd17669     1 YINASYIMGYYQSNE--FIITQHPLLHTIKDFWRMIWDHNAQLIVML-PDGQNMAEDEFVYWP---NKDEPINCETFKVT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1030 TrFRTDSGCYAT-TGLKMKHLLTGQER-----TVWHLQYTDWPEHGCPedlkgfLSYLEEIQSVRRHTNSTSDpqspnPP 1103
Cdd:cd17669    75 L-IAEEHKCLSNeEKLIIQDFILEATQddyvlEVRHFQCPKWPNPDSP------ISKTFELISIIKEEAANRD-----GP 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767979565 1104 LLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLI 1165
Cdd:cd17669   143 MIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 950-1166 3.63e-13

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: 69.66  E-value: 3.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  950 YINA----SHIKVSVsgiewdYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTaeEEGGREKSFRYWPRLGSrhntVTYGR 1025
Cdd:cd14634     1 YINAalmdSHKQPAA------FIVTQHPLPNTVADFWRLVFDYNCSSVVMLN--EMDAAQLCMQYWPEKTS----CCYGP 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1026 FKITTRFRTDSGCYATTGLKMKHLLTGQE--RTVWHLQYTDWPEH-GCPEDLKGFLsyleeiQSVRRHTNSTSDPQSPNP 1102
Cdd:cd14634    69 IQVEFVSADIDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSIL------KVVRRLEKWQEQYDGREG 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767979565 1103 PLLVHCSAGVGRTGVVILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1166
Cdd:cd14634   143 RTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
FERM_F1_FARP1_like cd17098
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, RhoGEF and ...
 26-106 1.02e-12

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: 64.54  E-value: 1.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   26 RIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQLdKYALEPTVYFGVVFYV 105
Cdd:cd17098     4 KVQMLDDTVHIFQVQQKALGEVLFDQVCKHLNLLESDYFGLEFTDPEGNKCWLDPEKPILRQV-KRPKDVVFKFVVKFYT 82


                  .
gi 767979565  106 P 106
Cdd:cd17098    83 P 83
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 967-1166 3.33e-12

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 66.97  E-value: 3.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  967 YIATQGPLQNTCQDFWQMVWEQGIAIIAMVTaeEEGGREKSFRYWPRLGsrhnTVTYGRFKITTrFRTDSGCYATTGL-K 1045
Cdd:cd14636    16 FIVTQHPLPNTVKDFWRLVYDYGCTSIVMLN--EVDLAQGCPQYWPEEG----MLRYGPIQVEC-MSCSMDCDVISRIfR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1046 MKHLLTGQE--RTVWHLQYTDWPEH-GCPEDLKGFLSYLEEIQSVRRHTNSTSDPQspnpplLVHCSAGVGRTGVVILSE 1122
Cdd:cd14636    89 ICNLTRPQEgyLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECDEGEGRT------IIHCLNGGGRSGMFCAIS 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 767979565 1123 IMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1166
Cdd:cd14636   163 IVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
FERM_F1_PTPN3_like cd17100
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 22-105 4.12e-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: 4.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   22 CLVariQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQN---QRRWVDLEKPLKKQLdKYALEPTVY 98
Cdd:cd17100     4 CIV---HFLDDTEQTFEVEKRDKGQVLLDKVFNHLELVEKDYFGLQFSDDSPatdSMRWLDPLKPIRKQI-KGGPPYYLN 79


                  ....*..
gi 767979565   99 FGVVFYV 105
Cdd:cd17100    80 FRVKFYV 86
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 967-1166 8.69e-11

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: 62.78  E-value: 8.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  967 YIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGgrEKSFRYWPRLG-SRHNTVTYGRFK-------ITTRFRTDSGC 1038
Cdd:cd14635    16 FIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPA--QLCPQYWPENGvHRHGPIQVEFVSadleediISRIFRIYNAA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1039 YATTGLKMkhlltgqertVWHLQYTDWPEH-GCPEDLKGFLSYLEEIQSVRRHTNSTSDPQspnpplLVHCSAGVGRTGV 1117
Cdd:cd14635    94 RPQDGYRM----------VQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNGGEGRT------VVHCLNGGGRSGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 767979565 1118 VILSEIMIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYRVLIQ 1166
Cdd:cd14635   158 FCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
FERM_C_FRMD3_FRMD5 cd13192
FERM domain C-lobe of FERM domain-containing protein 3 and 5 (FRMD3 and 5); FRMD3 (also called ...
 203-305 1.30e-09

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: 56.63  E-value: 1.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  203 AEMLYMQEVERMDGYGEESYPAKDSQGSDISIGACLEGIFVkHKNGRHPVVFRWHDIANMSHNKSFFALELANKEE---T 279
Cdd:cd13192     1 AEDNFLRKAATLETYGVDPHPVKDHRGNQLYLGFTHTGIVT-FQGGKRVHHFRWNDITKFNYEGKMFILHVMQKEEkkhT 79

                          90       100
                  ....*....|....*....|....*.
gi 767979565  280 IQFQTEDMETAKYIWRLCVARHKFYR 305
Cdd:cd13192    80 LGFKCPTPAACKHLWKCAVEQQAFYT 105
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 951-1157 1.63e-09

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 59.34  E-value: 1.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  951 INASHIKVSVSGIewdYIATQGPLQNTCQDFWQMVWEQGIAIIAMVTAEEEGGREKSFRYWPRLGsrhntvTYGRFKITT 1030
Cdd:cd14559    18 LNANRVQIGNKNV---AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFRQSG------TYGSVTVKS 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1031 RfRTDSGcYATTGLKMKHL---LTGQERT----VWHLqyTDWPEHGC--PEDLKGFLSYLEeiQSVRRHTN-----STSD 1096
Cdd:cd14559    89 K-KTGKD-ELVDGLKADMYnlkITDGNKTitipVVHV--TNWPDHTAisSEGLKELADLVN--KSAEEKRNfykskGSSA 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767979565 1097 PQSPNPPL-LVHCSAGVGRTGVVILSEIMIaclEHNEVLDIPRVLDMLRQQR-MMLVQTLCQY 1157
Cdd:cd14559   163 INDKNKLLpVIHCRAGVGRTGQLAAAMELN---KSPNNLSVEDIVSDMRTSRnGKMVQKDEQL 222
FERM_C_PTPN4_PTPN3_like cd13189
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and ...
 217-306 3.90e-09

FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and PTPN3); PTPN4 (also called PTPMEG, protein tyrosine phosphatase, megakaryocyte) is a cytoplasmic protein-tyrosine phosphatase (PTP) thought to play a role in cerebellar function. PTPMEG-knockout mice have impaired memory formation and cerebellar long-term depression. PTPN3/PTPH1 is a membrane-associated PTP that is implicated in regulating tyrosine phosphorylation of growth factor receptors, p97 VCP (valosin-containing protein, or Cdc48 in Saccharomyces cerevisiae), and HBV (Hepatitis B Virus) gene expression; it is mutated in a subset of colon cancers. PTPMEG and PTPN3/PTPH1 contains a N-terminal FERM domain, a middle PDZ domain, and a C-terminal phosphatase domain. PTP1/Tyrosine-protein phosphatase 1 from nematodes and a FERM_C repeat 1 from Tetraodon nigroviridis are also included in this cd. 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 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: 270010  Cd Length: 95  Bit Score: 55.01  E-value: 3.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  217 YGEESYPAKDSQGSDISIGACLEGIFVKHkNGRHPVVFRWHDIANMSHNKSFFALELANK----EETI-QFQTEDMETAK 291
Cdd:cd13189     2 YGVELHSARDSNNLELQIGVSSAGILVFQ-NGIRINTFPWSKIVKISFKRKQFFIQLRREpnesRDTIlGFNMLSYRACK 80

                          90
                  ....*....|....*
gi 767979565  292 YIWRLCVARHKFYRL 306
Cdd:cd13189    81 NLWKSCVEHHTFFRL 95
FERM_C_PTPH13 cd13187
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many ...
 222-303 4.32e-09

FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many functions of PTPN13 (also called PTPL1, PTP-BAS, hPTP1E, FAP1, or PTPL1). Mice lacking PTPN13 activity have abnormal regulation of signal transducer and activator of transcription signaling in their T cells, mild impairment of motor nerve repair, and a significant reduction in the growth of retinal glia cultures. It also plays a role in adipocyte differentiation. PTPN13 contains a kinase non-catalytic C-lobe domain (KIND), a FERM domain with two potential phosphatidylinositol 4,5-biphosphate [PtdIns(4,5)P2]-binding motifs, 5 PDZ domains, and a carboxy-terminal catalytic domain. There is an nteraction between the FERM domain of PTPL1 and PtdIns(4,5)P2 which is thought to regulate the membrane localization of PTPN13. PDZ are protein/protein interaction domains so there is the potential for numerous partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated PTPL1 substrates. 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: 270008  Cd Length: 103  Bit Score: 55.02  E-value: 4.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  222 YPAKDSQGSDISIGACLEGIFV--KHKNGRHPVV-FRWHDIANMSHNKSFFALElANKEETIQ--FQTEDMETAKYIWRL 296
Cdd:cd13187     8 YREKKSSTLSLWLGICSRGIIIyeEKNGARTPVLrFPWRETQKISFDKKKFTIE-SRGGSGIKhtFYTDSYKKSQYLLQL 86


                  ....*..
gi 767979565  297 CVARHKF 303
Cdd:cd13187    87 CSAQHKF 93
FERM_F1_ERM_like cd17097
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 35-104 2.56e-08

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: 52.28  E-value: 2.56e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   35 VEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQLDKYALEPTVYFGVVFY 104
Cdd:cd17097    12 LEFSIKPKAKGRELFDLVCRTIGLRETWYFGLQYENKKGRVAWLKPDKKVLTQDVSKNNTLKFFFLVKFY 81
FERM_F1_EPB41L5_like cd17108
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 23-104 3.00e-08

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


Pssm-ID: 340628  Cd Length: 81  Bit Score: 51.97  E-value: 3.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   23 LVARIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQLdKYALEPTVYFGVV 102
Cdd:cd17108     1 IQCKVILLDGTDLSIELPKKAKGQELYEQVFYHLDLIEKDYFGLQFMDAAQVQHWLDPTKKIKKQV-KIGPPYTLRFRVK 79


                  ..
gi 767979565  103 FY 104
Cdd:cd17108    80 FY 81
FERM_F1_EPB41L3 cd17203
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 23-106 9.90e-08

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: 50.71  E-value: 9.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   23 LVARIQLLNNEfvEFTLSVE--STGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQLDKYALEPTvyFG 100
Cdd:cd17203     2 MQCKVTLLDGS--EYTCEVEkrSKGQVLFDKVCEHLNLLEKDYFGLTYRDSENQKNWLDPAKEIKKQIRSGAWQFS--FN 77


                  ....*.
gi 767979565  101 VVFYVP 106
Cdd:cd17203    78 VKFYPP 83
FERM_F1_MYLIP cd17104
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in E3 ...
 22-99 1.86e-07

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: 49.58  E-value: 1.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   22 CLVARiqlLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQLD---KYALEPTVY 98
Cdd:cd17104     3 CLVSQ---PDSVVIEVEVDPKANGQECLDKVCQKLGIIEKDYFGLQYTGPKGERLWLNLRNRISRQLPgppPYRLRLRVK 79


                  .
gi 767979565   99 F 99
Cdd:cd17104    80 F 80
FERM_F1_FRMD3 cd17102
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 27-104 1.95e-07

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: 49.55  E-value: 1.95e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767979565   27 IQLL-NNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQLdKYALEPTVYFGVVFY 104
Cdd:cd17102     5 IRLLdDSEVICCEFKKDTKGQFLLDYVCNYLNLLEKDYFGLRYVDTEKQRHWLDPNKSIYKQL-KGVPPYVLCFRVKFY 82
FERM_F1_EPB41L4B cd17204
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 23-104 2.36e-07

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: 49.43  E-value: 2.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   23 LVARIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQLdKYALEPTVYFGVV 102
Cdd:cd17204     1 LTCRVLLLDGTDVSVELPKHAKGQDLFDQIVYHLDLVETDYFGLQFMDAAQVAHWLDHTKPIKKQI-KIGPPYTLHFRIK 79


                  ..
gi 767979565  103 FY 104
Cdd:cd17204    80 YY 81
FERM_F1_EPB41L cd17106
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 24-106 3.95e-07

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: 48.98  E-value: 3.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   24 VARIQLLNNefVEFTLSVE--STGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQLDKYALepTVYFGV 101
Cdd:cd17106     3 QCKVLLLDG--TEYTCEVEkrAKGQVLFDKVCEHLNLLEKDYFGLTYRDAQDQKNWLDPAKEIKKQIRSGPW--LFSFNV 78


                  ....*
gi 767979565  102 VFYVP 106
Cdd:cd17106    79 KFYPP 83
FERM_F1_EPB41 cd17105
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 26-106 8.71e-07

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: 47.88  E-value: 8.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   26 RIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQLDKYALEPTvyFGVVFYV 105
Cdd:cd17105     4 KVSLLDDTVYECEVEKHAKGQDLFKKVCEHLNLLEEDYFGLAIWDSPTSKTWLDPAKEIKKQVHGGPWEFT--FNVKFYP 81


                  .
gi 767979565  106 P 106
Cdd:cd17105    82 P 82
FERM_F1_PTPN4 cd17194
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 23-105 1.89e-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: 46.83  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   23 LVARIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQ-NQRRWVDLEKPLKKQLdKYALEPTVYFGV 101
Cdd:cd17194     2 VVCNILLLDNTVQAFKVNKHDQGQVLLDLVFKHLDLTERDYFGLQLADDStDNPRWLDPNKPIRKQL-KRGSPHNLNFRV 80


                  ....
gi 767979565  102 VFYV 105
Cdd:cd17194    81 KFFV 84
FERM_C_ERM cd13194
FERM domain C-lobe/F3 of the ERM family; The ERM family includes ezrin, radixin, moesin and ...
 217-304 1.01e-05

FERM domain C-lobe/F3 of the ERM family; The ERM family includes ezrin, radixin, moesin and merlin. They are composed of a N-terminal FERM (ERM) domain (also called N-ERMAD (N-terminal ERM association domain)), a coiled coil region (CRR), and a C-terminal domain CERMAD (C-terminal ERM association domain) which has an F-actin-binding site (ABD). Two actin-binding sites have been identified in the middle and N-terminal domains. Merlin is structurally similar to the ERM proteins, but instead of an actin-binding domain (ABD), it contains a C-terminal domain (CTD), just like the proteins from the 4.1 family. Activated ezrin, radixin and moesin are thought to be involved in the linking of actin filaments to CD43, CD44, ICAM1-3 cell adhesion molecules, various membrane channels and receptors, such as the Na+/H+ exchanger-3 (NHE3), cystic fibrosis transmembrane conductance regulator (CFTR), and the beta2-adrenergic receptor. The ERM proteins 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 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 of ERM 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: 270015  Cd Length: 97  Bit Score: 45.34  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  217 YGEESYPAKDSQGSDISIGACLEGIFVKHKNGR-HPVV-FRWHDIANMS-HNKSFFALELANKEETIQFQTEDMETAKYI 293
Cdd:cd13194     2 YGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKlTPKIgFPWSEIRNISfNDKKFVIKPIDKKAPDFVFYSPRLRINKRI 81

                          90
                  ....*....|.
gi 767979565  294 WRLCVARHKFY 304
Cdd:cd13194    82 LDLCMGNHELY 92
FERM_C_NBL4_NBL5 cd13186
FERM domain C-lobe of Novel band 4.1-like protein 4 and 5 (NBL4 and 5); NBL4 (also called ...
 218-305 1.13e-05

FERM domain C-lobe of Novel band 4.1-like protein 4 and 5 (NBL4 and 5); NBL4 (also called Erythrocyte protein band 4.1-like 4; Epb4 1l4) plays a role the beta-catenin/Tcf signaling pathway and is thought to be involved in establishing the cell polarity or proliferation. NBL4 may be also involved in adhesion, in cell motility and/or in cell-to-cell communication. No role for NBL5 has been proposed to date. Both NBL4 and NBL5 contain a N-terminal FERM domain which 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 is a member of the PH superfamily. 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: 270007  Cd Length: 92  Bit Score: 44.97  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  218 GEESYPAKDSQGSDISIGACLEGIFV---KHKNGrhpvVFRWHDIANMSHNKSFFALELANKEETIQ-----FQTEDMET 289
Cdd:cd13186     1 GVDLHPVKGEDGNEYFLGLTPTGILVfenKTKIG----LFFWPRITKLDFKGKKLKLVVKEKDDQEQehtfvFRLPNKKA 76

                          90
                  ....*....|....*.
gi 767979565  290 AKYIWRLCVARHKFYR 305
Cdd:cd13186    77 CKHLWKCAVEHHAFFR 92
FERM_F1_EPB41L2 cd17202
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 26-106 1.16e-05

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: 44.58  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   26 RIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQLDKYalePTVY-FGVVFY 104
Cdd:cd17202     5 KVTLLDGTEYSCDLEKRAKGQVLFDKVCEHLNLLEKDYFGLLYQVSANQKNWLDSTKEIKRQIRRL---PWLFtFNVKFY 81


                  ..
gi 767979565  105 VP 106
Cdd:cd17202    82 PP 83
FERM_F1_EPB41L1 cd17201
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 26-106 1.26e-05

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: 44.49  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   26 RIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQLDKYALepTVYFGVVFYV 105
Cdd:cd17201     5 KVTLLDGSEYECEVEKHARGQVLFDTVCEHLNLLEKDYFGLTFCDTESQKNWLDPSKEIKKQIRSGPW--HFAFTVKFYP 82


                  .
gi 767979565  106 P 106
Cdd:cd17201    83 P 83
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1070-1162 2.16e-05

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: 44.65  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1070 CPEDLKGFLSYLEEiqsvrrhtnstsdPQSPNPPLLVHCSAGVGRTGVVILseIMIACLEHNEVLDIprvLDMLRQQR-M 1148
Cdd:cd14494    38 TLAMVDRFLEVLDQ-------------AEKPGEPVLVHCKAGVGRTGTLVA--CYLVLLGGMSAEEA---VRIVRLIRpG 99

                          90
                  ....*....|....
gi 767979565 1149 MLVQTLCQYTFVYR 1162
Cdd:cd14494   100 GIPQTIEQLDFLIK 113
FERM_F1_PTPN13_like cd17101
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 27-107 2.60e-05

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: 44.09  E-value: 2.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   27 IQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYnKQNQRRWVDLEKPL------------KKQLDKYALE 94
Cdd:cd17101     6 VVLLNGQRLQVAVDVKTTVQDLFDQVCDHLGLQETELFGLAVL-KDGEYFFLDPDTKLskyapkgwkseaKKGLKGGKPV 84

                          90
                  ....*....|...
gi 767979565   95 PTVYFGVVFYVPS 107
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 ...
 26-88 2.93e-05

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: 43.63  E-value: 2.93e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767979565   26 RIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQL 88
Cdd:cd17190     4 RVKLLDNTTEPLEIEPKADGQALLSQVFKRLNLVESDYFGLEFQNSQSNWIWLEPMKLIVKQV 66
FERM_C_FARP1-like cd13193
FERM domain C-lobe of FERM, RhoGEF and pleckstrin domain-containing protein 1 and related ...
 211-308 3.60e-05

FERM domain C-lobe of FERM, RhoGEF and pleckstrin domain-containing protein 1 and related proteins; Members here include FARP1 (also called Chondrocyte-derived ezrin-like protein; PH domain-containing family C member 2), FARP2 (also called FIR/FERM domain including RhoGEF; FGD1-related Cdc42-GEF/FRG), and FRMD7(FERM domain containing 7). FARP1 and FARP2 are members of the Dbl family guanine nucleotide exchange factors (GEFs) which are upstream positive regulators of Rho GTPases. FARP1 has increased expression in differentiated chondrocytes. FARP2 is thought to regulate neurite remodeling by mediating the signaling pathways from membrane proteins to Rac. It is found in brain, lung, and testis, as well as embryonic hippocampal and cortical neurons. These members are composed of a N-terminal FERM domain, a proline-rich (PR) domain, Dbl-homology (DH), and two C-terminal PH domains. Other members in this family do not contain the DH domains such as the Human FERM domain containing protein 7 and Caenorhabditis elegans CFRM3, both of which have unknown functions. They contain an N-terminal FERM domain, a PH domain, followed by a FA (FERM adjacent) 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. 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: 270014  Cd Length: 122  Bit Score: 44.26  E-value: 3.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  211 VERMDGYGEESYPAKDSQGSDISIGACLEGIFVKHKNGRHPVvFRWHDIANMSHNKSFFALELANKE-----ETIQFQTE 285
Cdd:cd13193     3 ARRCELYGIRLHPAKDREGVKLNLAVAHMGILVFQGFTKINT-FSWAKIRKLSFKRKRFLIKLHPEAygsykDTVEFSFE 81

                          90       100
                  ....*....|....*....|...
gi 767979565  286 DMETAKYIWRLCVARHKFYRLNQ 308
Cdd:cd13193    82 SRNECKSFWKKCIEHHAFFRCSE 104
FERM_F1_FRMD4B cd17200
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 26-108 4.32e-05

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: 43.34  E-value: 4.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   26 RIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLE-KPLKKQLDKYALEPTVYFGVVFY 104
Cdd:cd17200     6 QVHLLDDRKLELLVQPKLLSRELLDLVASHFNLKEKEYFGITFIDDTGQSNWLQLDhRVLDHDLPKKSGPVTLYFAVRFY 85


                  ....
gi 767979565  105 VPSV 108
Cdd:cd17200    86 IESI 89
FERM_F1_EPB41L5 cd17205
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 21-99 4.79e-05

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: 43.10  E-value: 4.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   21 SCLVARIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQLD---KYALEPTV 97
Cdd:cd17205     1 SIITCRVSLLDGTDVSVDLPKKAKGQELFEQIMYHLDLIEKDYFGLRFMDSAQVAHWLDVTKSIKKQVKigpPYCLHLRV 80


                  ..
gi 767979565   98 YF 99
Cdd:cd17205    81 KF 82
FERM_F1_FARP1 cd17189
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 26-106 9.79e-05

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: 42.10  E-value: 9.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   26 RIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQLDKyALEPTVYFGVVFYV 105
Cdd:cd17189     4 KVQMLDDTQEVFEVPQRAPGKVLLDAVCSHLNLVEGDYFGLEFQDHRKVMVWLDLLKPIVKQIRR-PKHVVLRFVVKFFP 82


                  .
gi 767979565  106 P 106
Cdd:cd17189    83 P 83
FERM_F1_FRMD4 cd17103
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 25-108 1.24e-04

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: 41.88  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   25 ARIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEK-------PLKKQLDKYALeptv 97
Cdd:cd17103     5 CQVVLLDDRRLEILVQPKLLAGDLLDLVASHFNLKEKEYFGLAYEDETGHYNWLQLDKrvldhefPKKWSSGPLVL---- 80

                          90
                  ....*....|.
gi 767979565   98 YFGVVFYVPSV 108
Cdd:cd17103    81 HFAVKFYVESI 91
FERM_F1_PTPN3 cd17193
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 23-105 1.92e-04

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: 41.38  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   23 LVARIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQ-NQRRWVDLEKPLKKQLdKYALEPTVYFGV 101
Cdd:cd17193     2 VICNVHFLDGSVQSFKVNKQDTGQVLLDMAYNHLGLTEREYFGLQHNEDSvDSPRWLEPSKPIRKQL-KGGFPCSLHFRV 80


                  ....
gi 767979565  102 VFYV 105
Cdd:cd17193    81 RFFI 84
FERM_F1_Ezrin cd17239
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Ezrin and ...
 26-87 3.36e-04

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Ezrin and similar proteins; Ezrin, also termed cytovillin, or villin-2, or p81, 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). Ezrin is a tyrosine kinase substrate that functions as a cross-linker between actin cytoskeleton and plasma membrane. It has been implicated in the regulation of the proliferation, apoptosis, adhesion, invasion, metastasis and angiogenesis of cancer cells.


Pssm-ID: 340759  Cd Length: 85  Bit Score: 40.74  E-value: 3.36e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767979565   26 RIQLLNNEfVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQ 87
Cdd:cd17239     6 RVTTMDAE-LEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLQYVDNKGFPTWLKLDKKVSAQ 66
FERM_F1_FRMD7 cd17188
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 26-107 5.77e-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: 39.79  E-value: 5.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   26 RIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQLdKYALEPTVYFGVVFYV 105
Cdd:cd17188     5 KVQFLDDSQKVFVVDQKSTGKDLFNMSCSHLNLVEKEYFGLEFRNHAGNNVWLELLKPITKQI-KNPKELIFKFTVKFFP 83


                  ..
gi 767979565  106 PS 107
Cdd:cd17188    84 VD 85
FERM_F1_Merlin cd17186
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in merlin and ...
 20-104 6.11e-04

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: 39.67  E-value: 6.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   20 KSCLVaRIQLLNNEfVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQlDKYALEP-TVY 98
Cdd:cd17186     1 KTFTV-RIVTMDAE-MEFNCEMKWKGKDLFDLVCRTIGLRETWYFGLQYTDSKGTVAWLKMDKKVLDQ-DVPKEEPvTFH 77


                  ....*.
gi 767979565   99 FGVVFY 104
Cdd:cd17186    78 FLAKFY 83
FERM_F1_Radixin cd17238
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in radixin and ...
 26-87 6.97e-04

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in radixin and similar proteins; Radixin 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 the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Radixin plays important roles in cell polarity, cell motility, invasion and tumor progression. It mediates the binding of F-actin to the plasma membrane after a conformational activation through Akt2-dependent phosphorylation at Thr564. It is also involved in reversal learning and short-term memory by regulating synaptic GABAA receptor density.


Pssm-ID: 340758 [Multi-domain]  Cd Length: 83  Bit Score: 39.72  E-value: 6.97e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767979565   26 RIQLLNNEfVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQ 87
Cdd:cd17238     4 RVTTMDAE-LEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLKLNKKVTQQ 64
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1104-1162 1.03e-03

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 41.09  E-value: 1.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767979565 1104 LLVHCSAGVGRTGVVilseimIAC--LEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYR 1162
Cdd:cd14505   109 VLIHCKGGLGRTGLI------AACllLELGDTLDPEQAIAAVRALRPGAIQTPKQENFLHQ 163
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1103-1162 2.09e-03

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 39.57  E-value: 2.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565 1103 PLLVHCSAGVGRTGVVilseimIACLEHNEVLDIPRVLDMLRQQRMMLVQTLCQYTFVYR 1162
Cdd:COG2453    82 KVLVHCRGGIGRTGTV------AAAYLVLLGLSAEEALARVRAARPGAVETPAQRAFLER 135
FERM_C_MYLIP_IDOL cd13195
FERM domain C-lobe of E3 ubiquitin ligase myosin regulatory light chain-interacting protein ...
 217-305 2.35e-03

FERM domain C-lobe of E3 ubiquitin ligase myosin regulatory light chain-interacting protein (MYLIP; also called inducible degrader of the LDL receptor, IDOL); MYLIP/IDOL is a regulator of the LDL receptor (LDLR) pathway via the nuclear receptor liver X receptor (LXR). In response to cellular cholesterol loading, the activation of LXR leads to the induction of MYLIP expression. MYLIP stimulates ubiquitination of the LDLR on its cytoplasmic tail, directing its degradation. The LXR-MYLIP-LDLR pathway provides a complementary pathway to sterol regulatory element-binding proteins for the feedback inhibition of cholesterol uptake. MYLIP has an N-terminal FERM domain and in some cases a C-terminal RING 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. 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: 270016  Cd Length: 111  Bit Score: 38.77  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565  217 YGEESYPAKDSQGSDISIGACLEGIFVKHKNGRHPVVFRWHDI-ANMSHNKSFFA--LELANKEETIQFQTEDMETAKYI 293
Cdd:cd13195     1 YGVEFFEVRNIEGQKLLIGVGPHGITICNDDFEVIERIPYTAIqMATSSGRVFTLtyLSDDGSVKVLEFKLPSTRAASGL 80

                          90
                  ....*....|..
gi 767979565  294 WRLCVARHKFYR 305
Cdd:cd13195    81 YRAITEKHAFYR 92
FERM_F1_FRMD1 cd17197
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 26-105 2.38e-03

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: 38.63  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   26 RIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYnKQNQRRWVDLEKPLKKQL------------DKYAL 93
Cdd:cd17197     5 CVLLPNKEQLSLTVGVKATGQELFQQVCELLKIKEAHFFGLSVV-KNNEHIFMDLEQKLSKYFpkewkketgkgtEKFSI 83

                          90
                  ....*....|..
gi 767979565   94 EPTVYFGVVFYV 105
Cdd:cd17197    84 PFVACFRVQYYV 95
FERM_F1_ERM cd17187
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 26-87 2.48e-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: 2.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767979565   26 RIQLLNNEfVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQ 87
Cdd:cd17187     4 RVTTMDAE-LEFAIQPNTTGKQLFDQVVKTIGLREIWFFGLQYVDSKGYSTWLKLNKKVLSQ 64
FERM_F1_Moesin cd17237
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in moesin and ...
 26-104 4.35e-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: 37.42  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   26 RIQLLNNEfVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQlDKYALEPTVY-FGVVFY 104
Cdd:cd17237     5 RVTTMDAE-LEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQ-DVRKESPLLFkFRAKFY 82
FERM_F1_FRMD4A cd17199
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 26-108 8.11e-03

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: 36.87  E-value: 8.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979565   26 RIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKP-LKKQLDKYALEPTVYFGVVFY 104
Cdd:cd17199     6 QVHLLDDRKLELLVQPKLLAKELLDLVASHFNLKEKEYFGIAFTDETGHLNWLQLDRRvLEHDFPKKSGPVVLYFCVRFY 85


                  ....
gi 767979565  105 VPSV 108
Cdd:cd17199    86 IESI 89
 
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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