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Conserved domains on  [gi|386770278|ref|NP_001163309|]
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protein tyrosine phosphatase Meg, isoform I [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 692-961 1.43e-129

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: 389.77  E-value: 1.43e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 692 DYINANYVNMEIPG-GAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGEELQLaEGFSV 770
Cdd:cd14541    1 DYINANYVNMEIPGsGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQF-GNLQI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 771 RCLSEKPdeTGSFVFREFVLKDKH--EQRHIHHMQYLAWPDHCVPSDPNLFLEFTERVRAARnrtllqeieeslkqvrlm 848
Cdd:cd14541   80 TCVSEEV--TPSFAFREFILTNTNtgEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNR------------------ 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 849 dadadadengglmrerkcaasngatpedetpvstsvhqciSAANPPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPL 928
Cdd:cd14541  140 ----------------------------------------VGMVEPTVVHCSAGIGRTGVLITMETAMCLIEANEPVYPL 179

                        250       260       270
                 ....*....|....*....|....*....|...
gi 386770278 929 DIVRTMRDQRACMVQNVSQYRFVCECICAAYMK 961
Cdd:cd14541  180 DIVRTMRDQRAMLIQTPSQYRFVCEAILRVYEE 212
FERM_C_PTPN4_PTPN3_like cd13189
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and ...
 226-320 1.26e-55

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: 187.13  E-value: 1.26e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 226 LYGIDLHRATDSNGKELQLGVSAVGLLVFQHSLRVNTFSWSKMVKVSFKRKDFFIQLRREPSENYDTLLGFGMSSHKHAK 305
Cdd:cd13189    1 LYGVELHSARDSNNLELQIGVSSAGILVFQNGIRINTFPWSKIVKISFKRKQFFIQLRREPNESRDTILGFNMLSYRACK 80

                         90
                 ....*....|....*
gi 386770278 306 ALWKSCVEHHSFFRL 320
Cdd:cd13189   81 NLWKSCVEHHTFFRL 95
PDZ_PTPN3-4-like cd06706
PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein ...
 500-589 1.25e-49

PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein phosphatase non-receptor type 4 (PTNP4), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PTPN3, PTPN4 and related domains. PTPN3 (also known as protein-tyrosine phosphatase H1, PTP-H1) has a tumor-suppressive or a tumor-promoting role in many cancers. It serves as a specific phosphatase for the MAP kinase p38gamma; the two interact via their PDZ domains and cooperate to promote Ras-induced oncogenesis. Interaction partners of the PTPN3 PDZ domain include p38gamma and human papillomavirus E6 oncoprotein. PTPN4 (also known as protein-tyrosine phosphatase MEG1) plays a role in immunity, learning, synaptic plasticity or cell homeostasis. p38gamma is also an interaction partner of the PTPN4 PDZ domain: PTPN4 regulates neuronal cell homeostasis by protecting neurons against apoptosis; binding of the C terminus of p38gamma to the PDZ domain of PTPN4, antagonizes the catalytic autoinhibition of PTPN4, leading to cell apoptosis. Other interaction partners of the PTPN4 PDZ domain include glutamate receptor subunit GluN2A, and RABV strain G protein, among others. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN3-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


:

Pssm-ID: 467190 [Multi-domain]  Cd Length: 90  Bit Score: 169.80  E-value: 1.25e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 500 SDLITIRLQADEQGRYGFNVKGGVDLSLPVQVSKVVPHTPADRCTPRVCEGDEVLMINGRDVHGLRHEQVVAMIRDCRHQ 579
Cdd:cd06706    1 DGLVLIRMKPDENGRFGFNVKGGVDQKMPVIVSRVAPGTPADLCIPRLNEGDQVLLINGRDISEHTHDQVVMFIKASRER 80

                         90
                 ....*....|
gi 386770278 580 ASGELLLTVR 589
Cdd:cd06706   81 HSGELVLLVR 90
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 35-232 6.17e-45

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: 160.92  E-value: 6.17e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278    35 CVTVLFLDDITHTFRIEKRAKGSELLDQVFQYLELSERDYFGLLFPQKPGDVVRWVDAQKQFKKQcssvsLDNDAVPLLE 114
Cdd:smart00295   1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRHWLDPAKTLLDQ-----DVKSEPLTLY 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278   115 FRVKFFVSDPSRLQEEFTRY-QFYLQIKRNILLGKLPCSSNTQCLLASYTVQSELGDFNALEHQ-PGYLSGMQLLCDQT- 191
Cdd:smart00295  76 FRVKFYPPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDlRGELSLKRFLPKQLl 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 386770278   192 -----TEAERKVGELHKLHRGQLPADAEYNYLEHAKRLELYGIDLH 232
Cdd:smart00295 156 dsrklKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FA pfam08736
FERM adjacent (FA); This region is found adjacent to Band 4.1 / FERM domains (pfam00373) in a ...
 333-369 1.68e-13

FERM adjacent (FA); This region is found adjacent to Band 4.1 / FERM domains (pfam00373) in a subset of FERM containing protein. The region has been hypothesized to play a role in regulatory adaptation, based on similarity to other protein kinase substrates.


:

Pssm-ID: 462582  Cd Length: 44  Bit Score: 65.26  E-value: 1.68e-13
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 386770278  333 SLGSKFYYSGRTELQAVQESKQRGRIHKVFVRSPSKR 369
Cdd:pfam08736   4 SLGSKFRYSGRTQKQTVEDSSEILRPQPEFERSPSKR 40
 
Name Accession Description Interval E-value
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 692-961 1.43e-129

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: 389.77  E-value: 1.43e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 692 DYINANYVNMEIPG-GAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGEELQLaEGFSV 770
Cdd:cd14541    1 DYINANYVNMEIPGsGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQF-GNLQI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 771 RCLSEKPdeTGSFVFREFVLKDKH--EQRHIHHMQYLAWPDHCVPSDPNLFLEFTERVRAARnrtllqeieeslkqvrlm 848
Cdd:cd14541   80 TCVSEEV--TPSFAFREFILTNTNtgEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNR------------------ 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 849 dadadadengglmrerkcaasngatpedetpvstsvhqciSAANPPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPL 928
Cdd:cd14541  140 ----------------------------------------VGMVEPTVVHCSAGIGRTGVLITMETAMCLIEANEPVYPL 179

                        250       260       270
                 ....*....|....*....|....*....|...
gi 386770278 929 DIVRTMRDQRACMVQNVSQYRFVCECICAAYMK 961
Cdd:cd14541  180 DIVRTMRDQRAMLIQTPSQYRFVCEAILRVYEE 212
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
642-955 1.99e-87

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 280.70  E-value: 1.99e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278   642 LLAQYELMYR-KNPDLAITEARKPANAPKNRYRDISPYDCTRVSLVNSLT--GDYINANYVNMEIPGgavNRYIATQGPL 718
Cdd:smart00194   2 LEEEFEKLDRlKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGegSDYINASYIDGPNGP---KAYIATQGPL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278   719 ASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGEELQLAEGFSVRCLSEkpDETGSFVFREFVLKDK--HEQ 796
Cdd:smart00194  79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSV--EKVDDYTIRTLEVTNTgcSET 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278   797 RHIHHMQYLAWPDHCVPSDPNLFLEFTERVRaarnrtllqeieeslkqvrlmdadadadengglmrerkcaasngatped 876
Cdd:smart00194 157 RTVTHYHYTNWPDHGVPESPESILDLIRAVR------------------------------------------------- 187

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386770278   877 etpvstsvhQCISAANPPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRFVCECI 955
Cdd:smart00194 188 ---------KSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAI 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
666-955 8.31e-86

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 275.27  E-value: 8.31e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  666 NAPKNRYRDISPYDCTRVSLVNS-LTGDYINANYVNMEipgGAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVM 744
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDpGPSDYINASYIDGY---KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  745 ESGRQKCHQYWPVTGEELQLAEGFSVRCLSEKPDETGsFVFREFVLKDK--HEQRHIHHMQYLAWPDHCVPSDPNLFLEF 822
Cdd:pfam00102  78 EKGREKCAQYWPEEEGESLEYGDFTVTLKKEKEDEKD-YTVRTLEVSNGgsEETRTVKHFHYTGWPDHGVPESPNSLLDL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  823 TERVRAARNRTLlqeieeslkqvrlmdadadadengglmrerkcaasngatpedetpvstsvhqcisaaNPPVIVHCSAG 902
Cdd:pfam00102 157 LRKVRKSSLDGR---------------------------------------------------------SGPIVVHCSAG 179

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386770278  903 IGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRFVCECI 955
Cdd:pfam00102 180 IGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232
FERM_C_PTPN4_PTPN3_like cd13189
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and ...
 226-320 1.26e-55

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: 187.13  E-value: 1.26e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 226 LYGIDLHRATDSNGKELQLGVSAVGLLVFQHSLRVNTFSWSKMVKVSFKRKDFFIQLRREPSENYDTLLGFGMSSHKHAK 305
Cdd:cd13189    1 LYGVELHSARDSNNLELQIGVSSAGILVFQNGIRINTFPWSKIVKISFKRKQFFIQLRREPNESRDTILGFNMLSYRACK 80

                         90
                 ....*....|....*
gi 386770278 306 ALWKSCVEHHSFFRL 320
Cdd:cd13189   81 NLWKSCVEHHTFFRL 95
PDZ_PTPN3-4-like cd06706
PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein ...
 500-589 1.25e-49

PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein phosphatase non-receptor type 4 (PTNP4), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PTPN3, PTPN4 and related domains. PTPN3 (also known as protein-tyrosine phosphatase H1, PTP-H1) has a tumor-suppressive or a tumor-promoting role in many cancers. It serves as a specific phosphatase for the MAP kinase p38gamma; the two interact via their PDZ domains and cooperate to promote Ras-induced oncogenesis. Interaction partners of the PTPN3 PDZ domain include p38gamma and human papillomavirus E6 oncoprotein. PTPN4 (also known as protein-tyrosine phosphatase MEG1) plays a role in immunity, learning, synaptic plasticity or cell homeostasis. p38gamma is also an interaction partner of the PTPN4 PDZ domain: PTPN4 regulates neuronal cell homeostasis by protecting neurons against apoptosis; binding of the C terminus of p38gamma to the PDZ domain of PTPN4, antagonizes the catalytic autoinhibition of PTPN4, leading to cell apoptosis. Other interaction partners of the PTPN4 PDZ domain include glutamate receptor subunit GluN2A, and RABV strain G protein, among others. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN3-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467190 [Multi-domain]  Cd Length: 90  Bit Score: 169.80  E-value: 1.25e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 500 SDLITIRLQADEQGRYGFNVKGGVDLSLPVQVSKVVPHTPADRCTPRVCEGDEVLMINGRDVHGLRHEQVVAMIRDCRHQ 579
Cdd:cd06706    1 DGLVLIRMKPDENGRFGFNVKGGVDQKMPVIVSRVAPGTPADLCIPRLNEGDQVLLINGRDISEHTHDQVVMFIKASRER 80

                         90
                 ....*....|
gi 386770278 580 ASGELLLTVR 589
Cdd:cd06706   81 HSGELVLLVR 90
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 35-232 6.17e-45

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: 160.92  E-value: 6.17e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278    35 CVTVLFLDDITHTFRIEKRAKGSELLDQVFQYLELSERDYFGLLFPQKPGDVVRWVDAQKQFKKQcssvsLDNDAVPLLE 114
Cdd:smart00295   1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRHWLDPAKTLLDQ-----DVKSEPLTLY 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278   115 FRVKFFVSDPSRLQEEFTRY-QFYLQIKRNILLGKLPCSSNTQCLLASYTVQSELGDFNALEHQ-PGYLSGMQLLCDQT- 191
Cdd:smart00295  76 FRVKFYPPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDlRGELSLKRFLPKQLl 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 386770278   192 -----TEAERKVGELHKLHRGQLPADAEYNYLEHAKRLELYGIDLH 232
Cdd:smart00295 156 dsrklKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_F1_PTPN3_like cd17100
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 33-121 2.76e-38

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: 137.44  E-value: 2.76e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  33 QQCVTVLFLDDITHTFRIEKRAKGSELLDQVFQYLELSERDYFGLLFPQKP--GDVVRWVDAQKQFKKQCSSvsldnDAV 110
Cdd:cd17100    1 EVRCIVHFLDDTEQTFEVEKRDKGQVLLDKVFNHLELVEKDYFGLQFSDDSpaTDSMRWLDPLKPIRKQIKG-----GPP 75

                         90
                 ....*....|.
gi 386770278 111 PLLEFRVKFFV 121
Cdd:cd17100   76 YYLNFRVKFYV 86
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 655-951 8.05e-37

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 141.29  E-value: 8.05e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 655 DLAITEARKPANAPKNRYRDISPYDCTRVSLVNS--LTGDYINANYVN-MEIPggavNRYIATQGPLASTTTDFWRMVQQ 731
Cdd:PHA02747  40 DGLIANFEKPENQPKNRYWDIPCWDHNRVILDSGggSTSDYIHANWIDgFEDD----KKFIATQGPFAETCADFWKAVWQ 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 732 ESSHLLVMLT-TVMESGRQKCHQYWPVTGEELQLAEGFSVRCLSEKPDETGSFVFREFVLKDKHEQRHIHHMQYLAWPDH 810
Cdd:PHA02747 116 EHCSIIVMLTpTKGTNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQCSEWFED 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 811 CVPSDPNLFLEFtervraarnrtllqeieeslkqVRLMDadadadengglmRERKCAASNgATPEDetpvstsvhQCISa 890
Cdd:PHA02747 196 ETPSDHPDFIKF----------------------IKIID------------INRKKSGKL-FNPKD---------ALLC- 230

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386770278 891 anpPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRFV 951
Cdd:PHA02747 231 ---PIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFI 288
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
659-948 2.11e-33

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 130.60  E-value: 2.11e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 659 TEARKPANA---PKNRYRDISPYDCTRVSLvnslTGDYINANYVnmEIPGGavNRYIATQGPLASTTTDFWRMVQQESSH 735
Cdd:COG5599   32 NDPQYLQNIngsPLNRFRDIQPYKETALRA----NLGYLNANYI--QVIGN--HRYIATQYPLEEQLEDFFQMLFDNNTP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 736 LLVMLTT---VMESgRQKCHQYWPVTGEElqLAEGFSVRCLSEKPDETGsFVFREFVLK---DKHEQRHIHHMQYLAWPD 809
Cdd:COG5599  104 VLVVLASddeISKP-KVKMPVYFRQDGEY--GKYEVSSELTESIQLRDG-IEARTYVLTikgTGQKKIEIPVLHVKNWPD 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 810 HCVPSDPNLfleftervraarnRTLLQEIEESLKqvrlmdaDADADEngglmrerkcaasngatpedetpvstsvhqcis 889
Cdd:COG5599  180 HGAISAEAL-------------KNLADLIDKKEK-------IKDPDK--------------------------------- 206

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386770278 890 aaNPPViVHCSAGIGRTGVLILMdtaLALMEAREPVYPL-----DIVRTMRDQRAC-MVQNVSQY 948
Cdd:COG5599  207 --LLPV-VHCRAGVGRTGTLIAC---LALSKSINALVQItlsveEIVIDMRTSRNGgMVQTSEQL 265
FERM_C pfam09380
FERM C-terminal PH-like domain;
236-322 3.14e-29

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 111.58  E-value: 3.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  236 DSNGKELQLGVSAVGLLVFQHSLRV-NTFSWSKMVKVSFKRKDFFIQLRREPSEnydTLLGFGMSSHKHAKALWKSCVEH 314
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKIlNLFPWREIRKISFKRKKFLIKLRDKSSE---ETLGFYTESSRACKYLWKLCVEQ 77


                  ....*...
gi 386770278  315 HSFFRLKR 322
Cdd:pfam09380  78 HTFFRLRR 85
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 123-232 6.54e-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: 111.98  E-value: 6.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  123 DPSRLQEEFTRYQFYLQIKRNILLGKLPCSSNTQCLLASYTVQSELGDFNALEHQPGYLSG-----MQLLCDQTTEA-ER 196
Cdd:pfam00373   2 LELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLesflpKQLLRKMKSKElEK 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 386770278  197 KVGELHKLHRGQLPADAEYNYLEHAKRLELYGIDLH 232
Cdd:pfam00373  82 RVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 504-589 4.47e-15

PDZ domain; PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 71.16  E-value: 4.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  504 TIRLQADEQGRYGFNVKGGVDLSL-PVQVSKVVPHTPADRctPRVCEGDEVLMINGRDVHGLRHEQVVAMIRdcrhQASG 582
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKGGSDQGDpGIFVSEVLPGGAAEA--GGLKVGDRILSINGQDVENMTHEEAVLALK----GSGG 74


                  ....*..
gi 386770278  583 ELLLTVR 589
Cdd:pfam00595  75 KVTLTIL 81
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 502-591 4.44e-14

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 68.56  E-value: 4.44e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278   502 LITIRLQADEQGrYGFNVKGGVDLSLPVQVSKVVPHTPADRCtpRVCEGDEVLMINGRDVHGLRHEQVVAMIRdcrhQAS 581
Cdd:smart00228   2 PRLVELEKGGGG-LGFSLVGGKDEGGGVVVSSVVPGSPAAKA--GLRVGDVILEVNGTSVEGLTHLEAVDLLK----KAG 74

                           90
                   ....*....|
gi 386770278   582 GELLLTVRPQ 591
Cdd:smart00228  75 GKVTLTVLRG 84
FA pfam08736
FERM adjacent (FA); This region is found adjacent to Band 4.1 / FERM domains (pfam00373) in a ...
 333-369 1.68e-13

FERM adjacent (FA); This region is found adjacent to Band 4.1 / FERM domains (pfam00373) in a subset of FERM containing protein. The region has been hypothesized to play a role in regulatory adaptation, based on similarity to other protein kinase substrates.


Pssm-ID: 462582  Cd Length: 44  Bit Score: 65.26  E-value: 1.68e-13
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 386770278  333 SLGSKFYYSGRTELQAVQESKQRGRIHKVFVRSPSKR 369
Cdd:pfam08736   4 SLGSKFRYSGRTQKQTVEDSSEILRPQPEFERSPSKR 40
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 506-574 1.53e-04

C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440556 [Multi-domain]  Cd Length: 341  Bit Score: 44.86  E-value: 1.53e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386770278 506 RLQADEQGRYGFNvkgGVDLSLP---VQVSKVVPHTPADRctPRVCEGDEVLMINGRDVHGLRHEQVVAMIR 574
Cdd:COG0793   50 DFQESTSGEFGGL---GAELGEEdgkVVVVSVIPGSPAEK--AGIKPGDIILAIDGKSVAGLTLDDAVKLLR 116
 
Name Accession Description Interval E-value
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 692-961 1.43e-129

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: 389.77  E-value: 1.43e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 692 DYINANYVNMEIPG-GAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGEELQLaEGFSV 770
Cdd:cd14541    1 DYINANYVNMEIPGsGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQF-GNLQI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 771 RCLSEKPdeTGSFVFREFVLKDKH--EQRHIHHMQYLAWPDHCVPSDPNLFLEFTERVRAARnrtllqeieeslkqvrlm 848
Cdd:cd14541   80 TCVSEEV--TPSFAFREFILTNTNtgEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNR------------------ 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 849 dadadadengglmrerkcaasngatpedetpvstsvhqciSAANPPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPL 928
Cdd:cd14541  140 ----------------------------------------VGMVEPTVVHCSAGIGRTGVLITMETAMCLIEANEPVYPL 179

                        250       260       270
                 ....*....|....*....|....*....|...
gi 386770278 929 DIVRTMRDQRACMVQNVSQYRFVCECICAAYMK 961
Cdd:cd14541  180 DIVRTMRDQRAMLIQTPSQYRFVCEAILRVYEE 212
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 628-959 3.07e-106

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: 331.04  E-value: 3.07e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 628 QSLLLLSDGLASGALLAQYELMYRKNPDLAITEARKPANAPKNRYRDISPYDCTRVSLVNSltGDYINANYVNMEIPG-G 706
Cdd:cd14600    2 ESMAQLKKGLESGTVLIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQGN--EDYINASYVNMEIPSaN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 707 AVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGEELQLAeGFSVRCLSEkpDETGSFVFR 786
Cdd:cd14600   80 IVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYG-GFRVQCHSE--DCTIAYVFR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 787 EFVLKDKH--EQRHIHHMQYLAWPDHCVPSDPNLFLEFTERVRAARnrtllqeieeslkqvrlmdadadadengglmrer 864
Cdd:cd14600  157 EMLLTNTQtgEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKR---------------------------------- 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 865 kcaasngatpedetpvstsvhqcisAANPPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQN 944
Cdd:cd14600  203 -------------------------VENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQT 257

                        330
                 ....*....|....*
gi 386770278 945 VSQYRFVCECICAAY 959
Cdd:cd14600  258 SSQYKFVCEAILRVY 272
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
642-955 1.99e-87

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 280.70  E-value: 1.99e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278   642 LLAQYELMYR-KNPDLAITEARKPANAPKNRYRDISPYDCTRVSLVNSLT--GDYINANYVNMEIPGgavNRYIATQGPL 718
Cdd:smart00194   2 LEEEFEKLDRlKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGegSDYINASYIDGPNGP---KAYIATQGPL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278   719 ASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGEELQLAEGFSVRCLSEkpDETGSFVFREFVLKDK--HEQ 796
Cdd:smart00194  79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSV--EKVDDYTIRTLEVTNTgcSET 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278   797 RHIHHMQYLAWPDHCVPSDPNLFLEFTERVRaarnrtllqeieeslkqvrlmdadadadengglmrerkcaasngatped 876
Cdd:smart00194 157 RTVTHYHYTNWPDHGVPESPESILDLIRAVR------------------------------------------------- 187

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386770278   877 etpvstsvhQCISAANPPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRFVCECI 955
Cdd:smart00194 188 ---------KSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAI 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
666-955 8.31e-86

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 275.27  E-value: 8.31e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  666 NAPKNRYRDISPYDCTRVSLVNS-LTGDYINANYVNMEipgGAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVM 744
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDpGPSDYINASYIDGY---KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  745 ESGRQKCHQYWPVTGEELQLAEGFSVRCLSEKPDETGsFVFREFVLKDK--HEQRHIHHMQYLAWPDHCVPSDPNLFLEF 822
Cdd:pfam00102  78 EKGREKCAQYWPEEEGESLEYGDFTVTLKKEKEDEKD-YTVRTLEVSNGgsEETRTVKHFHYTGWPDHGVPESPNSLLDL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  823 TERVRAARNRTLlqeieeslkqvrlmdadadadengglmrerkcaasngatpedetpvstsvhqcisaaNPPVIVHCSAG 902
Cdd:pfam00102 157 LRKVRKSSLDGR---------------------------------------------------------SGPIVVHCSAG 179

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386770278  903 IGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRFVCECI 955
Cdd:pfam00102 180 IGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 692-959 2.12e-80

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: 259.88  E-value: 2.12e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 692 DYINANYVNMEIPG-GAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGEELQLAeGFSV 770
Cdd:cd14601    1 DYINANYINMEIPSsSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYG-GFQV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 771 RCLSEKPDEtgSFVFREFVLK--DKHEQRHIHHMQYLAWPDHCVPSDPNLFLEFTERVRAARnrtllqeieeslkqvrlm 848
Cdd:cd14601   80 TCHSEEGNP--AYVFREMTLTnlEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKR------------------ 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 849 dadADADEngglmrerkcaasngatpedetpvstsvhqcisaanpPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPL 928
Cdd:cd14601  140 ---AGKDE-------------------------------------PVVVHCSAGIGRTGVLITMETAMCLIECNQPVYPL 179

                        250       260       270
                 ....*....|....*....|....*....|.
gi 386770278 929 DIVRTMRDQRACMVQNVSQYRFVCECICAAY 959
Cdd:cd14601  180 DIVRTMRDQRAMMIQTPSQYRFVCEAILKVY 210
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 693-953 3.39e-69

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: 228.71  E-value: 3.39e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 693 YINANYVNMeipGGAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGEELQLAEGFSVRC 772
Cdd:cd00047    1 YINASYIDG---YRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 773 LSEkpDETGSFVFREFVLK--DKHEQRHIHHMQYLAWPDHCVPSDPNLFLEFTERVRAARNRTllqeieeslkqvrlmda 850
Cdd:cd00047   78 VSE--EELSDYTIRTLELSpkGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKP----------------- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 851 dadadengglmrerkcaasngatpedetpvstsvhqcisaaNPPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPLDI 930
Cdd:cd00047  139 -----------------------------------------NGPIVVHCSAGVGRTGTFIAIDILLERLEAEGEVDVFEI 177

                        250       260
                 ....*....|....*....|...
gi 386770278 931 VRTMRDQRACMVQNVSQYRFVCE 953
Cdd:cd00047  178 VKALRKQRPGMVQTLEQYEFIYE 200
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 693-951 2.64e-62

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 210.18  E-value: 2.64e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 693 YINANYVNMeiPGGAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPvTGEELQLAEGFSVRC 772
Cdd:cd18533    1 YINASYITL--PGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWP-SGEYEGEYGDLTVEL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 773 LSEKPDETGSFVFREFVL-KDKHEQRHIHHMQYLAWPDHCVPSDPNLFLeftervraarnrTLLQEIEESLKQVRLmdad 851
Cdd:cd18533   78 VSEEENDDGGFIVREFELsKEDGKVKKVYHIQYKSWPDFGVPDSPEDLL------------TLIKLKRELNDSASL---- 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 852 adadengglmrerkcaasngatpedetpvstsvhqcisaaNPPVIVHCSAGIGRTGVLILMDTALALMEA---------- 921
Cdd:cd18533  142 ----------------------------------------DPPIIVHCSAGVGRTGTFIALDSLLDELKRglsdsqdled 181

                        250       260       270
                 ....*....|....*....|....*....|.
gi 386770278 922 -REPVYplDIVRTMRDQRACMVQNVSQYRFV 951
Cdd:cd18533  182 sEDPVY--EIVNQLRKQRMSMVQTLRQYIFL 210
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 671-951 4.83e-60

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: 204.51  E-value: 4.83e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 671 RYRDISPYDCTRVSL--VNSLTG-DYINANYvnmeIPG-GAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMES 746
Cdd:cd14548    1 RYTNILPYDHSRVKLipINEEEGsDYINANY----IPGyNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 747 GRQKCHQYWPVTGEELQLAEgFSVRCLSEkpDETGSFVFREFVLKDKHEQRHIHHMQYLAWPDHCVPSDPNLFLEFTERV 826
Cdd:cd14548   77 GRVKCDHYWPFDQDPVYYGD-ITVTMLSE--SVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 827 RAARNRtllqeieeslkqvrlmdadadadENGglmrerkcaasngatpedetpvstsvhqcisaanpPVIVHCSAGIGRT 906
Cdd:cd14548  154 RDYIKQ-----------------------EKG-----------------------------------PTIVHCSAGVGRT 175

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 386770278 907 GVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRFV 951
Cdd:cd14548  176 GTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFL 220
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 666-951 1.84e-59

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 203.85  E-value: 1.84e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 666 NAPKNRYRDISPYDCTRVSLV---NSLTG-DYINANYVNMEIPGGAVNR----YIATQGPLASTTTDFWRMVQQESSHLL 737
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKdrdPNVPGsDYINANYIRNENEGPTTDEnaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 738 VMLTTVMESGRQKCHQYWPVTGEELQLAeGFSVRCLSEkpDETGSFVFREFVLK---DKHEQRHIHHMQYLAWPDHCVPS 814
Cdd:cd14544   81 VMTTKEVERGKNKCVRYWPDEGMQKQYG-PYRVQNVSE--HDTTDYTLRELQVSkldQGDPIREIWHYQYLSWPDHGVPS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 815 DPNLFLEFTERVraarNRtllqeieeslKQVRLMDADadadengglmrerkcaasngatpedetpvstsvhqcisaanpP 894
Cdd:cd14544  158 DPGGVLNFLEDV----NQ----------RQESLPHAG------------------------------------------P 181

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 895 VIVHCSAGIGRTGVLILMDTALALMEAREPVYPLDIVRTM---RDQRACMVQNVSQYRFV 951
Cdd:cd14544  182 IVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIQKTIqmvRSQRSGMVQTEAQYKFI 241
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 693-951 4.22e-57

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: 196.14  E-value: 4.22e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 693 YINANYVNMEIpGGAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWP-VTGEELQLAEG-FSV 770
Cdd:cd14540    1 YINASHITATV-GGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPtLGGEHDALTFGeYKV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 771 rcLSEKPDETGSFVFREFVLKDKHEQRH--IHHMQYLAWPDHCVPSDPNLFLEFTERVRAARNRTllqeieeslkqvrlm 848
Cdd:cd14540   80 --STKFSVSSGCYTTTGLRVKHTLSGQSrtVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHT--------------- 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 849 dadadadengglmrerkcaasNGATPEDETpvstsvhqcisaaNPPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPL 928
Cdd:cd14540  143 ---------------------NQDVAGHNR-------------NPPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIP 188

                        250       260
                 ....*....|....*....|...
gi 386770278 929 DIVRTMRDQRACMVQNVSQYRFV 951
Cdd:cd14540  189 RVLALLRHQRMLLVQTLAQYKFV 211
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 642-950 6.35e-57

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: 197.59  E-value: 6.35e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 642 LLAQYELMYRKNPDLAITEARKPANAPKNRYRDISPYDCTRVSLvNSLTG----DYINANYVNMEIPGgavNRYIATQGP 717
Cdd:cd14543    5 IYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKL-PKRNGdertDYINANFMDGYKQK---NAYIATQGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 718 LASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGEELQLAEGFSVRCLSekPDETGSFVFREFVLKDKH--E 795
Cdd:cd14543   81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLS--VENKEHYKKTTLEIHNTEtdE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 796 QRHIHHMQYLAWPDHCVPSDPNLFLEFTERVRAARNRTllqeieeslkqVRLMdadadADENGGlmrerkcaasngatpe 875
Cdd:cd14543  159 SRQVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALA-----------VKAM-----GDRWKG---------------- 206

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386770278 876 detpvstsvHQcisaANPPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRF 950
Cdd:cd14543  207 ---------HP----PGPPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYF 268
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 670-951 1.10e-55

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: 192.23  E-value: 1.10e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 670 NRYRDISPYDCTRVSL---VNSLTGDYINANYVNMeiPGGAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMEs 746
Cdd:cd14547    1 NRYKTILPNEHSRVCLpsvDDDPLSSYINANYIRG--YDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTE- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 747 GRQKCHQYWPVtgEELQLAEGFSVRCLSEKPDEtgSFVFREFVLKDKHEQRHIHHMQYLAWPDHCVPSDPNLFLEfterv 826
Cdd:cd14547   78 AKEKCAQYWPE--EENETYGDFEVTVQSVKETD--GYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLS----- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 827 raarnrtLLQEIEESLKQvrlmdadadadengglmrerkcaasngatpedetpvstsvhqciSAANPPVIVHCSAGIGRT 906
Cdd:cd14547  149 -------LVQEVEEARQT--------------------------------------------EPHRGPIVVHCSAGIGRT 177

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 386770278 907 GVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRFV 951
Cdd:cd14547  178 GCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFV 222
FERM_C_PTPN4_PTPN3_like cd13189
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and ...
 226-320 1.26e-55

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: 187.13  E-value: 1.26e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 226 LYGIDLHRATDSNGKELQLGVSAVGLLVFQHSLRVNTFSWSKMVKVSFKRKDFFIQLRREPSENYDTLLGFGMSSHKHAK 305
Cdd:cd13189    1 LYGVELHSARDSNNLELQIGVSSAGILVFQNGIRINTFPWSKIVKISFKRKQFFIQLRREPNESRDTILGFNMLSYRACK 80

                         90
                 ....*....|....*
gi 386770278 306 ALWKSCVEHHSFFRL 320
Cdd:cd13189   81 NLWKSCVEHHTFFRL 95
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 660-956 1.59e-54

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: 190.48  E-value: 1.59e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 660 EARKPANAPKNRYRDISPYDCTRVSLV----NSLTGDYINANYVNMEI--PGGAVNRYIATQGPLASTTTDFWRMVQQES 733
Cdd:cd14606   12 EGQRPENKSKNRYKNILPFDHSRVILQgrdsNIPGSDYINANYVKNQLlgPDENAKTYIASQGCLEATVNDFWQMAWQEN 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 734 SHLLVMLTTVMESGRQKCHQYWPVTGEELQLAEgFSVRCLSEK-PDETGSFVFREFVLKDKHEQRHIHHMQYLAWPDHCV 812
Cdd:cd14606   92 SRVIVMTTREVEKGRNKCVPYWPEVGMQRAYGP-YSVTNCGEHdTTEYKLRTLQVSPLDNGELIREIWHYQYLSWPDHGV 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 813 PSDPNLFLEFTERVraarnrtllQEIEESLKqvrlmdadadadengglmrerkcaasngatpedetpvstsvhqciSAAn 892
Cdd:cd14606  171 PSEPGGVLSFLDQI---------NQRQESLP---------------------------------------------HAG- 195

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386770278 893 pPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPLDIVRTM---RDQRACMVQNVSQYRFVCECIC 956
Cdd:cd14606  196 -PIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIQKTIqmvRAQRSGMVQTEAQYKFIYVAIA 261
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 693-955 2.31e-54

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: 187.97  E-value: 2.31e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 693 YINANYVNMEIpGGAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGEELQLAEG-FSVR 771
Cdd:cd14538    1 YINASHIRIPV-GGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLICGGrLEVS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 772 CLSEKPDEtgSFVFREFVLKDKH--EQRHIHHMQYLAWPDHCVPSDPNLFLEFTERVRAArnrtllqeieeslkqvrlmd 849
Cdd:cd14538   80 LEKYQSLQ--DFVIRRISLRDKEtgEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRI-------------------- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 850 adadadENGGlmrerkcaasngatpedetpvstsvhqcisaanpPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPLD 929
Cdd:cd14538  138 ------HNSG----------------------------------PIVVHCSAGIGRTGVLITIDVALGLIERDLPFDIQD 177

                        250       260
                 ....*....|....*....|....*.
gi 386770278 930 IVRTMRDQRACMVQNVSQYRFVCECI 955
Cdd:cd14538  178 IVKDLREQRQGMIQTKDQYIFCYKAC 203
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 637-951 3.06e-54

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: 190.59  E-value: 3.06e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 637 LASGALLAQYELMYRKNPDLAITEARKPANAPKNRYRDISPYDCTRVSLV---NSLTGdYINANYVNMEIpGGAVNRYIA 713
Cdd:cd14599    9 LEEGMVFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVptkENNTG-YINASHIKVTV-GGEEWHYIA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 714 TQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGEELQLAEGFSVRCLSEKPDETGSFVFREfvLKDK 793
Cdd:cd14599   87 TQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTG--LKVK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 794 H----EQRHIHHMQYLAWPDHCVPSDPNLFLEFTERVRAARNRTllqeieeslkqvrlmdadadadengglmrerkcaas 869
Cdd:cd14599  165 HllsgQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHT------------------------------------ 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 870 ngatpedeTPVSTSVHQCisaaNPPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYR 949
Cdd:cd14599  209 --------NSMLDSTKNC----NPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYK 276


                 ..
gi 386770278 950 FV 951
Cdd:cd14599  277 FV 278
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 664-958 6.94e-54

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: 187.60  E-value: 6.94e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 664 PANAPKNRYRDISPYDCTRVSL--VNSLTG-DYINANYVNmeipgG--AVNRYIATQGPLASTTTDFWRMVQQESSHLLV 738
Cdd:cd14553    1 EVNKPKNRYANVIAYDHSRVILqpIEGVPGsDYINANYCD-----GyrKQNAYIATQGPLPETFGDFWRMVWEQRSATIV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 739 MLTTVMESGRQKCHQYWPVTGEELQlaEGFSVRCLSEKpdETGSFVFREFVLKD--KHEQRHIHHMQYLAWPDHCVPSDP 816
Cdd:cd14553   76 MMTKLEERSRVKCDQYWPTRGTETY--GLIQVTLLDTV--ELATYTVRTFALHKngSSEKREVRQFQFTAWPDHGVPEHP 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 817 NLFLEFTERVRAARNRtllqeieeslkqvrlmDADadadengglmrerkcaasngatpedetpvstsvhqcisaanpPVI 896
Cdd:cd14553  152 TPFLAFLRRVKACNPP----------------DAG------------------------------------------PIV 173

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386770278 897 VHCSAGIGRTGVLILMDTALALMEAREPVyplDI---VRTMRDQRACMVQNVSQYRFVCECICAA 958
Cdd:cd14553  174 VHCSAGVGRTGCFIVIDSMLERIKHEKTV---DIyghVTCLRAQRNYMVQTEDQYIFIHDALLEA 235
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 670-955 7.60e-53

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: 184.71  E-value: 7.60e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 670 NRYRDISPYDCTRVSLV---NSLTGDYINANYvnmeIPG-GAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVME 745
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKpihEEPGSDYINANY----MPGyWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCME 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 746 SGRQKCHQYWPVTGEELqLAEGFSVRCLSEKPDEtgSFVFREFVLKDKHEQ--RHIHHMQYLAWPDHCVPSDPNLFLEFT 823
Cdd:cd14619   77 AGRVKCEHYWPLDYTPC-TYGHLRVTVVSEEVME--NWTVREFLLKQVEEQktLSVRHFHFTAWPDHGVPSSTDTLLAFR 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 824 ERVRaarnrtllQEIEESLkqvrlmdadadadengglmrerkcaaSNGatpedetpvstsvhqcisaanpPVIVHCSAGI 903
Cdd:cd14619  154 RLLR--------QWLDQTM--------------------------SGG----------------------PTVVHCSAGV 177

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 386770278 904 GRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRFVCECI 955
Cdd:cd14619  178 GRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCI 229
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 652-962 6.42e-52

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: 182.86  E-value: 6.42e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 652 KNPDLAITEARKPANAPKNRYRDISPYDCTRVSLVNSlTGDYINANYVNMEipgGAVNRYIATQGPLASTTTDFWRMVQQ 731
Cdd:cd14607   10 ESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNT-ENDYINASLVVIE---EAQRSYILTQGPLPNTCCHFWLMVWQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 732 ESSHLLVMLTTVMESGRQKCHQYWPVTGEELQLAE--GFSVRCLSEkpDETGSFVFREFVLKDKH--EQRHIHHMQYLAW 807
Cdd:cd14607   86 QKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKetGFSVKLLSE--DVKSYYTVHLLQLENINsgETRTISHFHYTTW 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 808 PDHCVPSDPNLFLEFTERVRAARnrtllqeieeslkqvrlmdadadadengglmrerkcaasngatpedetpvstsvhqC 887
Cdd:cd14607  164 PDFGVPESPASFLNFLFKVRESG--------------------------------------------------------S 187

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386770278 888 ISAANPPVIVHCSAGIGRTGVLILMDTALALMEAREP--VYPLDIVRTMRDQRACMVQNVSQYRFvcecicaAYMKI 962
Cdd:cd14607  188 LSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDPdsVDIKQVLLDMRKYRMGLIQTPDQLRF-------SYMAV 257
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 655-955 1.14e-51

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: 181.63  E-value: 1.14e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 655 DLAITEARKPANAPKNRYRDISPYDCTRVSLV---NSLTGDYINANYvnmeIPG-GAVNRYIATQGPLASTTTDFWRMVQ 730
Cdd:cd14614    1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVsmhEEEGSDYINANY----IPGyNSPQEYIATQGPLPETRNDFWKMVL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 731 QESSHLLVMLTTVMESGRQKCHQYWPVTGEELQLAEgFSVRCLSEkpDETGSFVFREFVLKDKHEQRHIHHMQYLAWPDH 810
Cdd:cd14614   77 QQKSQIIVMLTQCNEKRRVKCDHYWPFTEEPVAYGD-ITVEMLSE--EEQPDWAIREFRVSYADEVQDVMHFNYTAWPDH 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 811 CVPSdpnlflefterVRAARNrtLLQEIEeslkqvrlmdadadadengglMRERKCAASNGatpedetpvstsvhqcisa 890
Cdd:cd14614  154 GVPT-----------ANAAES--ILQFVQ---------------------MVRQQAVKSKG------------------- 180

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386770278 891 anpPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRFVCECI 955
Cdd:cd14614  181 ---PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 242
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 652-951 2.42e-51

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: 181.56  E-value: 2.42e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 652 KNPDLAITEA-RKPANAPKNRYRDISPYDCTRVSLvnSLT-----GDYINANYVNmeipgGAVN--RYIATQGPLASTTT 723
Cdd:cd14603   15 KADYVCSTVAgGRKENVKKNRYKDILPYDQTRVIL--SLLqeeghSDYINANFIK-----GVDGsrAYIATQGPLSHTVL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 724 DFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGEELQLAEgFSVRCLSEK-PDEtgSFVFREFVLKDKHEQRHIHHM 802
Cdd:cd14603   88 DFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPLQTGP-FTITLVKEKrLNE--EVILRTLKVTFQKESRSVSHF 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 803 QYLAWPDHCVPSDPNLFLEFTERVRAarnrtllqeieeslKQvrlmdadadadengglmrerkcaasnGATPEdetpvst 882
Cdd:cd14603  165 QYMAWPDHGIPDSPDCMLAMIELARR--------------LQ--------------------------GSGPE------- 197

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386770278 883 svhqcisaanpPVIVHCSAGIGRTGVLILMD--TALALMEAREPVYPL-DIVRTMRDQRACMVQNVSQYRFV 951
Cdd:cd14603  198 -----------PLCVHCSAGCGRTGVICTVDyvRQLLLTQRIPPDFSIfDVVLEMRKQRPAAVQTEEQYEFL 258
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 669-950 1.11e-50

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: 178.35  E-value: 1.11e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 669 KNRYRDISPYDCTRVSL-VNSLTGDYINANYVNMEIpggAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESG 747
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVkLKQGDNDYINASLVEVEE---AKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 748 RQKCHQYWPVTGEELQLAE--GFSVRCLSEkpDETGSFVFREFVLKDK--HEQRHIHHMQYLAWPDHCVPSDPNLFLEFT 823
Cdd:cd14545   78 QIKCAQYWPQGEGNAMIFEdtGLKVTLLSE--EDKSYYTVRTLELENLktQETREVLHFHYTTWPDFGVPESPAAFLNFL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 824 ERVRaarnrtllqeieeslkqvrlmdadadadENGGLMRErkcaasngatpedetpvstsvhqcisaANPPViVHCSAGI 903
Cdd:cd14545  156 QKVR----------------------------ESGSLSSD---------------------------VGPPV-VHCSAGI 179

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 386770278 904 GRTGVLILMDTALALMEAREPVyPLDI---VRTMRDQRACMVQNVSQYRF 950
Cdd:cd14545  180 GRSGTFCLVDTCLVLIEKGNPS-SVDVkkvLLEMRKYRMGLIQTPDQLRF 228
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 666-955 4.01e-50

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: 176.94  E-value: 4.01e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 666 NAPKNRYRDISPYDCTRVSLVNSltGDYINANYVNMEIpGGAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVME 745
Cdd:cd14597    3 NRKKNRYKNILPYDTTRVPLGDE--GGYINASFIKMPV-GDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 746 SGRQKCHQYWP-------VTGEELQLAegfsvrclSEKPDETGSFVFREFVLKD--KHEQRHIHHMQYLAWPDHCVPSDP 816
Cdd:cd14597   80 GGKIKCQRYWPeilgkttMVDNRLQLT--------LVRMQQLKNFVIRVLELEDiqTREVRHITHLNFTAWPDHDTPSQP 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 817 NLFLEFTERVRaarnrtllqeieeslkqvrlmdadadadengglmrerkcaasngatpedetpvstSVHQcisaaNPPVI 896
Cdd:cd14597  152 EQLLTFISYMR-------------------------------------------------------HIHK-----SGPII 171

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 386770278 897 VHCSAGIGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRFVCECI 955
Cdd:cd14597  172 THCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230
PDZ_PTPN3-4-like cd06706
PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein ...
 500-589 1.25e-49

PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein phosphatase non-receptor type 4 (PTNP4), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PTPN3, PTPN4 and related domains. PTPN3 (also known as protein-tyrosine phosphatase H1, PTP-H1) has a tumor-suppressive or a tumor-promoting role in many cancers. It serves as a specific phosphatase for the MAP kinase p38gamma; the two interact via their PDZ domains and cooperate to promote Ras-induced oncogenesis. Interaction partners of the PTPN3 PDZ domain include p38gamma and human papillomavirus E6 oncoprotein. PTPN4 (also known as protein-tyrosine phosphatase MEG1) plays a role in immunity, learning, synaptic plasticity or cell homeostasis. p38gamma is also an interaction partner of the PTPN4 PDZ domain: PTPN4 regulates neuronal cell homeostasis by protecting neurons against apoptosis; binding of the C terminus of p38gamma to the PDZ domain of PTPN4, antagonizes the catalytic autoinhibition of PTPN4, leading to cell apoptosis. Other interaction partners of the PTPN4 PDZ domain include glutamate receptor subunit GluN2A, and RABV strain G protein, among others. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN3-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467190 [Multi-domain]  Cd Length: 90  Bit Score: 169.80  E-value: 1.25e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 500 SDLITIRLQADEQGRYGFNVKGGVDLSLPVQVSKVVPHTPADRCTPRVCEGDEVLMINGRDVHGLRHEQVVAMIRDCRHQ 579
Cdd:cd06706    1 DGLVLIRMKPDENGRFGFNVKGGVDQKMPVIVSRVAPGTPADLCIPRLNEGDQVLLINGRDISEHTHDQVVMFIKASRER 80

                         90
                 ....*....|
gi 386770278 580 ASGELLLTVR 589
Cdd:cd06706   81 HSGELVLLVR 90
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 666-951 1.97e-48

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: 172.89  E-value: 1.97e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 666 NAPKNRYRDISPYDCTRVSL----VNSLTGDYINANYVNMEIPGGAVN-----RYIATQGPLASTTTDFWRMVQQESSHL 736
Cdd:cd14605    2 NKNKNRYKNILPFDHTRVVLhdgdPNEPVSDYINANIIMPEFETKCNNskpkkSYIATQGCLQNTVNDFWRMVFQENSRV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 737 LVMLTTVMESGRQKCHQYWPvtgEELQLAE--GFSVRCLSEKPDEtgSFVFREFVLK---DKHEQRHIHHMQYLAWPDHC 811
Cdd:cd14605   82 IVMTTKEVERGKSKCVKYWP---DEYALKEygVMRVRNVKESAAH--DYILRELKLSkvgQGNTERTVWQYHFRTWPDHG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 812 VPSDPNLFLEFTERVRaarnrtllqeieesLKQVRLMDADadadengglmrerkcaasngatpedetpvstsvhqcisaa 891
Cdd:cd14605  157 VPSDPGGVLDFLEEVH--------------HKQESIMDAG---------------------------------------- 182

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386770278 892 npPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPLDIVRTM---RDQRACMVQNVSQYRFV 951
Cdd:cd14605  183 --PVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIqmvRSQRSGMVQTEAQYRFI 243
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 670-954 9.62e-48

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: 170.00  E-value: 9.62e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 670 NRYRDISPYDCTRVSLVN--SLTGDYINANYvnmeIPGGAVNR-YIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMES 746
Cdd:cd14615    1 NRYNNVLPYDISRVKLSVqsHSTDDYINANY----MPGYNSKKeFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 747 GRQKCHQYWPVTGEelQLAEGFSVRCLSEKPDEtgSFVFREFVLKDKH--EQRHIHHMQYLAWPDHCVPSDPNLFLEFTE 824
Cdd:cd14615   77 GRTKCEEYWPSKQK--KDYGDITVTMTSEIVLP--EWTIRDFTVKNAQtnESRTVRHFHFTSWPDHGVPETTDLLINFRH 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 825 RVRaarnrtllqeieESLKQvrlmdadadadengglmrerkcaasngatpedetpvstsvhqciSAANPPVIVHCSAGIG 904
Cdd:cd14615  153 LVR------------EYMKQ--------------------------------------------NPPNSPILVHCSAGVG 176

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 386770278 905 RTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRFVCEC 954
Cdd:cd14615  177 RTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQC 226
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 646-950 1.11e-47

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 171.36  E-value: 1.11e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 646 YELMYRKNPDLAITEARKPANAPKNRYRDISPYDCTRVSLvNSLTGDYINANYVNMEipgGAVNRYIATQGPLASTTTDF 725
Cdd:cd14608    5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKL-HQEDNDYINASLIKME---EAQRSYILTQGPLPNTCGHF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 726 WRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGEELQLAEGFSVRCLSEKPDETGSFVFREFVLKD--KHEQRHIHHMQ 803
Cdd:cd14608   81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENltTQETREILHFH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 804 YLAWPDHCVPSDPNLFLEFTERVRaarnrtllqeieeslkqvrlmdadadadENGglmrerkcaasngatpedetpvsts 883
Cdd:cd14608  161 YTTWPDFGVPESPASFLNFLFKVR----------------------------ESG------------------------- 187

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 884 vhqCISAANPPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPLDIVRT---MRDQRACMVQNVSQYRF 950
Cdd:cd14608  188 ---SLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVlleMRKFRMGLIQTADQLRF 254
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 693-951 1.21e-47

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: 168.68  E-value: 1.21e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 693 YINANYVnmeiPGGAVNR-YIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGEELQlaEGFSVR 771
Cdd:cd14549    1 YINANYV----DGYNKARaYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETY--GNIQVT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 772 CLSEkpDETGSFVFREFVLKD--------KHEQRHIHHMQYLAWPDHCVPSDPnlfleftervraarnrtllqeieeslk 843
Cdd:cd14549   75 LLST--EVLATYTVRTFSLKNlklkkvkgRSSERVVYQYHYTQWPDHGVPDYT--------------------------- 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 844 qvrlmdadadadengglmrerkcaasngatpedeTPVSTSVHQCiSAANP----PVIVHCSAGIGRTGVLILMDTALALM 919
Cdd:cd14549  126 ----------------------------------LPVLSFVRKS-SAANPpgagPIVVHCSAGVGRTGTYIVIDSMLQQI 170

                        250       260       270
                 ....*....|....*....|....*....|..
gi 386770278 920 EAREPVYPLDIVRTMRDQRACMVQNVSQYRFV 951
Cdd:cd14549  171 QDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFI 202
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 670-955 5.33e-46

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: 165.12  E-value: 5.33e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 670 NRYRDISPYDCTRVSLvNSLTG----DYINANYvnmeIPG-GAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVM 744
Cdd:cd14618    1 NRYPHVLPYDHSRVRL-SQLGGephsDYINANF----IPGyTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGM 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 745 ESGRQKCHQYWPVTGEELQLAEgFSVRCLSEKPDEtgSFVFREFVL--KDKHEQRHIHHMQYLAWPDHCVPSDPNLFLEF 822
Cdd:cd14618   76 ENGRVLCDHYWPSESTPVSYGH-ITVHLLAQSSED--EWTRREFKLwhEDLRKERRVKHLHYTAWPDHGIPESTSSLMAF 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 823 TERVRaarnrtllQEIEeslkqvrlmdadadadengglmrerkcaASNGATpedetpvstsvhqcisaanpPVIVHCSAG 902
Cdd:cd14618  153 RELVR--------EHVQ----------------------------ATKGKG--------------------PTLVHCSAG 176

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 386770278 903 IGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRFVCECI 955
Cdd:cd14618  177 VGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 661-959 2.26e-45

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: 163.46  E-value: 2.26e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 661 ARKPANAPKNRYRDISPYDCTRV--SLVNSLTG-DYINANYVNMEIPGGAvnrYIATQGPLASTTTDFWRMVQQESSHLL 737
Cdd:cd14554    1 ANLPCNKFKNRLVNILPYESTRVclQPIRGVEGsDYINASFIDGYRQRGA---YIATQGPLAETTEDFWRMLWEHNSTII 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 738 VMLTTVMESGRQKCHQYWPVtgEELQLAEGFSVRCLSEKpdETGSFVFREFVLKDKH--EQRHIHHMQYLAWPDHCVPSD 815
Cdd:cd14554   78 VMLTKLREMGREKCHQYWPA--ERSARYQYFVVDPMAEY--NMPQYILREFKVTDARdgQSRTVRQFQFTDWPEQGVPKS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 816 PNLFLEFTERVraarNRTLLQEIEESlkqvrlmdadadadengglmrerkcaasngatpedetpvstsvhqcisaanpPV 895
Cdd:cd14554  154 GEGFIDFIGQV----HKTKEQFGQEG----------------------------------------------------PI 177

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386770278 896 IVHCSAGIGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRFvceCICAAY 959
Cdd:cd14554  178 TVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQF---CYRAAL 238
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 666-960 5.95e-45

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: 163.67  E-value: 5.95e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 666 NAPKNRYRDISPYDCTRVSL--VNSLTG-DYINANYVNMEipgGAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTT 742
Cdd:cd14626   41 NKPKNRYANVIAYDHSRVILtsVDGVPGsDYINANYIDGY---RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTR 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 743 VMESGRQKCHQYWPVTGEE----LQLAEGFSVrclsekpdETGSFVFREFVL--KDKHEQRHIHHMQYLAWPDHCVPSDP 816
Cdd:cd14626  118 LEEKSRVKCDQYWPIRGTEtygmIQVTLLDTV--------ELATYSVRTFALykNGSSEKREVRQFQFMAWPDHGVPEYP 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 817 NLFLEFTERVRAarnrtllqeieeslkqvrlmdadadadengglmrerkcaasngatpedetpvstsvhqCISAANPPVI 896
Cdd:cd14626  190 TPILAFLRRVKA----------------------------------------------------------CNPPDAGPMV 211

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386770278 897 VHCSAGIGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRFVCECICAAYM 960
Cdd:cd14626  212 VHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAAT 275
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 35-232 6.17e-45

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: 160.92  E-value: 6.17e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278    35 CVTVLFLDDITHTFRIEKRAKGSELLDQVFQYLELSERDYFGLLFPQKPGDVVRWVDAQKQFKKQcssvsLDNDAVPLLE 114
Cdd:smart00295   1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRHWLDPAKTLLDQ-----DVKSEPLTLY 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278   115 FRVKFFVSDPSRLQEEFTRY-QFYLQIKRNILLGKLPCSSNTQCLLASYTVQSELGDFNALEHQ-PGYLSGMQLLCDQT- 191
Cdd:smart00295  76 FRVKFYPPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDlRGELSLKRFLPKQLl 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 386770278   192 -----TEAERKVGELHKLHRGQLPADAEYNYLEHAKRLELYGIDLH 232
Cdd:smart00295 156 dsrklKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 670-951 7.19e-45

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: 161.63  E-value: 7.19e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 670 NRYRDISPYDCTRVSLVN---SLTGDYINANYvnmeIPGGAVNR-YIATQGPLASTTTDFWRMVQQESSHLLVMLTTVME 745
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNvddDPCSDYINASY----IPGNNFRReYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 746 SGRQKCHQYWPVTGEELQLAEgFSVRCLSEK--PDETgsfvFREFVLKDKHE---QRHIHHMQYLAWPDHCVPSDPNLFL 820
Cdd:cd14617   77 KGRVKCDHYWPADQDSLYYGD-LIVQMLSESvlPEWT----IREFKICSEEQldaPRLVRHFHYTVWPDHGVPETTQSLI 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 821 EFTERVRAARNRTllqeieeslkqvrlmdadadadENGGlmrerkcaasngatpedetpvstsvhqcisaanpPVIVHCS 900
Cdd:cd14617  152 QFVRTVRDYINRT----------------------PGSG----------------------------------PTVVHCS 175

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 386770278 901 AGIGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRFV 951
Cdd:cd14617  176 AGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYL 226
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 664-956 3.61e-44

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: 160.39  E-value: 3.61e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 664 PANAPKNRYRDISPYDCTRVSLVNSL----TGDYINANYVNMEipGGAVNRYIATQGPLASTTTDFWRMVQQESSHLLVM 739
Cdd:cd14612   13 PGHASKDRYKTILPNPQSRVCLRRAGsqeeEGSYINANYIRGY--DGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVM 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 740 LTTVMEsGRQKCHQYWPvtgEELQLAEGFSVRCLSEKpdETGSFVFREFVLKDKHEQRHIHHMQYLAWPDHCVPSDPNLF 819
Cdd:cd14612   91 ITKLKE-KKEKCVHYWP---EKEGTYGRFEIRVQDMK--ECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPESAGPL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 820 LEftervraarnrtLLQEIEESlkqvrlmdadadadengglmreRKCAASNGatpedetpvstsvhqcisaanpPVIVHC 899
Cdd:cd14612  165 LR------------LVAEVEES----------------------RQTAASPG----------------------PIVVHC 188

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 386770278 900 SAGIGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRFVCECIC 956
Cdd:cd14612  189 SAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTLA 245
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 693-950 1.57e-43

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: 157.22  E-value: 1.57e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 693 YINANYVNMEIpGGAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGEELQLAEGFSVRC 772
Cdd:cd14596    1 YINASYITMPV-GEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 773 lsEKPDETGSFVFREFVLKDKH--EQRHIHHMQYLAWPDHCVPSDPNLFLEFTERVRAarnrtllqeieeslkqvrlmda 850
Cdd:cd14596   80 --ENYQALQYFIIRIIKLVEKEtgENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRK---------------------- 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 851 dadadengglmrerkcaasngatpedetpvstsVHQcisaaNPPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPLDI 930
Cdd:cd14596  136 ---------------------------------VHN-----TGPIVVHCSAGIGRAGVLICVDVLLSLIEKDLSFNIKDI 177

                        250       260
                 ....*....|....*....|
gi 386770278 931 VRTMRDQRACMVQNVSQYRF 950
Cdd:cd14596  178 VREMRQQRYGMIQTKDQYLF 197
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 669-951 6.55e-43

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: 156.15  E-value: 6.55e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 669 KNRYRDISPYDCTRV--SLVNSLT-GDYINANYvnmeIPGGAVNR-YIATQGPLASTTTDFWRMVQQESSHLLVMLTTVM 744
Cdd:cd14602    1 KNRYKDILPYDHSRVelSLITSDEdSDYINANF----IKGVYGPRaYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 745 ESGRQKCHQYWPVTGEELQLAEGFSVRCLSEKpdETGSFVFREFVLKDKHEQRHIHHMQYLAWPDHCVPSDPNLFLEFTE 824
Cdd:cd14602   77 EMGKKKCERYWAEPGEMQLEFGPFSVTCEAEK--RKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIW 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 825 RVRaarnrtLLQEIEEslkqvrlmdadadadengglmrerkcaasngatpedetpvstsvhqcisaanPPVIVHCSAGIG 904
Cdd:cd14602  155 DVR------CYQEDDS----------------------------------------------------VPICIHCSAGCG 176

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 386770278 905 RTGVLILMDTALALMeaREPVYPLD-----IVRTMRDQRACMVQNVSQYRFV 951
Cdd:cd14602  177 RTGVICAIDYTWMLL--KDGIIPENfsvfsLIQEMRTQRPSLVQTKEQYELV 226
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 650-961 1.14e-42

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: 157.79  E-value: 1.14e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 650 YRKNPDLAITEARKPANAPKNRYRDISPYDCTRVSL---VNSLTGDYINANYVN-MEIPggavNRYIATQGPLASTTTDF 725
Cdd:cd14604   41 YRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLtlkTSSQDSDYINANFIKgVYGP----KAYIATQGPLANTVIDF 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 726 WRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGEELQLAEGFSVRCLSEKPdETGSFVfREFVLKDKHEQRHIHHMQYL 805
Cdd:cd14604  117 WRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQA-RTDYFI-RTLLLEFQNETRRLYQFHYV 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 806 AWPDHCVPSDPNLFLEFTervraarnrtllqeieeslkqvrlmdadadadengGLMRERKcaasngatPEDETPVstsvh 885
Cdd:cd14604  195 NWPDHDVPSSFDSILDMI-----------------------------------SLMRKYQ--------EHEDVPI----- 226

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386770278 886 qCIsaanppvivHCSAGIGRTGVLILMDTALALMEA---REPVYPLDIVRTMRDQRACMVQNVSQYRFVCECICAAYMK 961
Cdd:cd14604  227 -CI---------HCSAGCGRTGAICAIDYTWNLLKAgkiPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEK 295
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 693-951 3.06e-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: 153.35  E-value: 3.06e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 693 YINANYvnmeIPGGAVNR-YIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGEELQLAEGFSVR 771
Cdd:cd14542    1 YINANF----IKGVSGSKaYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKIS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 772 CLSEKpDETGSFVFREFVLKDKHEQRHIHHMQYLAWPDHCVPSDPNLFLEFTERVRAarnrtlLQEIEEslkqvrlmdad 851
Cdd:cd14542   77 LEKEK-RVGPDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRD------YQGSED----------- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 852 adadengglmrerkcaasngatpedetpvstsvhqcisaanPPVIVHCSAGIGRTGVLILMDTALALMEA--REPVYPL- 928
Cdd:cd14542  139 -----------------------------------------VPICVHCSAGCGRTGTICAIDYVWNLLKTgkIPEEFSLf 177

                        250       260
                 ....*....|....*....|...
gi 386770278 929 DIVRTMRDQRACMVQNVSQYRFV 951
Cdd:cd14542  178 DLVREMRKQRPAMVQTKEQYELV 200
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 669-951 4.81e-42

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: 154.64  E-value: 4.81e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 669 KNRYRDISPYDCTRVSLVNSLTGD----YINANYVNMEipGGAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVm 744
Cdd:cd14613   28 KNRYKTILPNPHSRVCLTSPDQDDplssYINANYIRGY--GGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNI- 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 745 ESGRQKCHQYWPvtgEELQLAEGFSVRCLSEKPDEtgSFVFREFVLKDKHEQRHIHHMQYLAWPDHCVPSDPNLFLEfte 824
Cdd:cd14613  105 EEMNEKCTEYWP---EEQVTYEGIEITVKQVIHAD--DYRLRLITLKSGGEERGLKHYWYTSWPDQKTPDNAPPLLQ--- 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 825 rvraarnrtLLQEIEESLKQVRLMDAdadadengglmrerkcaasngatpedetpvstsvhqcisaanpPVIVHCSAGIG 904
Cdd:cd14613  177 ---------LVQEVEEARQQAEPNCG-------------------------------------------PVIVHCSAGIG 204

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 386770278 905 RTGVLILmdTALALMEAR-EPVypLDIVRT---MRDQRACMVQNVSQYRFV 951
Cdd:cd14613  205 RTGCFIA--TSICCKQLRnEGV--VDILRTtcqLRLDRGGMIQTCEQYQFV 251
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 670-953 2.27e-41

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: 151.60  E-value: 2.27e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 670 NRYRDISPYDCTRVSLVN--SLTG-DYINANYVNMEIpggAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMES 746
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIAdaGVPGsDYINASYISGYL---CPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 747 GRQKCHQYWPVTGEELQLAEGFSVRCLSEkpDETGSFVFREFVLKDKHEQRHIHHMQYLAWPDHCVPSDPNLFLEFTERV 826
Cdd:cd14616   78 GRIRCHQYWPEDNKPVTVFGDIVITKLME--DVQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 827 RAARnrtllqeieeslkqvrlmdadadadengglmrerkcaasngatPEDETpvstsvhqcisaanpPVIVHCSAGIGRT 906
Cdd:cd14616  156 RASR-------------------------------------------AHDNT---------------PMIVHCSAGVGRT 177

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 386770278 907 GVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRFVCE 953
Cdd:cd14616  178 GVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 644-958 3.05e-41

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: 152.88  E-value: 3.05e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 644 AQYELMYRKNPDLAIT--EARKPANAPKNRYRDISPYDCTRVSL-----VNSLTGDYINANYVNMEIPGGAvnrYIATQG 716
Cdd:cd17667    3 EDFEEVQRCTADMNITaeHSNHPDNKHKNRYINILAYDHSRVKLrplpgKDSKHSDYINANYVDGYNKAKA---YIATQG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 717 PLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWP-----------VTGEELQLAEGFSVRCLS--EKPDETGSf 783
Cdd:cd17667   80 PLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPtenseeygniiVTLKSTKIHACYTVRRFSirNTKVKKGQ- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 784 vfrEFVLKDKHEQRHIHHMQYLAWPDHCVPSDPNLFLEFTERVRAARnrtllqeieeslkqvrlmdadadadengglmre 863
Cdd:cd17667  159 ---KGNPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAAR--------------------------------- 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 864 rkcaasngaTPEdetpvstsvhqcisaaNPPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQ 943
Cdd:cd17667  203 ---------TPE----------------MGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQ 257

                        330
                 ....*....|....*
gi 386770278 944 NVSQYRFVCECICAA 958
Cdd:cd17667  258 TEEQYIFIHDALLEA 272
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 666-958 5.75e-41

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: 152.55  E-value: 5.75e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 666 NAPKNRYRDISPYDCTRVSL--VNSLTG-DYINANYVNMEipgGAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTT 742
Cdd:cd14625   47 NKPKNRYANVIAYDHSRVILqpIEGIMGsDYINANYIDGY---RKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTK 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 743 VMESGRQKCHQYWPVTGEElqlAEGFSVRCLSEKPdETGSFVFREFVLKD--KHEQRHIHHMQYLAWPDHCVPSDPNLFL 820
Cdd:cd14625  124 LEEKSRIKCDQYWPSRGTE---TYGMIQVTLLDTI-ELATFCVRTFSLHKngSSEKREVRQFQFTAWPDHGVPEYPTPFL 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 821 EFTERVRAarnrtllqeieeslkqvrlmdadadadengglmrerkcaasngATPEDETpvstsvhqcisaanpPVIVHCS 900
Cdd:cd14625  200 AFLRRVKT-------------------------------------------CNPPDAG---------------PIVVHCS 221

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386770278 901 AGIGRTGVLILMDtalALMEAREPVYPLDI---VRTMRDQRACMVQNVSQYRFVCECICAA 958
Cdd:cd14625  222 AGVGRTGCFIVID---AMLERIKHEKTVDIyghVTLMRSQRNYMVQTEDQYSFIHDALLEA 279
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 693-951 2.37e-39

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: 144.97  E-value: 2.37e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 693 YINANYVN-MEIPggavNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGEELQLAEGFSVR 771
Cdd:cd14557    1 YINASYIDgFKEP----RKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 772 CLSEK--PDetgsFVFREFVLKDKHEQ---RHIHHMQYLAWPDHCVPSDPNLFLEFTERVRAARNrtllqeieeslkqvr 846
Cdd:cd14557   77 INEEKicPD----YIIRKLNINNKKEKgsgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNN--------------- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 847 lmdadadadengglmrerkcaasngatpedetpvstsvhqcisAANPPVIVHCSAGIGRTGVLILMDTALALMEAREPVY 926
Cdd:cd14557  138 -------------------------------------------FFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGRVD 174

                        250       260
                 ....*....|....*....|....*
gi 386770278 927 PLDIVRTMRDQRACMVQNVSQYRFV 951
Cdd:cd14557  175 VYGYVVKLRRQRCLMVQVEAQYILI 199
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 693-951 3.78e-39

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: 145.12  E-value: 3.78e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 693 YINANYVNMEIpGGAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWP--------VTGEELQL 764
Cdd:cd14598    1 YINASHIKVTV-GGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsrhntVTYGRFKI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 765 AEGFsvrclsekpdETGSFVFREFVLKDKH----EQRHIHHMQYLAWPDHCVPSDPNLFLEFTERVRAARNRTllqeiee 840
Cdd:cd14598   80 TTRF----------RTDSGCYATTGLKIKHlltgQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHT------- 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 841 slkqvrlmdaDADADENGglmrerkcaasngatpedetpvstsvhqcisaANPPVIVHCSAGIGRTGVLILMDTALALME 920
Cdd:cd14598  143 ----------NSTIDPKS--------------------------------PNPPVLVHCSAGVGRTGVVILSEIMIACLE 180

                        250       260       270
                 ....*....|....*....|....*....|....
gi 386770278 921 AREpvyPLDIVRT---MRDQRACMVQNVSQYRFV 951
Cdd:cd14598  181 HNE---MLDIPRVldmLRQQRMMMVQTLSQYTFV 211
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 666-958 7.80e-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: 144.78  E-value: 7.80e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 666 NAPKNRYRDISPYDCTRVSLV---NSLTGDYINANYVN-MEIPggavNRYIATQGPLASTTTDFWRMVQQESSHLLVMLT 741
Cdd:cd14630    3 NRNKNRYGNIISYDHSRVRLQlldGDPHSDYINANYIDgYHRP----RHYIATQGPMQETVKDFWRMIWQENSASVVMVT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 742 TVMESGRQKCHQYWPvtgEELQLAEGFSVRCLSEKPdeTGSFVFREFVLKDK--HEQRHIHHMQYLAWPDHCVPSDPNLF 819
Cdd:cd14630   79 NLVEVGRVKCVRYWP---DDTEVYGDIKVTLIETEP--LAEYVIRTFTVQKKgyHEIREIRQFHFTSWPDHGVPCYATGL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 820 LEFtervraarnrtllqeieesLKQVRLMDadadadengglmrerkcaasngatPEDETpvstsvhqcisaanpPVIVHC 899
Cdd:cd14630  154 LGF-------------------VRQVKFLN------------------------PPDAG---------------PIVVHC 175

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 386770278 900 SAGIGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRFVCECICAA 958
Cdd:cd14630  176 SAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEA 234
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 693-955 1.03e-38

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: 143.35  E-value: 1.03e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 693 YINANYVNMEIPGGAVnrYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGEELQLAegFSVRC 772
Cdd:cd14546    1 YINASTIYDHDPRNPA--YIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHI--YEVHL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 773 LSEKpDETGSFVFREFVLKD--KHEQRHIHHMQYLAWPDHCVPSDPNLFLEFTERVraarNRTllqeieeslkqvrlmda 850
Cdd:cd14546   77 VSEH-IWCDDYLVRSFYLKNlqTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKV----NKS----------------- 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 851 dadadengglMRERKCaasngatpedetpvstsvhqcisaanpPVIVHCSAGIGRTGVLILMDTALALME--AREpvypL 928
Cdd:cd14546  135 ----------YRGRSC---------------------------PIVVHCSDGAGRTGTYILIDMVLNRMAkgAKE----I 173

                        250       260       270
                 ....*....|....*....|....*....|
gi 386770278 929 DIVRT---MRDQRACMVQNVSQYRFVCECI 955
Cdd:cd14546  174 DIAATlehLRDQRPGMVKTKDQFEFVLTAV 203
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 661-950 2.59e-38

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: 144.87  E-value: 2.59e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 661 ARKPANAPKNRYRDISPYDCTRVSL--VNSLTG-DYINANYVNMEIPGGAvnrYIATQGPLASTTTDFWRMVQQESSHLL 737
Cdd:cd14628   47 ANLPCNKFKNRLVNIMPYESTRVCLqpIRGVEGsDYINASFIDGYRQQKA---YIATQGPLAETTEDFWRMLWEHNSTIV 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 738 VMLTTVMESGRQKCHQYWPvtGEELQLAEGFSVRCLSEKpdETGSFVFREFVLKDKH--EQRHIHHMQYLAWPDHCVPSD 815
Cdd:cd14628  124 VMLTKLREMGREKCHQYWP--AERSARYQYFVVDPMAEY--NMPQYILREFKVTDARdgQSRTVRQFQFTDWPEQGVPKS 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 816 PNLFLEFTERVraarnrtllQEIEESLKQvrlmdadadadengglmrerkcaasngatpedetpvstsvhqcisaaNPPV 895
Cdd:cd14628  200 GEGFIDFIGQV---------HKTKEQFGQ-----------------------------------------------DGPI 223

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 386770278 896 IVHCSAGIGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRF 950
Cdd:cd14628  224 SVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQF 278
FERM_F1_PTPN3_like cd17100
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 33-121 2.76e-38

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: 137.44  E-value: 2.76e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  33 QQCVTVLFLDDITHTFRIEKRAKGSELLDQVFQYLELSERDYFGLLFPQKP--GDVVRWVDAQKQFKKQCSSvsldnDAV 110
Cdd:cd17100    1 EVRCIVHFLDDTEQTFEVEKRDKGQVLLDKVFNHLELVEKDYFGLQFSDDSpaTDSMRWLDPLKPIRKQIKG-----GPP 75

                         90
                 ....*....|.
gi 386770278 111 PLLEFRVKFFV 121
Cdd:cd17100   76 YYLNFRVKFYV 86
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 666-958 4.25e-38

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: 144.10  E-value: 4.25e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 666 NAPKNRYRDISPYDCTRVsLVNSLTG----DYINANYVNMEipgGAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLT 741
Cdd:cd14624   47 NKPKNRYANVIAYDHSRV-LLSAIEGipgsDYINANYIDGY---RKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMT 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 742 TVMESGRQKCHQYWPVTGEElqlAEGFSVRCLSEKPdETGSFVFREFVL--KDKHEQRHIHHMQYLAWPDHCVPSDPNLF 819
Cdd:cd14624  123 KLEERSRVKCDQYWPSRGTE---TYGLIQVTLLDTV-ELATYCVRTFALykNGSSEKREVRQFQFTAWPDHGVPEHPTPF 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 820 LEFTERVRAarnrtllqeieeslkqvrlmdadadadengglmrerkcaasngATPEDETpvstsvhqcisaanpPVIVHC 899
Cdd:cd14624  199 LAFLRRVKT-------------------------------------------CNPPDAG---------------PMVVHC 220

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 386770278 900 SAGIGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRFVCECICAA 958
Cdd:cd14624  221 SAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEA 279
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 661-950 6.04e-38

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: 143.72  E-value: 6.04e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 661 ARKPANAPKNRYRDISPYDCTRVSL--VNSLTG-DYINANYVNMEIPGGAvnrYIATQGPLASTTTDFWRMVQQESSHLL 737
Cdd:cd14627   48 ANLPCNKFKNRLVNIMPYETTRVCLqpIRGVEGsDYINASFIDGYRQQKA---YIATQGPLAETTEDFWRMLWENNSTIV 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 738 VMLTTVMESGRQKCHQYWPvtGEELQLAEGFSVRCLSEKpdETGSFVFREFVLKDKH--EQRHIHHMQYLAWPDHCVPSD 815
Cdd:cd14627  125 VMLTKLREMGREKCHQYWP--AERSARYQYFVVDPMAEY--NMPQYILREFKVTDARdgQSRTVRQFQFTDWPEQGVPKS 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 816 PNLFLEFTERVraarnrtllQEIEESLKQvrlmdadadadengglmrerkcaasngatpedetpvstsvhqcisaaNPPV 895
Cdd:cd14627  201 GEGFIDFIGQV---------HKTKEQFGQ-----------------------------------------------DGPI 224

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 386770278 896 IVHCSAGIGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRF 950
Cdd:cd14627  225 SVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQF 279
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 693-958 6.99e-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: 140.82  E-value: 6.99e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 693 YINANYVN-MEIPggavNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPvtgEELQLAEGFSVR 771
Cdd:cd14555    1 YINANYIDgYHRP----NHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP---DDTEVYGDIKVT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 772 CLSEKPdeTGSFVFREFVLKDK--HEQRHIHHMQYLAWPDHCVPSDPNLFLEFTERVRAArnrtllqeieeslkqvrlmd 849
Cdd:cd14555   74 LVETEP--LAEYVVRTFALERRgyHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKAS-------------------- 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 850 adadadengglmrerkcaasngatpedeTPVSTSvhqcisaanpPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPLD 929
Cdd:cd14555  132 ----------------------------NPPSAG----------PIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYN 173

                        250       260
                 ....*....|....*....|....*....
gi 386770278 930 IVRTMRDQRACMVQNVSQYRFVCECICAA 958
Cdd:cd14555  174 CVKELRSRRVNMVQTEEQYIFIHDAILEA 202
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 661-950 9.49e-38

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: 143.33  E-value: 9.49e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 661 ARKPANAPKNRYRDISPYDCTRVSL--VNSLTG-DYINANYVNMEIPGGAvnrYIATQGPLASTTTDFWRMVQQESSHLL 737
Cdd:cd14629   48 ANLPCNKFKNRLVNIMPYELTRVCLqpIRGVEGsDYINASFIDGYRQQKA---YIATQGPLAETTEDFWRMLWEHNSTIV 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 738 VMLTTVMESGRQKCHQYWPvtGEELQLAEGFSVRCLSEKpdETGSFVFREFVLKDKH--EQRHIHHMQYLAWPDHCVPSD 815
Cdd:cd14629  125 VMLTKLREMGREKCHQYWP--AERSARYQYFVVDPMAEY--NMPQYILREFKVTDARdgQSRTIRQFQFTDWPEQGVPKT 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 816 PNLFLEFTERVraarnrtllQEIEESLKQvrlmdadadadengglmrerkcaasngatpedetpvstsvhqcisaaNPPV 895
Cdd:cd14629  201 GEGFIDFIGQV---------HKTKEQFGQ-----------------------------------------------DGPI 224

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 386770278 896 IVHCSAGIGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRF 950
Cdd:cd14629  225 TVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQL 279
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 650-950 1.30e-37

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: 142.48  E-value: 1.30e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 650 YRKNPDlAITEARKPANAPKNRYRDISPYDCTRVSL---VNSLTGDYINANYVNMEIPggAVNRYIATQGPLASTTTDFW 726
Cdd:cd14609   27 YQAEPN-TCSTAQGEANVKKNRNPDFVPYDHARIKLkaeSNPSRSDYINASPIIEHDP--RMPAYIATQGPLSHTIADFW 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 727 RMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGEELQlaEGFSVRCLSEKPdETGSFVFREFVLKD--KHEQRHIHHMQY 804
Cdd:cd14609  104 QMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLY--HIYEVNLVSEHI-WCEDFLVRSFYLKNvqTQETRTLTQFHF 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 805 LAWPDHCVPSDPNLFLEFTERVRAArnrtllqeieeslkqvrlmdadadadengglMRERKCaasngatpedetpvstsv 884
Cdd:cd14609  181 LSWPAEGIPSSTRPLLDFRRKVNKC-------------------------------YRGRSC------------------ 211

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386770278 885 hqcisaanpPVIVHCSAGIGRTGVLILMDTALALMEarEPVYPLDIVRTM---RDQRACMVQNVSQYRF 950
Cdd:cd14609  212 ---------PIIVHCSDGAGRTGTYILIDMVLNRMA--KGVKEIDIAATLehvRDQRPGMVRTKDQFEF 269
FERM_C_FARP1-like cd13193
FERM domain C-lobe of FERM, RhoGEF and pleckstrin domain-containing protein 1 and related ...
 219-338 2.48e-37

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: 135.93  E-value: 2.48e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 219 EHAKRLELYGIDLHRATDSNGKELQLGVSAVGLLVFQHSLRVNTFSWSKMVKVSFKRKDFFIQLRREPSENYDTLLGFGM 298
Cdd:cd13193    1 ETARRCELYGIRLHPAKDREGVKLNLAVAHMGILVFQGFTKINTFSWAKIRKLSFKRKRFLIKLHPEAYGSYKDTVEFSF 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 386770278 299 SSHKHAKALWKSCVEHHSFFRLKRPHRLSRFLN--ISLGSKF 338
Cdd:cd13193   81 ESRNECKSFWKKCIEHHAFFRCSEVPKPPSPKLrlFSRGSSF 122
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 655-951 8.05e-37

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 141.29  E-value: 8.05e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 655 DLAITEARKPANAPKNRYRDISPYDCTRVSLVNS--LTGDYINANYVN-MEIPggavNRYIATQGPLASTTTDFWRMVQQ 731
Cdd:PHA02747  40 DGLIANFEKPENQPKNRYWDIPCWDHNRVILDSGggSTSDYIHANWIDgFEDD----KKFIATQGPFAETCADFWKAVWQ 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 732 ESSHLLVMLT-TVMESGRQKCHQYWPVTGEELQLAEGFSVRCLSEKPDETGSFVFREFVLKDKHEQRHIHHMQYLAWPDH 810
Cdd:PHA02747 116 EHCSIIVMLTpTKGTNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQCSEWFED 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 811 CVPSDPNLFLEFtervraarnrtllqeieeslkqVRLMDadadadengglmRERKCAASNgATPEDetpvstsvhQCISa 890
Cdd:PHA02747 196 ETPSDHPDFIKF----------------------IKIID------------INRKKSGKL-FNPKD---------ALLC- 230

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386770278 891 anpPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRFV 951
Cdd:PHA02747 231 ---PIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFI 288
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 650-950 1.08e-36

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: 140.19  E-value: 1.08e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 650 YRKNPDLAITeARKPANAPKNRYRDISPYDCTRVSLV---NSLTGDYINANYVNMEIPGGAVnrYIATQGPLASTTTDFW 726
Cdd:cd14610   29 YQAEPNATNV-AQREENVQKNRSLAVLPYDHSRIILKaenSHSHSDYINASPIMDHDPRNPA--YIATQGPLPATVADFW 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 727 RMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGEELQlaEGFSVRCLSEKPdETGSFVFREFVLKD--KHEQRHIHHMQY 804
Cdd:cd14610  106 QMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLY--HIYEVNLVSEHI-WCEDFLVRSFYLKNlqTNETRTVTQFHF 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 805 LAWPDHCVPSDPNLFLEFTERVRAArnrtllqeieeslkqvrlmdadadadengglMRERKCaasngatpedetpvstsv 884
Cdd:cd14610  183 LSWNDQGVPASTRSLLDFRRKVNKC-------------------------------YRGRSC------------------ 213

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386770278 885 hqcisaanpPVIVHCSAGIGRTGVLILMDTALALME--AREpvypLDIVRT---MRDQRACMVQNVSQYRF 950
Cdd:cd14610  214 ---------PIIVHCSDGAGRSGTYILIDMVLNKMAkgAKE----IDIAATlehLRDQRPGMVQTKEQFEF 271
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 661-958 1.57e-36

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


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 139.41  E-value: 1.57e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 661 ARKPANAPKNRYRDISPYDCTRVSLvNSLTG----DYINANYVN-MEIPggavNRYIATQGPLASTTTDFWRMVQQESSH 735
Cdd:cd14633   35 AKKDENRMKNRYGNIIAYDHSRVRL-QPIEGetssDYINGNYIDgYHRP----NHYIATQGPMQETIYDFWRMVWHENTA 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 736 LLVMLTTVMESGRQKCHQYWPvtgEELQLAEGFSVRCLseKPDETGSFVFREFVLKDK--HEQRHIHHMQYLAWPDHCVP 813
Cdd:cd14633  110 SIIMVTNLVEVGRVKCCKYWP---DDTEIYKDIKVTLI--ETELLAEYVIRTFAVEKRgvHEIREIRQFHFTGWPDHGVP 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 814 SDPNLFLEFTERVRAarnrtllqeieeslkqvrlmdadadadengglmrerkcaasngatpedETPVSTSvhqcisaanp 893
Cdd:cd14633  185 YHATGLLGFVRQVKS------------------------------------------------KSPPNAG---------- 206

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386770278 894 PVIVHCSAGIGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRFVCECICAA 958
Cdd:cd14633  207 PLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEA 271
FERM_C_4_1_family cd13184
FERM domain C-lobe of Protein 4.1 family; The protein 4.1 family includes four well-defined ...
 227-320 3.40e-36

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: 131.68  E-value: 3.40e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 227 YGIDLHRATDSNGKELQLGVSAVGLLVFQHSLRVNTFSWSKMVKVSFKRKDFFIQLRREPSENYDTLLGFGMSSHKHAKA 306
Cdd:cd13184    1 YGVDLHPAKDSEGVDIMLGVCSSGLLVYRDRLRINRFAWPKVLKISYKRNNFYIKIRPGEFEQYETTIGFKLPNHRAAKR 80

                         90
                 ....*....|....
gi 386770278 307 LWKSCVEHHSFFRL 320
Cdd:cd13184   81 LWKVCVEHHTFFRL 94
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 687-958 3.41e-36

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 136.30  E-value: 3.41e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 687 NSLTGDYINANYVN-MEIPggavNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPvtgEELQLA 765
Cdd:cd14631    9 DDPSSDYINANYIDgYQRP----SHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP---DDTEVY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 766 EGFSVRCLSEKPdeTGSFVFREFVLKDK--HEQRHIHHMQYLAWPDHCVPSDPNLFLEFTERVRAArnrtllqeieeslk 843
Cdd:cd14631   82 GDFKVTCVEMEP--LAEYVVRTFTLERRgyNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLS-------------- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 844 qvrlmdadadadengglmrerkcaasngatpedeTPVSTSvhqcisaanpPVIVHCSAGIGRTGVLILMDTALALMEARE 923
Cdd:cd14631  146 ----------------------------------NPPSAG----------PIVVHCSAGAGRTGCYIVIDIMLDMAEREG 181

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 386770278 924 PVYPLDIVRTMRDQRACMVQNVSQYRFVCECICAA 958
Cdd:cd14631  182 VVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEA 216
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 669-951 5.23e-36

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: 136.20  E-value: 5.23e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 669 KNRYRDISPYDCTRVSL----VNSLTGDYINANYVNMEipGGAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVM 744
Cdd:cd14611    2 KNRYKTILPNPHSRVCLkpknSNDSLSTYINANYIRGY--GGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 745 ESgRQKCHQYWPvtgEELQLAEGFSVRCLSEKpdETGSFVFREFVLKDKHEQRHIHHMQYLAWPDHCVPSDPNLFLEfte 824
Cdd:cd14611   80 EK-NEKCVLYWP---EKRGIYGKVEVLVNSVK--ECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQ--- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 825 rvraarnrtLLQEIEEslkqvrlmdadadadengglmrERKCAASNGatpedetpvstsvhqcisaanpPVIVHCSAGIG 904
Cdd:cd14611  151 ---------LMLDVEE----------------------DRLASPGRG----------------------PVVVHCSAGIG 177

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 386770278 905 RTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRFV 951
Cdd:cd14611  178 RTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFV 224
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 642-962 1.95e-35

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 137.06  E-value: 1.95e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 642 LLAQYELMYRKNPDLAITEARKPANAPKNRYRDISPYDCTRVSLVNSLTG-DYINANYVNMEipgGAVNRYIATQGPLAS 720
Cdd:PHA02742  28 LKEEHEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDGGdDFINASYVDGH---NAKGRFICTQAPLEE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 721 TTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWpVTGEELQLAEG-FSVRCLSEKPDETGSFVFREFVLKDKHEQRHI 799
Cdd:PHA02742 105 TALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYW-MPHERGKATHGeFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDI 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 800 HHMQYLAWPDHCVPSDPNLFLEFTERVRAArnrtllqeieeslkqvrlmDADADADENGglmrerkcaasngatpedETP 879
Cdd:PHA02742 184 KHFAYEDWPHGGLPRDPNKFLDFVLAVREA-------------------DLKADVDIKG------------------ENI 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 880 VStsvhqcisaaNPPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQR-ACMvqNVSQYRFVCECICAA 958
Cdd:PHA02742 227 VK----------EPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRhNCL--SLPQQYIFCYFIVLI 294


                 ....
gi 386770278 959 YMKI 962
Cdd:PHA02742 295 FAKL 298
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 661-960 4.25e-34

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: 132.84  E-value: 4.25e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 661 ARKPANAPKNRYRDISPYDCTRVSLVnSLTG----DYINANYVNMEipgGAVNRYIATQGPLASTTTDFWRMVQQESSHL 736
Cdd:cd14621   47 ASKEENKEKNRYVNILPYDHSRVHLT-PVEGvpdsDYINASFINGY---QEKNKFIAAQGPKEETVNDFWRMIWEQNTAT 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 737 LVMLTTVMESGRQKCHQYWP-----------VTGEELQLAEGFSVR--CLSEKPDETGsfvfrefvlkdKHEQRHIHHMQ 803
Cdd:cd14621  123 IVMVTNLKERKECKCAQYWPdqgcwtygnirVSVEDVTVLVDYTVRkfCIQQVGDVTN-----------KKPQRLITQFH 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 804 YLAWPDHCVPSDPNLFLEFTERVRAarnrtllqeieeslkqvrlmdadadadengglmrerkcaasngatpedetpvsts 883
Cdd:cd14621  192 FTSWPDFGVPFTPIGMLKFLKKVKN------------------------------------------------------- 216

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386770278 884 vhqCISAANPPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRFVCECICAAYM 960
Cdd:cd14621  217 ---CNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYL 290
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 672-951 6.36e-34

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: 130.06  E-value: 6.36e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 672 YRDISPYDCTRVSLV---NSLTGDYINANYVNMEipgGAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGR 748
Cdd:cd14620    1 YPNILPYDHSRVILSqldGIPCSDYINASYIDGY---KEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 749 QKCHQYWPVTGEELQlaegFSVRCLSEKPDETGSFVFREFVLKDKHEQ-----RHIHHMQYLAWPDHCVPSDPNLFLEFT 823
Cdd:cd14620   78 EKCYQYWPDQGCWTY----GNIRVAVEDCVVLVDYTIRKFCIQPQLPDgckapRLVTQLHFTSWPDFGVPFTPIGMLKFL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 824 ERVRAArnrtllqeieeslkqvrlmdadadadengglmrerkcaasngatpedeTPVSTSvhqcisaanpPVIVHCSAGI 903
Cdd:cd14620  154 KKVKSV------------------------------------------------NPVHAG----------PIVVHCSAGV 175

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 386770278 904 GRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRFV 951
Cdd:cd14620  176 GRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFI 223
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 693-951 9.13e-34

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: 128.88  E-value: 9.13e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 693 YINANYVNMEipgGAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGEELQlaegFSVRC 772
Cdd:cd14551    1 YINASYIDGY---QEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTY----GNLRV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 773 LSEKPDETGSFVFREFVLK------DKHEQRHIHHMQYLAWPDHCVPSDPNLFLEFTERVRAARnrtllqeieeslkqvr 846
Cdd:cd14551   74 RVEDTVVLVDYTTRKFCIQkvnrgiGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSAN---------------- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 847 lmdadadadengglmrerkcaasngaTPEDEtpvstsvhqcisaanpPVIVHCSAGIGRTGVLILMDTALALMEAREPVY 926
Cdd:cd14551  138 --------------------------PPRAG----------------PIVVHCSAGVGRTGTFIVIDAMLDMMHAEGKVD 175

                        250       260
                 ....*....|....*....|....*
gi 386770278 927 PLDIVRTMRDQRACMVQNVSQYRFV 951
Cdd:cd14551  176 VFGFVSRIRQQRSQMVQTDMQYVFI 200
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 693-958 1.06e-33

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: 128.63  E-value: 1.06e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 693 YINANYVNMEipgGAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGEELQlaegfSVRC 772
Cdd:cd14632    1 YINANYIDGY---HRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYG-----DIKI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 773 LSEKPDETGSFVFREFVLKD-----KHEQRHIHhmqYLAWPDHCVPSDPNLFLEFTERVRAarnrtllqeieeslkqvrl 847
Cdd:cd14632   73 TLLKTETLAEYSVRTFALERrgysaRHEVKQFH---FTSWPEHGVPYHATGLLAFIRRVKA------------------- 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 848 mdadadadengglmrerkcaasngATPEDETpvstsvhqcisaanpPVIVHCSAGIGRTGVLILMDTALALMEAREPVYP 927
Cdd:cd14632  131 ------------------------STPPDAG---------------PVVVHCSAGAGRTGCYIVLDVMLDMAECEGVVDI 171

                        250       260       270
                 ....*....|....*....|....*....|.
gi 386770278 928 LDIVRTMRDQRACMVQNVSQYRFVCECICAA 958
Cdd:cd14632  172 YNCVKTLCSRRINMIQTEEQYIFIHDAILEA 202
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
659-948 2.11e-33

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 130.60  E-value: 2.11e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 659 TEARKPANA---PKNRYRDISPYDCTRVSLvnslTGDYINANYVnmEIPGGavNRYIATQGPLASTTTDFWRMVQQESSH 735
Cdd:COG5599   32 NDPQYLQNIngsPLNRFRDIQPYKETALRA----NLGYLNANYI--QVIGN--HRYIATQYPLEEQLEDFFQMLFDNNTP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 736 LLVMLTT---VMESgRQKCHQYWPVTGEElqLAEGFSVRCLSEKPDETGsFVFREFVLK---DKHEQRHIHHMQYLAWPD 809
Cdd:COG5599  104 VLVVLASddeISKP-KVKMPVYFRQDGEY--GKYEVSSELTESIQLRDG-IEARTYVLTikgTGQKKIEIPVLHVKNWPD 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 810 HCVPSDPNLfleftervraarnRTLLQEIEESLKqvrlmdaDADADEngglmrerkcaasngatpedetpvstsvhqcis 889
Cdd:COG5599  180 HGAISAEAL-------------KNLADLIDKKEK-------IKDPDK--------------------------------- 206

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386770278 890 aaNPPViVHCSAGIGRTGVLILMdtaLALMEAREPVYPL-----DIVRTMRDQRAC-MVQNVSQY 948
Cdd:COG5599  207 --LLPV-VHCRAGVGRTGTLIAC---LALSKSINALVQItlsveEIVIDMRTSRNGgMVQTSEQL 265
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 693-951 1.25e-32

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: 125.86  E-value: 1.25e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 693 YINANYVNmeipggAVNR---YIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGEELQ---LAE 766
Cdd:cd17668    1 YINANYVD------GYNKpkaYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYgnfLVT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 767 GFSVRCLSekpdetgSFVFREFVL----------KDKHEQRHIHHMQYLAWPDHCVPSDPNLFLEFTERVRAARnrtllq 836
Cdd:cd17668   75 QKSVQVLA-------YYTVRNFTLrntkikkgsqKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAK------ 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 837 eieeslkqvrlmdadadadengglmrerkcaasngatpedetpvstsvhqciSAANPPVIVHCSAGIGRTGVLILMDTAL 916
Cdd:cd17668  142 ----------------------------------------------------RHAVGPVVVHCSAGVGRTGTYIVLDSML 169

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 386770278 917 ALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRFV 951
Cdd:cd17668  170 QQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFI 204
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 693-950 3.69e-32

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: 124.42  E-value: 3.69e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 693 YINANYVNMEIPGGAvnRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPvTGEELQLAEGFSVRC 772
Cdd:cd14539    1 YINASLIEDLTPYCP--RFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWP-TERGQALVYGAITVS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 773 LSEKPDeTGSFVFREFVL--KDKHEQRHIHHMQYLAWPDHCVPSDPNLFLEFtervraarnrtlLQEIEESLKQVRLMDA 850
Cdd:cd14539   78 LQSVRT-TPTHVERIISIqhKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRF------------IEEVHSHYLQQRSLQT 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 851 dadadengglmrerkcaasngatpedetpvstsvhqcisaanpPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPL-D 929
Cdd:cd14539  145 -------------------------------------------PIVVHCSSGVGRTGAFCLLYAAVQEIEAGNGIPDLpQ 181

                        250       260
                 ....*....|....*....|.
gi 386770278 930 IVRTMRDQRACMVQNVSQYRF 950
Cdd:cd14539  182 LVRKMRQQRKYMLQEKEHLKF 202
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 663-950 7.66e-32

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 127.07  E-value: 7.66e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 663 KPANAPKNRYRDISPYDCTRVSLVN--SLT----GD----------------YINANYVNmeiPGGAVNRYIATQGPLAS 720
Cdd:PHA02746  48 KKENLKKNRFHDIPCWDHSRVVINAheSLKmfdvGDsdgkkievtsednaenYIHANFVD---GFKEANKFICAQGPKED 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 721 TTTDFWRMVQQESSHLLVMLTTVmESGRQKCHQYWpVTGEELQLAEG-FSVRCLSEKpdETGSFVFREFVLKDKHEQ--R 797
Cdd:PHA02746 125 TSEDFFKLISEHESQVIVSLTDI-DDDDEKCFELW-TKEEDSELAFGrFVAKILDII--EELSFTKTRLMITDKISDtsR 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 798 HIHHMQYLAWPDHCVPSDPNLFLEFTERVRaarnrtllQEIEESLKQvrlmdADADADENGglmrerkcaasngatpede 877
Cdd:PHA02746 201 EIHHFWFPDWPDNGIPTGMAEFLELINKVN--------EEQAELIKQ-----ADNDPQTLG------------------- 248

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386770278 878 tpvstsvhqcisaanpPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRF 950
Cdd:PHA02746 249 ----------------PIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAF 305
PHA02738 PHA02738
hypothetical protein; Provisional
 665-969 1.46e-31

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 126.19  E-value: 1.46e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 665 ANAPKNRYRDISPYDCTRVSLVNSLT-GDYINANYVN-MEipggAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTT 742
Cdd:PHA02738  48 KNRKLNRYLDAVCFDHSRVILPAERNrGDYINANYVDgFE----YKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCK 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 743 VMESGRQKCHQYWPVTgeelqlaegfsvrclsekpdETGSFVFREFVLKDKHEQRHIH-------------------HMQ 803
Cdd:PHA02738 124 KKENGREKCFPYWSDV--------------------EQGSIRFGKFKITTTQVETHPHyvkstllltdgtsatqtvtHFN 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 804 YLAWPDHCVPSDPNLFLEFTERVRAArnrtllqeiEESLKQVRLMDADadadengglmrerkcaasNGATPedetpvsts 883
Cdd:PHA02738 184 FTAWPDHDVPKNTSEFLNFVLEVRQC---------QKELAQESLQIGH------------------NRLQP--------- 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 884 vhqcisaanPPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYrFVCECICAAYMKIS 963
Cdd:PHA02738 228 ---------PPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQY-FFCYRAVKRYVNLT 297


                 ....*.
gi 386770278 964 RSSAAI 969
Cdd:PHA02738 298 VNKVSK 303
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 693-950 2.32e-31

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: 122.19  E-value: 2.32e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 693 YINANYVnmEIPG-GAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQ-KCHQYWPVTGEELQLAEGFSV 770
Cdd:cd17658    1 YINASLV--ETPAsESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEENESREFGRISV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 771 RCLSEKPDETgSFVFREFVLKDKHEQ---RHIHHMQYLAWPDHCVPSDpnlflefTERVRaarnrtllqEIEESLKQVrl 847
Cdd:cd17658   79 TNKKLKHSQH-SITLRVLEVQYIESEeppLSVLHIQYPEWPDHGVPKD-------TRSVR---------ELLKRLYGI-- 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 848 mdadadadengglmrerkcaasngatPEDETpvstsvhqcisaanpPVIVHCSAGIGRTGVLILMDTALALMEAREpVYP 927
Cdd:cd17658  140 --------------------------PPSAG---------------PIVVHCSAGIGRTGAYCTIHNTIRRILEGD-MSA 177

                        250       260
                 ....*....|....*....|....*.
gi 386770278 928 LDI---VRTMRDQRACMVQNVSQYRF 950
Cdd:cd17658  178 VDLsktVRKFRSQRIGMVQTQDQYIF 203
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 693-950 7.67e-30

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: 117.76  E-value: 7.67e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 693 YINANYV---NMEipggavNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGeelQLAEG-F 768
Cdd:cd14552    1 YINASFIdgyRQK------DAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDG---SVSSGdI 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 769 SVRClsEKPDETGSFVFREF-VLKDKHEQ-RHIHHMQYLAWPDHCVPSDPNLFLEFTERVRAARNRTllqeieeslkqvr 846
Cdd:cd14552   72 TVEL--KDQTDYEDYTLRDFlVTKGKGGStRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQS------------- 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 847 lmdadadadengglmrerkcaasngatpedetpvstsvhqcisaANPPVIVHCSAGIGRTGVLILMDTALALMEAREPVY 926
Cdd:cd14552  137 --------------------------------------------GNHPITVHCSAGAGRTGTFCALSTVLERVKAEGVLD 172

                        250       260
                 ....*....|....*....|....
gi 386770278 927 PLDIVRTMRDQRACMVQNVSQYRF 950
Cdd:cd14552  173 VFQVVKSLRLQRPHMVQTLEQYEF 196
FERM_C pfam09380
FERM C-terminal PH-like domain;
236-322 3.14e-29

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 111.58  E-value: 3.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  236 DSNGKELQLGVSAVGLLVFQHSLRV-NTFSWSKMVKVSFKRKDFFIQLRREPSEnydTLLGFGMSSHKHAKALWKSCVEH 314
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKIlNLFPWREIRKISFKRKKFLIKLRDKSSE---ETLGFYTESSRACKYLWKLCVEQ 77


                  ....*...
gi 386770278  315 HSFFRLKR 322
Cdd:pfam09380  78 HTFFRLRR 85
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 123-232 6.54e-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: 111.98  E-value: 6.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  123 DPSRLQEEFTRYQFYLQIKRNILLGKLPCSSNTQCLLASYTVQSELGDFNALEHQPGYLSG-----MQLLCDQTTEA-ER 196
Cdd:pfam00373   2 LELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLesflpKQLLRKMKSKElEK 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 386770278  197 KVGELHKLHRGQLPADAEYNYLEHAKRLELYGIDLH 232
Cdd:pfam00373  82 RVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 693-953 1.03e-28

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: 114.43  E-value: 1.03e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 693 YINANYVNMEIPGGAvnrYIATQGPLASTTTDFWRMVQQESSHLLVMLTTvMESGRQKCHQYWPvtgEELQLAEG-FSVR 771
Cdd:cd14556    1 YINAALLDSYKQPAA---FIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQ-LDPKDQSCPQYWP---DEGSGTYGpIQVE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 772 CLSEKPDEtgSFVFREFVL----KDKHEQRHIHHMQYLAWPDH-CVPSDPNLFLEftervraarnrtLLQEIEESLKQvr 846
Cdd:cd14556   74 FVSTTIDE--DVISRIFRLqnttRPQEGYRMVQQFQFLGWPRDrDTPPSKRALLK------------LLSEVEKWQEQ-- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 847 lmdadadadengglmrerkcaasngatpedetpvstsvhqcisAANPPVIVHCSAGIGRTGVLILMDTALALMEAREPVY 926
Cdd:cd14556  138 -------------------------------------------SGEGPIVVHCLNGVGRSGVFCAISSVCERIKVENVVD 174

                        250       260
                 ....*....|....*....|....*..
gi 386770278 927 PLDIVRTMRDQRACMVQNVSQYRFVCE 953
Cdd:cd14556  175 VFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 692-950 8.44e-28

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: 111.64  E-value: 8.44e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 692 DYINANYVNmeipgGAVNR--YIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGeelQLAEG-F 768
Cdd:cd14622    1 DYINASFID-----GYRQKdyFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEG---SVTHGeI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 769 SVRCLSEKPDETgsFVFREFVLKDKHEQ--RHIHHMQYLAWPDHCVPSDPNLFLEFTERVRAARNRTllqeieeslkqvr 846
Cdd:cd14622   73 TIEIKNDTLLET--ISIRDFLVTYNQEKqtRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQT------------- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 847 lmdadadadengglmrerkcaasngatpedetpvstsvhqcisaANPPVIVHCSAGIGRTGVLILMDTALALMEAREPVY 926
Cdd:cd14622  138 --------------------------------------------GNHPIVVHCSAGAGRTGTFIALSNILERVKAEGLLD 173

                        250       260
                 ....*....|....*....|....
gi 386770278 927 PLDIVRTMRDQRACMVQNVSQYRF 950
Cdd:cd14622  174 VFQTVKSLRLQRPHMVQTLEQYEF 197
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 693-950 9.98e-28

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: 111.33  E-value: 9.98e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 693 YINANYVNmeipGGAVNR-YIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGE-----ELQLAE 766
Cdd:cd14558    1 YINASFID----GYWGPKsLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKtygdiEVELKD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 767 gfsvrclSEKPdetGSFVFREFVLK--DKHEQRHIHHMQYLAWPDHCVPSDPnlfLEFTERVRAARnrtllqeieeslkq 844
Cdd:cd14558   77 -------TEKS---PTYTVRVFEIThlKRKDSRTVYQYQYHKWKGEELPEKP---KDLVDMIKSIK-------------- 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 845 vrlmdadadadengglmreRKCAASNGATPEdetpvstsvhqcisaaNPPVIVHCSAGIGRTGV----LILMDTAlalmE 920
Cdd:cd14558  130 -------------------QKLPYKNSKHGR----------------SVPIVVHCSDGSSRTGIfcalWNLLESA----E 170

                        250       260       270
                 ....*....|....*....|....*....|
gi 386770278 921 AREPVYPLDIVRTMRDQRACMVQNVSQYRF 950
Cdd:cd14558  171 TEKVVDVFQVVKALRKQRPGMVSTLEQYQF 200
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 132-224 3.83e-27

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


Pssm-ID: 271216  Cd Length: 99  Bit Score: 106.18  E-value: 3.83e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 132 TRYQFYLQIKRNILLGKLPCSSNTQCLLASYTVQSELGDFNALEHQPGYLSGMQLLCDQT------TEAERKVGELHKLH 205
Cdd:cd14473    1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLSLKRFLPKQLlkqrkpEEWEKRIVELHKKL 80

                         90
                 ....*....|....*....
gi 386770278 206 RGQLPADAEYNYLEHAKRL 224
Cdd:cd14473   81 RGLSPAEAKLKYLKIARKL 99
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
799-955 1.16e-26

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 105.13  E-value: 1.16e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278   799 IHHMQYLAWPDHCVPSDPNLFLEFTERVRAARNrtllqeieeslkqvrlmdadadadengglmrerkcaasngatpedet 878
Cdd:smart00404   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLN----------------------------------------------- 34

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386770278   879 pvstsvhqcISAANPPVIVHCSAGIGRTGVLILMDTALALMEAREP-VYPLDIVRTMRDQRACMVQNVSQYRFVCECI 955
Cdd:smart00404  35 ---------QSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVKELRSQRPGMVQTEEQYLFLYRAL 103
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 799-955 1.16e-26

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: 105.13  E-value: 1.16e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278   799 IHHMQYLAWPDHCVPSDPNLFLEFTERVRAARNrtllqeieeslkqvrlmdadadadengglmrerkcaasngatpedet 878
Cdd:smart00012   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLN----------------------------------------------- 34

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386770278   879 pvstsvhqcISAANPPVIVHCSAGIGRTGVLILMDTALALMEAREP-VYPLDIVRTMRDQRACMVQNVSQYRFVCECI 955
Cdd:smart00012  35 ---------QSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVKELRSQRPGMVQTEEQYLFLYRAL 103
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 671-950 3.23e-26

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: 107.82  E-value: 3.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 671 RYRDISPYDCTRVSLV---NSLTGDYINANYVNMEipgGAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESG 747
Cdd:cd14623    1 RVLQIIPYEFNRVIIPvkrGEENTDYVNASFIDGY---RQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 748 RQKCHQYWPVTGeeLQLAEGFSVRClsEKPDETGSFVFREFVLKDKHEQ--RHIHHMQYLAWPDHCVPSDpnlflefter 825
Cdd:cd14623   78 QEKCAQYWPSDG--SVSYGDITIEL--KKEEECESYTVRDLLVTNTRENksRQIRQFHFHGWPEVGIPSD---------- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 826 vraarNRTLLQEIEESLKQVRlmdadadadengglmrerkcaasngatpedetpvstsvhqciSAANPPVIVHCSAGIGR 905
Cdd:cd14623  144 -----GKGMINIIAAVQKQQQ------------------------------------------QSGNHPITVHCSAGAGR 176

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 386770278 906 TGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRF 950
Cdd:cd14623  177 TGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEF 221
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 504-589 2.28e-22

canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467153 [Multi-domain]  Cd Length: 81  Bit Score: 91.84  E-value: 2.28e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 504 TIRLQADEQGRYGFNVKGGVDLSLPVQVSKVVPHTPADRCtPRVCEGDEVLMINGRDVHGLRHEQVVAMIRdcrhQASGE 583
Cdd:cd00136    1 TVTLEKDPGGGLGFSIRGGKDGGGGIFVSRVEPGGPAARD-GRLRVGDRILEVNGVSLEGLTHEEAVELLK----SAGGE 75


                 ....*.
gi 386770278 584 LLLTVR 589
Cdd:cd00136   76 VTLTVR 81
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 ...
 228-319 1.27e-20

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: 87.34  E-value: 1.27e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 228 GIDLHRATDSNGKELQLGVSAVGLLVFQHSLRVNTFSWSKMVKVSFKRKDFFIQLRREPSENYDTLLGFGMSSHKHAKAL 307
Cdd:cd13186    1 GVDLHPVKGEDGNEYFLGLTPTGILVFENKTKIGLFFWPRITKLDFKGKKLKLVVKEKDDQEQEHTFVFRLPNKKACKHL 80

                         90
                 ....*....|..
gi 386770278 308 WKSCVEHHSFFR 319
Cdd:cd13186   81 WKCAVEHHAFFR 92
FERM_F1_FARP1_like cd17098
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, RhoGEF and ...
 34-124 5.15e-20

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: 85.34  E-value: 5.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  34 QCVTVLFLDDITHTFRIEKRAKGSELLDQVFQYLELSERDYFGLLFPQKPGDVVrWVDAQKQFKKQcssVSLDNDAVplL 113
Cdd:cd17098    1 LHVKVQMLDDTVHIFQVQQKALGEVLFDQVCKHLNLLESDYFGLEFTDPEGNKC-WLDPEKPILRQ---VKRPKDVV--F 74

                         90
                 ....*....|.
gi 386770278 114 EFRVKFFVSDP 124
Cdd:cd17098   75 KFVVKFYTPDP 85
FERM_C_FRMD3_FRMD5 cd13192
FERM domain C-lobe of FERM domain-containing protein 3 and 5 (FRMD3 and 5); FRMD3 (also called ...
 213-319 3.41e-19

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: 83.60  E-value: 3.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 213 AEYNYLEHAKRLELYGIDLHRATDSNGKELQLGVSAVGLLVFQHSLRVNTFSWSKMVKVSFKRKDFFIQLRRepSENYDT 292
Cdd:cd13192    1 AEDNFLRKAATLETYGVDPHPVKDHRGNQLYLGFTHTGIVTFQGGKRVHHFRWNDITKFNYEGKMFILHVMQ--KEEKKH 78

                         90       100
                 ....*....|....*....|....*..
gi 386770278 293 LLGFGMSSHKHAKALWKSCVEHHSFFR 319
Cdd:cd13192   79 TLGFKCPTPAACKHLWKCAVEQQAFYT 105
FERM_N pfam09379
FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the ...
 38-101 3.84e-19

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: 81.87  E-value: 3.84e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386770278   38 VLFLDDITHTFRIEKRAKGSELLDQVFQYLELSERDYFGLLFPQKpGDVVRWVDAQKQFKKQCS 101
Cdd:pfam09379   1 VRLLDGTVLEFDVQPKATGQVLLDQVCNHLNLKEKDYFGLQFLDD-NGEHRWLDLSKRLSKQAP 63
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
 35-119 7.95e-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: 81.87  E-value: 7.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  35 CVTVLFLDDITHTFRIEKRAKGSELLDQVFQYLELSERDYFGLLFPQkPGDVVRWVDAQKQFKKQcssvsLDNDAVPLLE 114
Cdd:cd01765    2 SCRVRLLDGTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFYED-NDGQKHWLDLDKKISKQ-----LKRSGPYQFY 75


                 ....*
gi 386770278 115 FRVKF 119
Cdd:cd01765   76 FRVKF 80
FERM_F1_PTPN4 cd17194
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 37-121 5.51e-18

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: 79.57  E-value: 5.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  37 TVLFLDDITHTFRIEKRAKGSELLDQVFQYLELSERDYFGLLFPQKPGDVVRWVDAQKQFKKQCSSVSLDNdavplLEFR 116
Cdd:cd17194    5 NILLLDNTVQAFKVNKHDQGQVLLDLVFKHLDLTERDYFGLQLADDSTDNPRWLDPNKPIRKQLKRGSPHN-----LNFR 79


                 ....*
gi 386770278 117 VKFFV 121
Cdd:cd17194   80 VKFFV 84
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 693-827 2.08e-16

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: 78.52  E-value: 2.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 693 YINANYVNmeipgG--AVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESgrQKCHQYWPVTGEELQlAEGFSV 770
Cdd:cd14550    1 YINASYLQ-----GyrRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELN--EDEPIYWPTKEKPLE-CETFKV 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386770278 771 RCLSEK---PDETGSFVFREFVLKDKHEQR--HIHHMQYLAWPDHCVPsdPNLFLEFTERVR 827
Cdd:cd14550   73 TLSGEDhscLSNEIRLIVRDFILESTQDDYvlEVRQFQCPSWPNPCSP--IHTVFELINTVQ 132
FERM_F1_EPB41L5_like cd17108
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 34-120 2.83e-15

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: 71.61  E-value: 2.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  34 QCvTVLFLDDITHTFRIEKRAKGSELLDQVFQYLELSERDYFGLLFpQKPGDVVRWVDAQKQFKKQcssvsLDNDAVPLL 113
Cdd:cd17108    2 QC-KVILLDGTDLSIELPKKAKGQELYEQVFYHLDLIEKDYFGLQF-MDAAQVQHWLDPTKKIKKQ-----VKIGPPYTL 74


                 ....*..
gi 386770278 114 EFRVKFF 120
Cdd:cd17108   75 RFRVKFY 81
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 504-589 4.47e-15

PDZ domain; PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 71.16  E-value: 4.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  504 TIRLQADEQGRYGFNVKGGVDLSL-PVQVSKVVPHTPADRctPRVCEGDEVLMINGRDVHGLRHEQVVAMIRdcrhQASG 582
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKGGSDQGDpGIFVSEVLPGGAAEA--GGLKVGDRILSINGQDVENMTHEEAVLALK----GSGG 74


                  ....*..
gi 386770278  583 ELLLTVR 589
Cdd:pfam00595  75 KVTLTIL 81
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 502-591 4.44e-14

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 68.56  E-value: 4.44e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278   502 LITIRLQADEQGrYGFNVKGGVDLSLPVQVSKVVPHTPADRCtpRVCEGDEVLMINGRDVHGLRHEQVVAMIRdcrhQAS 581
Cdd:smart00228   2 PRLVELEKGGGG-LGFSLVGGKDEGGGVVVSSVVPGSPAAKA--GLRVGDVILEVNGTSVEGLTHLEAVDLLK----KAG 74

                           90
                   ....*....|
gi 386770278   582 GELLLTVRPQ 591
Cdd:smart00228  75 GKVTLTVLRG 84
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 228-319 6.69e-14

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: 68.17  E-value: 6.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 228 GIDLHRATDSNGK--ELQLGVSAVGLLVFQHS--LRVNTFSWSKMVKVSFKR-KDFFIQLRREPSENYdtlLGFGMSSHK 302
Cdd:cd00836    1 GVEFFPVKDKSKKgsPIILGVNPEGISVYDELtgQPLVLFPWPNIKKISFSGaKKFTIVVADEDKQSK---LLFQTPSRQ 77

                         90
                 ....*....|....*..
gi 386770278 303 hAKALWKSCVEHHSFFR 319
Cdd:cd00836   78 -AKEIWKLIVGYHRFLL 93
PDZ_ZASP52-like cd23068
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ...
 504-589 7.03e-14

PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Drosophila melanogaster Zasp52 and related domains. Drosophila melanogaster Zasp52 (also known as Z band alternatively spliced PDZ-motif protein or Zasp) colocalizes with integrins at myotendinous junctions and with alpha-actinin at Z-disks and is required for muscle attachment as well as Z-disk assembly and maintenance. The Zasp52 actin-binding site includes the extended PDZ domain and the ZM region. The Zasp52-PDZ domain is required for myofibril assembly. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Zasp52-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467281 [Multi-domain]  Cd Length: 82  Bit Score: 67.55  E-value: 7.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 504 TIRLQADEQG-RYGFNVKGGVDLSLPVQVSKVVPHTPADRCTPRVceGDEVLMINGRDVHGLRHEQVVAMIRdcrhQASG 582
Cdd:cd23068    1 NIRLRRDDSNtPWGFRLQGGADFGQPLSIQKVNPGSPADKAGLRR--GDVILRINGTDTSNLTHKQAQDLIK----RAGN 74


                 ....*..
gi 386770278 583 ELLLTVR 589
Cdd:cd23068   75 DLQLTVQ 81
FA pfam08736
FERM adjacent (FA); This region is found adjacent to Band 4.1 / FERM domains (pfam00373) in a ...
 333-369 1.68e-13

FERM adjacent (FA); This region is found adjacent to Band 4.1 / FERM domains (pfam00373) in a subset of FERM containing protein. The region has been hypothesized to play a role in regulatory adaptation, based on similarity to other protein kinase substrates.


Pssm-ID: 462582  Cd Length: 44  Bit Score: 65.26  E-value: 1.68e-13
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 386770278  333 SLGSKFYYSGRTELQAVQESKQRGRIHKVFVRSPSKR 369
Cdd:pfam08736   4 SLGSKFRYSGRTQKQTVEDSSEILRPQPEFERSPSKR 40
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 693-950 3.24e-13

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


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 69.67  E-value: 3.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 693 YINANYVNMEIPGGAvnrYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESgrQKCHQYWPvtgEELQLAEG-FSVR 771
Cdd:cd14636    1 YINAALMDSYRQPAA---FIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLA--QGCPQYWP---EEGMLRYGpIQVE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 772 CLSEKPD-ETGSFVFREFVLKDKHEQR-HIHHMQYLAWPDHcvpsdpnlflefteRVRAARNRTLLQEIEESLKQvrlmd 849
Cdd:cd14636   73 CMSCSMDcDVISRIFRICNLTRPQEGYlMVQQFQYLGWASH--------------REVPGSKRSFLKLILQVEKW----- 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 850 adadadengglmrERKCAASNGATpedetpvstsvhqcisaanppvIVHCSAGIGRTGVLILMDTALALMEAREPVYPLD 929
Cdd:cd14636  134 -------------QEECDEGEGRT----------------------IIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFH 178

                        250       260
                 ....*....|....*....|.
gi 386770278 930 IVRTMRDQRACMVQNVSQYRF 950
Cdd:cd14636  179 AVKTLRNSKPNMVETPEQYRF 199
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 693-953 5.81e-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: 68.89  E-value: 5.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 693 YINANYVNMEIPGGAvnrYIATQGPLASTTTDFWRMVQQESSHLLVMLTTvMESGrQKCHQYWPvtgEELQLAEG-FSVR 771
Cdd:cd14634    1 YINAALMDSHKQPAA---FIVTQHPLPNTVADFWRLVFDYNCSSVVMLNE-MDAA-QLCMQYWP---EKTSCCYGpIQVE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 772 CLSEKPDETG-SFVFREF-VLKDKHEQRHIHHMQYLAWPDHcvpsdpnlflefteRVRAARNRTLLQEIEESLKQVRLMD 849
Cdd:cd14634   73 FVSADIDEDIiSRIFRICnMARPQDGYRIVQHLQYIGWPAY--------------RDTPPSKRSILKVVRRLEKWQEQYD 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 850 adadadenGGLMRerkcaasngatpedetpvstsvhqcisaanppVIVHCSAGIGRTGVLILMDTALALMEAREPVYPLD 929
Cdd:cd14634  139 --------GREGR--------------------------------TVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFH 178

                        250       260
                 ....*....|....*....|....
gi 386770278 930 IVRTMRDQRACMVQNVSQYRFVCE 953
Cdd:cd14634  179 TVKTLRNNKSNMVETLEQYKFVYE 202
FERM_F1_EPB41L2 cd17202
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 34-123 7.07e-13

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: 64.99  E-value: 7.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  34 QCvTVLFLDDITHTFRIEKRAKGSELLDQVFQYLELSERDYFGLLFpQKPGDVVRWVDAQKQFKKQCSSVSLdndavpLL 113
Cdd:cd17202    3 LC-KVTLLDGTEYSCDLEKRAKGQVLFDKVCEHLNLLEKDYFGLLY-QVSANQKNWLDSTKEIKRQIRRLPW------LF 74

                         90
                 ....*....|
gi 386770278 114 EFRVKFFVSD 123
Cdd:cd17202   75 TFNVKFYPPD 84
FERM_F1_EPB41L cd17106
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 33-123 1.01e-12

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: 64.38  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  33 QQCvTVLFLDDITHTFRIEKRAKGSELLDQVFQYLELSERDYFGLLFpQKPGDVVRWVDAQKQFKKQCSSVSLdndavpL 112
Cdd:cd17106    2 QQC-KVLLLDGTEYTCEVEKRAKGQVLFDKVCEHLNLLEKDYFGLTY-RDAQDQKNWLDPAKEIKKQIRSGPW------L 73

                         90
                 ....*....|.
gi 386770278 113 LEFRVKFFVSD 123
Cdd:cd17106   74 FSFNVKFYPPD 84
FERM_F1_FRMD3 cd17102
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 35-120 1.20e-12

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: 64.19  E-value: 1.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  35 CVTVLFLDD---ITHTFRieKRAKGSELLDQVFQYLELSERDYFGLLFPqkpgDVVR---WVD----AQKQFKKQCSSVs 104
Cdd:cd17102    2 KCTIRLLDDsevICCEFK--KDTKGQFLLDYVCNYLNLLEKDYFGLRYV----DTEKqrhWLDpnksIYKQLKGVPPYV- 74

                         90
                 ....*....|....*.
gi 386770278 105 ldndavplLEFRVKFF 120
Cdd:cd17102   75 --------LCFRVKFY 82
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 670-948 1.43e-12

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: 68.20  E-value: 1.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 670 NRYRDIspydCTRVSLVNsltGDYINANYVNMeipgGAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQ 749
Cdd:cd14559    1 NRFTNI----QTRVSTPV---GKNLNANRVQI----GNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRK 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 750 KCHQYWPVTGEelqlAEGFSVRCLSEKPDETGS-FVFREFVLKDKHEQRHIH----HMQylAWPDHCVPSDPNLfLEFTE 824
Cdd:cd14559   70 GLPPYFRQSGT----YGSVTVKSKKTGKDELVDgLKADMYNLKITDGNKTITipvvHVT--NWPDHTAISSEGL-KELAD 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 825 RVRAARnrtllqeiEESLKQVRLMDADADADENGGLmrerkcaasngatpedetpvstsvhqcisaanpPVIvHCSAGIG 904
Cdd:cd14559  143 LVNKSA--------EEKRNFYKSKGSSAINDKNKLL---------------------------------PVI-HCRAGVG 180

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 386770278 905 RTGVLIlmdTALALMEAREPVYPLDIVRTMRDQR-ACMVQNVSQY 948
Cdd:cd14559  181 RTGQLA---AAMELNKSPNNLSVEDIVSDMRTSRnGKMVQKDEQL 222
FERM_F1_EPB41L3 cd17203
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 34-123 3.54e-12

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: 63.04  E-value: 3.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  34 QCvTVLFLDDITHTFRIEKRAKGSELLDQVFQYLELSERDYFGLLFpQKPGDVVRWVDAQKQFKKQCSSVSLDndavplL 113
Cdd:cd17203    3 QC-KVTLLDGSEYTCEVEKRSKGQVLFDKVCEHLNLLEKDYFGLTY-RDSENQKNWLDPAKEIKKQIRSGAWQ------F 74

                         90
                 ....*....|
gi 386770278 114 EFRVKFFVSD 123
Cdd:cd17203   75 SFNVKFYPPD 84
FERM_F1_EPB41 cd17105
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 38-123 6.19e-12

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: 62.14  E-value: 6.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  38 VLFLDDITHTFRIEKRAKGSELLDQVFQYLELSERDYFGLLFPQKPGDVVrWVDAQKQFKKQCSSVSLDndavplLEFRV 117
Cdd:cd17105    5 VSLLDDTVYECEVEKHAKGQDLFKKVCEHLNLLEEDYFGLAIWDSPTSKT-WLDPAKEIKKQVHGGPWE------FTFNV 77


                 ....*.
gi 386770278 118 KFFVSD 123
Cdd:cd17105   78 KFYPPD 83
FERM_F1_PTPN3 cd17193
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 38-121 8.21e-12

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: 61.79  E-value: 8.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  38 VLFLDDITHTFRIEKRAKGSELLDQVFQYLELSERDYFGLLFPQKPGDVVRWVDAQKQFKKQ------CSsvsldndavp 111
Cdd:cd17193    6 VHFLDGSVQSFKVNKQDTGQVLLDMAYNHLGLTEREYFGLQHNEDSVDSPRWLEPSKPIRKQlkggfpCS---------- 75

                         90
                 ....*....|
gi 386770278 112 lLEFRVKFFV 121
Cdd:cd17193   76 -LHFRVRFFI 84
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 693-953 1.08e-11

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: 65.31  E-value: 1.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 693 YINANYVNMEIPGGAvnrYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQ-KCHQYWPVTGeeLQLAEGFSVR 771
Cdd:cd14637    1 YINAALTDSYTRSAA---FIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPG--LQQYGPMEVE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 772 CLSEKPDE-TGSFVFR-EFVLKDKHEQRHIHHMQYLAW-PDHCVPSDPNLFLEftervraarnrtLLQEIEESLKQVRlm 848
Cdd:cd14637   76 FVSGSADEdIVTRLFRvQNITRLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLH------------LLASVEKWQRESG-- 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 849 dadadadengglmrerkcaasNGATpedetpvstsvhqcisaanppvIVHCSAGIGRTGVLILMDTALALMEAREPVYPL 928
Cdd:cd14637  142 ---------------------EGRT----------------------VVHCLNGGGRSGTYCASAMILEMIRCHNIVDVF 178

                        250       260
                 ....*....|....*....|....*
gi 386770278 929 DIVRTMRDQRACMVQNVSQYRFVCE 953
Cdd:cd14637  179 YAVKTLRNYKPNMVETLEQYRFCYE 203
FERM_F1_EPB41L1 cd17201
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 38-123 1.91e-11

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: 61.05  E-value: 1.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  38 VLFLDDITHTFRIEKRAKGSELLDQVFQYLELSERDYFGLLF----PQKpgdvvRWVDAQKQFKKQCSSVSLDndavplL 113
Cdd:cd17201    6 VTLLDGSEYECEVEKHARGQVLFDTVCEHLNLLEKDYFGLTFcdteSQK-----NWLDPSKEIKKQIRSGPWH------F 74

                         90
                 ....*....|
gi 386770278 114 EFRVKFFVSD 123
Cdd:cd17201   75 AFTVKFYPPD 84
PDZ_SYNPO2-like cd10820
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related ...
 515-573 4.27e-11

PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNPO2, SYNPO2L, and related domains. SYNPO2 (also known as genethonin-2, myopodin) is a cytoskeleton adaptor protein. It participates in chaperone-assisted selective autophagy (CASA), a mechanism for the disposal of misfolded and damaged proteins and provides a link between the CASA chaperone complex and a membrane-tethering and fusion machinery that generates autophagosome membranes. The SYNPO2 PPxY motif binds CASA cochaperone BCL2-associated athanogene 3 (BAG3) and the SYNPO2 PDZ domain binds vacuolar protein sorting 18 homolog (VPS18). There are three isoforms of SYNPO2, which possess an amino-terminal PDZ domain (SYNPO2a, b, c); the short isoform SYNPO2d, lacks the PDZ domain. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SYNPO2-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467264 [Multi-domain]  Cd Length: 78  Bit Score: 59.63  E-value: 4.27e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 386770278 515 YGFNVKGGVDLSLPVQVSKVVPHTPAdrCTPRVCEGDEVLMINGRDVHGLRHEQVVAMI 573
Cdd:cd10820   10 WGFRLQGGSEQKKPLQVAKIRKKSKA--ALAGLCEGDELLSINGKPCADLSHSEAMDLI 66
FERM_F1_FRMD7 cd17188
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 38-124 4.79e-11

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: 59.82  E-value: 4.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  38 VLFLDDITHTFRIEKRAKGSELLDQVFQYLELSERDYFGLLFPQKPGDVVrWVDAQKQFKKQcssVSLDNDAVplLEFRV 117
Cdd:cd17188    6 VQFLDDSQKVFVVDQKSTGKDLFNMSCSHLNLVEKEYFGLEFRNHAGNNV-WLELLKPITKQ---IKNPKELI--FKFTV 79


                 ....*..
gi 386770278 118 KFFVSDP 124
Cdd:cd17188   80 KFFPVDP 86
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 693-816 4.91e-11

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: 63.09  E-value: 4.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 693 YINANYVnmeIPGGAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKChQYWPvTGEELQLAEGFSV-- 770
Cdd:cd17669    1 YINASYI---MGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWP-NKDEPINCETFKVtl 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 386770278 771 -----RCLSEKPDetgsFVFREFVLKDKHEQR--HIHHMQYLAWPDhcvPSDP 816
Cdd:cd17669   76 iaeehKCLSNEEK----LIIQDFILEATQDDYvlEVRHFQCPKWPN---PDSP 121
FERM_F1_PTPN14_like cd17099
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 36-120 8.63e-11

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: 59.17  E-value: 8.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  36 VTVLFLDDITHTFRIEKRAKGSELLDQVFQYLELSERDYFGLLFPQKpGDVVRWVDAQKQFKKQcssvsLDNDAV-PLLE 114
Cdd:cd17099    6 VRIQLLDNTVLECTLSPESTGQDCLEYVAQRLELREIEYFGLRYVNK-KGQLRWVDLEKPLKKQ-----LDKHAHePLLY 79


                 ....*.
gi 386770278 115 FRVKFF 120
Cdd:cd17099   80 FGVMFY 85
PDZ_syntrophin-like cd06801
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 504-589 9.94e-11

PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of syntrophins (including alpha-1-syntrophin, beta-1-syntrophin, beta-2-syntrophin, gamma-1-syntrophin, and gamma-2-syntrophin), and related domains. Syntrophins play a role in recruiting various signaling molecules into signaling complexes and help provide appropriate spatiotemporal regulation of signaling pathways. They function in cytoskeletal organization and maintenance; as components of the dystrophin-glycoprotein complex (DGC), they help maintain structural integrity of skeletal muscle fibers. They link voltage-gated sodium channels to the actin cytoskeleton and the extracellular matrix, and control the localization and activity of the actin reorganizing proteins such as PI3K, PI(3,4)P2 and TAPP1. Through association with various cytoskeletal proteins within the cells, they are involved in processes such as regulation of focal adhesions, myogenesis, calcium homeostasis, and cell migration. They also have roles in synapse formation and in the organization of utrophin, acetylcholine receptor, and acetylcholinesterase at the neuromuscular synapse. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This syntrophin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467262 [Multi-domain]  Cd Length: 83  Bit Score: 58.74  E-value: 9.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 504 TIRLQADEQGRYGFNVKGGVDLSLPVQVSKVVPHTPADRcTPRVCEGDEVLMINGRDVHGLRHEQVVAMIRDCrhqaSGE 583
Cdd:cd06801    2 TVRVVKQDVGGLGISIKGGAEHKMPILISKIFKGQAADQ-TGQLFVGDAILSVNGENLEDATHDEAVQALKNA----GDE 76


                 ....*.
gi 386770278 584 LLLTVR 589
Cdd:cd06801   77 VTLTVK 82
FERM_F1_EPB41L4B cd17204
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 38-123 1.95e-10

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: 57.91  E-value: 1.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  38 VLFLDDITHTFRIEKRAKGSELLDQVFQYLELSERDYFGLLFpQKPGDVVRWVDAQKQFKKQcssvsLDNDAVPLLEFRV 117
Cdd:cd17204    5 VLLLDGTDVSVELPKHAKGQDLFDQIVYHLDLVETDYFGLQF-MDAAQVAHWLDHTKPIKKQ-----IKIGPPYTLHFRI 78


                 ....*.
gi 386770278 118 KFFVSD 123
Cdd:cd17204   79 KYYSSE 84
PDZ_PDLIM-like cd06753
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 516-589 4.14e-10

PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZ-LIM family proteins including PDLIM1-7, and related domains. PDZ-LIM family proteins (also known as Zasp PDZ domain proteins) are involved in the rearrangement of the actin cytoskeleton; they mediate association with the cytoskeleton through alpha-actinin as well as with other proteins involved in signal transduction pathways. Members of this family include PDLIM1 (also known as C-terminal LIM domain protein 1, elfin, LIM domain protein CLP-36), PDLIM2 (also known as PDZ-LIM protein mystique), PDLIM3 (also known as actinin-associated LIM protein, alpha-actinin-2-associated LIM protein, ALP), PDLIM4 (also known as LIM protein RIL, Reversion-induced LIM protein), PDLIM5 (also known as enigma homolog, ENH, enigma-like PDZ and LIM domains protein), PDLIM6 (also known as LIM domain-binding protein 3, ZASP, Cypher, Oracle), and PDLIM7 (also known as PDZ and LIM domain protein 7, LIM mineralization protein, LMP; protein enigma). PDLIM1 has been shown to negatively regulate NF-kappaB-mediated signaling in the cytoplasm. PDLIM7 negatively regulates p53 through binding murine double minute 2 (MDM2). The PDZ domains of PDZ-LIM family proteins PDLIM1, 2, 3, 5, 6, 7 have been shown to bind actin. Other PDZ-LIM family PDZ domain binding partners include thyroid receptor interacting protein-6 (PDLIM4-PDZ), the LIM domain of PDLIM4 (PDLIM4-PDZ), tropomyosin (PDLIM7-PDZ), myotilin and calsarcin 1 (PDLIM6-PDZ), and proteins from the myotilin and FATZ (calsarcin/myozenin) families (PDLIM1, 3, 4, 6 PDZ domains). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDLIM-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467235 [Multi-domain]  Cd Length: 79  Bit Score: 56.77  E-value: 4.14e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386770278 516 GFNVKGGVDLSLPVQVSKVVPHTPADRCtpRVCEGDEVLMINGRDVHGLRHEQVVAMIRDCrhqaSGELLLTVR 589
Cdd:cd06753   11 GFRLQGGKDFNQPLTISRVTPGGKAAQA--NLRPGDVILAINGESTEGMTHLEAQNKIKAA----TGSLSLTLE 78
FERM_F1_EPB41L5 cd17205
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 38-123 4.91e-10

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: 56.97  E-value: 4.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  38 VLFLDDITHTFRIEKRAKGSELLDQVFQYLELSERDYFGLLFpQKPGDVVRWVDAQKQFKKQCSSVSldndavPL-LEFR 116
Cdd:cd17205    7 VSLLDGTDVSVDLPKKAKGQELFEQIMYHLDLIEKDYFGLRF-MDSAQVAHWLDVTKSIKKQVKIGP------PYcLHLR 79


                 ....*..
gi 386770278 117 VKFFVSD 123
Cdd:cd17205   80 VKFYSSE 86
FERM_F1_FARP2 cd17190
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 36-124 6.13e-10

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: 56.73  E-value: 6.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  36 VTVLFLDDITHTFRIEKRAKGSELLDQVFQYLELSERDYFGLLFPQKPGDVVrWVDAQKQFKKQcssvsLDNDAVPLLEF 115
Cdd:cd17190    3 LRVKLLDNTTEPLEIEPKADGQALLSQVFKRLNLVESDYFGLEFQNSQSNWI-WLEPMKLIVKQ-----VRRPKNTKLRL 76


                 ....*....
gi 386770278 116 RVKFFVSDP 124
Cdd:cd17190   77 AVKFFPPDP 85
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 506-588 7.23e-10

PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the Na+/H+ exchange regulatory cofactor (NHERF) family of multi-PDZ-domain-containing scaffolding proteins (NHERF1-4), and related domains. The NHERF family includes NHERF1 (also known as EBP50), NHERF2 (also known as E3KARP; TKA-1; SIP-1), NHERF3 (also known as CAP70; CLAMP; Napi-Cap-1; PDZD1) and NHERF4 (also known as IKEPP; PDZK2; Napi-Cap-2). NHERF1 and NHERF2 have tandem PDZ domains (PDZ1-2); NHERF3 and NHERF4 have four PDZ domains (PDZ1-4). NHERFs are involved in the regulation of multiple receptors or transporters, such as type II sodium-phosphate cotransporter (Npt2a), purinergic P2Y1 receptor P2Y1R, the beta2-adrenergic receptor (beta2-AR), parathyroid hormone receptor type 1 (PTHR), the lysophosphatidic acid receptors (LPARs), sodium-hydrogen exchanger 3 (NHE3), and cystic fibrosis transmembrane conductance regulator (CFTR). NHERF-PDZ1 domain interaction partners include Npt2a, purinergic P2Y1 receptor, beta2-AR, CFTR, PTHR, NH3, G-protein-coupled receptor kinase 6 (GRK6A), platelet-derived growth factor receptor (PDGFR), B1 subunit of the H+ATPase, cholesterol, receptor for activated C-kinase RACK1, aquaporin 9, among others. The NHERF PDZ2 domain interacts with fewer proteins: NHERF1 PDZ2 binds Npt2a, PTHR, beta-catenin, aquaporin 9, and RACK1; NHERF2 PDZ2 binds LPA2, P2Y1R, and NHE3, cGMP-dependent protein kinase type II (cGKII). NHERF4 PDZ1 and PDZ4 bind the epithelial Ca(2+) channels TRPV5 and TRPV6. NHERF2/NHERF3 heterodimerization is mediated by PDZ domains of NHERF2 and the C-terminal PDZ domain recognition motif of NHERF3. NHERF4 regulates several transporters mediating influx of xenobiotics and nutrients in the small intestine. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This NHERF-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467249 [Multi-domain]  Cd Length: 80  Bit Score: 56.29  E-value: 7.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 506 RLQADEQGrYGFNVKGgvDLSLPVQ-VSKVVPHTPADRCtpRVCEGDEVLMINGRDVHGLRHEQVVAMIRDCrhqaSGEL 584
Cdd:cd06768    4 HLVKGPEG-YGFNLHA--EKGRPGHfIREVDPGSPAERA--GLKDGDRLVEVNGENVEGESHEQVVEKIKAS----GNQV 74


                 ....
gi 386770278 585 LLTV 588
Cdd:cd06768   75 TLLV 78
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 227-320 7.35e-10

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: 56.53  E-value: 7.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 227 YGIDLHRATDSNGKELQLGVSAVGLLV-FQHSLRVNTFSWSKMVKVSFKRKDFFIQLRrEPSENYdtllGFGMSSHKHAK 305
Cdd:cd13188    1 YGEESFPAKDEQGNEVLIGASLEGIFVkHDNGRPPVFFRWEDIKNVINHKRTFSIECQ-NSEETV----QFQFEDAETAK 75

                         90
                 ....*....|....*
gi 386770278 306 ALWKSCVEHHSFFRL 320
Cdd:cd13188   76 YVWKLCVLQHKFYRQ 90
PDZ_rhophilin-like cd06712
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 504-576 7.39e-10

PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of rhophilin-1, rhophilin-2, and related domains. Rhophilin-1 (RHPN1, also known as GTP-Rho-binding protein 1) and rhophilin-2 (RHPN2, also known as GTP-Rho-binding protein 2) are Rho-GTP binding proteins involved in cytoskeletal dynamics. Rhophilin-2 inhibits RhoA's activity to induce F-actin stress fibers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This rhophilin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467196 [Multi-domain]  Cd Length: 78  Bit Score: 56.05  E-value: 7.39e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386770278 504 TIRLQADEQGrYGFNVKGGVdlslPVQVSKVVPHTPADRCTPRvcEGDEVLMINGRDVHGLRHEQVVAMIRDC 576
Cdd:cd06712    3 TVHLTKEEGG-FGFTLRGDS----PVQVASVDPGSCAAEAGLK--EGDYIVSVGGVDCKWSKHSEVVKLLKSA 68
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 693-813 7.72e-10

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: 59.69  E-value: 7.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 693 YINANYVnmeIPGGAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKcHQYWPvTGEELQLAEGFSVR- 771
Cdd:cd17670    1 YINASYI---MGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDE-FVYWP-SREESMNCEAFTVTl 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 386770278 772 ------CLSEKPdetgSFVFREFVLKDKHEQR--HIHHMQYLAWPDHCVP 813
Cdd:cd17670   76 iskdrlCLSNEE----QIIIHDFILEATQDDYvlEVRHFQCPKWPNPDAP 121
PDZ_SNX27-like cd23070
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density ...
 505-588 8.33e-10

PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SNX27, and related domains. SNX27 is involved in retrograde transport from endosome to plasma membrane. The PDZ domain of SNX27 links cargo identification to retromer-mediated transport. SNX27 binds to the retromer complex (vacuolar protein sorting 26(VPS26)-VPS29-VPS35), via its PDZ domain binding to VPS26. The SNX27 PDZ domain also binds to cargo including the G-protein-coupled receptors (GPCRs): beta2-adrenergic receptor (beta2AR), beta1AR, parathyroid hormone receptor (PTHR), alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPARs), NMDA receptors, 5-hydroxytryptamine 4a receptors, frizzled receptors, and somatostatin receptor subtype 5 (SSTR5). Additional binding partners of the SNX27 PDZ domain include G protein-gated inwardly rectifying potassium (Kir3) channels, angiotensin-converting enzyme 2 (ACE2), and PTEN (phosphatase and tensin homolog deleted on chromosome 10); PTEN binding to SNX27 prevents SNX27's association with the retromer complex. SNX27 has been reported to be a host factor needed for efficient entry of an engineered SARS-CoV-2 variant, the spike protein of which contains a deletion at the S1/S2 subunit cleavage site; the PDZ domain of SNX27 binds angiotensin-converting enzyme 2 (ACE2), and may be involved in recycling ACE2 to the plasma membrane, thereby promoting viral entry. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SNX27-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467283 [Multi-domain]  Cd Length: 93  Bit Score: 56.65  E-value: 8.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 505 IRLQADEQGrYGFNVKGGV-----------DLSLPVQ-VSKVVPHTPADRCTPRVceGDEVLMINGRDVHGLRHEQVVAM 572
Cdd:cd23070    3 VTIVKSETG-FGFNVRGQVseggqlrsingELYAPLQhVSAVLEGGAADKAGVRK--GDRILEVNGVNVEGATHKQVVDL 79

                         90
                 ....*....|....*.
gi 386770278 573 IRdcrhQASGELLLTV 588
Cdd:cd23070   80 IK----SGGDELTLTV 91
FERM_F1_EPB41L4A cd17107
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 36-123 1.19e-09

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: 55.81  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  36 VTVLFLDDITHTFRIE----KRAKGSELLDQVFQYLELSERDYFGLLFPQKPGDvVRWVDAQKQFKKQcssvsLDNDAVP 111
Cdd:cd17107    5 CEIVLLDESELILTIQqdgiKSSKGSVVLDVVFQHLNLLETDYFGLRYIDRQHQ-THWLDPAKTLSEQ-----LKLIGPP 78

                         90
                 ....*....|...
gi 386770278 112 -LLEFRVKFFVSD 123
Cdd:cd17107   79 yTLYFGVKFYAED 91
PDZ2_GRIP1-2-like cd06681
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 503-580 1.26e-09

PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467169 [Multi-domain]  Cd Length: 89  Bit Score: 55.70  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 503 ITIRLQAdEQGRYGFNVKGGVD----LSLPVQVSKVVPHTPADRcTPRVCEGDEVLMINGRDVHGLRHEQVVAMIRDCRH 578
Cdd:cd06681    3 VEVTLEK-EGNSFGFVIRGGAHedrnKSRPLTVTHVRPGGPADR-EGTIKPGDRLLSVDGISLHGATHAEAMSILKQCGQ 80


                 ..
gi 386770278 579 QA 580
Cdd:cd06681   81 EA 82
PDZ2-PTPN13_FRMPD2-like cd06792
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ...
 501-575 1.92e-09

PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of human PTPN13, and related domains. PTPN13, also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1), negatively regulates FAS-mediated apoptosis and NGFR-mediated pro-apoptotic signaling, and may also regulate phosphoinositide 3-kinase (PI3K) signaling. It contains 5 PDZ domains; interaction partners of its second PDZ domain (PDZ2) include the Fas receptor (TNFRSF6) and thyroid receptor-interacting protein 6 (TRIP6). The second PDZ (PDZ2) domain, but not PDZ1 or PDZ3, of FRMPD2 binds to GluN2A and GluN2B, two subunits of N-methyl-d-aspartic acid (NMDA) receptors. Other binding partners of the FRMPDZ2 PDZ2 domain include NOD2, and catenin family members, delta catenin (CTNND2), armadillo repeat gene deleted in velo-cardio-facial syndrome (ARVCF) and p0071 (also known as plakophilin 4; PKP4). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467254 [Multi-domain]  Cd Length: 87  Bit Score: 55.29  E-value: 1.92e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386770278 501 DLITIRLQADeQGRYGFNVKGGVDLSLP---VQVSKVVPHTPADrCTPRVCEGDEVLMINGRDVHGLRHEQVVAMIRD 575
Cdd:cd06792    1 DVFEVELSKK-DGSLGISVTGGINTSVRhggIYVKSLVPGGAAE-QDGRIQKGDRLLEVNGVSLEGVTHKQAVECLKN 76
PDZ_FRMPD1_3_4-like cd06769
PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related ...
 504-588 3.09e-09

PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of FRMPD1, FRMPD3, FRMPD4, and related domains. FRMPD1 (also known as FERM domain-containing protein 2, FRMD2), inhibits the malignant phenotype of lung cancer by activating the Hippo pathway via interaction with WWC3; the FRMPD1 PDZ domain binds WWC3. FRMPD3 is a target gene of the neuron-specific transcription factor NPAS4 that is involved in synaptic plasticity. FRMPD4 (also known as PDZ domain-containing protein 10, PDZD10, PDZK10, PSD-95-interacting regulator of spine morphogenesis, and Preso) regulates dendritic spine morphogenesis, and mGluR1/5 signaling; the FRMPD4 PDZ domain binds PAK-interacting exchange factor-beta (betaPix). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This FRMPD1,3,4-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467250 [Multi-domain]  Cd Length: 75  Bit Score: 54.17  E-value: 3.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 504 TIRLQADEQGRYGFNVKGgvdlSLPVQVSKVVPHTPAD-RCTPrvceGDEVLMINGRDVHGLRHEQVVAMIRDCRHqasg 582
Cdd:cd06769    1 TVEIQRDAVLGFGFVAGS----ERPVVVRSVTPGGPSEgKLLP----GDQILKINNEPVEDLPRERVIDLIRECKD---- 68


                 ....*.
gi 386770278 583 ELLLTV 588
Cdd:cd06769   69 SIVLTV 74
PDZ3_MAGI-1_3-like cd06733
PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 502-589 3.67e-09

PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467215 [Multi-domain]  Cd Length: 85  Bit Score: 54.54  E-value: 3.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 502 LITIRLQADEQGrYGFNVKGGVDLSLPVQVSKVVPHTPADRCTpRVCEGDEVLMINGRDVHGLRHEQVVAMIRDCRHQas 581
Cdd:cd06733    1 ELTVFLRRQETG-FGFRILGGTEEGSQVSIGAIVPGGAADLDG-RLRTGDELLSVDGVNVVGASHHKVVDLMGNAARN-- 76


                 ....*...
gi 386770278 582 GELLLTVR 589
Cdd:cd06733   77 GQVNLTVR 84
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 693-953 4.33e-09

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: 57.39  E-value: 4.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 693 YINANYVNMEIPGGAvnrYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESgrQKCHQYWPVTGeeLQLAEGFSVRC 772
Cdd:cd14635    1 YINAALMDSYKQPSA---FIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPA--QLCPQYWPENG--VHRHGPIQVEF 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 773 LSEKPDE-TGSFVFREF-VLKDKHEQRHIHHMQYLAWPDHcvpsdpnlflefteRVRAARNRTLLQEIeeslKQVRLMDA 850
Cdd:cd14635   74 VSADLEEdIISRIFRIYnAARPQDGYRMVQQFQFLGWPMY--------------RDTPVSKRSFLKLI----RQVDKWQE 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 851 DADADEngglmrerkcaasnGATpedetpvstsvhqcisaanppvIVHCSAGIGRTGVLILMDTALALMEAREPVYPLDI 930
Cdd:cd14635  136 EYNGGE--------------GRT----------------------VVHCLNGGGRSGTFCAISIVCEMLRHQRAVDVFHA 179

                        250       260
                 ....*....|....*....|...
gi 386770278 931 VRTMRDQRACMVQNVSQYRFVCE 953
Cdd:cd14635  180 VKTLRNNKPNMVDLLDQYKFCYE 202
PDZ_Lin-7-like cd06796
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 505-589 7.48e-09

PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Lin-7 (also known as LIN-7 or LIN7), and related domains. Lin-7 targets and organize protein complexes to epithelial and synaptic plasma membranes. There are three mammalian Lin-7 homologs: Lin-7A (protein lin-7 homolog A, also known as mammalian lin-seven protein 1 (MALS-1), vertebrate lin-7 homolog 1 (Veli-1), tax interaction protein 33); Lin-7B (also known as MALS-2, Veli-2); and Lin-7C (also known as MALS-3, Veli-3). Lin-7 is involved in localization of the Let-23 growth factor receptor to the basolateral membrane of epithelial cells, in tight junction localization of insulin receptor substrate p53 (IRSp53), in retaining gamma-aminobutyric (GABA) transporter (BGT-1) at the basolateral surface of epithelial cells, and in regulating recruitment of neurotransmitter receptors to the postsynaptic density (PSD). The Lin7 PDZ domain binds Let-23, BGT and beta-catenin, and NMDA (N-methyl-D-aspartate) receptor NR2B. Lin-7 also binds to the PDZ binding motif located in the C-terminal tail of Rhotekin, an effector protein for small GTPase Rho. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Lin-7-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467258 [Multi-domain]  Cd Length: 86  Bit Score: 53.60  E-value: 7.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 505 IRLQADEQGrYGFNVKGGVDLSLPVQVSKVVPHTPADRcTPRVCEGDEVLMINGRDVHGLRHEQVVAMIRdcrhQASGEL 584
Cdd:cd06796    5 VELPKTEEG-LGFNVMGGKEQNSPIYISRIIPGGVADR-HGGLKRGDQLLSVNGVSVEGEHHEKAVELLK----AAQGSV 78


                 ....*
gi 386770278 585 LLTVR 589
Cdd:cd06796   79 KLVVR 83
FERM_F1_MYLIP cd17104
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in E3 ...
 42-120 8.18e-09

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: 53.43  E-value: 8.18e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386770278  42 DDITHTFRIEKRAKGSELLDQVFQYLELSERDYFGLLFPQKPGDVVrWVDAQKQFKKQcssvsLDNDAVPLLEFRVKFF 120
Cdd:cd17104    9 DSVVIEVEVDPKANGQECLDKVCQKLGIIEKDYFGLQYTGPKGERL-WLNLRNRISRQ-----LPGPPPYRLRLRVKFF 81
FERM_F1_PTPN13_like cd17101
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 35-121 1.07e-08

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: 53.33  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  35 CVTVLFLDDITHTFRIEKRAKGSELLDQVFQYLELSERDYFGLLFpQKPGDVVrWVD--------AQKQFKKQCSSVSLD 106
Cdd:cd17101    3 YVNVVLLNGQRLQVAVDVKTTVQDLFDQVCDHLGLQETELFGLAV-LKDGEYF-FLDpdtklskyAPKGWKSEAKKGLKG 80

                         90
                 ....*....|....*
gi 386770278 107 NDAVPLLEFRVKFFV 121
Cdd:cd17101   81 GKPVFTLYFRVKFYV 95
FERM_C_MYLIP_IDOL cd13195
FERM domain C-lobe of E3 ubiquitin ligase myosin regulatory light chain-interacting protein ...
 227-319 2.48e-08

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: 53.02  E-value: 2.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 227 YGIDLHRATDSNGKELQLGVSAVGLLVFQHSLR-VNTFSWSKMVKVSFKRKDFFIQLRREPSEnyDTLLGFGMSSHKHAK 305
Cdd:cd13195    1 YGVEFFEVRNIEGQKLLIGVGPHGITICNDDFEvIERIPYTAIQMATSSGRVFTLTYLSDDGS--VKVLEFKLPSTRAAS 78

                         90
                 ....*....|....
gi 386770278 306 ALWKSCVEHHSFFR 319
Cdd:cd13195   79 GLYRAITEKHAFYR 92
PDZ6_PDZD2-PDZ3_hPro-IL-16-like cd06762
PDZ domain 6 of PDZ domain containing 2 (PDZD2), PDZ domain 3 of human pro-interleukin-16 ...
 505-578 3.45e-08

PDZ domain 6 of PDZ domain containing 2 (PDZD2), PDZ domain 3 of human pro-interleukin-16 (isoform 1, 1332 AA), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 6 of PDZD2, also known as KIAA0300, PIN-1, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains. PDZD2 is expressed at exceptionally high levels in the pancreas and certain cancer tissues, such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. This family also includes the third PDZ domain (PDZ3) of human pro-interleukin-16 (isoform 1, also known as nPro-IL-16). Precursor IL-16 is cleaved to produce pro-IL-16 and C-terminal mature IL-16. Pro-IL-16 functions as a regulator of T cell growth; mature IL-16 is a CD4 ligand that induces chemotaxis and CD25 expression in CD4+ T cells. IL-16 bioactivity has been closely associated with the progression of several different cancers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD2-like family PDZ6 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467243 [Multi-domain]  Cd Length: 86  Bit Score: 51.49  E-value: 3.45e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386770278 505 IRLQADEQGRYGFNVKGGVDLSL-PVQVSKVVPHTPADRcTPRVCEGDEVLMINGRDVHGLRHEQVVAMIRDCRH 578
Cdd:cd06762    4 VVLHKEEGSGLGFSLAGGSDLENkSITVHRVFPSGLAAQ-EGTIQKGDRILSINGKSLKGVTHGDALSVLKQARL 77
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 892-953 3.73e-08

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: 52.35  E-value: 3.73e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386770278 892 NPPVIVHCSAGIGRTGVLILMDTALALMEArepvyPLDIVRTMRDQR-ACMVQNVSQYRFVCE 953
Cdd:cd14494   56 GEPVLVHCKAGVGRTGTLVACYLVLLGGMS-----AEEAVRIVRLIRpGGIPQTIEQLDFLIK 113
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 502-575 4.21e-08

PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of harmonin isoforms a, b, and c, and related domains. Harmonin (also known as Usher Type 1C, PDZ-73 and AIE-75) is a key organizer of the Usher (USH) protein interactome. USH syndrome is the leading cause of hereditary sensory deaf-blindness in humans; three clinically distinct types of USH have been identified, type 1 to 3. The gene encoding harmonin (USH1C) is the causative gene for the USH type 1C phenotype. There are at least 10 alternatively spliced isoforms of harmonin, which are divided into three subclasses (a, b, and c). All isoforms contain the first two PDZ domains and the first coiled-coil domain. The a and b isoforms all have a third PDZ domain. The different PDZ domains are responsible for interactions with all known Usher syndrome type 1 proteins, and most Usher syndrome type 2 proteins. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This harmonin family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467219 [Multi-domain]  Cd Length: 85  Bit Score: 51.49  E-value: 4.21e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386770278 502 LITIRLQADEQGRYGFNVKGGVDLSLPVQVSKVVPHTPADRCTPRVceGDEVLMINGRDVHGLRHEQVVAMIRD 575
Cdd:cd06737    2 LRLVRLDRRGPESLGFSVRGGLEHGCGLFVSHVSPGSQADNKGLRV--GDEIVRINGYSISQCTHEEVINLIKT 73
PDZ1_MAGI-1_3-like cd06731
PDZ domain 1 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 502-572 5.96e-08

PDZ domain 1 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467213 [Multi-domain]  Cd Length: 85  Bit Score: 51.06  E-value: 5.96e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386770278 502 LITIRLQADEQGrYGFNVKGGVDLSLPVQVSKVVPHTPADRcTPRVCEGDEVLMINGRDVHGLRHEQVVAM 572
Cdd:cd06731    1 LIRTSLKKSARG-FGFTIIGGDEPDEFLQIKSVVPDGPAAL-DGKLRTGDVLVSVNDTCVLGYTHADVVKL 69
FERM_F1_FARP1 cd17189
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 36-123 6.73e-08

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: 50.96  E-value: 6.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  36 VTVLFLDDITHTFRIEKRAKGSELLDQVFQYLELSERDYFGLLFPQKPGDVVrWVDAQKQFKKQcssvsLDNDAVPLLEF 115
Cdd:cd17189    3 IKVQMLDDTQEVFEVPQRAPGKVLLDAVCSHLNLVEGDYFGLEFQDHRKVMV-WLDLLKPIVKQ-----IRRPKHVVLRF 76


                 ....*...
gi 386770278 116 RVKFFVSD 123
Cdd:cd17189   77 VVKFFPPD 84
PDZ4_MAGI-1_3-like cd06734
PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 515-590 7.38e-08

PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467216 [Multi-domain]  Cd Length: 84  Bit Score: 50.69  E-value: 7.38e-08
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gi 386770278 515 YGFNVKGGVDLSLPVQVSKVVPHTPADRCTP-RVceGDEVLMINGRDVHGLRHEQVVAMIRDcrhqaSG-ELLLTVRP 590
Cdd:cd06734   14 FGFVIISSVNKKSGSKIGRIIPGSPADRCGQlKV--GDRILAVNGISILNLSHGDIVNLIKD-----SGlSVTLTIVP 84
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 660-822 9.17e-08

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 54.97  E-value: 9.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 660 EARKPANAPKNRYRD------ISPYDCTRVSLVNSltGDYINANYV---NMEipggavNRYIATQGPLASTTTDFWRMVQ 730
Cdd:PHA02740  41 EANKACAQAENKAKDenlalhITRLLHRRIKLFND--EKVLDARFVdgyDFE------QKFICIINLCEDACDKFLQALS 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 731 QESSHLLVMLTTVMEsgrQKCH-QYWPVTGEELQLAEGFSVRCLS--EKPdetgSFVFREFVLKDKHEQ-RHIHHMQYLA 806
Cdd:PHA02740 113 DNKVQIIVLISRHAD---KKCFnQFWSLKEGCVITSDKFQIETLEiiIKP----HFNLTLLSLTDKFGQaQKISHFQYTA 185

                        170
                 ....*....|....*.
gi 386770278 807 WPDHCVPSDPNLFLEF 822
Cdd:PHA02740 186 WPADGFSHDPDAFIDF 201
PDZ4_GRIP1-2-like cd06686
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 507-584 3.96e-07

PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467174 [Multi-domain]  Cd Length: 99  Bit Score: 49.27  E-value: 3.96e-07
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gi 386770278 507 LQADEQGRYGFNVKGGV----DLSLPVQVSKVVPHTPADRCTPrVCEGDEVLMINGRDVHGLRHEQVVAMIRDCRHQASG 582
Cdd:cd06686   12 LRGDPLKGFGIQLQGGVfateTLSSPPLISFIEPDSPAERCGV-LQVGDRVLSINGIPTEDRTLEEANQLLRDSASKVTL 90


                 ..
gi 386770278 583 EL 584
Cdd:cd06686   91 EI 92
PDZ_PDZD11-like cd06752
PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic ...
 503-589 4.10e-07

PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZD11, and related domains. PDZD11 (also known as ATPase-interacting PDZ protein, plasma membrane calcium ATPase-interacting single-PDZ protein, PMCA-interacting single-PDZ protein, PISP) is involved in the dynamic assembly of apical junctions (AJs). It is recruited by PLEKHA7 to AJs to promote the efficient junctional recruitment and stabilization of nectins, and the efficient early phases of assembly of AJs in epithelial cells. The PDZD11 PDZ domain binds nectin-1 and nectin-3. PDZD11 also binds to a PDZ binding motif located in the C-terminal tail of the human sodium-dependent multivitamin transporter, to the cytoplasmic tail of the Menkes copper ATPase ATP7A, and to the cytoplasmic tail of all plasma membrane Ca2+-ATPase b-splice variants. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD11-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467234 [Multi-domain]  Cd Length: 83  Bit Score: 48.46  E-value: 4.10e-07
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gi 386770278 503 ITIRLQADEQgrYGFNVKGGVDLSLPVQVSKVVPHTPADRCTPRvcEGDEVLMINGRDVHGLRHEQVVAMIRDCRhqasg 582
Cdd:cd06752    3 VVLKRPPGEQ--LGFNIRGGKASGLGIFISKVIPDSDAHRLGLK--EGDQILSVNGVDFEDIEHSEAVKVLKTAR----- 73


                 ....*..
gi 386770278 583 ELLLTVR 589
Cdd:cd06752   74 EIQMRVR 80
PDZ_SYNJ2BP-like cd06709
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ...
 504-574 4.24e-07

PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNJ2BP, and related domains. SYNJ2BP (also known as mitochondrial outer membrane protein 25, OMP25) regulates endocytosis of activin type 2 receptor kinases through the Ral/RALBP1-dependent pathway and may be involved in suppression of activin-induced signal transduction. Binding partners of the SYNJ2BP PDZ domain include activin type II receptors (ActR-II), and SYNJ2. SYNJ2BP interacts with the PDZ binding motif of the Notch Delta-like ligand 1 (DLL1) and DLL4, promoting Delta-Notch signaling, and inhibiting sprouting angiogenesis. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SYNJ2BP-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467193 [Multi-domain]  Cd Length: 86  Bit Score: 48.44  E-value: 4.24e-07
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gi 386770278 504 TIRLQADEQGrYGFNVKGGVDLSL-----PVQVSKVVPHTPADRcTPRVCEGDEVLMINGRDVHGLRHEQVVAMIR 574
Cdd:cd06709    2 EITLKRGPSG-LGFNIVGGTDQPYipndsGIYVAKIKEDGAAAI-DGRLQEGDKILEINGQSLENLTHQDAVELFR 75
FERM_F1_ERM_like cd17097
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 48-120 5.52e-07

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: 48.04  E-value: 5.52e-07
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gi 386770278  48 FRIEKRAKGSELLDQVFQYLELSERDYFGLLFPQKPGDVVrWVDAQKQFKKQCSSvslDNDAVPLLeFRVKFF 120
Cdd:cd17097   14 FSIKPKAKGRELFDLVCRTIGLRETWYFGLQYENKKGRVA-WLKPDKKVLTQDVS---KNNTLKFF-FLVKFY 81
FERM_F1_PTPN21 cd17192
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 48-121 7.37e-07

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: 48.09  E-value: 7.37e-07
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gi 386770278  48 FRIEKRAKGSELLDQVFQYLELSERDYFGLLFPQKPGDvVRWVDAQKQFKKQCSSVSLDndavPLLEFRVKFFV 121
Cdd:cd17192   18 FTLSVESTGQECLEAVAQRLELREITYFSLWYYNKQNQ-QRWVDLEKPLKKQLDKYALE----PTVYFGVVFYV 86
PDZ4_LNX1_2-like cd06680
PDZ domain 4 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 504-588 1.11e-06

PDZ domain 4 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of LNX1 (also known as PDZ domain-containing RING finger protein 2, PDZRN2)and LNX2 (also known as PDZ domain-containing RING finger protein 1, PDZRN1), and related domains. LNX1 and LNX2 are Ring (Really Interesting New Gene) finger and PDZ domain-containing E3 ubiquitin ligases that bind to the cell fate determinant protein NUMB and mediate its ubiquitination. LNX1 can ubiquitinate a number of other ligands including PPFIA1, KLHL11, KIF7 and ERC2. LNX1 and LNX2 each have four PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This LNX family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467168 [Multi-domain]  Cd Length: 89  Bit Score: 47.34  E-value: 1.11e-06
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gi 386770278 504 TIRLQADEQGRYGFNVKGGVDLS---LPVQVSKVVPHTPAD-----RCtprvceGDEVLMINGRDVHGLRHEQVVAMIRD 575
Cdd:cd06680    2 DITLRRSSSGSLGFSIVGGYEEShgnQPFFVKSIVPGTPAYndgrlKC------GDIILAVNGVSTVGMSHAALVPLLKE 75

                         90
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gi 386770278 576 CRhqasGELLLTV 588
Cdd:cd06680   76 QR----GRVTLTV 84
PDZ_RGS12-like cd06710
PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 ...
 515-578 1.14e-06

PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RGS12, and related domains. RGS12 downregulates GPCR signal transduction by increasing the GTPase activity of G-protein alpha subunits, thereby driving G-proteins into their inactive GDP-bound form. The RGS12 PDZ domain can bind selectively to C-terminal (A/S)-T-X-(L/V) motifs as found within both the CXCR2 IL-8 receptor, and the alternative 3' exon form of RGS12. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RGS12-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467194 [Multi-domain]  Cd Length: 76  Bit Score: 46.86  E-value: 1.14e-06
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gi 386770278 515 YGFNVKGgvdlSLPVQVSKVVPHTPADRCTPRVceGDEVLMINGRDVHGLRHEQVVAMIRDCRH 578
Cdd:cd06710   12 YGFTISG----QAPCVLSCVVRGSPADVAGLKA--GDQILAVNGINVSKASHEDVVKLIGKCTG 69
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 512-589 1.25e-06

PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467186 [Multi-domain]  Cd Length: 89  Bit Score: 47.25  E-value: 1.25e-06
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gi 386770278 512 QGRYGFNVKGGVDLS-LP-------VQVSKVVPHTPADRCTPRVceGDEVLMINGRDV-HGLRHEQVVAMIRDCrhqasG 582
Cdd:cd06702    9 GGPLGLSIVGGSDHSsHPfgvdepgIFISKVIPDGAAAKSGLRI--GDRILSVNGKDLrHATHQEAVSALLSPG-----Q 81


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gi 386770278 583 ELLLTVR 589
Cdd:cd06702   82 EIKLLVR 88
PDZ2_L-delphilin-like cd06744
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
 511-582 1.33e-06

PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of delphilin (also known as glutamate receptor, ionotropic, delta 2-interacting protein 1, L-delphilin). Delphilin, a postsynaptic protein which it is selectively expressed at cerebellar Purkinje cells, links the glutamate receptor delta 2 subunit (GluRdelta2) with the actin cytoskeleton and various signaling molecules. Two alternatively spliced isoforms of delphilin have been characterized: L-delphilin has two PDZ domains, PDZ1 and PDZ2, and S-delphilin has a single PDZ domain (PDZ2). These two isoforms are differently palmitoylated and may be involved in controlling GluRdelta2 signaling in Purkinje cells. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This delphilin-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F


Pssm-ID: 467226 [Multi-domain]  Cd Length: 75  Bit Score: 46.89  E-value: 1.33e-06
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gi 386770278 511 EQGRYGFNVKGgvdlSLPVQVSKVVPHTPADRCTPRVceGDEVLMINGRDVHGLRHEQVVAMIrdcrhQASG 582
Cdd:cd06744    7 GNGSFGFTLRG----HAPVYIESVDPGSAAERAGLKP--GDRILFLNGLDVRNCSHDKVVSLL-----QGSG 67
PDZ2_PDZD7-like cd10834
PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 516-589 1.98e-06

PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of the long isoform 1 of PDZD7, and related domains. PDZD7 is critical for the organization of Usher syndrome type 2 (USH2) complex. Usher syndrome is the leading cause of hereditary sensory deaf-blindness in humans; USH2 is the most common sub-type. Formation of the USH2 complex is based upon heterodimerization between PDZD7 and whirlin (another PDZ domain-containing protein) and a subsequent dynamic interplay between USH2 proteins via their multiple PDZ domains. The PDZD7 PDZ2 domain binds GPR98 (also known as VLGR1) and usherin (USH2A). PDZD7 and whirlin form heterodimers through their multiple PDZ domains; whirlin and PDZD7 interact with usherin and GPR98 to form an interdependent ankle link complex. PDZD7 also interacts with myosin VIIa. PDZD7 also forms homodimers through its PDZ2 domain. Various isoforms of PDZD7 produced by alternative splicing have been identified; this subgroup includes the second PDZ domain of the canonical isoform of PDZD7- isoform 1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD7-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467270 [Multi-domain]  Cd Length: 85  Bit Score: 46.61  E-value: 1.98e-06
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gi 386770278 516 GFNVKGGVDLSLPVQVSKVVPHTPADRCTPRVceGDEVLMINGRDVHGLRHEQVVAMIRDCRHqasgeLLLTVR 589
Cdd:cd10834   16 GFNIRGGSEYGLGIYVSKVDPGGLAEQNGIKV--GDQILAVNGVSFEDITHSKAVEVLKSQTH-----LMLTIK 82
PDZ2_Scribble-like cd06703
PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 503-573 2.12e-06

PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467187 [Multi-domain]  Cd Length: 92  Bit Score: 46.87  E-value: 2.12e-06
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gi 386770278 503 ITIRLQADEQGrYGFNVKGGVDlSLP-------VQVSKVVPHTPADRcTPRVCEGDEVLMINGRDVHGLRHEQVVAMI 573
Cdd:cd06703    3 ITTTLIRDGKG-LGFSIAGGKG-STPfrdgdegIFISRITEGGAADR-DGKLQVGDRVLSINGVDVTEARHDQAVALL 77
PDZ13_MUPP1-like cd06676
PDZ domain 13 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 515-588 2.23e-06

PDZ domain 13 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 13 of MUPP1. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, PDZ9, and PDZ13. This MuPP1-like PDZ13 domain is therefore absent from PATJ. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ13 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467164 [Multi-domain]  Cd Length: 83  Bit Score: 46.56  E-value: 2.23e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386770278 515 YGFNVKGGVDLS---LPVQVSKVVPHTPADRCTpRVCEGDEVLMINGRDVHGLRHEQVVAMIRDCRhqasGELLLTV 588
Cdd:cd06676   11 LGFSIVGGFGSPhgdLPIYVKTVFEKGAAAEDG-RLKRGDQILAVNGESLEGVTHEEAVNILKKTK----GTVTLTV 82
FERM_C_ERM cd13194
FERM domain C-lobe/F3 of the ERM family; The ERM family includes ezrin, radixin, moesin and ...
 227-280 2.48e-06

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: 46.88  E-value: 2.48e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 386770278 227 YGIDLHRATDSNGKELQLGVSAVGLLVFQHSLRVN---TFSWSKMVKVSFKRKDFFI 280
Cdd:cd13194    2 YGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTpkiGFPWSEIRNISFNDKKFVI 58
PDZ1_ZO1-like cd06727
PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 504-589 4.01e-06

PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of ZO-1, -2, -3 and related domains. Zonula occludens proteins (ZO-1, ZO-2, ZO-3) are multi-PDZ domain proteins involved in the maintenance and biogenesis of multi-protein networks at the cytoplasmic surface of intercellular contacts in epithelial and endothelial cells. They have three N-terminal PDZ domains, PDZ1-3, followed by a Src homology-3 (SH3) domain and a guanylate kinase (GuK)-like domain. Among protein-protein interactions for all ZO proteins is the binding of the first PDZ domain (PDZ1) to the C-termini of claudins, and the homo- and hetero-dimerization of ZO-proteins via their second PDZ domain (PDZ2), which takes place by symmetrical domain swapping of the first two beta-strands of PDZ2. At the cell level, ZO-1 and ZO-2 are involved in polarity maintenance, gene transcription, cell proliferation, and tumor cell metastasis. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This ZO family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467209 [Multi-domain]  Cd Length: 87  Bit Score: 45.73  E-value: 4.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 504 TIRLQADEQGRYGFNVKGGVDLSLP------VQVSKVVPHTPADRctpRVCEGDEVLMINGRDVHGLRHEQVVAMIRDCR 577
Cdd:cd06727    2 TVTLHRAPGFGFGIAVSGGRDNPHFqsgdtsIVISDVLKGGPAEG---KLQENDRVVSVNGVSMENVEHSFAVQILRKCG 78

                         90
                 ....*....|..
gi 386770278 578 HQASgellLTVR 589
Cdd:cd06727   79 KTAN----ITVK 86
PDZ12_MUPP1-like cd06675
PDZ domain 12 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 10 of protein-associated tight ...
 503-588 4.55e-06

PDZ domain 12 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 10 of protein-associated tight junction (PATJ, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 12 of MUPP1, PDZ domain 10 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like PDZ12 family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F


Pssm-ID: 467163 [Multi-domain]  Cd Length: 86  Bit Score: 45.82  E-value: 4.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 503 ITIRLQADEQGRYGFNVKGGVDLSL---PVQVSKVVPHTPADRcTPRVCEGDEVLMINGRDVHGLRHEQVVAMIRdcrhQ 579
Cdd:cd06675    1 RTVEIKRGPQDSLGISIAGGVGSPLgdvPVFIAMIQPNGVAAQ-TGKLKVGDRIVSINGQSTDGLTHSEAVNLLK----N 75


                 ....*....
gi 386770278 580 ASGELLLTV 588
Cdd:cd06675   76 ASGTIILQV 84
PDZ_tamalin_CYTIP-like cd06713
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ ...
 515-576 4.68e-06

PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of tamalin, cytohesin-1-interacting protein, and related domains. Tamalin (trafficking regulator and scaffold protein tamalin, also known as general receptor for phosphoinositides 1-associated scaffold protein, GRASP) functions to link receptors, including group 1 metabotropic glutamate receptors (mGluRs), to neuronal proteins. The tamalin PDZ domain binds the C-terminal domains of group I mGluRs; it also binds potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 (HCN2), neurotrophin-3 (NT3) TrkCT1-truncated receptor, SAP90/PSD-95-associated protein, and tamalin itself. CYTIP (cytohesin-1-interacting protein, also known as Pleckstrin homology Sec7 and coiled-coil domain-binding protein) sequesters cytohesin-1 in the cytoplasm, limiting its interaction with beta2 integrins; cytohesin-1 binds the CYTIP coiled coil domain. The CYTIP PDZ domain can bind the C-terminal peptide of protocadherin alpha-1 (PCDHA1), indicating a possible interaction between the two. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This tamalin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467197 [Multi-domain]  Cd Length: 91  Bit Score: 45.69  E-value: 4.68e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386770278 515 YGFNVKGGVDLSLPVQVSKVVPHTPADRCTPRVceGDEVLMINGRDVHGLRHEQVVAMIRDC 576
Cdd:cd06713   23 YGLHHKNSNEVEMCTYVCRVHEDSPAYLAGLTA--GDVILSVNGVSVEGASHQEIVELIRSS 82
PDZ_Par6-like cd06718
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ...
 504-590 7.69e-06

PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F (RhoGAP100F), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Par6 (also known as PAR6 or Par-6), RhoGAP100F, and related domains. Par6 is part of a conserved machinery that directs metazoan cell polarity, a process necessary for the function of diverse cell types. Par6 forms a cell polarity-regulatory complex with atypical protein kinase C (aPKC) and Par3. Par6 can also directly associate with PALS1 (proteins associated with Lin7, also known as Stardust) providing a link between the Par3/aPKC/Par6 complex and the PALS1-PATJ (protein-associated TJ) complex. Binding partners of the Par6-PDZ domain include Par3, PALS1/Stardust; leucine-rich repeat-containing protein netrin-G ligand-2 (NGL-2), human crumbs (CRB3) involve in the morphogenesis of the tight junctions in mammalian epithelial cells, and PAR-6 co-operates with the Par6 semi-CRIB domain to bind CDC42. CDC42 regulates the Par6 PDZ domain through an allosteric CRIB-PDZ transition. Drosophila RhoGAP100F, also known as synapse defective protein 1 homolog (syd-1 homolog), is a GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound form. The RhoGAP100F-PDZ domain binds the neurexin C terminus to control synapse formation at the Drosophila neuromuscular junction. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Par6-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467202 [Multi-domain]  Cd Length: 84  Bit Score: 44.87  E-value: 7.69e-06
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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 504 TIRLQADEQGRYGFNVKGG--VDLSLPVQVSKVVPHTPADrCTPRVCEGDEVLMINGRDVHGLRHEQVVAMIrdcrhQAS 581
Cdd:cd06718    2 RVELIKPPGKPLGFYIRDGngVERVPGIFISRLVLGSLAD-STGLLAVGDEILEVNGVEVTGKSLDDVTDMM-----VAP 75


                 ....*....
gi 386770278 582 GELLLTVRP 590
Cdd:cd06718   76 TRLIITVKP 84
PDZ_GOPC-like cd06800
PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and ...
 503-588 7.70e-06

PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of GOPC and related domains. GOPC, also known as PIST (PDZ domain protein interacting specifically with TC10), FIG (fused in glioblastoma), and CAL (CFTR-associated ligand), regulates the trafficking of a wide array of proteins, including small GTPases, receptors, and cell surface molecules such as cadherin 23 and CFTR. It may regulate CFTR chloride currents and acid-sensing ASIC3 currents by modulating cell surface expression of both channels, and may play a role in autophagy. Interaction partners of the GOPC PDZ domains include: FZD5, FZD8, ASIC3, CFTR, MUC3, ARFRP1, Ggamma13, neuroligin, and Stargazin. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GOPC-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467261 [Multi-domain]  Cd Length: 83  Bit Score: 45.05  E-value: 7.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 503 ITIRLQADEQGRYGFNVKGGVDLSLPVQVSKVVPHTPADRCTpRVCEGDEVLMINGRDVHGLRHEQVVAMIRdcrhQASG 582
Cdd:cd06800    1 RKVLLSKEPHEGLGISITGGKEHGVPILISEIHEGQPADRCG-GLYVGDAILSVNGIDLRDAKHKEAVTILS----QQRG 75


                 ....*.
gi 386770278 583 ELLLTV 588
Cdd:cd06800   76 EITLEV 81
PDZ3_PDZD2-PDZ1_hPro-IL-16-like cd06759
PDZ domain 3 of PDZ domain containing 2 (PDZD2), PDZ domain 1 of human pro-interleukin-16 ...
 516-589 7.71e-06

PDZ domain 3 of PDZ domain containing 2 (PDZD2), PDZ domain 1 of human pro-interleukin-16 (isoform 1, 1332 AA), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of PDZD2, also known as KIAA0300, PIN-1, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains. PDZD2 is expressed at exceptionally high levels in the pancreas and certain cancer tissues, such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. This family also includes the first PDZ domain (PDZ1) of human pro-interleukin-16 (isoform 1, also known as nPro-Il-16; 1332 amino-acid protein). Precursor IL-16 is cleaved to produce pro-IL-16 and mature IL-16 (derived from the C-terminal 121 AA). Pro-IL-16 functions as a regulator of T cell growth; mature IL-16 is a CD4 ligand that induces chemotaxis and CD25 expression in CD4+ T cells. IL-16 bioactivity has been closely associated with the progression of several different cancers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD2-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467240 [Multi-domain]  Cd Length: 87  Bit Score: 44.96  E-value: 7.71e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386770278 516 GFNVKGGVDL---SLPVQVSKVVPHTPA--DRctpRVCEGDEVLMINGRDVHGLRHEQVVAMIRDCRhqaSGELLLTVR 589
Cdd:cd06759   15 GFSIVGGRDSprgPMGIYVKTIFPGGAAaeDG---RLKEGDEILEVNGESLQGLTHQEAIQKFKQIK---KGLVVLTVR 87
PDZ1_PTPN13_FRMPD2-like cd06694
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ...
 501-574 8.04e-06

PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], FRMPD2 (also known as PDZ domain-containing protein 4; PDZ domain-containing protein 5C), and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. FRMPD2 is localized in the basolateral membranes of polarized epithelial cells and is associated with tight junction formation and immune response; it contains 3 PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467180 [Multi-domain]  Cd Length: 92  Bit Score: 45.08  E-value: 8.04e-06
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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386770278 501 DLITIRLQADEQGRYGFNVKGG---VDLSLPVQVSKVVPHTPADRcTPRVCEGDEVLMINGRDVHGLRHEQVVAMIR 574
Cdd:cd06694    1 EIVIVTLKKDPQKGLGFTIVGGensGSLDLGIFVKSIIPGGPADK-DGRIKPGDRIIAINGQSLEGKTHHAAVEIIQ 76
FERM_C_FRMD1_FRMD6 cd13185
FERM domain C-lobe of FERM domain containing 1 and 6 proteins; FRMD6 (also called willin and ...
 226-317 1.05e-05

FERM domain C-lobe of FERM domain containing 1 and 6 proteins; FRMD6 (also called willin and hEx/human expanded) is localized throughout the cytoplasm or along the plasma membrane. The Drosophilla protein Ex is a regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in organ size control and is tumor suppression by restricting proliferation and promoting apoptosis. Surprisingly, hEx is thought to function independently of the Hippo pathway. Instead it is hypothesized that hEx inhibits progression through the S phase of the cell cycle by upregulating p21(Cip1) and downregulating Cyclin A. It is also implicated in the progression of Alzheimer disease. Not much is known about FRMD1 to date. Both FRMD1 and FRMD6 contains a single 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: 270006  Cd Length: 107  Bit Score: 45.38  E-value: 1.05e-05
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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 226 LYGIDLHRATDSNgkELQLGVSAVGLLVFQHSLRVN----TFSWSKMVKVSFKRKDFFIQlrrepSENYDTLLGFGMSSH 301
Cdd:cd13185    7 LYRLRKSKKETPG--SVLLGITAKGIQIYQESDGEQqllrTFPWSNIGKLSFDRKKFEIR-----PEGSLRKLTYYTSSD 79

                         90
                 ....*....|....*.
gi 386770278 302 KHAKALWKSCVEHHSF 317
Cdd:cd13185   80 EKSKYLLALCRETHQF 95
PDZ2_PDZD2-like cd06758
PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 ...
 531-574 1.26e-05

PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of PDZD2, also known as KIAA0300, PIN-1, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains, and is expressed at exceptionally high levels in the pancreas and certain cancer tissues such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD2-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467239 [Multi-domain]  Cd Length: 88  Bit Score: 44.65  E-value: 1.26e-05
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                 ....*....|....*....|....*....|....*....|....
gi 386770278 531 VSKVVPHTPADRCTpRVCEGDEVLMINGRDVHGLRHEQVVAMIR 574
Cdd:cd06758   33 VAGVEEGGSADRDG-RLKKGDELLMINGQSLIGLSHQEAVAILR 75
PDZ3_PTPN13_FRMPD2-like cd06695
PDZ domain 3 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), FERM and PDZ ...
 516-590 1.58e-05

PDZ domain 3 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], FRMPD2 (also known as PDZ domain-containing protein 4; PDZ domain-containing protein 5C), and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). FRMPD2 is localized in the basolateral membranes of polarized epithelial cells and is associated with tight junction formation and immune response; it contains 3 PDZ domains). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467181 [Multi-domain]  Cd Length: 90  Bit Score: 44.17  E-value: 1.58e-05
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gi 386770278 516 GFNVKGGvDLSLP-------VQVSKVVPHTPADRCTpRVCEGDEVLMINGRDVHGLRHEQVVAMIRDcrhqASGELLLTV 588
Cdd:cd06695   14 GFSFLGG-ENNSPedpfsglVRIKKLFPGQPAAESG-LIQEGDVILAVNGEPLKGLSYQEVLSLLRG----APPEVTLLL 87


                 ...
gi 386770278 589 -RP 590
Cdd:cd06695   88 cRP 90
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 871-951 1.92e-05

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 45.72  E-value: 1.92e-05
                         10        20        30        40        50        60        70        80
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gi 386770278 871 GATPEDE---TPVSTSVHQCISAaNPPVIVHCSAGIGRTGVLIlmdtALALMEAREPVYPLDIVRTMRDQRACMVQNVSQ 947
Cdd:cd14505   83 GGVPSDIaqwQELLEELLSALEN-GKKVLIHCKGGLGRTGLIA----ACLLLELGDTLDPEQAIAAVRALRPGAIQTPKQ 157


                 ....
gi 386770278 948 YRFV 951
Cdd:cd14505  158 ENFL 161
PDZ5_MAGI-1_3-like cd06735
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 502-586 2.22e-05

PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5, and belongs to this MAGI1,2,3-like family. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ5 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467217 [Multi-domain]  Cd Length: 84  Bit Score: 43.72  E-value: 2.22e-05
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gi 386770278 502 LITIRLQADEQGrYGFNVKGGVDLS-LPVQVSKVVPHTPADRCTpRVCEGDEVLMINGRDVHGLRHEQVVAMIRdcRHQA 580
Cdd:cd06735    1 YYSVELERGPKG-FGFSIRGGREYNnMPLYVLRLAEDGPAQRDG-RLRVGDQILEINGESTQGMTHAQAIELIR--SGGS 76


                 ....*.
gi 386770278 581 SGELLL 586
Cdd:cd06735   77 VVRLLL 82
PDZ5_DrPTPN13-like cd23060
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ...
 504-588 2.71e-05

PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of Danio rerio Ptpn13, and related domains. Protein-tyrosine phosphatases (PTPs) dephosphorylate phosphotyrosyl residues in proteins that are phosphorylated by protein tyrosine kinases (PTKs). Danio rerio Ptpn13 is a classical non-receptor-like PTP. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467273 [Multi-domain]  Cd Length: 80  Bit Score: 43.11  E-value: 2.71e-05
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gi 386770278 504 TIRLQADEQGRYGFNVKGGVDLSlPVQVSKVVPHTPADRcTPRVCEGDEVLMINGRDVHGLRHEQVVAMIRdcrhQASGE 583
Cdd:cd23060    1 QIELEKPANGGLGFSLVGGEGGS-GIFVKSISPGGVADR-DGRLQVGDRLLQVNGESVIGLSHSKAVNILR----KAKGT 74


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gi 386770278 584 LLLTV 588
Cdd:cd23060   75 VQLTV 79
PDZ2_MAGI-1_3-like cd06732
PDZ domain 2 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 542-576 3.14e-05

PDZ domain 2 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467214 [Multi-domain]  Cd Length: 82  Bit Score: 43.31  E-value: 3.14e-05
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gi 386770278 542 RCtPRVCEGDEVLMINGRDVHGLRHEQVVAMIRDC 576
Cdd:cd06732   36 RC-RGLQEGDLIVEINGQNVQNLSHAQVVDVLKEC 69
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 531-574 3.87e-05

circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CPP (also known as tail-specific protease, PRC protein, Protease Re, and Photosystem II D1 protein processing peptidase), and related domains. CPP belongs to the peptidase S41A family. It cleaves a C-terminal 11 residue peptide from the precursor form of penicillin-binding protein 3, and may have a role in protecting bacterium from thermal and osmotic stresses. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This CPP-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467623 [Multi-domain]  Cd Length: 88  Bit Score: 43.24  E-value: 3.87e-05
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gi 386770278 531 VSKVVPHTPADRCtpRVCEGDEVLMINGRDVHGLRHEQVVAMIR 574
Cdd:cd06782   18 VVSPIPGGPAEKA--GIKPGDVIVAVDGESVRGMSLDEVVKLLR 59
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
884-953 4.02e-05

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 44.58  E-value: 4.02e-05
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gi 386770278 884 VHQCIsAANPPVIVHCSAGIGRTGVLIlmdtALALMEAREPvyPLDIVRTMRDQRACMVQNVSQYRFVCE 953
Cdd:COG2453   73 IDEAL-REGKKVLVHCRGGIGRTGTVA----AAYLVLLGLS--AEEALARVRAARPGAVETPAQRAFLER 135
FERM_F1_PTPN14 cd17191
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 54-121 4.36e-05

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: 43.11  E-value: 4.36e-05
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gi 386770278  54 AKGSELLDQVFQYLELSERDYFGLLFPQKpGDVVRWVDAQKQFKKQCSSVSLDndavPLLEFRVKFFV 121
Cdd:cd17191   24 STGQECLEAVAQRLELRETHYFGLWFLSK-SQQARWVELEKPLKKQLDKFANE----PLLFFGVMFYV 86
PDZ3_LNX1_2-like cd06679
PDZ domain 3 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 502-576 4.57e-05

PDZ domain 3 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of LNX1 (also known as PDZ domain-containing RING finger protein 2, PDZRN2) and LNX2 (also known as PDZ domain-containing RING finger protein 1, PDZRN1), and related domains. LNX1 and LNX2 are Ring (Really Interesting New Gene) finger and PDZ domain-containing E3 ubiquitin ligases that bind to the cell fate determinant protein NUMB and mediate its ubiquitination. LNX1 can ubiquitinate a number of other ligands including PPFIA1, KLHL11, KIF7 and ERC2. LNX1 and LNX2 each have four PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This LNX family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467167 [Multi-domain]  Cd Length: 88  Bit Score: 43.01  E-value: 4.57e-05
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gi 386770278 502 LITIRLQADEQgrYGFNVKGGVD---LSLPVQVSKVVPHTPADRcTPRVCEGDEVLMINGRDVHGLRHEQVVAMIRDC 576
Cdd:cd06679    2 TVTIKKEPSES--LGISVAGGRGsrrGDLPIYVTNVQPDGCLGR-DGRIKKGDVLLSINGISLTNLSHSEAVAVLKAS 76
PDZ_RGS3-like cd06711
PDZ domain of regulator of G-protein signaling 3 (RGS3), and related domains; PDZ (PSD-95 ...
 515-577 5.52e-05

PDZ domain of regulator of G-protein signaling 3 (RGS3), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RGS3, and related domains. RGS3 down-regulates GPCR signal transduction by increasing the GTPase activity of G-protein alpha subunits, thereby driving G-proteins into their inactive GDP-bound form. It downregulates G-protein-mediated release of inositol phosphates and activation of MAP kinases. In Eph/ephrin signaling, RGS3 binds via its PDZ domain to the cytoplasmic C terminus of Eph receptor tyrosine kinase EphB. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RGS3-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467195 [Multi-domain]  Cd Length: 77  Bit Score: 42.38  E-value: 5.52e-05
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gi 386770278 515 YGFNVKGgvdlSLPVQVSKVVPHTPADRCTprVCEGDEVLMINGRDVHGLRHEQVVAMIRDCR 577
Cdd:cd06711   12 FGFTICD----DSPVRVQAVDPGGPAEQAG--LQQGDTVLQINGQPVERSKCVELAHAIRNCP 68
PDZ1_INAD-like cd23063
PDZ domain 1 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 507-575 6.69e-05

PDZ domain 1 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of INAD, and related domains. INAD assembles key enzymes of the Drosophila compound eye photo-transduction pathway into a supramolecular complex, supporting efficient and fast light signaling. It contains 5 PDZ domains arranged in tandem (PDZ1-PDZ5) which independently bind various proteins. INAD PDZ2 binds eye-specific protein kinase C, INAD PDZ3 binds transient receptor potential (TRP) channel, and INAD PDZ4,5 tandem binds NORPA (phospholipase Cbeta, PLCbeta). Mutations of the inaD gene that lead to disruption of each of these interactions impair fly photo signal transduction. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This INAD-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467276 [Multi-domain]  Cd Length: 87  Bit Score: 42.50  E-value: 6.69e-05
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gi 386770278 507 LQADEQGRYGFNVKGG-VDLSLPVQVS-----KVVPHTPADRCTpRVCEGDEVLMINGRDVHGLRHEQVVAMIRD 575
Cdd:cd23063    4 IEKTEKKSFGICIVRGeVKVSPNTKTTgifikGIIPDSPAHKCG-RLKVGDRILSVNGNDVRNSTEQAAIDLIKE 77
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 895-953 7.18e-05

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 45.03  E-value: 7.18e-05
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gi 386770278 895 VIVHCSAGIGRTGVLIlmdtALALMEArEPVYPLDIVRTMRDQRACMVQNVSQYRFVCE 953
Cdd:cd14506  112 VAVHCHAGLGRTGVLI----ACYLVYA-LRMSADQAIRLVRSKRPNSIQTRGQVLCVRE 165
PDZ1_PDZD7-like cd10833
PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 504-558 7.76e-05

PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of the long isoform 1 of PDZD7, and related domains. PDZD7 is critical for the organization of Usher syndrome type 2 (USH2) complex. Usher syndrome is the leading cause of hereditary sensory deaf-blindness in humans; USH2 is the most common sub-type. Formation of the USH2 complex is based upon heterodimerization between PDZD7 and whirlin (another PDZ domain-containing protein) and a subsequent dynamic interplay between USH2 proteins via their multiple PDZ domains. The PDZD7 PDZ2 domain binds GPR98 (also known as VLGR1) and usherin (USH2A). PDZD7 and whirlin form heterodimers through their multiple PDZ domains; whirlin and PDZD7 interact with usherin and GPR98 to form an interdependent ankle link complex. PDZD7 also interacts with myosin VIIa. PDZD7 also forms homodimers through its PDZ2 domain. Various isoforms of PDZD7 produced by alternative splicing have been identified; this subgroup includes the first PDZ domain of the canonical isoform of PDZD7- isoform 1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD7-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467269 [Multi-domain]  Cd Length: 84  Bit Score: 42.04  E-value: 7.76e-05
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gi 386770278 504 TIRLQADEQGRYGFNVKGGVDLSLPVQVSKVVPHTPADRCTprVCEGDEVLMING 558
Cdd:cd10833    3 TVTVEKSPDGSLGFSVRGGSEHGLGIFVSKVEEGSAAERAG--LCVGDKITEVNG 55
PDZ_CNK1_2_3-like cd06748
PDZ domain of connector enhancer of kinase suppressor of ras 1 (CNK1), CNK2, CNK3, and related ...
 531-589 7.94e-05

PDZ domain of connector enhancer of kinase suppressor of ras 1 (CNK1), CNK2, CNK3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CNK1 (also known as connector enhancer of KSR 1 (CNKSR1), CNK homolog protein 1, connector enhancer of KSR-like), CNK2 (also known as CNKSR2, CNK homolog protein 2), and CNK3 (also known as CNKSR3, CNK homolog protein 3, CNKSR family member 3, maguin-like). CNK proteins modulate Ras-mediated signaling, acting downstream of Ras as a scaffold for the Raf/MEK/ERK kinase cascade. They also modulate signaling mediated via Rho family small GTPases, through interactions with various guanine nucleotide exchange factors (GEFs) and GTPase activating proteins (GAPs), and modulate the insulin signaling pathway through interactions with the Arf guanine nucleotide exchange factors. CNK proteins also regulate cell proliferation and migration by acting as scaffolds for the PI3K/Akt and JNK signaling cascades. CNK2 plays a role in the molecular processes that govern morphology of the postsynaptic density (PSD), and influences subcellular localization of the regulatory NCK-interacting kinase TNIK. TNIK binds a region of CNK2 including the PDZ and the DUF domain; this region also binds the kinase MINK1. CNK2 may also influence the membrane localization of MINK1. CNK3 plays a part in transepithelial sodium transport; it coordinates assembly of an epithelial sodium channel (ENaC)-regulatory complex. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This CNK1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.


Pssm-ID: 467230 [Multi-domain]  Cd Length: 81  Bit Score: 41.82  E-value: 7.94e-05
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gi 386770278 531 VSKVVPHTPADRCTpRVCEGDEVLMINGRDVHGLRHEQVVAMIRdcrhQASGELLLTVR 589
Cdd:cd06748   28 ITGTKENSPADRCG-KIHAGDEVIQVNYQTVVGWQLKNLVRALR----EDPHGVTLTLK 81
PDZ2_MUPP1-like cd06667
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 503-576 9.39e-05

PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F


Pssm-ID: 467155 [Multi-domain]  Cd Length: 80  Bit Score: 41.88  E-value: 9.39e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386770278 503 ITIRLQADEQGrYGFNVKGGVdlSLPVQVSKVVPHTPADRcTPRVCEGDEVLMINGRDVHGLRHEQVVAMIRDC 576
Cdd:cd06667    1 EVIELVNDGSG-LGFGIVGGK--STGVVVKTILPGGVADR-DGRLRSGDHILQIGDTNLRGMGSEQVAQVLRQC 70
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 531-589 1.04e-04

PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 40.97  E-value: 1.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386770278  531 VSKVVPHTPADRCTprVCEGDEVLMINGRDVHGLrhEQVVAMIRDCRHQasgELLLTVR 589
Cdd:pfam17820   2 VTAVVPGSPAERAG--LRVGDVILAVNGKPVRSL--EDVARLLQGSAGE---SVTLTVR 53
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 892-938 1.09e-04

protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), also known as protein-tyrosine phosphatases of regenerating liver (PRLs) constitute a family of small, prenylated phosphatases that are the most oncogenic of all PTPs. They stimulate progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. They associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation. Vertebrates contain three members: PRL-1, PRL-2, and PRL-3.


Pssm-ID: 350350 [Multi-domain]  Cd Length: 156  Bit Score: 43.36  E-value: 1.09e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 386770278 892 NPPVIVHCSAGIGRTGVLIlmdtALALMEAREPvyPLDIVRTMRDQR 938
Cdd:cd14500   95 GACIAVHCVAGLGRAPVLV----AIALIELGMK--PEDAVEFIRKKR 135
PDZ_SHANK1_3-like cd06746
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ...
 531-588 1.19e-04

PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SHANK1, SHANK2, SHANK3, and related domains. SHANK family proteins, SHANK1 (also known as somatostatin receptor-interacting protein, SSTR-interacting protein, SSTRIP), SHANK2 (also known as cortactin-binding protein 1, proline-rich synapse-associated protein 1), and SHANK3 (proline-rich synapse-associated protein 2) are synaptic scaffolding proteins which are highly enriched in the post-synaptic densities of excitatory synapses. They have been implicated in synaptic transmission, synapse formation, synaptic plasticity, and cytoskeletal remodeling, and are regulators of Cav1 calcium current and CREB target expression. Many protein ligands have been identified for the Shank PDZ domain, such as GKAP (also known as SAPAP), betaPIX (a guanine nucleotide exchange factor used by Rho GTPase family members Rac1 and Cdc42), alpha-latrotoxin, neuroligin, group I metabotropic glutamate receptors (mGluRs), and L-type calcium channels. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SHANK-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.


Pssm-ID: 467228 [Multi-domain]  Cd Length: 101  Bit Score: 42.20  E-value: 1.19e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 386770278 531 VSKVVPHTPADRCTPRVceGDEVLMINGRDVHGLRHEQVVAMIRdcrhQASGELLLTV 588
Cdd:cd06746   46 LESVDPGGVADKAGLKK--GDFLLEINGEDVVKASHEQVVNLIR----QSGNTLVLKV 97
PDZ4_PTPN13-like cd06696
PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 503-576 1.34e-04

PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)] and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467182 [Multi-domain]  Cd Length: 85  Bit Score: 41.52  E-value: 1.34e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386770278 503 ITIRLQADEQGRYGFNVKGGVDlSLPVQVSKVVpHTPA---DRCTPrvceGDEVLMINGRDVHGLRHEQVVAMIRDC 576
Cdd:cd06696    4 LEVTLTKSEKGSLGFTVTKGKD-DNGCYIHDIV-QDPAksdGRLRP----GDRLIMVNGVDVTNMSHTEAVSLLRAA 74
PDZ_ARHGEF11-12-like cd23069
PDZ domain of ARHGEF11, ARHGEF12, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 507-574 1.38e-04

PDZ domain of ARHGEF11, ARHGEF12, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of ARHGEF11, ARHGEF12, and related domains. This subfamily includes the GEFs (guanine exchange factors) ARHGEF11 (Rho guanine nucleotide exchange factor 11, known as PDZ-RhoGEF) and ARHGEF12 (Rho guanine nucleotide exchange factor 12, also known as leukemia-associated RhoGEF). GEFs activate Rho GTPases by promoting GTP binding. ARHGEF11/12 are regulators of G protein signaling (RGS) domain-containing GEFs; the RGS domain mediates their binding to and activation of Galpha (and Gq also in the case of ARHGEF12), in response to G-protein coupled receptor activation. ARHGEF11 and 12 are involved in serum-signaling, and regulate Yes-Associated Protein (YAP1)-dependent transcription. The ARHGEF12 PDZ domain binds plexin-B1 and the receptor tyrosine kinase insulin-like growth factor receptor (IGF-R1) beta-subunit. ARHGEF12 also interacts with glutamate receptor delta-1(GluD1), a postsynaptic organizer of inhibitory synapses in cortical pyramidal neurons. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This ARHGEF11-12-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467282 [Multi-domain]  Cd Length: 76  Bit Score: 41.22  E-value: 1.38e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386770278 507 LQADEQGrYGFNVKGgvdlSLPVQVSKVVPHTPADRCTprVCEGDEVLMINGRDVHGLRHEQVVAMIR 574
Cdd:cd23069    6 IQRDENG-YGLTVSG----DNPVFVQSVKEGGAAYRAG--VQEGDRIIKVNGTLVTHSNHLEVVKLIK 66
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 506-574 1.53e-04

C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440556 [Multi-domain]  Cd Length: 341  Bit Score: 44.86  E-value: 1.53e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386770278 506 RLQADEQGRYGFNvkgGVDLSLP---VQVSKVVPHTPADRctPRVCEGDEVLMINGRDVHGLRHEQVVAMIR 574
Cdd:COG0793   50 DFQESTSGEFGGL---GAELGEEdgkVVVVSVIPGSPAEK--AGIKPGDIILAIDGKSVAGLTLDDAVKLLR 116
PDZ_PICK1-like cd06722
PDZ domain of PICK1 (protein interacting with C-kinase 1) and similar domains; PDZ (PSD-95 ...
 504-574 1.86e-04

PDZ domain of PICK1 (protein interacting with C-kinase 1) and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PICK1, and related domains. PICK1 (also known as PRKCA-binding protein and protein kinase C-alpha-binding protein) plays a key role in regulating trafficking of binding partners by altering either their subcellular targeting and/or surface expression. PICK1 plays a role in synaptic plasticity by regulating the trafficking and internalization of amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) receptors; the PICK1-PDZ domain binds the AMPA receptor subunits. The PICK1 PDZ domain also binds glutamate transporters, Eph receptors, metabotropic glutamate receptors, and ASICs (acid-sensing ion channels), among others. Clustering and synaptic targeting of PICK1 requires direct interaction between the PDZ domain and lipid membranes. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PICK-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.


Pssm-ID: 467205 [Multi-domain]  Cd Length: 84  Bit Score: 40.86  E-value: 1.86e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386770278 504 TIRLQADEQGRYGFNVKGGVDLSLPVQVSKVVPHTPADRcTPRVCEGDEVLMINGRDVHGLRHEQVVAMIR 574
Cdd:cd06722    2 TVTLKKDAQNLIGISIGGGAPYCPCLYIVQVFDNTPAAK-DGTLAAGDEIVGVNGKSVKGKTKVEVAKMIQ 71
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 884-951 2.72e-04

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 42.70  E-value: 2.72e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386770278 884 VHQCISAANPP---VIVHCSAGIGRTGVLIlmdtALALMEaREPVYPLDIVRTMRDQRACMVqNVSQYRFV 951
Cdd:PTZ00242  87 LDQEFAKQSTPpetIAVHCVAGLGRAPILV----ALALVE-YGGMEPLDAVGFVREKRKGAI-NQTQLQFL 151
PDZ2_FL-whirlin cd06741
PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 505-589 2.97e-04

PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of the full-length isoform of whirlin and related domains. Whirlin is an essential protein for developmental pathways in photoreceptor cells of the retina and hair cells of the inner ear. The full-length whirlin isoform has two harmonin N-like domains, three PDZ domains, a proline-rich region, and a PDZ-binding motif. Whirlin isoforms may form different complexes at the periciliary membrane complex (PMC) in photoreceptors, and the stereociliary tip and base in inner ear hair cells. It interacts with ADGRV1 and usherin at the PMC; with SANS and RpgrORF15 at the connecting cilium in photoreceptors; with EPS8, MYO15A, p55, and CASK proteins at the stereociliary tip of inner ear hair cells; and with ADGRV1, usherin, and PDZD7 at the stereociliary base in inner ear hair cells. Mutations in the gene encoding whirlin (WHRN; also known as USH2D and DFNB31), have been found to cause either USH2 subtype (USH2D) or autosomal recessive non-syndromic deafness type 31 (DFNB31). Whirlin is the key protein in the USH2 complex (whirlin, usherin and GPR98) which recruits other USH2 causative proteins at the periciliary membrane in photoreceptors and the ankle link of the stereocilia in hair cells. Whirlin's interaction with espin, another stereociliary protein, may be important for the architecture of the USH2 complex. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This whirlin family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467223 [Multi-domain]  Cd Length: 84  Bit Score: 40.32  E-value: 2.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 505 IRLQADEQGRYGFNVKGGVDLSLPVQVSKVVPHTPADRCTPRVceGDEVLMINGRDVHGLRHEQVVAMIRDCRHqasgeL 584
Cdd:cd06741    4 VNLVVEDGQSLGLMIRGGAEYGLGIYVTGVDPGSVAENAGLKV--GDQILEVNGRSFLDITHDEAVKILKSSKH-----L 76


                 ....*
gi 386770278 585 LLTVR 589
Cdd:cd06741   77 IMTVK 81
PDZ1_PTPN13-like cd23072
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 501-576 8.66e-04

PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467285 [Multi-domain]  Cd Length: 92  Bit Score: 39.40  E-value: 8.66e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386770278 501 DLITIRLQADEQGRYGFNVKGGVD---LSLPVQVSKVVPHTPADrCTPRVCEGDEVLMINGRDVHGLRHEQVVAMIRDC 576
Cdd:cd23072    1 EITLVNLKKDAKYGLGFQIVGGEKsgrLDLGIFISSITPGGPAD-LDGRLKPGDRLISVNDVSLEGLSHDAAVEILQNA 78
PDZ_densin_erbin-like cd06749
PDZ domain of densin, erbin, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 516-589 8.79e-04

PDZ domain of densin, erbin, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of densin, erbin, and related domains. Densin (also known as leucine-rich repeat-containing protein 7, LRRC7, densin-180, protein LAP1) and erbin (also known as densin-180-like protein, Erbb2-interacting protein, protein LAP2) belong to the LAP (leucine-rich repeat and PDZ domain) family of scaffolding proteins that play roles in the maintenance of cell shape and apical-basal polarity. Densin and erbin are components of the excitatory postsynaptic compartment and are regulators of dendritic morphology and postsynaptic structure. The densin PDZ domain binds CaV1.3 alpha1 subunit, delta-catenin, and MAGUIN-1. Binding partners of the erbin PDZ domain include ErbB receptor tyrosine kinase ErbB2, HTLV-1 Tax1, Cav1.3 Ca2+channels, and constituents of the cadherin:catenin cell adhesion complex, in particular delta-catenin, p0071 and ARVCF. The erbin PDZ domain binds Smad3, a transductor of the TGFbeta pathway, possibly by a novel interface of binding. Erbin and two other LAP proteins (scribble and lano) redundantly regulate epithelial polarity and apical adhesion complex. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This densin and erbin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467231 [Multi-domain]  Cd Length: 87  Bit Score: 39.23  E-value: 8.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 516 GFNVKGGVDLS--------LPVQVSKVVPHTPADRCtprVCEGDEVLMINGRDVHGLRHEQVVAMIRDCRHQASgelLLT 587
Cdd:cd06749   12 GFSISGGIGSQgnpfrpddDGIFVTKVQPDGPASKL---LQPGDKILEVNGYDFVNIEHGQAVSLLKSFQNTVD---LVV 85


                 ..
gi 386770278 588 VR 589
Cdd:cd06749   86 ER 87
PDZ_RapGEF2_RapGEF6-like cd06755
PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange ...
 516-589 1.13e-03

PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange factor 6, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Rap guanine nucleotide exchange factor 2 (RapGEF2, also named RA-GEF-1, PDZ-GEF1, CNrasGEF and nRapGEP) and Rap guanine nucleotide exchange factor 6 (RapGEF6, also named RA-GEF-2 and PDZ-GEF2). RapGEF2 and RapGEF6 constitute a subfamily of guanine nucleotide exchange factors (GEFs) for RAP small GTPases that is characterized by the possession of the PDZ and Ras/Rap-associating domains. They activate Rap small GTPases, by catalyzing the release of GDP from the inactive GDP-bound forms, thereby accelerating GTP loading to yield the active GTP-bound forms. The PDZ domain of RapGEF6 (also known as PDZ-GEF2) binds junctional adhesion molecule A (JAM-A). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RapGEF2 and RapGEF6 family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467237 [Multi-domain]  Cd Length: 83  Bit Score: 38.78  E-value: 1.13e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386770278 516 GFNVKGGVDLSLPVQVSKVVPHTPADRCTPRvcEGDEVLMINGRDVHGLRHEQVVAMIRDCRHqasgeLLLTVR 589
Cdd:cd06755   15 HFSLLGGSEKGFGIFVSKVEKGSKAAEAGLK--RGDQILEVNGQNFENITLKKALEILRNNTH-----LSITVK 81
PDZ_TAX1BP3-like cd10822
PDZ domain of tax1-binding protein 3 (TAX1BP3), and related domains; PDZ (PSD-95 (Postsynaptic ...
 505-574 1.21e-03

PDZ domain of tax1-binding protein 3 (TAX1BP3), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of TAX1BP3, and related domains. TAX1BP3 (also known as glutaminase-interacting protein 3, tax interaction protein 1, TIP-1, tax-interacting protein 1) may regulate a number of protein-protein interactions by competing for PDZ domain binding sites. TAX1BP3 binds beta-catenin and may act as an inhibitor of the Wnt signaling pathway. It competes with LIN7A (also known as Lin-7A or LIN-7A) for inward rectifier potassium channel 4 (KCNJ4) binding, and thereby promotes KCNJ4 internalization. It may play a role in the Rho signaling pathway, and in the activation of CDC42 by the viral protein HPV16 E6. Binding partners of the TAX1BP3 PDZ domain include beta-catenin, KCNJ4, glutaminase liver isoform (GLS2), rho guanine nucleotide exchange factor 16 (ARHGEF16), rhotekin, and CDK5 regulatory subunit-associated protein 3 (also known as LAPZ). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This TAX1BP3-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467265 [Multi-domain]  Cd Length: 94  Bit Score: 38.86  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 505 IRLQADEQG---RYGFNVKGGVD-------LSLP---VQVSKVVPHTPADRCTPRVceGDEVLMINGRDVHGLRHEQVVA 571
Cdd:cd10822    2 IEIHKLRQGenlILGFSIGGGIDqdpsknpFSYTdkgIYVTRVSEGGPAEKAGLQV--GDKILQVNGWDMTMVTHKQAVK 79


                 ...
gi 386770278 572 MIR 574
Cdd:cd10822   80 RLT 82
PDZ3_Dlg1-2-4-like cd06795
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 504-574 1.35e-03

PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of Drosophila Dlg1, human Dlg1, 2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197; SAP-97), Dlg2 (also known as channel-associated protein of synapse-110; postsynaptic density protein 93, PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95; synapse-associated protein 90, SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling, regulating surface expression of NMDA receptors in dorsal horn neurons of the spinal cord; it interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. The Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development; postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467257 [Multi-domain]  Cd Length: 91  Bit Score: 38.88  E-value: 1.35e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386770278 504 TIRLQADEQGrYGFNVKGGVDlSLPVQVSKVVPHTPADRCTpRVCEGDEVLMINGRDVHGLRHEQVVAMIR 574
Cdd:cd06795    4 KIVLHKGSTG-LGFNIVGGED-GEGIFISFILAGGPADLSG-ELRRGDQILSVNGVDLRNATHEQAAAALK 71
PDZ1_Scribble-like cd06704
PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 503-576 1.59e-03

PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467188 [Multi-domain]  Cd Length: 87  Bit Score: 38.41  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 503 ITIRLQADEQGrYGFNVKGGVDlSLPVQ-------VSKVVPHTPADRCTPRVceGDEVLMINGRDVHGLRHEQVVAMIRD 575
Cdd:cd06704    1 LTITIERQTGG-LGISIAGGKG-STPYKgddegifISRVTEGGPAAKAGVRV--GDKLLEVNGVDLVDADHHEAVEALKN 76


                 .
gi 386770278 576 C 576
Cdd:cd06704   77 S 77
FERM_C_PTPH13 cd13187
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many ...
 228-317 1.64e-03

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: 38.84  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 228 GIDLHRATD---SNGKELQLGVSAVGLLVF--QHSLRVNT--FSWSKMVKVSFKRKDFFIQLRREPSENydtlLGFGMSS 300
Cdd:cd13187    1 GVHFHRVYRekkSSTLSLWLGICSRGIIIYeeKNGARTPVlrFPWRETQKISFDKKKFTIESRGGSGIK----HTFYTDS 76

                         90
                 ....*....|....*..
gi 386770278 301 HKHAKALWKSCVEHHSF 317
Cdd:cd13187   77 YKKSQYLLQLCSAQHKF 93
FERM_F1_FRMD4 cd17103
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 35-122 1.72e-03

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: 38.42  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278  35 CVTVLfLDDITHTFRIEKRAKGSELLDQVFQYLELSERDYFGLLFpQKPGDVVRWVDAQK-----QFKKQCSSvsldndA 109
Cdd:cd17103    5 CQVVL-LDDRRLEILVQPKLLAGDLLDLVASHFNLKEKEYFGLAY-EDETGHYNWLQLDKrvldhEFPKKWSS------G 76

                         90
                 ....*....|...
gi 386770278 110 VPLLEFRVKFFVS 122
Cdd:cd17103   77 PLVLHFAVKFYVE 89
PDZ7_PDZD2-PDZ4_hPro-IL-16-like cd06763
PDZ domain 7 of PDZ domain containing 2 (PDZD2), PDZ domain 4 of human pro-interleukin-16 ...
 502-566 1.95e-03

PDZ domain 7 of PDZ domain containing 2 (PDZD2), PDZ domain 4 of human pro-interleukin-16 (isoform 1, 1332 AA), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 7 of PDZD2, also known as KIAA0300, PIN-1, PAPIN, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains. PDZD2 is expressed at exceptionally high levels in the pancreas and certain cancer tissues, such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. This family include the PDZ domain of the secreted mature form of human interleukin-16 (IL-16); this is the fourth PDZ domain (PDZ4) of human pro-interleukin-16 (isoform 1, also known as nPro-Il-16). Precursor IL-16 is cleaved to produce pro-IL-16 and C-terminal mature IL-16. Pro-IL-16 functions as a regulator of T cell growth; mature IL-16 is a CD4 ligand that induces chemotaxis and CD25 expression in CD4+ T cells. IL-16 bioactivity has been closely associated with the progression of several different cancers PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD2-like family PDZ7 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467244 [Multi-domain]  Cd Length: 86  Bit Score: 38.36  E-value: 1.95e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386770278 502 LITIRLQADEQGrYGFNVKGGVDLSL---PVQVSKVVPHTPADRCTpRVCEGDEVLMINGRDVHGLRH 566
Cdd:cd06763    1 AVTVELEKGSAG-LGFSLEGGKGSPLgdrPLTIKRIFKGGAAEQSG-VLQVGDEILQINGTSLQGLTR 66
PDZ11_MUPP1-PDZ9_PATJ-like cd06674
PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ ...
 529-588 2.04e-03

PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 11 of MUPP1, PDZ domain 9 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ11 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467162 [Multi-domain]  Cd Length: 87  Bit Score: 38.03  E-value: 2.04e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 529 VQVSKVVPHTPADRCTpRVCEGDEVLMINGRDVHGLRHEQVVAMIRDCrhqaSGELLLTV 588
Cdd:cd06674   29 VFVSDIVKGGAADADG-RLMQGDQILSVNGEDVRNASQEAAAALLKCA----QGKVRLEV 83
PDZ2_DLG5-like cd06765
PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 522-585 2.21e-03

PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg5-like family PSZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467246 [Multi-domain]  Cd Length: 77  Bit Score: 37.71  E-value: 2.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386770278 522 GVDLSLPVQVSKVVPHTPADRcTPRVCEGDEVLMINGRDVHGLRHEQVVAMIRDCRHQASGELL 585
Cdd:cd06765   11 GISLENGVFISRIVPGSPAAK-EGSLTVGDRIIAINGIALDNKSLSECEALLRSCRDSLSLSLM 73
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 502-589 2.46e-03

PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of the full-length isoform of whirlin and related domains. Whirlin is an essential protein for developmental pathways in photoreceptor cells of the retina and hair cells of the inner ear. The full-length whirlin isoform has two harmonin N-like domains, three PDZ domains, a proline-rich region, and a PDZ-binding motif. Whirlin isoforms may form different complexes at the periciliary membrane complex (PMC) in photoreceptors, and the stereociliary tip and base in inner ear hair cells. It interacts with ADGRV1 and usherin at the PMC; with SANS and RpgrORF15 at the connecting cilium in photoreceptors; with EPS8, MYO15A, p55, and CASK proteins at the stereociliary tip of inner ear hair cells; and with ADGRV1, usherin, and PDZD7 at the stereociliary base in inner ear hair cells. Mutations in the gene encoding whirlin (WHRN; also known as USH2D and DFNB31), have been found to cause either USH2 subtype (USH2D) or autosomal recessive non-syndromic deafness type 31 (DFNB31). Whirlin is the key protein in the USH2 complex (whirlin, usherin and GPR98) which recruits other USH2 causative proteins at the periciliary membrane in photoreceptors and the ankle link of the stereocilia in hair cells. Whirlin's interaction with espin, another stereociliary protein, may be important for the architecture of the USH2 complex. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This whirlin family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467222 [Multi-domain]  Cd Length: 82  Bit Score: 37.73  E-value: 2.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 502 LITIRLQADEQGrYGFNVKGGVDLSLPVQVSKVVPHTPADRCTPRVceGDEVLMINGRDVHGLRHEQVVAMIRDCRhqas 581
Cdd:cd06740    3 QVTLKRSKSHEG-LGFSIRGGAEHGVGIYVSLVEPGSLAEKEGLRV--GDQILRVNDVSFEKVTHAEAVKILRVSK---- 75


                 ....*...
gi 386770278 582 gELLLTVR 589
Cdd:cd06740   76 -KLVLSVR 82
FERM_F1_ERM cd17187
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 48-120 3.82e-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: 37.45  E-value: 3.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386770278  48 FRIEKRAKGSELLDQVFQYLELSERDYFGLLFPQKPGDVVrWVDAQKQFKKQcsSVSLDNdavPLL-EFRVKFF 120
Cdd:cd17187   14 FAIQPNTTGKQLFDQVVKTIGLREIWFFGLQYVDSKGYST-WLKLNKKVLSQ--DVKKEN---PLQfKFRAKFY 81
PDZ4_MUPP1-like cd06668
PDZ domain 4 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 531-575 3.83e-03

PDZ domain 4 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F


Pssm-ID: 467156 [Multi-domain]  Cd Length: 88  Bit Score: 37.28  E-value: 3.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 386770278 531 VSKVVPHTPADRCTpRVCEGDEVLMINGRDVHGLRHEQVVAMIRD 575
Cdd:cd06668   34 IRSILPEGPVGRNG-KLFSGDELLEVNGIQLLGLSHKEVVSILKE 77
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 884-951 6.21e-03

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 38.03  E-value: 6.21e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770278 884 VHQCIsAANPPVIVHCSAGIGRTGvlilmdTALA--LMEAREpVYPLDIVRTMRDQRACMVQNVSQYRFV 951
Cdd:cd14504   75 VEEAN-AKNEAVLVHCLAGKGRTG------TMLAcyLVKTGK-ISAVDAINEIRRIRPGSIETSEQEKFV 136
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 871-923 7.15e-03

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


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 38.59  E-value: 7.15e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386770278 871 GATPEDETpvstsVHQCISA---ANPPVIVHCSAGIGRTGVLIlmdtALALM-----EARE 923
Cdd:cd14499   90 GSTPSDDI-----VKKFLDIcenEKGAIAVHCKAGLGRTGTLI----ACYLMkhygfTARE 141
 
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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