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Conserved domains on  [gi|528504074|ref|XP_687930|]
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tyrosine-protein phosphatase non-receptor type 3 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 561-833 0e+00

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


The actual alignment was detected with superfamily member cd14600:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 274  Bit Score: 562.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 561 EESMARLEKGLVTGTLLLHFEKLYRKKEGMLMSCAKQSENMDKNRYKDVLPYDITRVVLQEeGDDYINASHVKTEPAG-- 638
Cdd:cd14600    1 EESMAQLKKGLESGTVLIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQG-NEDYINASYVNMEIPSan 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 639 CVLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHPPEVRDYGYLQVCCHSEECNLAYVTRQLT 718
Cdd:cd14600   80 IVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREML 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 719 LTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMRQESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVY 798
Cdd:cd14600  160 LTNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVY 239

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 528504074 799 PLEVITLMREQRAMLVQTSCQFTFVCEAILRVYRE 833
Cdd:cd14600  240 PLDIVRKMRDQRAMMVQTSSQYKFVCEAILRVYEE 274
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 33-223 7.52e-55

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: 188.27  E-value: 7.52e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074    33 CLVLFPDGTTQNFTVNKHDAGHLLFDLACEHLNIVEKQYFSMQISEDTSSSPRWLDPNKPFKKQLKGSPPFFLMFRVRFF 112
Cdd:smart00295   2 LKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRHWLDPAKTLLDQDVKSEPLTLYFRVKFY 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074   113 ISDPNSLQHEQTRH-FYFLQIRKDICEGRLKCPLSSAVVLASYSVQSELGDYNPETPT--GYLSKTHFIPEQ------DQ 183
Cdd:smart00295  82 PPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDlrGELSLKRFLPKQlldsrkLK 161

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 528504074   184 EFLLKVESLHPQHKGLSQSDAELCYLNTARTLDLYGVELH 223
Cdd:smart00295 162 EWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
PDZ_PTPN3-4-like cd06706
PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein ...
 437-526 1.04e-50

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: 172.50  E-value: 1.04e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 437 GDLLLVRISPDQDGKFGFNVKGGVDQKMPLAISHVNLASPAGRCVPPLMEGDQVLLINGRDISEHTHQQVVMFIKASRES 516
Cdd:cd06706    1 DGLVLIRMKPDENGRFGFNVKGGVDQKMPVIVSRVAPGTPADLCIPRLNEGDQVLLINGRDISEHTHDQVVMFIKASRER 80

                         90
                 ....*....|
gi 528504074 517 HSKELALLVR 526
Cdd:cd06706   81 HSGELVLLVR 90
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 217-309 4.19e-44

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13189:

Pssm-ID: 473070  Cd Length: 95  Bit Score: 154.01  E-value: 4.19e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 217 LYGVELHHAQDASNPAVWVGITSGGVALFCHLICSSFFPWINIIKISFKRKRFFVHLRRKHGELGHHVVSLSMPNSRACK 296
Cdd:cd13189    1 LYGVELHSARDSNNLELQIGVSSAGILVFQNGIRINTFPWSKIVKISFKRKQFFIQLRREPNESRDTILGFNMLSYRACK 80

                         90
                 ....*....|...
gi 528504074 297 NLWRSCVDHHTFY 309
Cdd:cd13189   81 NLWKSCVEHHTFF 93
 
Name Accession Description Interval E-value
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 561-833 0e+00

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: 562.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 561 EESMARLEKGLVTGTLLLHFEKLYRKKEGMLMSCAKQSENMDKNRYKDVLPYDITRVVLQEeGDDYINASHVKTEPAG-- 638
Cdd:cd14600    1 EESMAQLKKGLESGTVLIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQG-NEDYINASYVNMEIPSan 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 639 CVLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHPPEVRDYGYLQVCCHSEECNLAYVTRQLT 718
Cdd:cd14600   80 IVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREML 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 719 LTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMRQESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVY 798
Cdd:cd14600  160 LTNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVY 239

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 528504074 799 PLEVITLMREQRAMLVQTSCQFTFVCEAILRVYRE 833
Cdd:cd14600  240 PLDIVRKMRDQRAMMVQTSSQYKFVCEAILRVYEE 274
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
579-829 1.05e-104

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 323.46  E-value: 1.05e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074   579 HFEKLYRKKEGML-MSCAKQSENMDKNRYKDVLPYDITRVVLQ---EEGDDYINASHVKTEPAGcvLQYIAAQGPLPHTC 654
Cdd:smart00194   5 EFEKLDRLKPDDEsCTVAAFPENRDKNRYKDVLPYDHTRVKLKpppGEGSDYINASYIDGPNGP--KAYIATQGPLPSTV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074   655 THFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWP-HPPEVRDYGYLQVCCHSEECNLAYVTRQLTLTNTQSGQQRSITHL 733
Cdd:smart00194  83 EDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPdEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVTHY 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074   734 QYVAWPDHGVPEDSSDFLDFVKSVR-SMRQESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAM 812
Cdd:smart00194 163 HYTNWPDHGVPESPESILDLIRAVRkSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPG 242

                          250
                   ....*....|....*..
gi 528504074   813 LVQTSCQFTFVCEAILR 829
Cdd:smart00194 243 MVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
600-828 1.73e-95

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 298.39  E-value: 1.73e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  600 NMDKNRYKDVLPYDITRVVLQEEGD--DYINASHVKTEPAGcvLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTE 677
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPGpsDYINASYIDGYKKP--KKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  678 RGRTKCHQYWP-HPPEVRDYGYLQVCCHSEECNLA-YVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVK 755
Cdd:pfam00102  79 KGREKCAQYWPeEEGESLEYGDFTVTLKKEKEDEKdYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528504074  756 SVRSMRQE--SVPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAIL 828
Cdd:pfam00102 159 KVRKSSLDgrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 33-223 7.52e-55

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: 188.27  E-value: 7.52e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074    33 CLVLFPDGTTQNFTVNKHDAGHLLFDLACEHLNIVEKQYFSMQISEDTSSSPRWLDPNKPFKKQLKGSPPFFLMFRVRFF 112
Cdd:smart00295   2 LKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRHWLDPAKTLLDQDVKSEPLTLYFRVKFY 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074   113 ISDPNSLQHEQTRH-FYFLQIRKDICEGRLKCPLSSAVVLASYSVQSELGDYNPETPT--GYLSKTHFIPEQ------DQ 183
Cdd:smart00295  82 PPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDlrGELSLKRFLPKQlldsrkLK 161

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 528504074   184 EFLLKVESLHPQHKGLSQSDAELCYLNTARTLDLYGVELH 223
Cdd:smart00295 162 EWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
PDZ_PTPN3-4-like cd06706
PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein ...
 437-526 1.04e-50

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: 172.50  E-value: 1.04e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 437 GDLLLVRISPDQDGKFGFNVKGGVDQKMPLAISHVNLASPAGRCVPPLMEGDQVLLINGRDISEHTHQQVVMFIKASRES 516
Cdd:cd06706    1 DGLVLIRMKPDENGRFGFNVKGGVDQKMPVIVSRVAPGTPADLCIPRLNEGDQVLLINGRDISEHTHDQVVMFIKASRER 80

                         90
                 ....*....|
gi 528504074 517 HSKELALLVR 526
Cdd:cd06706   81 HSGELVLLVR 90
FERM_C_PTPN4_PTPN3_like cd13189
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and ...
 217-309 4.19e-44

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: 154.01  E-value: 4.19e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 217 LYGVELHHAQDASNPAVWVGITSGGVALFCHLICSSFFPWINIIKISFKRKRFFVHLRRKHGELGHHVVSLSMPNSRACK 296
Cdd:cd13189    1 LYGVELHSARDSNNLELQIGVSSAGILVFQNGIRINTFPWSKIVKISFKRKQFFIQLRREPNESRDTILGFNMLSYRACK 80

                         90
                 ....*....|...
gi 528504074 297 NLWRSCVDHHTFY 309
Cdd:cd13189   81 NLWKSCVEHHTFF 93
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 597-835 3.87e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 153.23  E-value: 3.87e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 597 QSENMDKNRYKDVLPYDITRVVLQEE--GDDYINASHVKTEPAGcvLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTT 674
Cdd:PHA02742  49 ELKNMKKCRYPDAPCFDRNRVILKIEdgGDDFINASYVDGHNAK--GRFICTQAPLEETALDFWQAIFQDQVRVIVMITK 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 675 LTERGRTKCHQYW-PHPPEVRDYGYLQVCCHSEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDF 753
Cdd:PHA02742 127 IMEDGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDF 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 754 VKSVRSM------------RQESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFT 821
Cdd:PHA02742 207 VLAVREAdlkadvdikgenIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYI 286

                        250
                 ....*....|....
gi 528504074 822 FvCEAILRVYREKV 835
Cdd:PHA02742 287 F-CYFIVLIFAKLM 299
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
596-820 1.76e-31

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 124.43  E-value: 1.76e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 596 KQSENMDKNRYKDVLPYDITRVvlqEEGDDYINASHVKtepAGCVLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTL 675
Cdd:COG5599   38 QNINGSPLNRFRDIQPYKETAL---RANLGYLNANYIQ---VIGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASD 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 676 TE--RGRTKCHQYWPHPPEvrdygYLQVCCHSEECNLAYVTRQLT-----LTNTQSGQ-QRSITHLQYVAWPDHGVPeDS 747
Cdd:COG5599  112 DEisKPKVKMPVYFRQDGE-----YGKYEVSSELTESIQLRDGIEartyvLTIKGTGQkKIEIPVLHVKNWPDHGAI-SA 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 748 SDFLDFVKSVRSMRQESV----PLMVHCSAGIGRTGVLITMeTAMTLMEKEKPVYPL---EVITLMREQRAM-LVQTSCQ 819
Cdd:COG5599  186 EALKNLADLIDKKEKIKDpdklLPVVHCRAGVGRTGTLIAC-LALSKSINALVQITLsveEIVIDMRTSRNGgMVQTSEQ 264


                 .
gi 528504074 820 F 820
Cdd:COG5599  265 L 265
FERM_F1_PTPN3_like cd17100
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 31-113 3.06e-31

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: 117.02  E-value: 3.06e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  31 LLCLVLFPDGTTQNFTVNKHDAGHLLFDLACEHLNIVEKQYFSMQISEDTSS--SPRWLDPNKPFKKQLKGSPPFFLMFR 108
Cdd:cd17100    2 VRCIVHFLDDTEQTFEVEKRDKGQVLLDKVFNHLELVEKDYFGLQFSDDSPAtdSMRWLDPLKPIRKQIKGGPPYYLNFR 81


                 ....*
gi 528504074 109 VRFFI 113
Cdd:cd17100   82 VKFYV 86
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 115-223 3.76e-31

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 118.14  E-value: 3.76e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  115 DPNSLQHEQTRHFYFLQIRKDICEGRLKCPLSSAVVLASYSVQSELGDYNPET-PTGYLSKTHFIPEQDQEFL------L 187
Cdd:pfam00373   2 LELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSShTSEYLSLESFLPKQLLRKMkskeleK 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 528504074  188 KVESLHPQHKGLSQSDAELCYLNTARTLDLYGVELH 223
Cdd:pfam00373  82 RVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_C pfam09380
FERM C-terminal PH-like domain;
227-312 9.90e-23

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 92.70  E-value: 9.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  227 DASNPAVWVGITSGGVALFCHLICSS-FFPWINIIKISFKRKRFFVHLRRKHGElghHVVSLSMPNSRACKNLWRSCVDH 305
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKILnLFPWREIRKISFKRKKFLIKLRDKSSE---ETLGFYTESSRACKYLWKLCVEQ 77


                  ....*..
gi 528504074  306 HTFYNRK 312
Cdd:pfam09380  78 HTFFRLR 84
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 441-526 2.21e-13

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 66.15  E-value: 2.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  441 LVRISPDQDGKFGFNVKGGVDQK-MPLAISHVNLASPAGRcvPPLMEGDQVLLINGRDISEHTHQQVVMFIKASreshSK 519
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKGGSDQGdPGIFVSEVLPGGAAEA--GGLKVGDRILSINGQDVENMTHEEAVLALKGS----GG 74


                  ....*..
gi 528504074  520 ELALLVR 526
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 ...
 441-529 1.43e-12

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: 63.94  E-value: 1.43e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074   441 LVRISPDQDGkFGFNVKGGVDQKMPLAISHVNLASPAGRCvpPLMEGDQVLLINGRDISEHTHQQVVMFIKASREShske 520
Cdd:smart00228   4 LVELEKGGGG-LGFSLVGGKDEGGGVVVSSVVPGSPAAKA--GLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGK---- 76


                   ....*....
gi 528504074   521 LALLVRRKG 529
Cdd:smart00228  77 VTLTVLRGG 85
 
Name Accession Description Interval E-value
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 561-833 0e+00

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: 562.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 561 EESMARLEKGLVTGTLLLHFEKLYRKKEGMLMSCAKQSENMDKNRYKDVLPYDITRVVLQEeGDDYINASHVKTEPAG-- 638
Cdd:cd14600    1 EESMAQLKKGLESGTVLIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQG-NEDYINASYVNMEIPSan 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 639 CVLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHPPEVRDYGYLQVCCHSEECNLAYVTRQLT 718
Cdd:cd14600   80 IVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREML 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 719 LTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMRQESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVY 798
Cdd:cd14600  160 LTNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVY 239

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 528504074 799 PLEVITLMREQRAMLVQTSCQFTFVCEAILRVYRE 833
Cdd:cd14600  240 PLDIVRKMRDQRAMMVQTSSQYKFVCEAILRVYEE 274
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 625-833 4.45e-120

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: 361.26  E-value: 4.45e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 625 DYINASHVKTE-P-AGCVLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHPPEVRDYGYLQVC 702
Cdd:cd14541    1 DYINANYVNMEiPgSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 703 CHSEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMRQESV-PLMVHCSAGIGRTGVL 781
Cdd:cd14541   81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVePTVVHCSAGIGRTGVL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528504074 782 ITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAILRVYRE 833
Cdd:cd14541  161 ITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRVYEE 212
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
579-829 1.05e-104

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 323.46  E-value: 1.05e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074   579 HFEKLYRKKEGML-MSCAKQSENMDKNRYKDVLPYDITRVVLQ---EEGDDYINASHVKTEPAGcvLQYIAAQGPLPHTC 654
Cdd:smart00194   5 EFEKLDRLKPDDEsCTVAAFPENRDKNRYKDVLPYDHTRVKLKpppGEGSDYINASYIDGPNGP--KAYIATQGPLPSTV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074   655 THFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWP-HPPEVRDYGYLQVCCHSEECNLAYVTRQLTLTNTQSGQQRSITHL 733
Cdd:smart00194  83 EDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPdEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVTHY 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074   734 QYVAWPDHGVPEDSSDFLDFVKSVR-SMRQESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAM 812
Cdd:smart00194 163 HYTNWPDHGVPESPESILDLIRAVRkSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPG 242

                          250
                   ....*....|....*..
gi 528504074   813 LVQTSCQFTFVCEAILR 829
Cdd:smart00194 243 MVQTEEQYIFLYRAILE 259
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 625-833 3.84e-103

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: 317.66  E-value: 3.84e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 625 DYINASHVKTEPAGCVL--QYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHPPEVRDYGYLQVC 702
Cdd:cd14601    1 DYINANYINMEIPSSSIinRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 703 CHSEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMRQ-ESVPLMVHCSAGIGRTGVL 781
Cdd:cd14601   81 CHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAgKDEPVVVHCSAGIGRTGVL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528504074 782 ITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAILRVYRE 833
Cdd:cd14601  161 ITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYEE 212
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
600-828 1.73e-95

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 298.39  E-value: 1.73e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  600 NMDKNRYKDVLPYDITRVVLQEEGD--DYINASHVKTEPAGcvLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTE 677
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPGpsDYINASYIDGYKKP--KKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  678 RGRTKCHQYWP-HPPEVRDYGYLQVCCHSEECNLA-YVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVK 755
Cdd:pfam00102  79 KGREKCAQYWPeEEGESLEYGDFTVTLKKEKEDEKdYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528504074  756 SVRSMRQE--SVPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAIL 828
Cdd:pfam00102 159 KVRKSSLDgrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 626-825 8.22e-79

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 252.98  E-value: 8.22e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 626 YINASHVKTEPAGCvlQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHPPEV-RDYGYLQVCCH 704
Cdd:cd00047    1 YINASYIDGYRGPK--EYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKpLEYGDITVTLV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 705 SEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVR-SMRQESVPLMVHCSAGIGRTGVLIT 783
Cdd:cd00047   79 SEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRkEARKPNGPIVVHCSAGVGRTGTFIA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 528504074 784 METAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCE 825
Cdd:cd00047  159 IDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 576-822 3.92e-71

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: 234.95  E-value: 3.92e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 576 LLLHFEKLYRKKEGMLMSCAKQSENMDKNRYKDVLPYDITRVVL----QEEGDDYINASHV---KTEPAgcvlqYIAAQG 648
Cdd:cd14543    5 IYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLpkrnGDERTDYINANFMdgyKQKNA-----YIATQG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 649 PLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHPPEVR-DYGYLQVCCHSEECNLAYVTRQLTLTNTQSGQQ 727
Cdd:cd14543   80 PLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSlRYGDLTVTNLSVENKEHYKKTTLEIHNTETDES 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 728 RSITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMRQESV--------------PLMVHCSAGIGRTGVLITMETAMTLMEK 793
Cdd:cd14543  160 RQVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVkamgdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQLED 239

                        250       260
                 ....*....|....*....|....*....
gi 528504074 794 EKPVYPLEVITLMREQRAMLVQTSCQFTF 822
Cdd:cd14543  240 VGTLNVMQTVRRMRTQRAFSIQTPDQYYF 268
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 626-830 4.18e-71

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: 233.12  E-value: 4.18e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 626 YINASHVKTEPAGCVLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWP-----HPPEVrdYGYLQ 700
Cdd:cd14540    1 YINASHITATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPtlggeHDALT--FGEYK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 701 VCCHSEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMRQESV----------PLMVH 770
Cdd:cd14540   79 VSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNqdvaghnrnpPTLVH 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 771 CSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAILRV 830
Cdd:cd14540  159 CSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQY 218
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 567-829 5.74e-69

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: 229.88  E-value: 5.74e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 567 LEKGLVTGTLLLHFEKLYRKKEGMLMSCAKQSENMDKNRYKDVLPYDITRVVL---QEEGDDYINASHVKTEPAGCVLQY 643
Cdd:cd14599    5 LERKLEEGMVFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELvptKENNTGYINASHIKVTVGGEEWHY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 644 IAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWP-----HPPEVrdYGYLQVCCHSEECNLAYVTRQLT 718
Cdd:cd14599   85 IATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPklgskHSSAT--YGKFKVTTKFRTDSGCYATTGLK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 719 LTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMRQES-----------VPLMVHCSAGIGRTGVLITMETA 787
Cdd:cd14599  163 VKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTnsmldstkncnPPIVVHCSAGVGRTGVVILTELM 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 528504074 788 MTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAILR 829
Cdd:cd14599  243 IGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 600-828 1.10e-68

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: 227.28  E-value: 1.10e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 600 NMDKNRYKDVLPYDITRVVLQE----EGDDYINASHVKtepaGCVLQ--YIAAQGPLPHTCTHFWRSVWEQDVNVIIMLT 673
Cdd:cd14553    3 NKPKNRYANVIAYDHSRVILQPiegvPGSDYINANYCD----GYRKQnaYIATQGPLPETFGDFWRMVWEQRSATIVMMT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 674 TLTERGRTKCHQYWP-HPPEVrdYGYLQVCChSEECNLAYVT-RQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFL 751
Cdd:cd14553   79 KLEERSRVKCDQYWPtRGTET--YGLIQVTL-LDTVELATYTvRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFL 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528504074 752 DFVKSVRSMRQ-ESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAIL 828
Cdd:cd14553  156 AFLRRVKACNPpDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALL 233
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 605-823 9.93e-68

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: 224.16  E-value: 9.93e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 605 RYKDVLPYDITRVVLQ----EEGDDYINASHVktePA-GCVLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERG 679
Cdd:cd14548    1 RYTNILPYDHSRVKLIpineEEGSDYINANYI---PGyNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 680 RTKCHQYWPHPPEVRDYGYLQVCCHSEECNLAYVTRQLTLTNTQsgQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVR- 758
Cdd:cd14548   78 RVKCDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERGD--EVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRd 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528504074 759 SMRQESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFV 823
Cdd:cd14548  156 YIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFL 220
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 626-830 1.33e-65

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: 217.63  E-value: 1.33e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 626 YINASHVKTEPAGCVLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHPPEVRD--YGYLQVCC 703
Cdd:cd14538    1 YINASHIRIPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLicGGRLEVSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 704 HSEEcNLAYVT-RQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMRQeSVPLMVHCSAGIGRTGVLI 782
Cdd:cd14538   81 EKYQ-SLQDFViRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHN-SGPIVVHCSAGIGRTGVLI 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 528504074 783 TMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAILRV 830
Cdd:cd14538  159 TIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 584-831 2.54e-65

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: 219.31  E-value: 2.54e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 584 YRKKEGMLMSCAKQSENMDKNRYKDVLPYDITRVVL----QEEGDDYINASHVKtepaGCV--LQYIAAQGPLPHTCTHF 657
Cdd:cd14603   14 FKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILsllqEEGHSDYINANFIK----GVDgsRAYIATQGPLSHTVLDF 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 658 WRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHPPEVRDYGYLQVC-CHSEECNLAYVTRQLTLTNTQsgQQRSITHLQYV 736
Cdd:cd14603   90 WRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPLQTGPFTITlVKEKRLNEEVILRTLKVTFQK--ESRSVSHFQYM 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 737 AWPDHGVPEDSSDFLDFVKSVRSMRQES-VPLMVHCSAGIGRTGVLITMETAMTLMEKEKpVYP----LEVITLMREQRA 811
Cdd:cd14603  168 AWPDHGIPDSPDCMLAMIELARRLQGSGpEPLCVHCSAGCGRTGVICTVDYVRQLLLTQR-IPPdfsiFDVVLEMRKQRP 246

                        250       260
                 ....*....|....*....|
gi 528504074 812 MLVQTSCQFTFVCEAILRVY 831
Cdd:cd14603  247 AAVQTEEQYEFLYHTVAQMF 266
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 603-822 9.44e-65

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: 216.49  E-value: 9.44e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 603 KNRYKDVLPYDITRVV--LQEEGDDYINASHVKTEPAGcvLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGR 680
Cdd:cd14545    1 LNRYRDRDPYDHDRSRvkLKQGDNDYINASLVEVEEAK--RSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 681 TKCHQYWPH---PPEVRDYGYLQVCCHSEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSV 757
Cdd:cd14545   79 IKCAQYWPQgegNAMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKV 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 758 R---SMRQESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKP--VYPLEVITLMREQRAMLVQTSCQFTF 822
Cdd:cd14545  159 ResgSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 595-828 1.54e-63

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: 214.89  E-value: 1.54e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 595 AKQSENMDKNRYKDVLPYDITRVVLQEEGDDYINASHVKTEPAGcvLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTT 674
Cdd:cd14608   20 AKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQ--RSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNR 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 675 LTERGRTKCHQYWPHPPE---VRDYGYLQVCCHSEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFL 751
Cdd:cd14608   98 VMEKGSLKCAQYWPQKEEkemIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFL 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 752 DFVKSVR---SMRQESVPLMVHCSAGIGRTGVLITMETAMTLMEKEK---PVYPLEVITLMREQRAMLVQTSCQFTFVCE 825
Cdd:cd14608  178 NFLFKVResgSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKdpsSVDIKKVLLEMRKFRMGLIQTADQLRFSYL 257


                 ...
gi 528504074 826 AIL 828
Cdd:cd14608  258 AVI 260
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 595-827 5.47e-63

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: 212.52  E-value: 5.47e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 595 AKQSENMDKNRYKDVLPYDITRVVLQEEGDDYINASHVKTEPAGcvLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTT 674
Cdd:cd14607   19 AKYPENRNRNRYRDVSPYDHSRVKLQNTENDYINASLVVIEEAQ--RSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 675 LTERGRTKCHQYWPHPPE----VRDYGYlQVCCHSEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDF 750
Cdd:cd14607   97 IVEKDSVKCAQYWPTDEEevlsFKETGF-SVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWPDFGVPESPASF 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 751 LDFVKSVR---SMRQESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKP--VYPLEVITLMREQRAMLVQTSCQFTFVCE 825
Cdd:cd14607  176 LNFLFKVResgSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDPdsVDIKQVLLDMRKYRMGLIQTPDQLRFSYM 255


                 ..
gi 528504074 826 AI 827
Cdd:cd14607  256 AV 257
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 599-830 1.75e-62

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: 210.46  E-value: 1.75e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 599 ENMDKNRYKDVLPYDITRVVLQEEGDdYINASHVKTEPAGCVLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTER 678
Cdd:cd14597    2 ENRKKNRYKNILPYDTTRVPLGDEGG-YINASFIKMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 679 GRTKCHQYWPHPPEVRDY--GYLQVCCHSEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKS 756
Cdd:cd14597   81 GKIKCQRYWPEILGKTTMvdNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLTFISY 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528504074 757 VRSMrQESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAILRV 830
Cdd:cd14597  161 MRHI-HKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVILYV 233
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 626-823 2.42e-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: 209.03  E-value: 2.42e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 626 YINASHVKTEPAGcVLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHPPEVRDYGYLQVCC-- 703
Cdd:cd18533    1 YINASYITLPGTS-SKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELvs 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 704 HSEECNLAYVTRQLTLTNTQsGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMRQ---ESVPLMVHCSAGIGRTGV 780
Cdd:cd18533   80 EEENDDGGFIVREFELSKED-GKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDsasLDPPIIVHCSAGVGRTGT 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 528504074 781 LITMETAMTLMEKEK-----------PVYplEVITLMREQRAMLVQTSCQFTFV 823
Cdd:cd18533  159 FIALDSLLDELKRGLsdsqdledsedPVY--EIVNQLRKQRMSMVQTLRQYIFL 210
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 600-827 2.47e-62

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: 210.40  E-value: 2.47e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 600 NMDKNRYKDVLPYDITRVVLQE-----EGDDYINASHVKTEPAG-----CVLQYIAAQGPLPHTCTHFWRSVWEQDVNVI 669
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDrdpnvPGSDYINANYIRNENEGpttdeNAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 670 IMLTTLTERGRTKCHQYWPHPPEVRDYGYLQVCCHSEECNLAYVTRQLTLTNTQSGQ-QRSITHLQYVAWPDHGVPEDSS 748
Cdd:cd14544   81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDpIREIWHYQYLSWPDHGVPSDPG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 749 DFLDFVKSVRSmRQESV----PLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEV---ITLMREQRAMLVQTSCQFT 821
Cdd:cd14544  161 GVLNFLEDVNQ-RQESLphagPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIqktIQMVRSQRSGMVQTEAQYK 239


                 ....*.
gi 528504074 822 FVCEAI 827
Cdd:cd14544  240 FIYVAV 245
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 604-829 1.07e-60

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: 205.51  E-value: 1.07e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 604 NRYKDVLPYDITRVVL----QEEGDDYINASHVktePA-GCVLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTER 678
Cdd:cd14619    1 NRFRNVLPYDWSRVPLkpihEEPGSDYINANYM---PGyWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 679 GRTKCHQYWPHPPEVRDYGYLQVCCHSEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVR 758
Cdd:cd14619   78 GRVKCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528504074 759 S---MRQESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAILR 829
Cdd:cd14619  158 QwldQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 600-828 1.78e-60

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: 205.07  E-value: 1.78e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 600 NMDKNRYKDVLPYDITRVVLQE----EGDDYINASHV---KTEPAgcvlqYIAAQGPLPHTCTHFWRSVWEQDVNVIIML 672
Cdd:cd14554    6 NKFKNRLVNILPYESTRVCLQPirgvEGSDYINASFIdgyRQRGA-----YIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 673 TTLTERGRTKCHQYWPHPPEVRdYGYLQVCCHSEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLD 752
Cdd:cd14554   81 TKLREMGREKCHQYWPAERSAR-YQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFID 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528504074 753 FVKSVRSMRQ---ESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAIL 828
Cdd:cd14554  160 FIGQVHKTKEqfgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 626-823 5.25e-60

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: 202.20  E-value: 5.25e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 626 YINASHVK--TEPAGcvlqYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHpPEVRDYGYLQVCC 703
Cdd:cd14549    1 YINANYVDgyNKARA----YIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPK-EGTETYGNIQVTL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 704 HSEECNLAYVTRQLTLTNTQ------SGQQRSITHLQYVAWPDHGVPEDSSDFLDFV-KSVRSMRQESVPLMVHCSAGIG 776
Cdd:cd14549   76 LSTEVLATYTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVrKSSAANPPGAGPIVVHCSAGVG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 528504074 777 RTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFV 823
Cdd:cd14549  156 RTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFI 202
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 604-823 5.52e-58

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: 197.73  E-value: 5.52e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 604 NRYKDVLPYDITRVVLQEEG---DDYINASHV-----KTEpagcvlqYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTL 675
Cdd:cd14615    1 NRYNNVLPYDISRVKLSVQShstDDYINANYMpgynsKKE-------FIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKC 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 676 TERGRTKCHQYWPhPPEVRDYGYLQVCCHSEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVK 755
Cdd:cd14615   74 VEQGRTKCEEYWP-SKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRH 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528504074 756 SVRS-MRQESV--PLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFV 823
Cdd:cd14615  153 LVREyMKQNPPnsPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 600-828 2.26e-56

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: 195.25  E-value: 2.26e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 600 NMDKNRYKDVLPYDITRVVLQE----EGDDYINASHV---KTEPAgcvlqYIAAQGPLPHTCTHFWRSVWEQDVNVIIML 672
Cdd:cd14626   41 NKPKNRYANVIAYDHSRVILTSvdgvPGSDYINANYIdgyRKQNA-----YIATQGPLPETLSDFWRMVWEQRTATIVMM 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 673 TTLTERGRTKCHQYWPhPPEVRDYGYLQVCCHSEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLD 752
Cdd:cd14626  116 TRLEEKSRVKCDQYWP-IRGTETYGMIQVTLLDTVELATYSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILA 194

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528504074 753 FVKSVRSMRQ-ESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAIL 828
Cdd:cd14626  195 FLRRVKACNPpDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALL 271
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 604-823 2.32e-56

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: 193.00  E-value: 2.32e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 604 NRYKDVLPYDITRVVLQEEGDD----YINASHVKTePAGCVLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERg 679
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDDplssYINANYIRG-YDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 680 RTKCHQYWPHPpEVRDYGYLQVCCHSEECNLAYVTRQLTLTNtqSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVRS 759
Cdd:cd14547   79 KEKCAQYWPEE-ENETYGDFEVTVQSVKETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEE 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528504074 760 MRQESV---PLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFV 823
Cdd:cd14547  156 ARQTEPhrgPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFV 222
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 583-829 5.11e-56

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: 193.94  E-value: 5.11e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 583 LYRKKEGMlmscakQSENMDKNRYKDVLPYDITRVVLQEE-----GDDYINASHVKTE---PAGCVLQYIAAQGPLPHTC 654
Cdd:cd14606    7 LHQRLEGQ------RPENKSKNRYKNILPFDHSRVILQGRdsnipGSDYINANYVKNQllgPDENAKTYIASQGCLEATV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 655 THFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHPPEVRDYGYLQVCCHSEECNLAYVTRQLTLTNTQSGQQ-RSITHL 733
Cdd:cd14606   81 NDFWQMAWQENSRVIVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELiREIWHY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 734 QYVAWPDHGVPEDSSDFLDFVKSVrSMRQESV----PLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEV---ITLM 806
Cdd:cd14606  161 QYLSWPDHGVPSEPGGVLSFLDQI-NQRQESLphagPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIqktIQMV 239

                        250       260
                 ....*....|....*....|...
gi 528504074 807 REQRAMLVQTSCQFTFVCEAILR 829
Cdd:cd14606  240 RAQRSGMVQTEAQYKFIYVAIAQ 262
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 599-827 5.51e-56

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 193.31  E-value: 5.51e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 599 ENMDKNRYKDVLPYDITRVVLQ-----EEGDDYINAS------HVKTEPAGCVLQYIAAQGPLPHTCTHFWRSVWEQDVN 667
Cdd:cd14605    1 ENKNKNRYKNILPFDHTRVVLHdgdpnEPVSDYINANiimpefETKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 668 VIIMLTTLTERGRTKCHQYWPHPPEVRDYGYLQVCCHSEECNLAYVTRQLTLTNT-QSGQQRSITHLQYVAWPDHGVPED 746
Cdd:cd14605   81 VIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLSKVgQGNTERTVWQYHFRTWPDHGVPSD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 747 SSDFLDFVKSVRsMRQESV----PLMVHCSAGIGRTGVLITMETAMTLMeKEKPV-----YPlEVITLMREQRAMLVQTS 817
Cdd:cd14605  161 PGGVLDFLEEVH-HKQESImdagPVVVHCSAGIGRTGTFIVIDILIDII-REKGVdcdidVP-KTIQMVRSQRSGMVQTE 237

                        250
                 ....*....|
gi 528504074 818 CQFTFVCEAI 827
Cdd:cd14605  238 AQYRFIYMAV 247
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 626-832 2.41e-55

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: 190.19  E-value: 2.41e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 626 YINASHVKTEPAGCVLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHPPEVRD---YGYLQVC 702
Cdd:cd14598    1 YINASHIKVTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHNtvtYGRFKIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 703 CHSEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMRQES----------VPLMVHCS 772
Cdd:cd14598   81 TRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTnstidpkspnPPVLVHCS 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 773 AGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAILRVYR 832
Cdd:cd14598  161 AGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 562-828 2.49e-55

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: 192.64  E-value: 2.49e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 562 ESMARLEKGLVTGTLLLHFEKLYRKK-EGMLMSCAKQSENMDKNRYKDVLPYDITRVVLQE----EGDDYINASHV---K 633
Cdd:cd14627   14 QKLAQVEVGEHVTGMELEFKRLANSKaHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPirgvEGSDYINASFIdgyR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 634 TEPAgcvlqYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHPPEVRdYGYLQVCCHSEECNLAYV 713
Cdd:cd14627   94 QQKA-----YIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSAR-YQYFVVDPMAEYNMPQYI 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 714 TRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMRQ---ESVPLMVHCSAGIGRTGVLITMETAMTL 790
Cdd:cd14627  168 LREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEqfgQDGPISVHCSAGVGRTGVFITLSIVLER 247

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 528504074 791 MEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAIL 828
Cdd:cd14627  248 MRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAAL 285
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 562-828 6.62e-55

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: 191.48  E-value: 6.62e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 562 ESMARLEKGLVTGTLLLHFEKLYRKK-EGMLMSCAKQSENMDKNRYKDVLPYDITRVVLQE----EGDDYINASHV---K 633
Cdd:cd14628   13 QKLTQIETGENVTGMELEFKRLASSKaHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPirgvEGSDYINASFIdgyR 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 634 TEPAgcvlqYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHPPEVRdYGYLQVCCHSEECNLAYV 713
Cdd:cd14628   93 QQKA-----YIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSAR-YQYFVVDPMAEYNMPQYI 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 714 TRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMRQ---ESVPLMVHCSAGIGRTGVLITMETAMTL 790
Cdd:cd14628  167 LREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEqfgQDGPISVHCSAGVGRTGVFITLSIVLER 246

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 528504074 791 MEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAIL 828
Cdd:cd14628  247 MRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAAL 284
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 604-828 6.64e-55

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: 189.38  E-value: 6.64e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 604 NRYKDVLPYDITRVVL----QEEGDDYINASHVK--TEPAgcvlQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTE 677
Cdd:cd14618    1 NRYPHVLPYDHSRVRLsqlgGEPHSDYINANFIPgyTSPQ----EFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGME 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 678 RGRTKCHQYWPHPPEVRDYGYLQVCCHSEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSV 757
Cdd:cd14618   77 NGRVLCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELV 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528504074 758 R---SMRQESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAIL 828
Cdd:cd14618  157 RehvQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 33-223 7.52e-55

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: 188.27  E-value: 7.52e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074    33 CLVLFPDGTTQNFTVNKHDAGHLLFDLACEHLNIVEKQYFSMQISEDTSSSPRWLDPNKPFKKQLKGSPPFFLMFRVRFF 112
Cdd:smart00295   2 LKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRHWLDPAKTLLDQDVKSEPLTLYFRVKFY 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074   113 ISDPNSLQHEQTRH-FYFLQIRKDICEGRLKCPLSSAVVLASYSVQSELGDYNPETPT--GYLSKTHFIPEQ------DQ 183
Cdd:smart00295  82 PPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDlrGELSLKRFLPKQlldsrkLK 161

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 528504074   184 EFLLKVESLHPQHKGLSQSDAELCYLNTARTLDLYGVELH 223
Cdd:smart00295 162 EWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 604-823 1.64e-53

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: 185.51  E-value: 1.64e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 604 NRYKDVLPYDITRVVLQEEGD----DYINASHVktepAGCVL--QYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTE 677
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDdpcsDYINASYI----PGNNFrrEYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 678 RGRTKCHQYWPHPPEVRDYGYLQVCCHSEECNLAYVTRQLTLTN-TQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKS 756
Cdd:cd14617   77 KGRVKCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKICSeEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRT 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 757 VR---SMRQESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFV 823
Cdd:cd14617  157 VRdyiNRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYL 226
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 600-828 2.87e-53

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: 186.84  E-value: 2.87e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 600 NMDKNRYKDVLPYDITRVVLQE----EGDDYINASHV---KTEPAgcvlqYIAAQGPLPHTCTHFWRSVWEQDVNVIIML 672
Cdd:cd14625   47 NKPKNRYANVIAYDHSRVILQPiegiMGSDYINANYIdgyRKQNA-----YIATQGPLPETFGDFWRMVWEQRSATVVMM 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 673 TTLTERGRTKCHQYWPHpPEVRDYGYLQVCCHSEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLD 752
Cdd:cd14625  122 TKLEEKSRIKCDQYWPS-RGTETYGMIQVTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLA 200

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528504074 753 FVKSVRSMR-QESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAIL 828
Cdd:cd14625  201 FLRRVKTCNpPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALL 277
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 600-828 4.22e-53

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: 186.47  E-value: 4.22e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 600 NMDKNRYKDVLPYDITRVVLQE----EGDDYINASHV---KTEPAgcvlqYIAAQGPLPHTCTHFWRSVWEQDVNVIIML 672
Cdd:cd14629   53 NKFKNRLVNIMPYELTRVCLQPirgvEGSDYINASFIdgyRQQKA-----YIATQGPLAETTEDFWRMLWEHNSTIVVML 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 673 TTLTERGRTKCHQYWPHPPEVRdYGYLQVCCHSEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLD 752
Cdd:cd14629  128 TKLREMGREKCHQYWPAERSAR-YQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFID 206

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528504074 753 FVKSVRSMRQ---ESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAIL 828
Cdd:cd14629  207 FIGQVHKTKEqfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAAL 285
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 581-835 1.16e-52

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 185.52  E-value: 1.16e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 581 EKLYRKKEGmlmscaKQSENMDKNRYKDVLPYDITRVVL----QEEGDDYINASHVK--TEPAGcvlqYIAAQGPLPHTC 654
Cdd:cd14604   44 EKIYPTATG------EKEENVKKNRYKDILPFDHSRVKLtlktSSQDSDYINANFIKgvYGPKA----YIATQGPLANTV 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 655 THFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWP-HPPEVRDYGYLQVCCHSEECNLAYVTRQLTLTNTQsgQQRSITHL 733
Cdd:cd14604  114 IDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPlYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQN--ETRRLYQF 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 734 QYVAWPDHGVPEDSSDFLDFVKSVRSMRQ-ESVPLMVHCSAGIGRTGVLITMETAMTLME-----KEKPVYPLevITLMR 807
Cdd:cd14604  192 HYVNWPDHDVPSSFDSILDMISLMRKYQEhEDVPICIHCSAGCGRTGAICAIDYTWNLLKagkipEEFNVFNL--IQEMR 269

                        250       260
                 ....*....|....*....|....*...
gi 528504074 808 EQRAMLVQTSCQFTFVCEAILRVYREKV 835
Cdd:cd14604  270 TQRHSAVQTKEQYELVHRAIAQLFEKQL 297
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 626-832 3.45e-52

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: 181.10  E-value: 3.45e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 626 YINASHVKTEPAGCVLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHPPEV-RDYGYLQVccH 704
Cdd:cd14596    1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEpMELENYQL--R 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 705 SEECN-LAYVT-RQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMRQESvPLMVHCSAGIGRTGVLI 782
Cdd:cd14596   79 LENYQaLQYFIiRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTG-PIVVHCSAGIGRAGVLI 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 528504074 783 TMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAILRVYR 832
Cdd:cd14596  158 CVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 595-827 3.08e-51

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: 181.02  E-value: 3.08e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 595 AKQSENMDKNRYKDVLPYDITRVVLQEEGD----DYINAS----HVKTEPAgcvlqYIAAQGPLPHTCTHFWRSVWEQDV 666
Cdd:cd14610   39 AQREENVQKNRSLAVLPYDHSRIILKAENShshsDYINASpimdHDPRNPA-----YIATQGPLPATVADFWQMVWESGC 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 667 NVIIMLTTLTERGRTKCHQYWPHppEVRD-YGYLQVCCHSEE--CNlAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGV 743
Cdd:cd14610  114 VVIVMLTPLAENGVKQCYHYWPD--EGSNlYHIYEVNLVSEHiwCE-DFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGV 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 744 PEDSSDFLDFVKSV-RSMRQESVPLMVHCSAGIGRTGVLITMETAMTLMEK-EKPVYPLEVITLMREQRAMLVQTSCQFT 821
Cdd:cd14610  191 PASTRSLLDFRRKVnKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKgAKEIDIAATLEHLRDQRPGMVQTKEQFE 270


                 ....*.
gi 528504074 822 FVCEAI 827
Cdd:cd14610  271 FALTAV 276
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 600-823 5.89e-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: 178.93  E-value: 5.89e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 600 NMDKNRYKDVLPYDITRVVL----QEEGDDYINASHVKTEPAgcVLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTL 675
Cdd:cd14614   12 NRCKNRYTNILPYDFSRVKLvsmhEEEGSDYINANYIPGYNS--PQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQC 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 676 TERGRTKCHQYWPHPPEVRDYGYLQVCCHSEECNLAYVTRQLTLTNTQSGQQrsITHLQYVAWPDHGVP--EDSSDFLDF 753
Cdd:cd14614   90 NEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQD--VMHFNYTAWPDHGVPtaNAAESILQF 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528504074 754 VKSVRSMRQESV-PLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFV 823
Cdd:cd14614  168 VQMVRQQAVKSKgPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFI 238
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 603-831 6.86e-51

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus.


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 178.50  E-value: 6.86e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 603 KNRYKDVLPYDITRVVLQ----EEGDDYINASHVKT--EPAGcvlqYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLT 676
Cdd:cd14602    1 KNRYKDILPYDHSRVELSlitsDEDSDYINANFIKGvyGPRA----YIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 677 ERGRTKCHQYWPHPPEVR-DYGYLQVCCHSEECNLAYVTRqlTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVK 755
Cdd:cd14602   77 EMGKKKCERYWAEPGEMQlEFGPFSVTCEAEKRKSDYIIR--TLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIW 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 756 SVRSMRQ-ESVPLMVHCSAGIGRTGVLITME-TAMTLMEKEKP----VYPLevITLMREQRAMLVQTSCQFTFVCEAILR 829
Cdd:cd14602  155 DVRCYQEdDSVPICIHCSAGCGRTGVICAIDyTWMLLKDGIIPenfsVFSL--IQEMRTQRPSLVQTKEQYELVYNAVIE 232


                 ..
gi 528504074 830 VY 831
Cdd:cd14602  233 LF 234
PDZ_PTPN3-4-like cd06706
PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein ...
 437-526 1.04e-50

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: 172.50  E-value: 1.04e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 437 GDLLLVRISPDQDGKFGFNVKGGVDQKMPLAISHVNLASPAGRCVPPLMEGDQVLLINGRDISEHTHQQVVMFIKASRES 516
Cdd:cd06706    1 DGLVLIRMKPDENGRFGFNVKGGVDQKMPVIVSRVAPGTPADLCIPRLNEGDQVLLINGRDISEHTHDQVVMFIKASRER 80

                         90
                 ....*....|
gi 528504074 517 HSKELALLVR 526
Cdd:cd06706   81 HSGELVLLVR 90
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 580-828 1.94e-50

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: 178.69  E-value: 1.94e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 580 FEKLYRKKEGMLMSC--AKQSENMDKNRYKDVLPYDITRVVLQ------EEGDDYINASHVktEPAGCVLQYIAAQGPLP 651
Cdd:cd17667    5 FEEVQRCTADMNITAehSNHPDNKHKNRYINILAYDHSRVKLRplpgkdSKHSDYINANYV--DGYNKAKAYIATQGPLK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 652 HTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPhPPEVRDYGYLQVCCHSEECNLAYVTRQLTLTNTQ-------- 723
Cdd:cd17667   83 STFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWP-TENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKvkkgqkgn 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 724 -SGQQ--RSITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMRQ-ESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYP 799
Cdd:cd17667  162 pKGRQneRTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTpEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNV 241

                        250       260
                 ....*....|....*....|....*....
gi 528504074 800 LEVITLMREQRAMLVQTSCQFTFVCEAIL 828
Cdd:cd17667  242 LGFLKHIRTQRNYLVQTEEQYIFIHDALL 270
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 600-828 2.71e-50

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: 178.39  E-value: 2.71e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 600 NMDKNRYKDVLPYDITRVVLQE----EGDDYINASHV---KTEPAgcvlqYIAAQGPLPHTCTHFWRSVWEQDVNVIIML 672
Cdd:cd14624   47 NKPKNRYANVIAYDHSRVLLSAiegiPGSDYINANYIdgyRKQNA-----YIATQGALPETFGDFWRMIWEQRSATVVMM 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 673 TTLTERGRTKCHQYWPhPPEVRDYGYLQVCCHSEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLD 752
Cdd:cd14624  122 TKLEERSRVKCDQYWP-SRGTETYGLIQVTLLDTVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLA 200

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528504074 753 FVKSVRSMR-QESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAIL 828
Cdd:cd14624  201 FLRRVKTCNpPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALL 277
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 606-828 1.68e-49

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: 174.36  E-value: 1.68e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 606 YKDVLPYDITRVVLQE----EGDDYINASHVK--TEPAgcvlQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERG 679
Cdd:cd14620    1 YPNILPYDHSRVILSQldgiPCSDYINASYIDgyKEKN----KFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 680 RTKCHQYWPHpPEVRDYGYLQVCCHSEECNLAYVTRQLTLTNTQSGQQRS---ITHLQYVAWPDHGVPEDSSDFLDFVKS 756
Cdd:cd14620   77 EEKCYQYWPD-QGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCKAprlVTQLHFTSWPDFGVPFTPIGMLKFLKK 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528504074 757 VRSMR-QESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAIL 828
Cdd:cd14620  156 VKSVNpVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 599-828 1.85e-49

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: 174.44  E-value: 1.85e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 599 ENMDKNRYKDVLPYDITRVVLQE-EGD---DYINASHVKT--EPAgcvlQYIAAQGPLPHTCTHFWRSVWEQDVNVIIML 672
Cdd:cd14630    2 ENRNKNRYGNIISYDHSRVRLQLlDGDphsDYINANYIDGyhRPR----HYIATQGPMQETVKDFWRMIWQENSASVVMV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 673 TTLTERGRTKCHQYWPHPPEVrdYGYLQVCCHSEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLD 752
Cdd:cd14630   78 TNLVEVGRVKCVRYWPDDTEV--YGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLG 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528504074 753 FVKSVRSMR-QESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAIL 828
Cdd:cd14630  156 FVRQVKFLNpPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAIL 232
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 626-823 4.14e-49

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: 172.22  E-value: 4.14e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 626 YINASHVKTePAGCvLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHPPE-VRDYGYLQVCCH 704
Cdd:cd14542    1 YINANFIKG-VSGS-KAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEeQLQFGPFKISLE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 705 SEE-CNLAYVTRQLTLTNTQsgQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMRQ-ESVPLMVHCSAGIGRTGVLI 782
Cdd:cd14542   79 KEKrVGPDFLIRTLKVTFQK--ESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGsEDVPICVHCSAGCGRTGTIC 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 528504074 783 TMETAMTLMEKEK--PVYPL-EVITLMREQRAMLVQTSCQFTFV 823
Cdd:cd14542  157 AIDYVWNLLKTGKipEEFSLfDLVREMRKQRPAMVQTKEQYELV 200
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 593-827 6.41e-49

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: 174.46  E-value: 6.41e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 593 SCAKQSENMDKNRYKDVLPYDITRVVLQEEGD----DYINAS----HVKTEPAgcvlqYIAAQGPLPHTCTHFWRSVWEQ 664
Cdd:cd14609   35 STAQGEANVKKNRNPDFVPYDHARIKLKAESNpsrsDYINASpiieHDPRMPA-----YIATQGPLSHTIADFWQMVWEN 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 665 DVNVIIMLTTLTERGRTKCHQYWPhppevrDYGylQVCCHSEECNLA--------YVTRQLTLTNTQSGQQRSITHLQYV 736
Cdd:cd14609  110 GCTVIVMLTPLVEDGVKQCDRYWP------DEG--SSLYHIYEVNLVsehiwcedFLVRSFYLKNVQTQETRTLTQFHFL 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 737 AWPDHGVPEDSSDFLDFVKSV-RSMRQESVPLMVHCSAGIGRTGVLITMETAMTLMEKE-KPVYPLEVITLMREQRAMLV 814
Cdd:cd14609  182 SWPAEGIPSSTRPLLDFRRKVnKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHVRDQRPGMV 261

                        250
                 ....*....|...
gi 528504074 815 QTSCQFTFVCEAI 827
Cdd:cd14609  262 RTKDQFEFALTAV 274
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 626-823 9.43e-49

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: 171.16  E-value: 9.43e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 626 YINASHVK--TEPagcvLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHPPE-VRDYGYLQVC 702
Cdd:cd14557    1 YINASYIDgfKEP----RKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEgSRAFGDVVVK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 703 CHSEECNLAYVTRQLTLTNT-QSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMRQE-SVPLMVHCSAGIGRTGV 780
Cdd:cd14557   77 INEEKICPDYIIRKLNINNKkEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFfSGPIVVHCSAGVGRTGT 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 528504074 781 LITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFV 823
Cdd:cd14557  157 YIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILI 199
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 582-831 7.67e-48

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: 172.13  E-value: 7.67e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 582 KLYRKKEGMLMSC--------AKQSENMDKNRYKDVLPYDITRVVLQE-EG---DDYINASHVKTEPAGCvlQYIAAQGP 649
Cdd:cd14621   26 KLFREEFNALPACpiqatceaASKEENKEKNRYVNILPYDHSRVHLTPvEGvpdSDYINASFINGYQEKN--KFIAAQGP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 650 LPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHpPEVRDYGYLQVCCHSEECNLAYVTRQLTLTN----TQSG 725
Cdd:cd14621  104 KEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPD-QGCWTYGNIRVSVEDVTVLVDYTVRKFCIQQvgdvTNKK 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 726 QQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMR-QESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVIT 804
Cdd:cd14621  183 PQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNpQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVS 262

                        250       260
                 ....*....|....*....|....*..
gi 528504074 805 LMREQRAMLVQTSCQFTFVCEAILRVY 831
Cdd:cd14621  263 RIRAQRCQMVQTDMQYVFIYQALLEHY 289
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 626-828 1.07e-47

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: 168.62  E-value: 1.07e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 626 YINASHVK--TEPAGcvlqYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHPPEvRDYGYLQVCC 703
Cdd:cd17668    1 YINANYVDgyNKPKA----YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGS-EEYGNFLVTQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 704 HSEECNLAYVTRQLTLTNT------QSG--QQRSITHLQYVAWPDHGVPEDSSDFLDFV-KSVRSMRQESVPLMVHCSAG 774
Cdd:cd17668   76 KSVQVLAYYTVRNFTLRNTkikkgsQKGrpSGRVVTQYHYTQWPDMGVPEYTLPVLTFVrKASYAKRHAVGPVVVHCSAG 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 528504074 775 IGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAIL 828
Cdd:cd17668  156 VGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 603-823 4.25e-47

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


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 168.09  E-value: 4.25e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 603 KNRYKDVLPYDITRVVL-----QEEGDDYINASHVKTEpAGCVLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTE 677
Cdd:cd14612   18 KDRYKTILPNPQSRVCLrragsQEEEGSYINANYIRGY-DGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 678 RgRTKCHQYWPHPPEVrdYGYLQVCCHS-EECNlAYVTRQLTLtnTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKS 756
Cdd:cd14612   97 K-KEKCVHYWPEKEGT--YGRFEIRVQDmKECD-GYTIRDLTI--QLEEESRSVKHYWFSSWPDHQTPESAGPLLRLVAE 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 757 VRSMRQESV---PLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFV 823
Cdd:cd14612  171 VEESRQTAAspgPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 604-825 7.40e-47

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type tyrosine-protein phosphatase Q (PTPRQ or R-PTP-Q), also called phosphatidylinositol phosphatase PTPRQ, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRQ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (18 in PTPRQ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It displays low tyrosine-protein phosphatase activity; rather, it functions as a phosphatidylinositol phosphatase required for auditory processes. It regulates the levels of phosphatidylinositol 4,5-bisphosphate (PIP2) in the basal region of hair bundles. It can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates.


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 166.62  E-value: 7.40e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 604 NRYKDVLPYDITRVVLQEE----GDDYINASHVktepAG--CVLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTE 677
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADagvpGSDYINASYI----SGylCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 678 RGRTKCHQYWPHPPE-VRDYGYLQVCCHSEECNLAYVTRQLTLtnTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKS 756
Cdd:cd14616   77 KGRIRCHQYWPEDNKpVTVFGDIVITKLMEDVQIDWTIRDLKI--ERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKL 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 757 VRSMR-QESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCE 825
Cdd:cd14616  155 VRASRaHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 595-828 2.20e-46

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: 167.14  E-value: 2.20e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 595 AKQSENMDKNRYKDVLPYDITRVVLQ----EEGDDYINASHVKT--EPAgcvlQYIAAQGPLPHTCTHFWRSVWEQDVNV 668
Cdd:cd14633   35 AKKDENRMKNRYGNIIAYDHSRVRLQpiegETSSDYINGNYIDGyhRPN----HYIATQGPMQETIYDFWRMVWHENTAS 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 669 IIMLTTLTERGRTKCHQYWPHPPEVrdYGYLQVCCHSEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSS 748
Cdd:cd14633  111 IIMVTNLVEVGRVKCCKYWPDDTEI--YKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHAT 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 749 DFLDFVKSVRSMRQESV-PLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAI 827
Cdd:cd14633  189 GLLGFVRQVKSKSPPNAgPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 268


                 .
gi 528504074 828 L 828
Cdd:cd14633  269 L 269
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 626-823 3.10e-46

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: 164.32  E-value: 3.10e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 626 YINASHVKTEPAGCvlQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHPPEvRDYGYLQVCCHS 705
Cdd:cd14551    1 YINASYIDGYQEKN--KFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGC-WTYGNLRVRVED 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 706 EECNLAYVTRQLTLTNTQSG----QQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMR-QESVPLMVHCSAGIGRTGV 780
Cdd:cd14551   78 TVVLVDYTTRKFCIQKVNRGigekRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANpPRAGPIVVHCSAGVGRTGT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 528504074 781 LITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFV 823
Cdd:cd14551  158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFI 200
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 626-827 6.59e-46

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: 163.38  E-value: 6.59e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 626 YINAS----HVKTEPAgcvlqYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHP-PEVrdYGYLQ 700
Cdd:cd14546    1 YINAStiydHDPRNPA-----YIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEgSEV--YHIYE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 701 VCCHSEE--CNlAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSV-RSMRQESVPLMVHCSAGIGR 777
Cdd:cd14546   74 VHLVSEHiwCD-DYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVnKSYRGRSCPIVVHCSDGAGR 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528504074 778 TGVLITMETAMTLMEK-EKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAI 827
Cdd:cd14546  153 TGTYILIDMVLNRMAKgAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 626-822 1.63e-45

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: 162.17  E-value: 1.63e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 626 YINASHVKTEPAGCVlQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWphpPEVR----DYGYLQV 701
Cdd:cd14539    1 YINASLIEDLTPYCP-RFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYW---PTERgqalVYGAITV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 702 CCHSEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVRS----MRQESVPLMVHCSAGIGR 777
Cdd:cd14539   77 SLQSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHShylqQRSLQTPIVVHCSSGVGR 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 528504074 778 TGVLITMETAMTLMEKEKPVYPL-EVITLMREQRAMLVQTSCQFTF 822
Cdd:cd14539  157 TGAFCLLYAAVQEIEAGNGIPDLpQLVRKMRQQRKYMLQEKEHLKF 202
FERM_C_PTPN4_PTPN3_like cd13189
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and ...
 217-309 4.19e-44

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: 154.01  E-value: 4.19e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 217 LYGVELHHAQDASNPAVWVGITSGGVALFCHLICSSFFPWINIIKISFKRKRFFVHLRRKHGELGHHVVSLSMPNSRACK 296
Cdd:cd13189    1 LYGVELHSARDSNNLELQIGVSSAGILVFQNGIRINTFPWSKIVKISFKRKQFFIQLRREPNESRDTILGFNMLSYRACK 80

                         90
                 ....*....|...
gi 528504074 297 NLWRSCVDHHTFY 309
Cdd:cd13189   81 NLWKSCVEHHTFF 93
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 605-822 4.64e-44

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: 159.05  E-value: 4.64e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 605 RYKDVLPYDITRVVLQ----EEGDDYINASHVKTEPAGcvLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGR 680
Cdd:cd14623    1 RVLQIIPYEFNRVIIPvkrgEENTDYVNASFIDGYRQK--DSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 681 TKCHQYWPHPPEVrDYGYLQVCCHSEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVRSM 760
Cdd:cd14623   79 EKCAQYWPSDGSV-SYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQ 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528504074 761 RQES--VPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTF 822
Cdd:cd14623  158 QQQSgnHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEF 221
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 626-828 7.04e-44

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: 157.39  E-value: 7.04e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 626 YINASHVK--TEPAgcvlQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHPPEVrdYGYLQVCC 703
Cdd:cd14555    1 YINANYIDgyHRPN----HYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEV--YGDIKVTL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 704 HSEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMRQESV-PLMVHCSAGIGRTGVLI 782
Cdd:cd14555   75 VETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAgPIVVHCSAGAGRTGCYI 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 528504074 783 TMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAIL 828
Cdd:cd14555  155 VIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 603-823 9.66e-44

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: 158.16  E-value: 9.66e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 603 KNRYKDVLPYDITRVVLQEEGDD-----YINASHVKTEpAGCVLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTE 677
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKPKNSNdslstYINANYIRGY-GGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 678 RGRtKCHQYWPHPPEVrdYGYLQVCCHS-EECNlAYVTRQLTLTntQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKS 756
Cdd:cd14611   81 KNE-KCVLYWPEKRGI--YGKVEVLVNSvKECD-NYTIRNLTLK--QGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLD 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 757 VRSMRQESV---PLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFV 823
Cdd:cd14611  155 VEEDRLASPgrgPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFV 224
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 616-828 5.54e-43

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: 155.56  E-value: 5.54e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 616 RVVLQ----EEGDDYINASHVK--TEPAgcvlQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPH 689
Cdd:cd14631    1 RVILQpvedDPSSDYINANYIDgyQRPS----HYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 690 PPEVrdYGYLQVCCHSEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMRQESV-PLM 768
Cdd:cd14631   77 DTEV--YGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAgPIV 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 769 VHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAIL 828
Cdd:cd14631  155 VHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 626-827 9.02e-43

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: 154.35  E-value: 9.02e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 626 YINASHVKtepaGCVLQ--YIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHPPEVrDYGYLQVCC 703
Cdd:cd14552    1 YINASFID----GYRQKdaYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSV-SSGDITVEL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 704 HSEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMRQES--VPLMVHCSAGIGRTGVL 781
Cdd:cd14552   76 KDQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSgnHPITVHCSAGAGRTGTF 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 528504074 782 ITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAI 827
Cdd:cd14552  156 CALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 597-835 3.87e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 153.23  E-value: 3.87e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 597 QSENMDKNRYKDVLPYDITRVVLQEE--GDDYINASHVKTEPAGcvLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTT 674
Cdd:PHA02742  49 ELKNMKKCRYPDAPCFDRNRVILKIEdgGDDFINASYVDGHNAK--GRFICTQAPLEETALDFWQAIFQDQVRVIVMITK 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 675 LTERGRTKCHQYW-PHPPEVRDYGYLQVCCHSEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDF 753
Cdd:PHA02742 127 IMEDGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDF 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 754 VKSVRSM------------RQESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFT 821
Cdd:PHA02742 207 VLAVREAdlkadvdikgenIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYI 286

                        250
                 ....*....|....
gi 528504074 822 FvCEAILRVYREKV 835
Cdd:PHA02742 287 F-CYFIVLIFAKLM 299
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 603-823 4.11e-39

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific PTP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome.


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 145.78  E-value: 4.11e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 603 KNRYKDVLPYDITRVVL-QEEGDD----YINASHVKTEpAGCVLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTE 677
Cdd:cd14613   28 KNRYKTILPNPHSRVCLtSPDQDDplssYINANYIRGY-GGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEE 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 678 RGRtKCHQYWPHppEVRDYGYLQVCCHSEECNLAYVTRQLTLTNtqSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSV 757
Cdd:cd14613  107 MNE-KCTEYWPE--EQVTYEGIEITVKQVIHADDYRLRLITLKS--GGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQEV 181

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 758 RSMRQE----SVPLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFV 823
Cdd:cd14613  182 EEARQQaepnCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFV 251
PHA02738 PHA02738
hypothetical protein; Provisional
 600-829 5.38e-39

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 147.38  E-value: 5.38e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 600 NMDKNRYKDVLPYDITRVVLQEEGD--DYINASHVKTEPAGcvLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTE 677
Cdd:PHA02738  49 NRKLNRYLDAVCFDHSRVILPAERNrgDYINANYVDGFEYK--KKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 678 RGRTKCHQYWP--HPPEVRdYGYLQVCCHSEECNLAYVTRQLTLTNTQSGQQrSITHLQYVAWPDHGVPEDSSDFLDFVK 755
Cdd:PHA02738 127 NGREKCFPYWSdvEQGSIR-FGKFKITTTQVETHPHYVKSTLLLTDGTSATQ-TVTHFNFTAWPDHDVPKNTSEFLNFVL 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 756 SVRS----MRQESV----------PLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFT 821
Cdd:PHA02738 205 EVRQcqkeLAQESLqighnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYF 284


                 ....*...
gi 528504074 822 FVCEAILR 829
Cdd:PHA02738 285 FCYRAVKR 292
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 626-828 1.18e-38

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: 142.88  E-value: 1.18e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 626 YINASHVKTEPAGCvlQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHPPEVrdYGYLQVCCHS 705
Cdd:cd14632    1 YINANYIDGYHRSN--HFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDT--YGDIKITLLK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 706 EECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVR-SMRQESVPLMVHCSAGIGRTGVLITM 784
Cdd:cd14632   77 TETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKaSTPPDAGPVVVHCSAGAGRTGCYIVL 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 528504074 785 ETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAIL 828
Cdd:cd14632  157 DVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 625-822 1.29e-37

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: 139.76  E-value: 1.29e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 625 DYINASHVKTEPAGCVlqYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHPPEVrDYGYLQVCCH 704
Cdd:cd14622    1 DYINASFIDGYRQKDY--FIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSV-THGEITIEIK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 705 SEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMRQES--VPLMVHCSAGIGRTGVLI 782
Cdd:cd14622   78 NDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTgnHPIVVHCSAGAGRTGTFI 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 528504074 783 TMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTF 822
Cdd:cd14622  158 ALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEF 197
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 626-822 4.34e-37

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: 138.37  E-value: 4.34e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 626 YINASHVKTEPAGCVLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRT-KCHQYWP-HPPEVRDYGYLQVCC 703
Cdd:cd17658    1 YINASLVETPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPaEENESREFGRISVTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 704 HSEECNLAYVT-RQLTLTNTQSGQQ-RSITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMRQESVPLMVHCSAGIGRTGVL 781
Cdd:cd17658   81 KKLKHSQHSITlRVLEVQYIESEEPpLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPPSAGPIVVHCSAGIGRTGAY 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 528504074 782 ITME-TAMTLMEKEKPVYPL-EVITLMREQRAMLVQTSCQFTF 822
Cdd:cd17658  161 CTIHnTIRRILEGDMSAVDLsKTVRKFRSQRIGMVQTQDQYIF 203
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 626-822 4.62e-37

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: 137.91  E-value: 4.62e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 626 YINASHVKtepaG--CVLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKCHQYWPHppEVRDYGYLQVCC 703
Cdd:cd14558    1 YINASFID----GywGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGD--EKKTYGDIEVEL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 704 HSEECNLAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVR-------SMRQESVPLMVHCSAGIG 776
Cdd:cd14558   75 KDTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKqklpyknSKHGRSVPIVVHCSDGSS 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 528504074 777 RTGV----LITMETAmtlmEKEKPVYPLEVITLMREQRAMLVQTSCQFTF 822
Cdd:cd14558  155 RTGIfcalWNLLESA----ETEKVVDVFQVVKALRKQRPGMVSTLEQYQF 200
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 591-823 1.07e-36

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 140.52  E-value: 1.07e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 591 LMSCAKQSENMDKNRYKDVLPYDITRVVLQEEG---DDYINASHVK--TEPAgcvlQYIAAQGPLPHTCTHFWRSVWEQD 665
Cdd:PHA02747  42 LIANFEKPENQPKNRYWDIPCWDHNRVILDSGGgstSDYIHANWIDgfEDDK----KFIATQGPFAETCADFWKAVWQEH 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 666 VNVIIMLT-TLTERGRTKCHQYWphppevrdygylqvcCHSEECNL----------------AYVTRQLTLTNTQSGQQR 728
Cdd:PHA02747 118 CSIIVMLTpTKGTNGEEKCYQYW---------------CLNEDGNIdmedfrietlktsvraKYILTLIEITDKILKDSR 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 729 SITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMRQESV-----------PLMVHCSAGIGRTGVLITMETAMTLMEKEKPV 797
Cdd:PHA02747 183 KISHFQCSEWFEDETPSDHPDFIKFIKIIDINRKKSGklfnpkdallcPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAI 262

                        250       260
                 ....*....|....*....|....*.
gi 528504074 798 YPLEVITLMREQRAMLVQTSCQFTFV 823
Cdd:PHA02747 263 CLAKTAEKIREQRHAGIMNFDDYLFI 288
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 597-836 2.55e-34

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 134.00  E-value: 2.55e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 597 QSENMDKNRYKDVLPYDITRVVL-----------------------QEEGDDYINASHVKTEPAgcVLQYIAAQGPLPHT 653
Cdd:PHA02746  48 KKENLKKNRFHDIPCWDHSRVVInaheslkmfdvgdsdgkkievtsEDNAENYIHANFVDGFKE--ANKFICAQGPKEDT 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 654 CTHFWRSVWEQDVNVIIMLTTlTERGRTKCHQYWPHPPEVR-DYGYLQVCCHSEECNLAYVTRQLTLTNTQSGQQRSITH 732
Cdd:PHA02746 126 SEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWTKEEDSElAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHH 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 733 LQYVAWPDHGVPEDSSDFLDFVKSVRSMRQESV-----------PLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLE 801
Cdd:PHA02746 205 FWFPDWPDNGIPTGMAEFLELINKVNEEQAELIkqadndpqtlgPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGE 284

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 528504074 802 VITLMREQRAMLVQTSCQFTFVCEAILRVYREKVK 836
Cdd:PHA02746 285 IVLKIRKQRHSSVFLPEQYAFCYKALKYAIIEEAK 319
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
596-820 1.76e-31

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 124.43  E-value: 1.76e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 596 KQSENMDKNRYKDVLPYDITRVvlqEEGDDYINASHVKtepAGCVLQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTL 675
Cdd:COG5599   38 QNINGSPLNRFRDIQPYKETAL---RANLGYLNANYIQ---VIGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASD 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 676 TE--RGRTKCHQYWPHPPEvrdygYLQVCCHSEECNLAYVTRQLT-----LTNTQSGQ-QRSITHLQYVAWPDHGVPeDS 747
Cdd:COG5599  112 DEisKPKVKMPVYFRQDGE-----YGKYEVSSELTESIQLRDGIEartyvLTIKGTGQkKIEIPVLHVKNWPDHGAI-SA 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 748 SDFLDFVKSVRSMRQESV----PLMVHCSAGIGRTGVLITMeTAMTLMEKEKPVYPL---EVITLMREQRAM-LVQTSCQ 819
Cdd:COG5599  186 EALKNLADLIDKKEKIKDpdklLPVVHCRAGVGRTGTLIAC-LALSKSINALVQITLsveEIVIDMRTSRNGgMVQTSEQ 264


                 .
gi 528504074 820 F 820
Cdd:COG5599  265 L 265
FERM_F1_PTPN3_like cd17100
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 31-113 3.06e-31

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: 117.02  E-value: 3.06e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  31 LLCLVLFPDGTTQNFTVNKHDAGHLLFDLACEHLNIVEKQYFSMQISEDTSS--SPRWLDPNKPFKKQLKGSPPFFLMFR 108
Cdd:cd17100    2 VRCIVHFLDDTEQTFEVEKRDKGQVLLDKVFNHLELVEKDYFGLQFSDDSPAtdSMRWLDPLKPIRKQIKGGPPYYLNFR 81


                 ....*
gi 528504074 109 VRFFI 113
Cdd:cd17100   82 VKFYV 86
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 115-223 3.76e-31

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 118.14  E-value: 3.76e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  115 DPNSLQHEQTRHFYFLQIRKDICEGRLKCPLSSAVVLASYSVQSELGDYNPET-PTGYLSKTHFIPEQDQEFL------L 187
Cdd:pfam00373   2 LELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSShTSEYLSLESFLPKQLLRKMkskeleK 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 528504074  188 KVESLHPQHKGLSQSDAELCYLNTARTLDLYGVELH 223
Cdd:pfam00373  82 RVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
729-828 6.43e-31

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 117.07  E-value: 6.43e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074   729 SITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMRQ---ESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKP-VYPLEVIT 804
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqseSSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                           90       100
                   ....*....|....*....|....
gi 528504074   805 LMREQRAMLVQTSCQFTFVCEAIL 828
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALL 104
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 729-828 6.43e-31

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: 117.07  E-value: 6.43e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074   729 SITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMRQ---ESVPLMVHCSAGIGRTGVLITMETAMTLMEKEKP-VYPLEVIT 804
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqseSSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                           90       100
                   ....*....|....*....|....
gi 528504074   805 LMREQRAMLVQTSCQFTFVCEAIL 828
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALL 104
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 626-825 3.67e-29

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: 115.20  E-value: 3.67e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 626 YINASHVK--TEPAGcvlqYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTkCHQYWPHpPEVRDYGYLQVCC 703
Cdd:cd14556    1 YINAALLDsyKQPAA----FIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQS-CPQYWPD-EGSGTYGPIQVEF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 704 HSEECNLAYVTRQLTLTNTQSGQQ--RSITHLQYVAWPDHG-VPEDSSDFLDFVKSVRSMRQES--VPLMVHCSAGIGRT 778
Cdd:cd14556   75 VSTTIDEDVISRIFRLQNTTRPQEgyRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSgeGPIVVHCLNGVGRS 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 528504074 779 GVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCE 825
Cdd:cd14556  155 GVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
FERM_F1_PTPN3 cd17193
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 31-113 5.80e-29

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: 110.71  E-value: 5.80e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  31 LLCLVLFPDGTTQNFTVNKHDAGHLLFDLACEHLNIVEKQYFSMQISEDTSSSPRWLDPNKPFKKQLKGSPPFFLMFRVR 110
Cdd:cd17193    2 VICNVHFLDGSVQSFKVNKQDTGQVLLDMAYNHLGLTEREYFGLQHNEDSVDSPRWLEPSKPIRKQLKGGFPCSLHFRVR 81


                 ...
gi 528504074 111 FFI 113
Cdd:cd17193   82 FFI 84
FERM_F1_PTPN4 cd17194
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 31-113 1.67e-28

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: 109.24  E-value: 1.67e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  31 LLCLVLFPDGTTQNFTVNKHDAGHLLFDLACEHLNIVEKQYFSMQISEDTSSSPRWLDPNKPFKKQLKGSPPFFLMFRVR 110
Cdd:cd17194    2 VVCNILLLDNTVQAFKVNKHDQGQVLLDLVFKHLDLTERDYFGLQLADDSTDNPRWLDPNKPIRKQLKRGSPHNLNFRVK 81


                 ...
gi 528504074 111 FFI 113
Cdd:cd17194   82 FFV 84
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 124-215 2.57e-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: 106.56  E-value: 2.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 124 TRHFYFLQIRKDICEGRLKCPLSSAVVLASYSVQSELGDYNPETPT-GYLSKTHFIPEQ------DQEFLLKVESLHPQH 196
Cdd:cd14473    1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKpKYLSLKRFLPKQllkqrkPEEWEKRIVELHKKL 80

                         90
                 ....*....|....*....
gi 528504074 197 KGLSQSDAELCYLNTARTL 215
Cdd:cd14473   81 RGLSPAEAKLKYLKIARKL 99
FERM_C_4_1_family cd13184
FERM domain C-lobe of Protein 4.1 family; The protein 4.1 family includes four well-defined ...
 218-309 3.07e-24

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: 97.39  E-value: 3.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 218 YGVELHHAQDASNPAVWVGITSGGVALFCHLICSSFFPWINIIKISFKRKRFFVHLRRKHGELGHHVVSLSMPNSRACKN 297
Cdd:cd13184    1 YGVDLHPAKDSEGVDIMLGVCSSGLLVYRDRLRINRFAWPKVLKISYKRNNFYIKIRPGEFEQYETTIGFKLPNHRAAKR 80

                         90
                 ....*....|..
gi 528504074 298 LWRSCVDHHTFY 309
Cdd:cd13184   81 LWKVCVEHHTFF 92
FERM_C pfam09380
FERM C-terminal PH-like domain;
227-312 9.90e-23

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 92.70  E-value: 9.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  227 DASNPAVWVGITSGGVALFCHLICSS-FFPWINIIKISFKRKRFFVHLRRKHGElghHVVSLSMPNSRACKNLWRSCVDH 305
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKILnLFPWREIRKISFKRKKFLIKLRDKSSE---ETLGFYTESSRACKYLWKLCVEQ 77


                  ....*..
gi 528504074  306 HTFYNRK 312
Cdd:pfam09380  78 HTFFRLR 84
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
 31-111 7.27e-22

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: 90.34  E-value: 7.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  31 LLCLVLFPDGTTQNFTVNKHDAGHLLFDLACEHLNIVEKQYFSMQIsEDTSSSPRWLDPNKPFKKQLKGSPPFFLMFRVR 110
Cdd:cd01765    1 ISCRVRLLDGTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFY-EDNDGQKHWLDLDKKISKQLKRSGPYQFYFRVK 79


                 .
gi 528504074 111 F 111
Cdd:cd01765   80 F 80
FERM_C_FARP1-like cd13193
FERM domain C-lobe of FERM, RhoGEF and pleckstrin domain-containing protein 1 and related ...
 211-322 1.13e-20

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: 88.17  E-value: 1.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 211 TARTLDLYGVELHHAQDASNPAVWVGITSGGVALFCHLICSSFFPWINIIKISFKRKRFFVHLRRKHGELGHHVVSLSMP 290
Cdd:cd13193    2 TARRCELYGIRLHPAKDREGVKLNLAVAHMGILVFQGFTKINTFSWAKIRKLSFKRKRFLIKLHPEAYGSYKDTVEFSFE 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 528504074 291 NSRACKNLWRSCVDHHTFYN----RKPSHSASKLSS 322
Cdd:cd13193   82 SRNECKSFWKKCIEHHAFFRcsevPKPPSPKLRLFS 117
FERM_F1_EPB41L5_like cd17108
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 31-112 1.09e-19

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: 83.94  E-value: 1.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  31 LLCLVLFPDGTTQNFTVNKHDAGHLLFDLACEHLNIVEKQYFSMQISeDTSSSPRWLDPNKPFKKQLKGSPPFFLMFRVR 110
Cdd:cd17108    1 IQCKVILLDGTDLSIELPKKAKGQELYEQVFYHLDLIEKDYFGLQFM-DAAQVQHWLDPTKKIKKQVKIGPPYTLRFRVK 79


                 ..
gi 528504074 111 FF 112
Cdd:cd17108   80 FY 81
FERM_C_FRMD3_FRMD5 cd13192
FERM domain C-lobe of FERM domain-containing protein 3 and 5 (FRMD3 and 5); FRMD3 (also called ...
 204-309 3.93e-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: 83.21  E-value: 3.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 204 AELCYLNTARTLDLYGVELHHAQDASNPAVWVGITSGGVALFCHLICSSFFPWINIIKISFKRKRFFVHLRRKhgELGHH 283
Cdd:cd13192    1 AEDNFLRKAATLETYGVDPHPVKDHRGNQLYLGFTHTGIVTFQGGKRVHHFRWNDITKFNYEGKMFILHVMQK--EEKKH 78

                         90       100
                 ....*....|....*....|....*.
gi 528504074 284 VVSLSMPNSRACKNLWRSCVDHHTFY 309
Cdd:cd13192   79 TLGFKCPTPAACKHLWKCAVEQQAFY 104
FERM_F1_EPB41L1 cd17201
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 31-115 8.52e-19

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: 81.47  E-value: 8.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  31 LLCLVLFPDGTTQNFTVNKHDAGHLLFDLACEHLNIVEKQYFSMQISeDTSSSPRWLDPNKPFKKQLKGSPPFFlMFRVR 110
Cdd:cd17201    2 AICKVTLLDGSEYECEVEKHARGQVLFDTVCEHLNLLEKDYFGLTFC-DTESQKNWLDPSKEIKKQIRSGPWHF-AFTVK 79


                 ....*
gi 528504074 111 FFISD 115
Cdd:cd17201   80 FYPPD 84
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 626-828 1.22e-18

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: 85.07  E-value: 1.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 626 YINASHVKT--EPAGcvlqYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTerGRTKCHQYWPHPPEVRdYGYLQV-- 701
Cdd:cd14634    1 YINAALMDShkQPAA----FIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMD--AAQLCMQYWPEKTSCC-YGPIQVef 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 702 -CCHSEECNLAYVTRQLTLTNTQSGqQRSITHLQYVAWPDH-GVPEDSSDFLDFVKSVRSMRQE----SVPLMVHCSAGI 775
Cdd:cd14634   74 vSADIDEDIISRIFRICNMARPQDG-YRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydgrEGRTVVHCLNGG 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 528504074 776 GRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAIL 828
Cdd:cd14634  153 GRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVAL 205
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 626-822 3.68e-18

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: 83.92  E-value: 3.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 626 YINASHVKT--EPAGcvlqYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLT-ERGrtkCHQYWPHPPEVRdYGYLQVC 702
Cdd:cd14636    1 YINAALMDSyrQPAA----FIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDlAQG---CPQYWPEEGMLR-YGPIQVE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 703 CHSEECNLAYVTRQLTLTNTQSGQQ--RSITHLQYVAWPDH-GVPEDSSDFLDFVKSVRSMRQESVP----LMVHCSAGI 775
Cdd:cd14636   73 CMSCSMDCDVISRIFRICNLTRPQEgyLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECDEgegrTIIHCLNGG 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 528504074 776 GRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTF 822
Cdd:cd14636  153 GRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRF 199
FERM_F1_FARP1_like cd17098
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, RhoGEF and ...
 31-116 2.54e-17

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: 77.25  E-value: 2.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  31 LLCLVLFPDGTTQNFTVNKHDAGHLLFDLACEHLNIVEKQYFSMQISeDTSSSPRWLDPNKPFKKQLKGSPPFFLMFRVR 110
Cdd:cd17098    1 LHVKVQMLDDTVHIFQVQQKALGEVLFDQVCKHLNLLESDYFGLEFT-DPEGNKCWLDPEKPILRQVKRPKDVVFKFVVK 79


                 ....*.
gi 528504074 111 FFISDP 116
Cdd:cd17098   80 FYTPDP 85
FERM_F1_FRMD3 cd17102
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 36-112 5.50e-17

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: 76.51  E-value: 5.50e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528504074  36 LFPDGTTQNFTVNKHDAGHLLFDLACEHLNIVEKQYFSMQISeDTSSSPRWLDPNKPFKKQLKGSPPFFLMFRVRFF 112
Cdd:cd17102    7 LLDDSEVICCEFKKDTKGQFLLDYVCNYLNLLEKDYFGLRYV-DTEKQRHWLDPNKSIYKQLKGVPPYVLCFRVKFY 82
FERM_F1_EPB41L4B cd17204
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 31-115 8.51e-17

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: 76.01  E-value: 8.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  31 LLCLVLFPDGTTQNFTVNKHDAGHLLFDLACEHLNIVEKQYFSMQISeDTSSSPRWLDPNKPFKKQLKGSPPFFLMFRVR 110
Cdd:cd17204    1 LTCRVLLLDGTDVSVELPKHAKGQDLFDQIVYHLDLVETDYFGLQFM-DAAQVAHWLDHTKPIKKQIKIGPPYTLHFRIK 79


                 ....*
gi 528504074 111 FFISD 115
Cdd:cd17204   80 YYSSE 84
FERM_N pfam09379
FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the ...
 35-98 8.78e-17

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: 74.93  E-value: 8.78e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528504074   35 VLFPDGTTQNFTVNKHDAGHLLFDLACEHLNIVEKQYFSMQIsEDTSSSPRWLDPNKPFKKQLK 98
Cdd:pfam09379   1 VRLLDGTVLEFDVQPKATGQVLLDQVCNHLNLKEKDYFGLQF-LDDNGEHRWLDLSKRLSKQAP 63
FERM_F1_EPB41L2 cd17202
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 31-115 2.37e-16

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: 74.62  E-value: 2.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  31 LLCLVLFPDGTTQNFTVNKHDAGHLLFDLACEHLNIVEKQYFSMqISEDTSSSPRWLDPNKPFKKQLKGSPPFFlMFRVR 110
Cdd:cd17202    2 VLCKVTLLDGTEYSCDLEKRAKGQVLFDKVCEHLNLLEKDYFGL-LYQVSANQKNWLDSTKEIKRQIRRLPWLF-TFNVK 79


                 ....*
gi 528504074 111 FFISD 115
Cdd:cd17202   80 FYPPD 84
FERM_F1_EPB41L3 cd17203
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 31-115 4.98e-16

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: 73.82  E-value: 4.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  31 LLCLVLFPDGTTQNFTVNKHDAGHLLFDLACEHLNIVEKQYFSMQIsEDTSSSPRWLDPNKPFKKQLKGSPPFFlMFRVR 110
Cdd:cd17203    2 MQCKVTLLDGSEYTCEVEKRSKGQVLFDKVCEHLNLLEKDYFGLTY-RDSENQKNWLDPAKEIKKQIRSGAWQF-SFNVK 79


                 ....*
gi 528504074 111 FFISD 115
Cdd:cd17203   80 FYPPD 84
FERM_F1_EPB41L cd17106
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 32-115 5.26e-16

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: 73.63  E-value: 5.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  32 LCLVLFPDGTTQNFTVNKHDAGHLLFDLACEHLNIVEKQYFSMQIsEDTSSSPRWLDPNKPFKKQLKGSPPFFlMFRVRF 111
Cdd:cd17106    3 QCKVLLLDGTEYTCEVEKRAKGQVLFDKVCEHLNLLEKDYFGLTY-RDAQDQKNWLDPAKEIKKQIRSGPWLF-SFNVKF 80


                 ....
gi 528504074 112 FISD 115
Cdd:cd17106   81 YPPD 84
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 626-828 2.87e-15

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 75.33  E-value: 2.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 626 YINASHVK--TEPAGcvlqYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRT-KCHQYWPHpPEVRDYGYLQVC 702
Cdd:cd14637    1 YINAALTDsyTRSAA----FIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPE-PGLQQYGPMEVE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 703 CHSEECNLAYVTRQLTLTNTQSGQ--QRSITHLQYVAW-PDHGVPEDSSDFLDFVKSVRSMRQESVP--LMVHCSAGIGR 777
Cdd:cd14637   76 FVSGSADEDIVTRLFRVQNITRLQegHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGEgrTVVHCLNGGGR 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528504074 778 TGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAIL 828
Cdd:cd14637  156 SGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206
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 ...
 219-309 4.49e-15

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: 71.16  E-value: 4.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 219 GVELHHAQDASNPAVWVGITSGGVALFCHLICSSFFPWINIIKISFKRKRFFVHLRRKHGELGHHVVSLSMPNSRACKNL 298
Cdd:cd13186    1 GVDLHPVKGEDGNEYFLGLTPTGILVFENKTKIGLFFWPRITKLDFKGKKLKLVVKEKDDQEQEHTFVFRLPNKKACKHL 80

                         90
                 ....*....|.
gi 528504074 299 WRSCVDHHTFY 309
Cdd:cd13186   81 WKCAVEHHAFF 91
FERM_F1_EPB41 cd17105
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 33-115 4.65e-15

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: 71.00  E-value: 4.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  33 CLVLFPDGTTQNFTVNKHDAGHLLFDLACEHLNIVEKQYFSMQISeDTSSSPRWLDPNKPFKKQLKGsPPFFLMFRVRFF 112
Cdd:cd17105    3 CKVSLLDDTVYECEVEKHAKGQDLFKKVCEHLNLLEEDYFGLAIW-DSPTSKTWLDPAKEIKKQVHG-GPWEFTFNVKFY 80


                 ...
gi 528504074 113 ISD 115
Cdd:cd17105   81 PPD 83
FERM_F1_MYLIP cd17104
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in E3 ...
 31-112 1.22e-14

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: 69.61  E-value: 1.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  31 LLCLVLFPDGTTQNFTVNKHDAGHLLFDLACEHLNIVEKQYFSMQISeDTSSSPRWLDPNKPFKKQLKGSPPFFLMFRVR 110
Cdd:cd17104    1 MLCLVSQPDSVVIEVEVDPKANGQECLDKVCQKLGIIEKDYFGLQYT-GPKGERLWLNLRNRISRQLPGPPPYRLRLRVK 79


                 ..
gi 528504074 111 FF 112
Cdd:cd17104   80 FF 81
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 441-526 1.32e-14

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: 69.49  E-value: 1.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 441 LVRISPDQDGKFGFNVKGGVDQKMPLAISHVNLASPAGRCvPPLMEGDQVLLINGRDISEHTHQQVVMFIKASreshSKE 520
Cdd:cd00136    1 TVTLEKDPGGGLGFSIRGGKDGGGGIFVSRVEPGGPAARD-GRLRVGDRILEVNGVSLEGLTHEEAVELLKSA----GGE 75


                 ....*.
gi 528504074 521 LALLVR 526
Cdd:cd00136   76 VTLTVR 81
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 626-828 1.50e-14

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 73.10  E-value: 1.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 626 YINASHVKTEPAGCvlQYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGRTKChQYWPHPPEVRDYGYLQVCCHS 705
Cdd:cd17669    1 YINASYIMGYYQSN--EFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKDEPINCETFKVTLIA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 706 EEC-------NLayVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVP-EDSSDFLDFVKSVRSMRQEsvPLMVHCSAGIGR 777
Cdd:cd17669   78 EEHkclsneeKL--IIQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISIIKEEAANRDG--PMIVHDEHGGVT 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528504074 778 TGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAIL 828
Cdd:cd17669  154 AGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 626-797 3.15e-14

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: 71.97  E-value: 3.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 626 YINASHvktepagcvLQ-------YIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTERGrtKCHQYWPHPPEVRDYGY 698
Cdd:cd14550    1 YINASY---------LQgyrrsneFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPLECET 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 699 LQVC-------CHSEECNLayVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPedSSDFLDFVKSVRSMRQESV-PLMVH 770
Cdd:cd14550   70 FKVTlsgedhsCLSNEIRL--IVRDFILESTQDDYVLEVRQFQCPSWPNPCSP--IHTVFELINTVQEWAQQRDgPIVVH 145

                        170       180       190
                 ....*....|....*....|....*....|..
gi 528504074 771 -----CSAGigrTGVLITmeTAMTLMEKEKPV 797
Cdd:cd14550  146 dryggVQAA---TFCALT--TLHQQLEHESSV 172
FERM_F1_EPB41L5 cd17205
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 29-115 6.29e-14

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: 67.76  E-value: 6.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  29 SGLLCLVLFPDGTTQNFTVNKHDAGHLLFDLACEHLNIVEKQYFSMQISeDTSSSPRWLDPNKPFKKQLKGSPPFFLMFR 108
Cdd:cd17205    1 SIITCRVSLLDGTDVSVDLPKKAKGQELFEQIMYHLDLIEKDYFGLRFM-DSAQVAHWLDVTKSIKKQVKIGPPYCLHLR 79


                 ....*..
gi 528504074 109 VRFFISD 115
Cdd:cd17205   80 VKFYSSE 86
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 626-828 1.34e-13

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: 70.48  E-value: 1.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 626 YINASHVKTEPAGCvlQYIAAQGPLPHTCTHFWRSVWEQDVNVIIML---TTLTERGRTkchqYWPHPPEVRDYGYLQV- 701
Cdd:cd17670    1 YINASYIMGYYRSN--EFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQGLAEDEFV----YWPSREESMNCEAFTVt 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 702 -------CCHSEEcnlAYVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSS-DFLDFVKSvRSMRQESvPLMVHCSA 773
Cdd:cd17670   75 liskdrlCLSNEE---QIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTfELINVIKE-EALTRDG-PTIVHDEF 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 528504074 774 GIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAIL 828
Cdd:cd17670  150 GAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 626-828 1.37e-13

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 70.49  E-value: 1.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 626 YINASHVKT--EPAGcvlqYIAAQGPLPHTCTHFWRSVWEQDVNVIIMLTTLTErgRTKCHQYWPHpPEVRDYGYLQVCC 703
Cdd:cd14635    1 YINAALMDSykQPSA----FIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDP--AQLCPQYWPE-NGVHRHGPIQVEF 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 704 HSEECNLAYVTRQLTLTNTQSGQQ--RSITHLQYVAWPDH-GVPEDSSDFLDFVKSVRSMRQE----SVPLMVHCSAGIG 776
Cdd:cd14635   74 VSADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEynggEGRTVVHCLNGGG 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528504074 777 RTGVLITMETAMTLMEKEKPVYPLEVITLMREQRAMLVQTSCQFTFVCEAIL 828
Cdd:cd14635  154 RSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205
FERM_F1_EPB41L4A cd17107
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 33-115 1.50e-13

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: 66.98  E-value: 1.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  33 CLVLFPDGTTQNFTVNKHDA----GHLLFDLACEHLNIVEKQYFSMQISeDTSSSPRWLDPNKPFKKQLKG-SPPFFLMF 107
Cdd:cd17107    5 CEIVLLDESELILTIQQDGIksskGSVVLDVVFQHLNLLETDYFGLRYI-DRQHQTHWLDPAKTLSEQLKLiGPPYTLYF 83


                 ....*...
gi 528504074 108 RVRFFISD 115
Cdd:cd17107   84 GVKFYAED 91
PDZ_ZASP52-like cd23068
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ...
 441-527 1.55e-13

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: 66.40  E-value: 1.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 441 LVRisPDQDGKFGFNVKGGVDQKMPLAISHVNLASPAGRCvpPLMEGDQVLLINGRDISEHTHQQVVMFIKASreshSKE 520
Cdd:cd23068    4 LRR--DDSNTPWGFRLQGGADFGQPLSIQKVNPGSPADKA--GLRRGDVILRINGTDTSNLTHKQAQDLIKRA----GND 75


                 ....*..
gi 528504074 521 LALLVRR 527
Cdd:cd23068   76 LQLTVQR 82
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 441-526 2.21e-13

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 66.15  E-value: 2.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  441 LVRISPDQDGKFGFNVKGGVDQK-MPLAISHVNLASPAGRcvPPLMEGDQVLLINGRDISEHTHQQVVMFIKASreshSK 519
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKGGSDQGdPGIFVSEVLPGGAAEA--GGLKVGDRILSINGQDVENMTHEEAVLALKGS----GG 74


                  ....*..
gi 528504074  520 ELALLVR 526
Cdd:pfam00595  75 KVTLTIL 81
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 585-831 3.49e-13

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 71.15  E-value: 3.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 585 RKKEGMLMSCAkQSEN--MDKNRYKDVLPYDITRVVLQEEGDdYINASHVktEPAGCVLQYIAAQGPLPHTCTHFWRSVW 662
Cdd:PHA02740  37 EHEDEANKACA-QAENkaKDENLALHITRLLHRRIKLFNDEK-VLDARFV--DGYDFEQKFICIINLCEDACDKFLQALS 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 663 EQDVNVIIMLTTLTERgrtKCH-QYWP-HPPEVRDYGYLQVCCHSEECNLAYVTRQLTLTNtQSGQQRSITHLQYVAWPD 740
Cdd:PHA02740 113 DNKVQIIVLISRHADK---KCFnQFWSlKEGCVITSDKFQIETLEIIIKPHFNLTLLSLTD-KFGQAQKISHFQYTAWPA 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 741 HGVPEDSSDFLDFVKSVRSM-----RQESV----PLMVHCSAGIGRTGVLITMETAMTLMEKEKPVYPLEVITLMREQRA 811
Cdd:PHA02740 189 DGFSHDPDAFIDFFCNIDDLcadleKHKADgkiaPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKY 268

                        250       260
                 ....*....|....*....|
gi 528504074 812 MLVQTSCQFTFvCEAILRVY 831
Cdd:PHA02740 269 GCMNCLDDYVF-CYHLIAAY 287
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 723-825 7.52e-13

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: 68.14  E-value: 7.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 723 QSGQQRSITHLQYvAWPDHGVPedSSDF-LDFVKSVRSMRQESVPLMVHCSAGIGRTGVLItmetAMTLMEKEKpVYPLE 801
Cdd:cd14506   70 EAFMRAGIYFYNF-GWKDYGVP--SLTTiLDIVKVMAFALQEGGKVAVHCHAGLGRTGVLI----ACYLVYALR-MSADQ 141

                         90       100
                 ....*....|....*....|....
gi 528504074 802 VITLMREQRAMLVQTSCQFTFVCE 825
Cdd:cd14506  142 AIRLVRSKRPNSIQTRGQVLCVRE 165
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 441-529 1.43e-12

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: 63.94  E-value: 1.43e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074   441 LVRISPDQDGkFGFNVKGGVDQKMPLAISHVNLASPAGRCvpPLMEGDQVLLINGRDISEHTHQQVVMFIKASREShske 520
Cdd:smart00228   4 LVELEKGGGG-LGFSLVGGKDEGGGVVVSSVVPGSPAAKA--GLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGK---- 76


                   ....*....
gi 528504074   521 LALLVRRKG 529
Cdd:smart00228  77 VTLTVLRGG 85
FERM_F1_FRMD7 cd17188
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 35-116 3.51e-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: 3.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  35 VLFPDGTTQNFTVNKHDAGHLLFDLACEHLNIVEKQYFSMQISeDTSSSPRWLDPNKPFKKQLKGSPPFFLMFRVRFFIS 114
Cdd:cd17188    6 VQFLDDSQKVFVVDQKSTGKDLFNMSCSHLNLVEKEYFGLEFR-NHAGNNVWLELLKPITKQIKNPKELIFKFTVKFFPV 84


                 ..
gi 528504074 115 DP 116
Cdd:cd17188   85 DP 86
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
713-825 5.98e-11

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 61.14  E-value: 5.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 713 VTRQLTLT-----NTQSGQQRSITHLqYVAWPDHGVPEDSsDFLDFVKSVRSMRQESVPLMVHCSAGIGRTGVLItmetA 787
Cdd:COG2453   26 IDAVVSLTeeeelLLGLLEEAGLEYL-HLPIPDFGAPDDE-QLQEAVDFIDEALREGKKVLVHCRGGIGRTGTVA----A 99

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 528504074 788 MTLMEKEKPvyPLEVITLMREQRAMLVQTSCQFTFVCE 825
Cdd:COG2453  100 AYLVLLGLS--AEEALARVRAARPGAVETPAQRAFLER 135
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 219-309 3.61e-10

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: 57.38  E-value: 3.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 219 GVELHHAQDASNPA--VWVGITSGGVALFCH----LICSsfFPWINIIKISFKR-KRFFVHLRRKHGELGHHVVSLSmpn 291
Cdd:cd00836    1 GVEFFPVKDKSKKGspIILGVNPEGISVYDEltgqPLVL--FPWPNIKKISFSGaKKFTIVVADEDKQSKLLFQTPS--- 75

                         90
                 ....*....|....*...
gi 528504074 292 sRACKNLWRSCVDHHTFY 309
Cdd:cd00836   76 -RQAKEIWKLIVGYHRFL 92
PDZ_syntrophin-like cd06801
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 442-526 2.14e-09

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: 54.89  E-value: 2.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 442 VRISPDQDGKFGFNVKGGVDQKMPLAISHVNLASPAGRCvPPLMEGDQVLLINGRDISEHTHQQVVMFIKASreshSKEL 521
Cdd:cd06801    3 VRVVKQDVGGLGISIKGGAEHKMPILISKIFKGQAADQT-GQLFVGDAILSVNGENLEDATHDEAVQALKNA----GDEV 77


                 ....*
gi 528504074 522 ALLVR 526
Cdd:cd06801   78 TLTVK 82
FERM_F1_FARP1 cd17189
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 39-115 7.86e-09

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: 53.27  E-value: 7.86e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528504074  39 DGTTQNFTVNKHDAGHLLFDLACEHLNIVEKQYFSMQIsEDTSSSPRWLDPNKPFKKQLKGSPPFFLMFRVRFFISD 115
Cdd:cd17189    9 DDTQEVFEVPQRAPGKVLLDAVCSHLNLVEGDYFGLEF-QDHRKVMVWLDLLKPIVKQIRRPKHVVLRFVVKFFPPD 84
PDZ_PDLIM-like cd06753
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 452-527 1.01e-08

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: 52.92  E-value: 1.01e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504074 452 FGFNVKGGVDQKMPLAISHVNLASPAGRCvpPLMEGDQVLLINGRDISEHTHQQVVMFIKASREShskeLALLVRR 527
Cdd:cd06753   10 WGFRLQGGKDFNQPLTISRVTPGGKAAQA--NLRPGDVILAINGESTEGMTHLEAQNKIKAATGS----LSLTLER 79
FERM_F1_FARP2 cd17190
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 31-116 1.02e-08

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: 52.87  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  31 LLCLVLFPDGTTQNFTVNKHDAGHLLFDLACEHLNIVEKQYFSMQIsEDTSSSPRWLDPNKPFKKQLKGSPPFFLMFRVR 110
Cdd:cd17190    1 LQLRVKLLDNTTEPLEIEPKADGQALLSQVFKRLNLVESDYFGLEF-QNSQSNWIWLEPMKLIVKQVRRPKNTKLRLAVK 79


                 ....*.
gi 528504074 111 FFISDP 116
Cdd:cd17190   80 FFPPDP 85
PDZ_SYNPO2-like cd10820
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related ...
 450-525 2.06e-08

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: 51.93  E-value: 2.06e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504074 450 GKFGFNVKGGVDQKMPLAISHVNLASPAGRCVppLMEGDQVLLINGRDISEHTHQQVVMFIKASREShskeLALLV 525
Cdd:cd10820    8 APWGFRLQGGSEQKKPLQVAKIRKKSKAALAG--LCEGDELLSINGKPCADLSHSEAMDLIDSSGDT----LQLLI 77
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 716-820 3.88e-08

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 54.71  E-value: 3.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 716 QLTLTNTQSGQQRSITHLQYVAWPDHGvPEDSSDFLDFVKSVRSMRQESVPL-----------------MVHCSAGIGRT 778
Cdd:cd14559  104 MYNLKITDGNKTITIPVVHVTNWPDHT-AISSEGLKELADLVNKSAEEKRNFykskgssaindknkllpVIHCRAGVGRT 182

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 528504074 779 GVLItmeTAMTLMEKEKPVYPLEVITLMREQR-AMLVQTSCQF 820
Cdd:cd14559  183 GQLA---AAMELNKSPNNLSVEDIVSDMRTSRnGKMVQKDEQL 222
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 439-529 8.20e-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: 50.33  E-value: 8.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 439 LLLVRISPDQDGKFGFNVKGGVDQKMPLAISHVNLASPAGRcvPPLMEGDQVLLINGRDISEHTHQQVVMFIKAsreshS 518
Cdd:cd06737    2 LRLVRLDRRGPESLGFSVRGGLEHGCGLFVSHVSPGSQADN--KGLRVGDEIVRINGYSISQCTHEEVINLIKT-----K 74

                         90
                 ....*....|.
gi 528504074 519 KELALLVRRKG 529
Cdd:cd06737   75 KTVSLKVRHVG 85
FERM_F1_PTPN14_like cd17099
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 39-112 2.11e-07

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: 49.15  E-value: 2.11e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528504074  39 DGTTQNFTVNKHDAGHLLFDLACEHLNIVEKQYFSMQIsEDTSSSPRWLDPNKPFKKQL-KGSPPFFLMFRVRFF 112
Cdd:cd17099   12 DNTVLECTLSPESTGQDCLEYVAQRLELREIEYFGLRY-VNKKGQLRWVDLEKPLKKQLdKHAHEPLLYFGVMFY 85
PDZ_Lin-7-like cd06796
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 446-516 6.83e-07

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: 47.82  E-value: 6.83e-07
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gi 528504074 446 PDQDGKFGFNVKGGVDQKMPLAISHV---NLASPAGRcvppLMEGDQVLLINGRDISEHTHQQVVMFIKASRES 516
Cdd:cd06796    8 PKTEEGLGFNVMGGKEQNSPIYISRIipgGVADRHGG----LKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGS 77
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 726-823 1.05e-06

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 49.18  E-value: 1.05e-06
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gi 528504074 726 QQRSITHLQYVAwPDHGVPEDSSDFLDFVKSVRSMRQESVPLMVHCSAGIGRTGVLItmetAMTLMEKEKPVYPLEVITL 805
Cdd:cd14505   69 QQAGITWHHLPI-PDGGVPSDIAQWQELLEELLSALENGKKVLIHCKGGLGRTGLIA----ACLLLELGDTLDPEQAIAA 143

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gi 528504074 806 MREQRAMLVQTSCQFTFV 823
Cdd:cd14505  144 VRALRPGAIQTPKQENFL 161
FERM_F1_ERM_like cd17097
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 45-112 1.11e-06

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: 47.27  E-value: 1.11e-06
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gi 528504074  45 FTVNKHDAGHLLFDLACEHLNIVEKQYFSMQiSEDTSSSPRWLDPNKPFKKQLKGSP-PFFLMFRVRFF 112
Cdd:cd17097   14 FSIKPKAKGRELFDLVCRTIGLRETWYFGLQ-YENKKGRVAWLKPDKKVLTQDVSKNnTLKFFFLVKFY 81
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 441-525 1.35e-06

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: 46.66  E-value: 1.35e-06
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gi 528504074 441 LVRISPDQDGkFGFNVKGGVDQKMPLaISHVNLASPAGRCvpPLMEGDQVLLINGRDISEHTHQQVVMFIKASreshSKE 520
Cdd:cd06768    2 LCHLVKGPEG-YGFNLHAEKGRPGHF-IREVDPGSPAERA--GLKDGDRLVEVNGENVEGESHEQVVEKIKAS----GNQ 73


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gi 528504074 521 LALLV 525
Cdd:cd06768   74 VTLLV 78
PDZ_SYNJ2BP-like cd06709
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ...
 452-515 2.07e-06

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: 46.52  E-value: 2.07e-06
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gi 528504074 452 FGFNVKGGVDQK-MP----LAISHVNLASPA---GRcvppLMEGDQVLLINGRDISEHTHQQVVMFIKASRE 515
Cdd:cd06709   12 LGFNIVGGTDQPyIPndsgIYVAKIKEDGAAaidGR----LQEGDKILEINGQSLENLTHQDAVELFRNAGE 79
PDZ4_MAGI-1_3-like cd06734
PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 438-513 3.58e-06

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: 45.68  E-value: 3.58e-06
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gi 528504074 438 DLLLVRisPDQDGkFGFNVKGGVDQKMPLAISHVNLASPAGRCvPPLMEGDQVLLINGRDISEHTHQQVVMFIKAS 513
Cdd:cd06734    3 DVTLTR--RENEG-FGFVIISSVNKKSGSKIGRIIPGSPADRC-GQLKVGDRILAVNGISILNLSHGDIVNLIKDS 74
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 446-527 4.23e-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: 45.71  E-value: 4.23e-06
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gi 528504074 446 PDQDGKFGFNVKGGVD-------QKMP-LAISHVNLASPAGRCvpPLMEGDQVLLINGRDISEHTHQQVVMFIKASresh 517
Cdd:cd06702    6 VKAGGPLGLSIVGGSDhsshpfgVDEPgIFISKVIPDGAAAKS--GLRIGDRILSVNGKDLRHATHQEAVSALLSP---- 79

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gi 528504074 518 SKELALLVRR 527
Cdd:cd06702   80 GQEIKLLVRH 89
FERM_C_MYLIP_IDOL cd13195
FERM domain C-lobe of E3 ubiquitin ligase myosin regulatory light chain-interacting protein ...
 218-309 4.52e-06

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: 46.09  E-value: 4.52e-06
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gi 528504074 218 YGVELHHAQDASNPAVWVGITSGGValfchLICSS------FFPWINIIKISFKRKRFFVHLRRKHGElgHHVVSLSMPN 291
Cdd:cd13195    1 YGVEFFEVRNIEGQKLLIGVGPHGI-----TICNDdfevieRIPYTAIQMATSSGRVFTLTYLSDDGS--VKVLEFKLPS 73

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gi 528504074 292 SRACKNLWRSCVDHHTFY 309
Cdd:cd13195   74 TRAASGLYRAITEKHAFY 91
PDZ_SNX27-like cd23070
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density ...
 441-525 4.73e-06

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: 45.48  E-value: 4.73e-06
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gi 528504074 441 LVRISPDQDGkFGFNVKGGVDQKMPL---------AISHVNL------ASPAGrcvppLMEGDQVLLINGRDISEHTHQQ 505
Cdd:cd23070    2 VVTIVKSETG-FGFNVRGQVSEGGQLrsingelyaPLQHVSAvleggaADKAG-----VRKGDRILEVNGVNVEGATHKQ 75

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gi 528504074 506 VVMFIKASreshSKELALLV 525
Cdd:cd23070   76 VVDLIKSG----GDELTLTV 91
PDZ1_PDZD7-like cd10833
PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 439-529 4.88e-06

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: 45.50  E-value: 4.88e-06
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gi 528504074 439 LLLVRISPDQDGKFGFNVKGGVDQKMPLAISHV---NLASPAGRCVpplmeGDQVLLINGRDISEHTHQQVVMFIKAsre 515
Cdd:cd10833    1 IHTVTVEKSPDGSLGFSVRGGSEHGLGIFVSKVeegSAAERAGLCV-----GDKITEVNGVSLENITMSSAVKVLTG--- 72

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gi 528504074 516 shSKELALLVRRKG 529
Cdd:cd10833   73 --SNRLRMVVRRMG 84
PDZ5_MAGI-1_3-like cd06735
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 452-527 4.92e-06

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: 45.26  E-value: 4.92e-06
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gi 528504074 452 FGFNVKGGVD-QKMPLAISHVNLASPAGRCvPPLMEGDQVLLINGRDISEHTHQQVVMFIKasreSHSKELALLVRR 527
Cdd:cd06735   13 FGFSIRGGREyNNMPLYVLRLAEDGPAQRD-GRLRVGDQILEINGESTQGMTHAQAIELIR----SGGSVVRLLLRR 84
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 739-823 6.63e-06

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 46.50  E-value: 6.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 739 PDHGVPEDSS--DFLDFVKSVRSMRQesvPLMVHCSAGIGRTGvliTMeTAMTLMEKEKpVYPLEVITLMREQRAMLVQT 816
Cdd:cd14504   58 EDYTPPTLEQidEFLDIVEEANAKNE---AVLVHCLAGKGRTG---TM-LACYLVKTGK-ISAVDAINEIRRIRPGSIET 129


                 ....*..
gi 528504074 817 SCQFTFV 823
Cdd:cd14504  130 SEQEKFV 136
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 218-311 7.37e-06

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: 44.97  E-value: 7.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 218 YGVELHHAQDASNPAVWVGIT-SGGVALFCHLICSSFFPWINIIKISFkRKRFFVHLRRKHGElghhVVSLSMPNSRACK 296
Cdd:cd13188    1 YGEESFPAKDEQGNEVLIGASlEGIFVKHDNGRPPVFFRWEDIKNVIN-HKRTFSIECQNSEE----TVQFQFEDAETAK 75

                         90
                 ....*....|....*
gi 528504074 297 NLWRSCVDHHTFYNR 311
Cdd:cd13188   76 YVWKLCVLQHKFYRQ 90
FERM_F1_FRMD4 cd17103
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 33-114 7.61e-06

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


Pssm-ID: 340623  Cd Length: 91  Bit Score: 44.97  E-value: 7.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  33 CLVLFPDGTTQNFTVN-KHDAGHLLfDLACEHLNIVEKQYFSMQIsEDTSSSPRWLDPNK-------PFKkqlKGSPPFF 104
Cdd:cd17103    5 CQVVLLDDRRLEILVQpKLLAGDLL-DLVASHFNLKEKEYFGLAY-EDETGHYNWLQLDKrvldhefPKK---WSSGPLV 79

                         90
                 ....*....|
gi 528504074 105 LMFRVRFFIS 114
Cdd:cd17103   80 LHFAVKFYVE 89
PDZ4_GRIP1-2-like cd06686
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 442-535 7.73e-06

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: 45.03  E-value: 7.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 442 VRISPDQDGKFGFNVKGGVDQKMPL----AISHVNLASPAGRC-VppLMEGDQVLLINGRDISEHTHQQVVMFIkasRES 516
Cdd:cd06686   10 VILRGDPLKGFGIQLQGGVFATETLssppLISFIEPDSPAERCgV--LQVGDRVLSINGIPTEDRTLEEANQLL---RDS 84

                         90
                 ....*....|....*....
gi 528504074 517 HSKelallvrrkgVSLRVE 535
Cdd:cd06686   85 ASK----------VTLEIE 93
PDZ_PDZD11-like cd06752
PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic ...
 453-517 8.26e-06

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: 44.61  E-value: 8.26e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528504074 453 GFNVKGGVDQKMPLAISHVNLASPAGRCvpPLMEGDQVLLINGRDISEHTHQQVVMFIKASRESH 517
Cdd:cd06752   14 GFNIRGGKASGLGIFISKVIPDSDAHRL--GLKEGDQILSVNGVDFEDIEHSEAVKVLKTAREIQ 76
FERM_C_FRMD4A_FRMD4B cd13191
FERM domain C-lobe of FERM domain-containing protein 4A and 4B (FRMD4A and 4B); FRMD4A is part ...
 219-309 1.37e-05

FERM domain C-lobe of FERM domain-containing protein 4A and 4B (FRMD4A and 4B); FRMD4A is part of the Par-3/FRMD4A/cytohesin-1 complex that activates Arf6, a central player in actin cytoskeleton dynamics and membrane trafficking, during junctional remodeling and epithelial polarization. The Par-3/Par-6/aPKC/Cdc42 complex regulates the conversion of primordial adherens junctions (AJs) into belt-like AJs and the formation of linear actin cables. When primordial AJs are formed, Par-3 recruits scaffolding protein FRMD4A which connects Par-3 and the Arf6 guanine-nucleotide exchange factor (GEF), cytohesin-1. FRMD4B (also called GRP1-binding protein, GRSP1) is a novel member of GRP1 signaling complexes that are recruited to plasma membrane ruffles in response to insulin receptor signaling. The GRSP1/FRMD4B protein contains a FERM protein domain as well as two coiled coil domains and may function as a scaffolding protein. GRP1 and GRSP1 interact through the coiled coil domains in the two proteins. 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: 270012  Cd Length: 113  Bit Score: 45.03  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 219 GVELHHAQDASNPAVWVGITSGGVALFCH---LICSSFFPWINIIKISFKRKRFFV----------HLRRKHGELGHHVV 285
Cdd:cd13191    1 GVHYYEVKDKNGIPWWLGVSYKGIGQYDLqdkVKPRKFFQWKQLENLYFRDRKFSIevrdprrnshRSRRTFQSSSVSVH 80

                         90       100
                 ....*....|....*....|....
gi 528504074 286 SLSMPNSRACKNLWRSCVDHHTFY 309
Cdd:cd13191   81 VWYGQTPALCKTIWSMAIAQHQFY 104
PDZ_RGS12-like cd06710
PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 ...
 452-514 1.66e-05

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: 43.39  E-value: 1.66e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528504074 452 FGFNVKGgvdqKMPLAISHVNLASPAGrcVPPLMEGDQVLLINGRDISEHTHQQVVMFIKASR 514
Cdd:cd06710   12 YGFTISG----QAPCVLSCVVRGSPAD--VAGLKAGDQILAVNGINVSKASHEDVVKLIGKCT 68
PDZ3_MAGI-1_3-like cd06733
PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 448-527 1.73e-05

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: 43.75  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 448 QDGKFGFNVKGGVDQKMPLAISHVNLASPA---GRcvppLMEGDQVLLINGRDISEHTHQQVVMFIKASreSHSKELALL 524
Cdd:cd06733    9 QETGFGFRILGGTEEGSQVSIGAIVPGGAAdldGR----LRTGDELLSVDGVNVVGASHHKVVDLMGNA--ARNGQVNLT 82


                 ...
gi 528504074 525 VRR 527
Cdd:cd06733   83 VRR 85
PDZ7_MUPP1-PD6_PATJ-like cd06671
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ...
 468-513 1.88e-05

PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 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 7 of MUPP1 and PDZ domain 6 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 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: 467159 [Multi-domain]  Cd Length: 96  Bit Score: 43.85  E-value: 1.88e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 528504074 468 ISHVNLASPAGRCvPPLMEGDQVLLINGRDISEHTHQQVVMFIKAS 513
Cdd:cd06671   40 IKHVLEDSPAGRN-GTLKTGDRILEVNGVDLRNATHEEAVEAIRNA 84
PDZ2_L-delphilin-like cd06744
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
 441-513 3.10e-05

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: 42.65  E-value: 3.10e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528504074 441 LVRISPdQDGKFGFNVKGgvdqKMPLAISHVNLASPAGRCvpPLMEGDQVLLINGRDISEHTHQQVVMFIKAS 513
Cdd:cd06744    1 TVRVYR-GNGSFGFTLRG----HAPVYIESVDPGSAAERA--GLKPGDRILFLNGLDVRNCSHDKVVSLLQGS 66
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 439-526 5.15e-05

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: 42.35  E-value: 5.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 439 LLLVRISPDQDGkFGFNVKGGVDQKMPLAISHVNLASPAGRcvPPLMEGDQVLLINGRDISEHTHQQVVMFIKAsreshS 518
Cdd:cd06740    3 QVTLKRSKSHEG-LGFSIRGGAEHGVGIYVSLVEPGSLAEK--EGLRVGDQILRVNDVSFEKVTHAEAVKILRV-----S 74


                 ....*...
gi 528504074 519 KELALLVR 526
Cdd:cd06740   75 KKLVLSVR 82
FERM_F1_PTPN13_like cd17101
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 34-113 5.61e-05

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


Pssm-ID: 340621  Cd Length: 97  Bit Score: 42.55  E-value: 5.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  34 LVLFPDGTTQNFTVNKHDAGHLLFDLACEHLNIVEKQYF--SMQISEDTssspRWLDPN----KPFKKQLK--------- 98
Cdd:cd17101    5 NVVLLNGQRLQVAVDVKTTVQDLFDQVCDHLGLQETELFglAVLKDGEY----FFLDPDtklsKYAPKGWKseakkglkg 80

                         90
                 ....*....|....*
gi 528504074  99 GSPPFFLMFRVRFFI 113
Cdd:cd17101   81 GKPVFTLYFRVKFYV 95
PDZ1_MAGI-1_3-like cd06731
PDZ domain 1 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 452-509 5.70e-05

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: 42.20  E-value: 5.70e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528504074 452 FGFNVKGGVDQKMPLAISHVNLASPA---GRcvppLMEGDQVLLINGRDISEHTHQQVV-MF 509
Cdd:cd06731   13 FGFTIIGGDEPDEFLQIKSVVPDGPAaldGK----LRTGDVLVSVNDTCVLGYTHADVVkLF 70
PDZ_TAX1BP3-like cd10822
PDZ domain of tax1-binding protein 3 (TAX1BP3), and related domains; PDZ (PSD-95 (Postsynaptic ...
 451-527 8.45e-05

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: 41.94  E-value: 8.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 451 KFGFNVKGGVDQ---KMPLA-------ISHVNLASPAGRCvpPLMEGDQVLLINGRDISEHTHQQVVMFIKASREShske 520
Cdd:cd10822   14 ILGFSIGGGIDQdpsKNPFSytdkgiyVTRVSEGGPAEKA--GLQVGDKILQVNGWDMTMVTHKQAVKRLTKKKPV---- 87


                 ....*..
gi 528504074 521 LALLVRR 527
Cdd:cd10822   88 LRMLVTR 94
FERM_F1_FRMD4B cd17200
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 30-113 8.49e-05

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


Pssm-ID: 340720  Cd Length: 89  Bit Score: 42.18  E-value: 8.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074  30 GLLCLVLFPDGTTQNFTVNKHDAGHLLFDLACEHLNIVEKQYFSMQISEDTSSSP------RWLDPNKPfkkqlKGSPPF 103
Cdd:cd17200    2 GRHCQVHLLDDRKLELLVQPKLLSRELLDLVASHFNLKEKEYFGITFIDDTGQSNwlqldhRVLDHDLP-----KKSGPV 76

                         90
                 ....*....|
gi 528504074 104 FLMFRVRFFI 113
Cdd:cd17200   77 TLYFAVRFYI 86
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 737-810 3.84e-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: 41.82  E-value: 3.84e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528504074 737 AWPDHGVPEDS--SDFLDFVKSVrsMRQESVP---LMVHCSAGIGRTGVLItmetAMTLMEKEKPvyPLEVITLMREQR 810
Cdd:cd14500   65 PFDDGSPPPDDvvDDWLDLLKTR--FKEEGKPgacIAVHCVAGLGRAPVLV----AIALIELGMK--PEDAVEFIRKKR 135
PDZ_shroom2_3_4-like cd06750
PDZ domain of shroom2, shroom3, shroom4, and related domains; PDZ (PSD-95 (Postsynaptic ...
 453-527 3.94e-04

PDZ domain of shroom2, shroom3, shroom4, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of shroom2, shroom3, shroom4, and related domains. Shroom family proteins shroom2 (also known as apical-like protein; protein APXL), shroom3 (also known as shroom-related protein), and shroom4 (also known as second homolog of apical protein) are essential regulators of cell morphology during animal development; they regulate cell architecture by directing the subcellular distribution and activation of Rho kinase (ROCK), which results in the localized activation of non-muscle myosin. The interaction between shroom and ROCK is mediated by the shroom domain 2 (SD2). 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 shroom2,3,4-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467232 [Multi-domain]  Cd Length: 82  Bit Score: 40.01  E-value: 3.94e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528504074 453 GFNVKGGVDQKMPLAISHVNLASPAGRcVPPLMEGDQVLLINGRDISEhTHQQVVMFIKASReshsKELALLVRR 527
Cdd:cd06750   14 GFTLKGGLEHGEPLVISKIEEGGKAAS-VGKLQVGDEVVNINGVPLSG-SRQEAIQLVKGSH----KTLKLVVRR 82
PRK15375 PRK15375
type III secretion system effector GTPase-activating protein SptP;
672-820 3.96e-04

type III secretion system effector GTPase-activating protein SptP;


Pssm-ID: 185273 [Multi-domain]  Cd Length: 535  Bit Score: 44.02  E-value: 3.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 672 LTTLTERGRTKCHQYwphPPEVR-DYGYLQVCCHSEECNLAY---VTRQLTLTNTQSGQQRSITHLQYVAWPDHGvPEDS 747
Cdd:PRK15375 364 LVVLTSEDQMQAKQL---PPYFRgSYTFGEVHTNSQKVSSASqgeAIDQYNMQLSCGEKRYTIPVLHVKNWPDHQ-PLPS 439

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 748 SDFLDFVKS-VRSMRQESVP---------LMVHCSAGIGRTGvliTMETAMTLmeKEKPVYPLEVITL-MREQR-AMLVQ 815
Cdd:PRK15375 440 TDQLEYLADrVKNSNQNGAPgrsssdkhlPMIHCLGGVGRTG---TMAAALVL--KDNPHSNLEQVRAdFRNSRnNRMLE 514


                 ....*
gi 528504074 816 TSCQF 820
Cdd:PRK15375 515 DASQF 519
PDZ_ARHGEF11-12-like cd23069
PDZ domain of ARHGEF11, ARHGEF12, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 442-524 4.06e-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: 39.68  E-value: 4.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 442 VRISPDQDGkFGFNVKGgvdqKMPLAISHVNLASPAGRCvpPLMEGDQVLLINGRDISEHTHQQVVMFIKAsreSHSKEL 521
Cdd:cd23069    4 VVIQRDENG-YGLTVSG----DNPVFVQSVKEGGAAYRA--GVQEGDRIIKVNGTLVTHSNHLEVVKLIKS---GSYVAL 73


                 ...
gi 528504074 522 ALL 524
Cdd:cd23069   74 TLL 76
PDZ2-PTPN13_FRMPD2-like cd06792
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ...
 448-511 4.23e-04

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: 39.89  E-value: 4.23e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 448 QDGKFGFNVKGGVDQKMPLA---ISHVNLASPA---GRcvppLMEGDQVLLINGRDISEHTHQQVVMFIK 511
Cdd:cd06792   10 KDGSLGISVTGGINTSVRHGgiyVKSLVPGGAAeqdGR----IQKGDRLLEVNGVSLEGVTHKQAVECLK 75
PDZ2_FL-whirlin cd06741
PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 450-529 4.40e-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: 39.94  E-value: 4.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 450 GKFGFNVKGGVDQKMPLAISHVNLASPAGRCvpPLMEGDQVLLINGRDISEHTHQQVVMFIKAsreshSKELALLVRRKG 529
Cdd:cd06741   12 QSLGLMIRGGAEYGLGIYVTGVDPGSVAENA--GLKVGDQILEVNGRSFLDITHDEAVKILKS-----SKHLIMTVKDVG 84
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 766-825 5.56e-04

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: 40.41  E-value: 5.56e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528504074 766 PLMVHCSAGIGRTGVLITMetaMTLMEKEKPVYplEVITLMREQR-AMLVQTSCQFTFVCE 825
Cdd:cd14494   58 PVLVHCKAGVGRTGTLVAC---YLVLLGGMSAE--EAVRIVRLIRpGGIPQTIEQLDFLIK 113
PDZ1_INAD-like cd23063
PDZ domain 1 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 442-511 8.95e-04

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: 39.03  E-value: 8.95e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504074 442 VRISPDQDGKFGF-----NVKGGVDQKMP-LAISHVNLASPAGRCvPPLMEGDQVLLINGRDISEHTHQQVVMFIK 511
Cdd:cd23063    2 VVIEKTEKKSFGIcivrgEVKVSPNTKTTgIFIKGIIPDSPAHKC-GRLKVGDRILSVNGNDVRNSTEQAAIDLIK 76
PDZ_GOPC-like cd06800
PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and ...
 442-507 1.19e-03

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: 38.51  E-value: 1.19e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504074 442 VRISPDQDGKFGFNVKGGVDQKMPLAISHVNLASPAGRCvPPLMEGDQVLLINGRDISEHTHQQVV 507
Cdd:cd06800    3 VLLSKEPHEGLGISITGGKEHGVPILISEIHEGQPADRC-GGLYVGDAILSVNGIDLRDAKHKEAV 67
PDZ_FRMPD1_3_4-like cd06769
PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related ...
 442-516 1.23e-03

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: 38.38  E-value: 1.23e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504074 442 VRISPDQDGKFGFNVKGgvdqKMPLAISHVNLASPA-GRCVPplmeGDQVLLINGRDISEHTHQQVVMFIKASRES 516
Cdd:cd06769    2 VEIQRDAVLGFGFVAGS----ERPVVVRSVTPGGPSeGKLLP----GDQILKINNEPVEDLPRERVIDLIRECKDS 69
PDZ3_Dlg1-2-4-like cd06795
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 453-513 1.61e-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: 38.49  E-value: 1.61e-03
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gi 528504074 453 GFNVKGGVDQKmPLAISHVNLASPA---GRcvppLMEGDQVLLINGRDISEHTHQQVVMFIKAS 513
Cdd:cd06795   15 GFNIVGGEDGE-GIFISFILAGGPAdlsGE----LRRGDQILSVNGVDLRNATHEQAAAALKNA 73
PDZ2_MAGI-1_3-like cd06732
PDZ domain 2 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 479-527 1.82e-03

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: 37.92  E-value: 1.82e-03
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gi 528504074 479 RCvPPLMEGDQVLLINGRDISEHTHQQVVMFIKasreSHSK--ELALLVRR 527
Cdd:cd06732   36 RC-RGLQEGDLIVEINGQNVQNLSHAQVVDVLK----ECPKgsEVTLLVQR 81
PDZ2_GRIP1-2-like cd06681
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 449-525 1.82e-03

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: 37.98  E-value: 1.82e-03
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gi 528504074 449 DGKFGFNVKGGVDQKM----PLAISHVNLASPA---GRCVPplmeGDQVLLINGRDISEHTHQQVVMFIKASreshSKEL 521
Cdd:cd06681   11 GNSFGFVIRGGAHEDRnksrPLTVTHVRPGGPAdreGTIKP----GDRLLSVDGISLHGATHAEAMSILKQC----GQEA 82


                 ....
gi 528504074 522 ALLV 525
Cdd:cd06681   83 TLLI 86
PDZ_SHANK1_3-like cd06746
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ...
 452-513 2.00e-03

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: 38.34  E-value: 2.00e-03
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gi 528504074 452 FGFNVKGGVDQKMPLA------------ISHVNLASPAGRCvpPLMEGDQVLLINGRDISEHTHQQVVMFIKAS 513
Cdd:cd06746   18 FGFVLRGAKAVGPILEftptpafpalqyLESVDPGGVADKA--GLKKGDFLLEINGEDVVKASHEQVVNLIRQS 89
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 739-782 2.05e-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: 39.74  E-value: 2.05e-03
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gi 528504074 739 PDHGVPEDS--SDFLDFVKSvrsmrqESVPLMVHCSAGIGRTGVLI 782
Cdd:cd14499   88 PDGSTPSDDivKKFLDICEN------EKGAIAVHCKAGLGRTGTLI 127
FERM_C_FRMD1_FRMD6 cd13185
FERM domain C-lobe of FERM domain containing 1 and 6 proteins; FRMD6 (also called willin and ...
 216-269 2.16e-03

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: 38.44  E-value: 2.16e-03
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gi 528504074 216 DLYGVELHHAQDASNpaVWVGITSGGV-----ALFCHLICSSFfPWINIIKISFKRKRF 269
Cdd:cd13185    6 HLYRLRKSKKETPGS--VLLGITAKGIqiyqeSDGEQQLLRTF-PWSNIGKLSFDRKKF 61
PDZ2_PDZD2-like cd06758
PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 ...
 447-513 2.36e-03

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: 37.72  E-value: 2.36e-03
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gi 528504074 447 DQDGkFGFNVKGGV-DQKMPLAI--SHVNLASPAGRCvPPLMEGDQVLLINGRDISEHTHQQVVMFIKAS 513
Cdd:cd06758   10 EKGG-LGIQITGGKgSKRGDIGIfvAGVEEGGSADRD-GRLKKGDELLMINGQSLIGLSHQEAVAILRSS 77
PDZ_RapGEF2_RapGEF6-like cd06755
PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange ...
 446-513 2.50e-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: 37.63  E-value: 2.50e-03
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gi 528504074 446 PDQDGKFGFNVKGGVDQKMPLAISHVNLASPA---GrcvppLMEGDQVLLINGRDISEHTHQQVVMFIKAS 513
Cdd:cd06755    8 PSRESPLHFSLLGGSEKGFGIFVSKVEKGSKAaeaG-----LKRGDQILEVNGQNFENITLKKALEILRNN 73
PDZ2_harmonin cd06738
PDZ domain 2 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 450-526 2.54e-03

PDZ domain 2 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 2 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 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: 467220 [Multi-domain]  Cd Length: 82  Bit Score: 37.68  E-value: 2.54e-03
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gi 528504074 450 GKFGFNVKGGVDQKMPLAISHVN---LASPAGrcvppLMEGDQVLLINGRDISEHTHQQVVMFIKASReshskELALLVR 526
Cdd:cd06738   13 RGLGCSISSGPTQKPGIFISNVKpgsLAEEVG-----LEVGDQIVEVNGTSFTNVDHKEAVMALKSSR-----HLTITVR 82
PDZ2-PDZRN4-like cd06716
PDZ domain 2 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 438-527 3.02e-03

PDZ domain 2 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PDZRN4, PDZRN3-B, and related domains. PDZRN4 (also known as ligand of numb protein X 4, and SEMACAP3-like protein) contains an N-terminal RING domain and two tandem repeat PDZ domains. It is involved in the progression of cancer, including human liver cancer and breast cancer, and may contribute to the tumorigenesis of rectal adenocarcinoma. Danio rerio PDZRN3-B may participate in neurogenesis: the first PDZ domain of Danio rerio Pdzrn3 interacts with Kidins220 (Kinase D-interacting substrate 220 kD, also named Ankyrin Repeat-Rich Membrane Spanning), a crucial mediator of signal transduction in neural tissues. 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 PDZRN4-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: 467200 [Multi-domain]  Cd Length: 88  Bit Score: 37.64  E-value: 3.02e-03
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gi 528504074 438 DLLLVRISPDQdgKFGFNVKGGVDQKMPLAI--SHVNLASPA---GRcvppLMEGDQVLLINGRDIseHTHQQVVMFIKA 512
Cdd:cd06716    5 EVTLKRSNSQE--KLGLTLCYRTDDEEDTGIyvSEVDPNSIAakdGR----IREGDQILQINGVDV--QNREEAIALLSE 76

                         90
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gi 528504074 513 SREShskeLALLVRR 527
Cdd:cd06716   77 EEKS----ITLLVAR 87
FERM_F1_Moesin cd17237
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in moesin and ...
 45-112 3.56e-03

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


Pssm-ID: 340757  Cd Length: 84  Bit Score: 37.42  E-value: 3.56e-03
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gi 528504074  45 FTVNKHDAGHLLFDLACEHLNIVEKQYFSMQIsEDTSSSPRWLDPNKPFKKQ-LKGSPPFFLMFRVRFF 112
Cdd:cd17237   15 FAIQPNTTGKQLFDQVVKTIGLREVWFFGLQY-QDTKGFSTWLKLNKKVTAQdVRKESPLLFKFRAKFY 82
Y_phosphatase3 pfam13350
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
 735-791 3.74e-03

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


Pssm-ID: 463853 [Multi-domain]  Cd Length: 243  Bit Score: 39.92  E-value: 3.74e-03
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gi 528504074  735 YVAWPDHGVPEdssdfldFVKSVRSMRQESVPLMVHCSAGIGRTGVLitmeTAMTLM 791
Cdd:pfam13350 107 YRDMVTSARAA-------YRALFEALADNDGPVLFHCTAGKDRTGVA----AALLLS 152
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 ...
 453-527 3.91e-03

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: 37.24  E-value: 3.91e-03
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gi 528504074 453 GFNVKGGVDQKM-PLAISHV---NLASPAGRcvppLMEGDQVLLINGRDISEHTHQQVVMFIKASReshSKELALLVRR 527
Cdd:cd06762   15 GFSLAGGSDLENkSITVHRVfpsGLAAQEGT----IQKGDRILSINGKSLKGVTHGDALSVLKQAR---LPKVAVVVIR 86
PDZ_tamalin_CYTIP-like cd06713
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ ...
 468-513 4.04e-03

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: 37.22  E-value: 4.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 528504074 468 ISHVNLASPAGRCvpPLMEGDQVLLINGRDISEHTHQQVVMFIKAS 513
Cdd:cd06713   39 VCRVHEDSPAYLA--GLTAGDVILSVNGVSVEGASHQEIVELIRSS 82
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
 726-790 4.04e-03

Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in abundance in seeds and acting as an inorganic phosphate reservoir. Phytases are phosphatases that hydrolyze phytate to less-phosphorylated myo-inositol derivatives and inorganic phosphate. The active-site sequence (HCXXGXGR) of the phytase identified from the gut micro-organizm Selenomonas ruminantium forms a loop (P loop) at the base of a substrate binding pocket that is characteriztic of protein tyrosine phosphatases (PTPs). The depth of this pocket is an important determinant of the substrate specificity of PTPs. In humans this enzyme is thought to aid bone mineralization and salvage the inositol moiety prior to apoptosis.


Pssm-ID: 464208 [Multi-domain]  Cd Length: 157  Bit Score: 38.83  E-value: 4.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528504074  726 QQRSITHLQY--VAWPDHGVPEDSsDFLDFVKSVRSMrQESVPLMVHCSAGIGRTgvliTmeTAMTL 790
Cdd:pfam14566  94 LKAEGPGVDYrrIPITDEKAPLEE-DFDALISIVKDA-PEDTALVFNCQMGRGRT----T--TAMVI 152
PDZ_rhophilin-like cd06712
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 448-534 4.26e-03

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: 36.79  E-value: 4.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 448 QDGKFGFNVKGGVdqkmPLAISHVN---LASPAGrcvppLMEGDQVLLINGRDISEHTHQQVVMFIKASREshskelall 524
Cdd:cd06712    9 EEGGFGFTLRGDS----PVQVASVDpgsCAAEAG-----LKEGDYIVSVGGVDCKWSKHSEVVKLLKSAGE--------- 70

                         90
                 ....*....|
gi 528504074 525 vrrKGVSLRV 534
Cdd:cd06712   71 ---EGLELQV 77
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 738-810 4.29e-03

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 38.85  E-value: 4.29e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528504074 738 WP--DHGVPEDS--SDFLDFVKSVRSmRQESVP--LMVHCSAGIGRTGVLItmetAMTLMEKeKPVYPLEVITLMREQR 810
Cdd:PTZ00242  67 WPfdDGAPPPKAviDNWLRLLDQEFA-KQSTPPetIAVHCVAGLGRAPILV----ALALVEY-GGMEPLDAVGFVREKR 139
PDZ4_PTPN13-like cd06696
PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 448-527 5.52e-03

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: 36.52  E-value: 5.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 448 QDGKFGFNVKGGVDQkMPLAISHVnLASPA---GRcvppLMEGDQVLLINGRDISEHTHQQVVMFIKASreshSKELALL 524
Cdd:cd06696   12 EKGSLGFTVTKGKDD-NGCYIHDI-VQDPAksdGR----LRPGDRLIMVNGVDVTNMSHTEAVSLLRAA----PKEVTLV 81


                 ...
gi 528504074 525 VRR 527
Cdd:cd06696   82 LGR 84
PDZ_densin_erbin-like cd06749
PDZ domain of densin, erbin, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 452-527 5.93e-03

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: 36.54  E-value: 5.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 452 FGFNVKGGVDQK--------MPLAISHVNLASPAGRCVPPlmeGDQVLLINGRDISEHTHQQVVMFIKASRESHSkelaL 523
Cdd:cd06749   11 LGFSISGGIGSQgnpfrpddDGIFVTKVQPDGPASKLLQP---GDKILEVNGYDFVNIEHGQAVSLLKSFQNTVD----L 83


                 ....
gi 528504074 524 LVRR 527
Cdd:cd06749   84 VVER 87
PDZ2_Scribble-like cd06703
PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 484-528 6.07e-03

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: 36.86  E-value: 6.07e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 528504074 484 LMEGDQVLLINGRDISEHTHQQVVMFIKasreSHSKELALLVRRK 528
Cdd:cd06703   51 LQVGDRVLSINGVDVTEARHDQAVALLT----SSSPTITLVVERE 91
DSP_DUSP5 cd14639
dual specificity phosphatase domain of dual specificity protein phosphatase 5; Dual ...
 690-823 6.66e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 5; Dual specificity protein phosphatase 5 (DUSP5) functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other mitogen-activated protein kinase (MAPK) phosphatases (MKPs), it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class I subfamily and is a mitogen- and stress-inducible nuclear MKP. DUSP5 preferentially dephosphorylates extracellular signal-regulated kinase (ERK), and is involved in ERK signaling and ERK-dependent inflammatory gene expression in adipocytes. It also plays a role in regulating pressure-dependent myogenic cerebral arterial constriction, which is crucial for the maintenance of constant cerebral blood flow to the brain. DUSP5 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350487 [Multi-domain]  Cd Length: 138  Bit Score: 37.97  E-value: 6.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 690 PPEVRDYGYLQVCCHSEECNLA---YVTRQLTLTNTQSGQQRSITHLQYVAWPDHGVPEDSSDFLDFVKSVRSMRQESVP 766
Cdd:cd14639    1 PVEILPFLYLGSAYHASKCEFLanlHITALLNVSRRSSEACKGQYHYKWIPVEDSHTADISSHFQEAIDFIDCVRRAGGK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 528504074 767 LMVHCSAGIGRTGVLitmetAMTLMEKEKPVYPLEVITLMREQRAMLvqtSCQFTFV 823
Cdd:cd14639   81 VLVHCEAGISRSPTI-----CMAYLMKTKRFRLEEAFDYIKQRRSLI---SPNFGFM 129
PDZ2_PDZD7-like cd10834
PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 447-529 7.73e-03

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: 36.21  E-value: 7.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504074 447 DQDGKF-GFNVKGGVDQKMPLAISHVNLASPAGRcvPPLMEGDQVLLINGRDISEHTHQQVVMFIKAsreshSKELALLV 525
Cdd:cd10834    9 TSDDYClGFNIRGGSEYGLGIYVSKVDPGGLAEQ--NGIKVGDQILAVNGVSFEDITHSKAVEVLKS-----QTHLMLTI 81


                 ....
gi 528504074 526 RRKG 529
Cdd:cd10834   82 KEVG 85
 
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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