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Conserved domains on  [gi|218505829|ref|NP_035337|]
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tyrosine-protein phosphatase non-receptor type 3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 631-904 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: 599.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 631 EGSMELLKKGLESGTVLIQFEQLYRKKPGLAVSFAKLPQNLDKNRYKDVLPYDTTRVLLQGNEDYINASYVNMEMPAANL 710
Cdd:cd14600    1 EESMAQLKKGLESGTVLIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQGNEDYINASYVNMEIPSANI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 711 VNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQCQTEDCTIAYVSREMLV 790
Cdd:cd14600   81 VNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 791 TNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVDGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYP 870
Cdd:cd14600  161 TNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYP 240

                        250       260       270
                 ....*....|....*....|....*....|....
gi 218505829 871 LDIVRKMRDQRAMMVQTSSQYKFVCEAILRVYEE 904
Cdd:cd14600  241 LDIVRKMRDQRAMMVQTSSQYKFVCEAILRVYEE 274
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 31-222 9.18e-57

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: 194.05  E-value: 9.18e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829    31 CSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPVDSPRWLEASKPLRKQLKGGFPCTLHFRVRYF 110
Cdd:smart00295   2 LKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRHWLDPAKTLLDQDVKSEPLTLYFRVKFY 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829   111 IPDPNTLQQEQTRH-LYFLQLKMDVCEGRLTCPLNSAVVLASYAVQSHFGDFNSSIH-HPGYLADSQFIPDQ------ND 182
Cdd:smart00295  82 PPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQlldsrkLK 161

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 218505829   183 DFLSKVESLHEQHSGLKQSEAESCYINIARTLDFYGVELH 222
Cdd:smart00295 162 EWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
PDZ_PTPN3-4-like cd06706
PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein ...
 506-595 1.93e-56

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: 188.67  E-value: 1.93e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 506 GYLVLIRITPDEEGRFGFNLKGGVDQKMPLVVSRINPESPADTCMPKLNEGDQIVLINGRDISEHTHDQVVMFIKASRES 585
Cdd:cd06706    1 DGLVLIRMKPDENGRFGFNVKGGVDQKMPVIVSRVAPGTPADLCIPRLNEGDQVLLINGRDISEHTHDQVVMFIKASRER 80

                         90
                 ....*....|
gi 218505829 586 HSRELALVIR 595
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 ...
 216-309 3.46e-56

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: 188.29  E-value: 3.46e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 216 FYGVELHGGRDLHNLDLMIGIASAGIAVYRKYICTSFYPWVNILKISFKRKKFFIHQRQKQAESREHIVAFNMLNYRSCK 295
Cdd:cd13189    1 LYGVELHSARDSNNLELQIGVSSAGILVFQNGIRINTFPWSKIVKISFKRKQFFIQLRREPNESRDTILGFNMLSYRACK 80

                         90
                 ....*....|....
gi 218505829 296 NLWKSCVEHHSFFQ 309
Cdd:cd13189   81 NLWKSCVEHHTFFR 94
 
Name Accession Description Interval E-value
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 631-904 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: 599.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 631 EGSMELLKKGLESGTVLIQFEQLYRKKPGLAVSFAKLPQNLDKNRYKDVLPYDTTRVLLQGNEDYINASYVNMEMPAANL 710
Cdd:cd14600    1 EESMAQLKKGLESGTVLIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQGNEDYINASYVNMEIPSANI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 711 VNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQCQTEDCTIAYVSREMLV 790
Cdd:cd14600   81 VNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 791 TNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVDGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYP 870
Cdd:cd14600  161 TNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYP 240

                        250       260       270
                 ....*....|....*....|....*....|....
gi 218505829 871 LDIVRKMRDQRAMMVQTSSQYKFVCEAILRVYEE 904
Cdd:cd14600  241 LDIVRKMRDQRAMMVQTSSQYKFVCEAILRVYEE 274
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
649-900 4.01e-107

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 331.55  E-value: 4.01e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829   649 QFEQLYRKKPG-LAVSFAKLPQNLDKNRYKDVLPYDTTRVLLQGNE----DYINASYVNMEmpaaNLVNKYIATQGPLPN 723
Cdd:smart00194   5 EFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPgegsDYINASYIDGP----NGPKAYIATQGPLPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829   724 TCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDI-MDHGIFHIQCQTEDCTIAYVSREMLVTNTETGEEHTVT 802
Cdd:smart00194  81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEpLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829   803 HLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVDGE-PALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQR 881
Cdd:smart00194 161 HYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTgPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQR 240

                          250
                   ....*....|....*....
gi 218505829   882 AMMVQTSSQYKFVCEAILR 900
Cdd:smart00194 241 PGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
670-899 1.68e-103

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 321.11  E-value: 1.68e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  670 NLDKNRYKDVLPYDTTRVLLQ---GNEDYINASYVNMEmpaaNLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTL 746
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTgdpGPSDYINASYIDGY----KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  747 TERGRTKCHQYWPDPP-DIMDHGIFHIQCQ-TEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEF 824
Cdd:pfam00102  77 EEKGREKCAQYWPEEEgESLEYGDFTVTLKkEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDL 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 218505829  825 VKYVRSLRVDGE--PALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:pfam00102 157 LRKVRKSSLDGRsgPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 31-222 9.18e-57

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: 194.05  E-value: 9.18e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829    31 CSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPVDSPRWLEASKPLRKQLKGGFPCTLHFRVRYF 110
Cdd:smart00295   2 LKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRHWLDPAKTLLDQDVKSEPLTLYFRVKFY 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829   111 IPDPNTLQQEQTRH-LYFLQLKMDVCEGRLTCPLNSAVVLASYAVQSHFGDFNSSIH-HPGYLADSQFIPDQ------ND 182
Cdd:smart00295  82 PPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQlldsrkLK 161

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 218505829   183 DFLSKVESLHEQHSGLKQSEAESCYINIARTLDFYGVELH 222
Cdd:smart00295 162 EWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
PDZ_PTPN3-4-like cd06706
PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein ...
 506-595 1.93e-56

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: 188.67  E-value: 1.93e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 506 GYLVLIRITPDEEGRFGFNLKGGVDQKMPLVVSRINPESPADTCMPKLNEGDQIVLINGRDISEHTHDQVVMFIKASRES 585
Cdd:cd06706    1 DGLVLIRMKPDENGRFGFNVKGGVDQKMPVIVSRVAPGTPADLCIPRLNEGDQVLLINGRDISEHTHDQVVMFIKASRER 80

                         90
                 ....*....|
gi 218505829 586 HSRELALVIR 595
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 ...
 216-309 3.46e-56

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: 188.29  E-value: 3.46e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 216 FYGVELHGGRDLHNLDLMIGIASAGIAVYRKYICTSFYPWVNILKISFKRKKFFIHQRQKQAESREHIVAFNMLNYRSCK 295
Cdd:cd13189    1 LYGVELHSARDSNNLELQIGVSSAGILVFQNGIRINTFPWSKIVKISFKRKQFFIQLRREPNESRDTILGFNMLSYRACK 80

                         90
                 ....*....|....
gi 218505829 296 NLWKSCVEHHSFFQ 309
Cdd:cd13189   81 NLWKSCVEHHTFFR 94
FERM_F1_PTPN3 cd17193
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 28-111 1.77e-49

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: 169.26  E-value: 1.77e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  28 EVICSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPVDSPRWLEASKPLRKQLKGGFPCTLHFRV 107
Cdd:cd17193    1 EVICNVHFLDGSVQSFKVNKQDTGQVLLDMAYNHLGLTEREYFGLQHNEDSVDSPRWLEPSKPIRKQLKGGFPCSLHFRV 80


                 ....
gi 218505829 108 RYFI 111
Cdd:cd17193   81 RFFI 84
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 669-902 1.02e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 157.86  E-value: 1.02e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 669 QNLDKNRYKDVLPYDTTRVLL---QGNEDYINASYVNmempAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTT 745
Cdd:PHA02742  51 KNMKKCRYPDAPCFDRNRVILkieDGGDDFINASYVD----GHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITK 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 746 LTERGRTKCHQYW-PDPPDIMDHGIFHIQCQTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEF 824
Cdd:PHA02742 127 IMEDGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDF 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 825 VKYVRSL------------RVDGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYK 892
Cdd:PHA02742 207 VLAVREAdlkadvdikgenIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYI 286

                        250
                 ....*....|
gi 218505829 893 FvCEAILRVY 902
Cdd:PHA02742 287 F-CYFIVLIF 295
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 112-222 1.52e-33

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 125.07  E-value: 1.52e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  112 PDPNTLQQEQTRHLYFLQLKMDVCEGRLTCPLNSAVVLASYAVQSHFGDFNSSIHHPGYLADSQFIPDQN------DDFL 185
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLlrkmksKELE 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 218505829  186 SKVESLHEQHSGLKQSEAESCYINIARTLDFYGVELH 222
Cdd:pfam00373  81 KRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
666-891 1.54e-33

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 130.60  E-value: 1.54e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 666 KLPQNLDKNRYKDVLPYDTTRVllQGNEDYINASYVNMEMPaanlvNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTT 745
Cdd:COG5599   38 QNINGSPLNRFRDIQPYKETAL--RANLGYLNANYIQVIGN-----HRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLAS 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 746 LTE--RGRTKCHQYWPDPPDIMDHGIFHIQCQTEDCTIAYVSREMLVTNTETGEEHT-VTHLQYVAWPDHGVPdDSSDFL 822
Cdd:COG5599  111 DDEisKPKVKMPVYFRQDGEYGKYEVSSELTESIQLRDGIEARTYVLTIKGTGQKKIeIPVLHVKNWPDHGAI-SAEALK 189

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 218505829 823 EFVKYV----RSLRVDGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYP--LDIVRKMRDQRAM-MVQTSSQY 891
Cdd:COG5599  190 NLADLIdkkeKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVQITLsvEEIVIDMRTSRNGgMVQTSEQL 265
FERM_C pfam09380
FERM C-terminal PH-like domain;
226-312 2.82e-30

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 114.27  E-value: 2.82e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  226 DLHNLDLMIGIASAGIAVYRKYICTS-FYPWVNILKISFKRKKFFIHQRQKqaeSREHIVAFNMLNYRSCKNLWKSCVEH 304
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKILnLFPWREIRKISFKRKKFLIKLRDK---SSEETLGFYTESSRACKYLWKLCVEQ 77


                  ....*...
gi 218505829  305 HSFFQAKK 312
Cdd:pfam09380  78 HTFFRLRR 85
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 510-595 1.14e-18

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 81.17  E-value: 1.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  510 LIRITPDEEGRFGFNLKGGVDQK-MPLVVSRINPESPADTcmPKLNEGDQIVLINGRDISEHTHDQVVMFIKASREshsr 588
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKGGSDQGdPGIFVSEVLPGGAAEA--GGLKVGDRILSINGQDVENMTHEEAVLALKGSGG---- 74


                  ....*..
gi 218505829  589 ELALVIR 595
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 ...
 508-597 4.30e-16

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: 73.95  E-value: 4.30e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829   508 LVLIRITPDEEGrFGFNLKGGVDQKMPLVVSRINPESPADTCmpKLNEGDQIVLINGRDISEHTHDQVVMFIKASREShs 587
Cdd:smart00228   2 PRLVELEKGGGG-LGFSLVGGKDEGGGVVVSSVVPGSPAAKA--GLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGK-- 76

                           90
                   ....*....|
gi 218505829   588 reLALVIRRK 597
Cdd:smart00228  77 --VTLTVLRG 84
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 495-600 1.19e-04

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


Pssm-ID: 440556 [Multi-domain]  Cd Length: 341  Bit Score: 45.25  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 495 QYYCDKSDDGDGYLVLIR-------------ITPDEEGRFGFNLKG-----GVDQKMP---LVVSRINPESPADTcmPKL 553
Cdd:COG0793   12 DNYVDEYDDRDLAEGALNgmlgelgdphsyyLDPEEYEDFQESTSGefgglGAELGEEdgkVVVVSVIPGSPAEK--AGI 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 218505829 554 NEGDQIVLINGRDISEHTHDQVVMFIKA----------SRESHSRELALVIRRKAVR 600
Cdd:COG0793   90 KPGDIILAIDGKSVAGLTLDDAVKLLRGkagtkvtltiKRPGEGEPITVTLTRAEIK 146
 
Name Accession Description Interval E-value
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 631-904 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: 599.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 631 EGSMELLKKGLESGTVLIQFEQLYRKKPGLAVSFAKLPQNLDKNRYKDVLPYDTTRVLLQGNEDYINASYVNMEMPAANL 710
Cdd:cd14600    1 EESMAQLKKGLESGTVLIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQGNEDYINASYVNMEIPSANI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 711 VNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQCQTEDCTIAYVSREMLV 790
Cdd:cd14600   81 VNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 791 TNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVDGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYP 870
Cdd:cd14600  161 TNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYP 240

                        250       260       270
                 ....*....|....*....|....*....|....
gi 218505829 871 LDIVRKMRDQRAMMVQTSSQYKFVCEAILRVYEE 904
Cdd:cd14600  241 LDIVRKMRDQRAMMVQTSSQYKFVCEAILRVYEE 274
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 694-904 7.33e-151

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: 442.92  E-value: 7.33e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 694 DYINASYVNMEMPAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQ 773
Cdd:cd14541    1 DYINANYVNMEIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 774 CQTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVD-GEPALVHCSAGIGRTGVL 852
Cdd:cd14541   81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGmVEPTVVHCSAGIGRTGVL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 218505829 853 VTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAILRVYEE 904
Cdd:cd14541  161 ITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRVYEE 212
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 694-904 1.31e-120

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: 364.65  E-value: 1.31e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 694 DYINASYVNMEMPAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQ 773
Cdd:cd14601    1 DYINANYINMEIPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 774 CQTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVDG-EPALVHCSAGIGRTGVL 852
Cdd:cd14601   81 CHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKdEPVVVHCSAGIGRTGVL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 218505829 853 VTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAILRVYEE 904
Cdd:cd14601  161 ITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYEE 212
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
649-900 4.01e-107

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 331.55  E-value: 4.01e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829   649 QFEQLYRKKPG-LAVSFAKLPQNLDKNRYKDVLPYDTTRVLLQGNE----DYINASYVNMEmpaaNLVNKYIATQGPLPN 723
Cdd:smart00194   5 EFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPgegsDYINASYIDGP----NGPKAYIATQGPLPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829   724 TCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDI-MDHGIFHIQCQTEDCTIAYVSREMLVTNTETGEEHTVT 802
Cdd:smart00194  81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEpLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829   803 HLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVDGE-PALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQR 881
Cdd:smart00194 161 HYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTgPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQR 240

                          250
                   ....*....|....*....
gi 218505829   882 AMMVQTSSQYKFVCEAILR 900
Cdd:smart00194 241 PGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
670-899 1.68e-103

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 321.11  E-value: 1.68e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  670 NLDKNRYKDVLPYDTTRVLLQ---GNEDYINASYVNMEmpaaNLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTL 746
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTgdpGPSDYINASYIDGY----KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  747 TERGRTKCHQYWPDPP-DIMDHGIFHIQCQ-TEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEF 824
Cdd:pfam00102  77 EEKGREKCAQYWPEEEgESLEYGDFTVTLKkEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDL 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 218505829  825 VKYVRSLRVDGE--PALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:pfam00102 157 LRKVRKSSLDGRsgPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 695-896 1.60e-80

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: 258.75  E-value: 1.60e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 695 YINASYVNMEMPAanlvNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDI-MDHGIFHIQ 773
Cdd:cd00047    1 YINASYIDGYRGP----KEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKpLEYGDITVT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 774 CQTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVDGE-PALVHCSAGIGRTGVL 852
Cdd:cd00047   77 LVSEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNgPIVVHCSAGVGRTGTF 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 218505829 853 VTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCE 896
Cdd:cd00047  157 IAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 695-901 1.43e-71

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 234.96  E-value: 1.43e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 695 YINASYVNMEMPAANLVnkYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQC 774
Cdd:cd14538    1 YINASHIRIPVGGDTYH--YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLICGGRLEV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 775 QTEDCTI--AYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVDGePALVHCSAGIGRTGVL 852
Cdd:cd14538   79 SLEKYQSlqDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHNSG-PIVVHCSAGIGRTGVL 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 218505829 853 VTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAILRV 901
Cdd:cd14538  158 ITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 635-900 1.37e-70

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: 235.28  E-value: 1.37e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 635 ELLKKGLESGTVLIQFEQLYRKKPGLAVSFAKLPQNLDKNRYKDVLPYDTTRVLL----QGNEDYINASYVNMEMPAANL 710
Cdd:cd14599    3 KTLERKLEEGMVFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELvptkENNTGYINASHIKVTVGGEEW 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 711 vnKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWP---DPPDIMDHGIFHIQCQTEDCTIAYVSRE 787
Cdd:cd14599   83 --HYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPklgSKHSSATYGKFKVTTKFRTDSGCYATTG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 788 MLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLR------VDGE-----PALVHCSAGIGRTGVLVTME 856
Cdd:cd14599  161 LKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRrhtnsmLDSTkncnpPIVVHCSAGVGRTGVVILTE 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 218505829 857 TAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAILR 900
Cdd:cd14599  241 LMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 649-893 3.05e-69

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: 231.10  E-value: 3.05e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 649 QFEQLYRKKPGLAVSFAKLPQNLDKNRYKDVLPYDTTRVLLQ---GNE--DYINASYVNmempAANLVNKYIATQGPLPN 723
Cdd:cd14543    8 EYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPkrnGDErtDYINANFMD----GYKQKNAYIATQGPLPK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 724 TCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWP-DPPDIMDHGIFHIQCQTEDCTIAYVSREMLVTNTETGEEHTVT 802
Cdd:cd14543   84 TYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPlEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVT 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 803 HLQYVAWPDHGVPDDSS---DFLEFVKYVRSLRVD-----------GEPALVHCSAGIGRTGVLVTMEtaMCLiERNLPV 868
Cdd:cd14543  164 HFQFTSWPDFGVPSSAAallDFLGEVRQQQALAVKamgdrwkghppGPPIVVHCSAGIGRTGTFCTLD--ICL-SQLEDV 240

                        250       260
                 ....*....|....*....|....*...
gi 218505829 869 YPLDI---VRKMRDQRAMMVQTSSQYKF 893
Cdd:cd14543  241 GTLNVmqtVRRMRTQRAFSIQTPDQYYF 268
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 669-901 1.05e-68

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: 228.18  E-value: 1.05e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 669 QNLDKNRYKDVLPYDTTRVLLQGNEDYINASYVNMEMPAANLVnkYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTE 748
Cdd:cd14597    2 ENRKKNRYKNILPYDTTRVPLGDEGGYINASFIKMPVGDEEFV--YIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 749 RGRTKCHQYWPDPPD--IMDHGIFHIQCQTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVK 826
Cdd:cd14597   80 GGKIKCQRYWPEILGktTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLTFIS 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 218505829 827 YVRSLRVDGePALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAILRV 901
Cdd:cd14597  160 YMRHIHKSG-PIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVILYV 233
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 695-894 5.50e-68

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: 225.21  E-value: 5.50e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 695 YINASYVNMEmpaANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQC 774
Cdd:cd18533    1 YINASYITLP---GTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVEL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 775 Q--TEDCTIAYVSREMLVTnTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLR---VDGEPALVHCSAGIGRT 849
Cdd:cd18533   78 VseEENDDGGFIVREFELS-KEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNdsaSLDPPIIVHCSAGVGRT 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 218505829 850 GVLVTMETAMCLIERNL-----------PVYplDIVRKMRDQRAMMVQTSSQYKFV 894
Cdd:cd18533  157 GTFIALDSLLDELKRGLsdsqdledsedPVY--EIVNQLRKQRMSMVQTLRQYIFL 210
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 675-894 1.27e-65

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: 219.15  E-value: 1.27e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 675 RYKDVLPYDTTRVLLQG-----NEDYINASYvnmeMPAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTER 749
Cdd:cd14548    1 RYTNILPYDHSRVKLIPineeeGSDYINANY----IPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 750 GRTKCHQYWPDPPDIMDHGIFHIQCQTEDCTIAYVSREMLVTNTEtgEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVR 829
Cdd:cd14548   77 GRVKCDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERGD--EVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVR 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 218505829 830 SLRV-DGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFV 894
Cdd:cd14548  155 DYIKqEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFL 220
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 670-899 1.89e-64

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: 216.49  E-value: 1.89e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 670 NLDKNRYKDVLPYDTTRVLLQGNE-----DYINASYVNMEMPAanlvNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLT 744
Cdd:cd14553    3 NKPKNRYANVIAYDHSRVILQPIEgvpgsDYINANYCDGYRKQ----NAYIATQGPLPETFGDFWRMVWEQRSATIVMMT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 745 TLTERGRTKCHQYWPDpPDIMDHGIfhIQCQTEDCT--IAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFL 822
Cdd:cd14553   79 KLEERSRVKCDQYWPT-RGTETYGL--IQVTLLDTVelATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 823 EFVKYVRSLR-VDGEPALVHCSAGIGRTGVLVTMEtamCLIERNLPVYPLDI---VRKMRDQRAMMVQTSSQYKFVCEAI 898
Cdd:cd14553  156 AFLRRVKACNpPDAGPIVVHCSAGVGRTGCFIVID---SMLERIKHEKTVDIyghVTCLRAQRNYMVQTEDQYIFIHDAL 232


                 .
gi 218505829 899 L 899
Cdd:cd14553  233 L 233
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 674-900 2.84e-64

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: 215.91  E-value: 2.84e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 674 NRYKDVLPYDTTRVLL-----QGNEDYINASYvnmeMPAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTE 748
Cdd:cd14619    1 NRFRNVLPYDWSRVPLkpiheEPGSDYINANY----MPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCME 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 749 RGRTKCHQYWPDPPDIMDHGIFHIQCQTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYV 828
Cdd:cd14619   77 AGRVKCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLL 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 218505829 829 RS---LRVDGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAILR 900
Cdd:cd14619  157 RQwldQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 695-901 3.52e-64

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: 215.40  E-value: 3.52e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 695 YINASYVNMEMPAANLvnKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPD---PPDIMDHGIFH 771
Cdd:cd14540    1 YINASHITATVGGKQR--FYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTlggEHDALTFGEYK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 772 IQCQTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLR------VDGE----PALVH 841
Cdd:cd14540   79 VSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRrhtnqdVAGHnrnpPTLVH 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 842 CSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAILRV 901
Cdd:cd14540  159 CSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQY 218
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 671-893 1.34e-63

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: 214.18  E-value: 1.34e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 671 LDKNRYKDVLPYDTTRVLLQGNE-DYINASYVnmEMPAANlvNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTER 749
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLKQGDnDYINASLV--EVEEAK--RSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 750 GRTKCHQYWP---DPPDIMDHGIFHIQCQTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVK 826
Cdd:cd14545   77 GQIKCAQYWPqgeGNAMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQ 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218505829 827 YVR---SLRVDGEPALVHCSAGIGRTGVLVTMETAMCLIERN--LPVYPLDIVRKMRDQRAMMVQTSSQYKF 893
Cdd:cd14545  157 KVResgSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGnpSSVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 695-901 1.34e-63

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: 213.07  E-value: 1.34e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 695 YINASYVNMEMPAANLVnkYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDI-MDHGIFHIQ 773
Cdd:cd14596    1 YINASYITMPVGEEELF--YIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEpMELENYQLR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 774 CQTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVDGePALVHCSAGIGRTGVLV 853
Cdd:cd14596   79 LENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTG-PIVVHCSAGIGRAGVLI 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 218505829 854 TMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAILRV 901
Cdd:cd14596  158 CVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEV 205
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 670-898 1.06e-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: 212.32  E-value: 1.06e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 670 NLDKNRYKDVLPYDTTRVLLQGNE------DYINASYV--NMEMPAANLVNK-YIATQGPLPNTCAQFWQVVWDQKLSLV 740
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDRDpnvpgsDYINANYIrnENEGPTTDENAKtYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 741 VMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQCQTEDCTIAYVSREMLVTNTETGE-EHTVTHLQYVAWPDHGVPDDSS 819
Cdd:cd14544   81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDpIREIWHYQYLSWPDHGVPSDPG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 820 ---DFLEFVKYVRSLRVDGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDI---VRKMRDQRAMMVQTSSQYKF 893
Cdd:cd14544  161 gvlNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIqktIQMVRSQRSGMVQTEAQYKF 240


                 ....*
gi 218505829 894 VCEAI 898
Cdd:cd14544  241 IYVAV 245
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 656-898 6.59e-61

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: 207.51  E-value: 6.59e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 656 KKPGLAVSFAKLPQNLDKNRYKDVLPYDTTRVLLQGNE-DYINASYVNMEMPAanlvNKYIATQGPLPNTCAQFWQVVWD 734
Cdd:cd14607   10 ESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEnDYINASLVVIEEAQ----RSYILTQGPLPNTCCHFWLMVWQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 735 QKLSLVVMLTTLTERGRTKCHQYWPDPPDIM----DHGiFHIQCQTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWP 810
Cdd:cd14607   86 QKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVlsfkETG-FSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWP 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 811 DHGVPDDSSDFLEFVKYVR---SLRVDGEPALVHCSAGIGRTGVLVTMETAMCLIERNLP--VYPLDIVRKMRDQRAMMV 885
Cdd:cd14607  165 DFGVPESPASFLNFLFKVResgSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDPdsVDIKQVLLDMRKYRMGLI 244

                        250
                 ....*....|...
gi 218505829 886 QTSSQYKFVCEAI 898
Cdd:cd14607  245 QTPDQLRFSYMAV 257
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 654-902 1.17e-60

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: 207.37  E-value: 1.17e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 654 YRKKPGLAVSFAKLPQNLDKNRYKDVLPYDTTRVLL-----QGNEDYINASYVNmempAANLVNKYIATQGPLPNTCAQF 728
Cdd:cd14603   14 FKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILsllqeEGHSDYINANFIK----GVDGSRAYIATQGPLSHTVLDF 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 729 WQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQCQTEDCTIAYVSREMLVTNTETgEEHTVTHLQYVA 808
Cdd:cd14603   90 WRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTFQK-ESRSVSHFQYMA 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 809 WPDHGVPDDSSDFLEFVKYVRSLRVDG-EPALVHCSAGIGRTGVLVTME--TAMCLIERNLPVYPL-DIVRKMRDQRAMM 884
Cdd:cd14603  169 WPDHGIPDSPDCMLAMIELARRLQGSGpEPLCVHCSAGCGRTGVICTVDyvRQLLLTQRIPPDFSIfDVVLEMRKQRPAA 248

                        250
                 ....*....|....*...
gi 218505829 885 VQTSSQYKFVCEAILRVY 902
Cdd:cd14603  249 VQTEEQYEFLYHTVAQMF 266
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 650-899 4.82e-60

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: 206.03  E-value: 4.82e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 650 FEQLYRKKPGLAVSFAKLPQNLDKNRYKDVLPYDTTRVLL-QGNEDYINASYVNMEMPAanlvNKYIATQGPLPNTCAQF 728
Cdd:cd14608    5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLhQEDNDYINASLIKMEEAQ----RSYILTQGPLPNTCGHF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 729 WQVVWDQKLSLVVMLTTLTERGRTKCHQYWP---DPPDIMDHGIFHIQCQTEDCTIAYVSREMLVTNTETGEEHTVTHLQ 805
Cdd:cd14608   81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPqkeEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 806 YVAWPDHGVPDDSSDFLEFVKYVR---SLRVDGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVR---KMRD 879
Cdd:cd14608  161 YTTWPDFGVPESPASFLNFLFKVResgSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKvllEMRK 240

                        250       260
                 ....*....|....*....|
gi 218505829 880 QRAMMVQTSSQYKFVCEAIL 899
Cdd:cd14608  241 FRMGLIQTADQLRFSYLAVI 260
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 674-894 2.75e-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: 199.27  E-value: 2.75e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 674 NRYKDVLPYDTTRVLL----QGNEDYINASYvnmeMPAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTER 749
Cdd:cd14615    1 NRYNNVLPYDISRVKLsvqsHSTDDYINANY----MPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 750 GRTKCHQYWPDPPDiMDHGIFHIQCQTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVR 829
Cdd:cd14615   77 GRTKCEEYWPSKQK-KDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVR 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 218505829 830 ---SLRVDGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFV 894
Cdd:cd14615  156 eymKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 674-894 1.48e-57

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: 197.23  E-value: 1.48e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 674 NRYKDVLPYDTTRVLLQGNED-----YINASYV---NMEMPAanlvnkYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTT 745
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDdplssYINANYIrgyDGEEKA------YIATQGPLPNTVADFWRMVWQEKTPIIVMITN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 746 LTERgRTKCHQYWPDPPDiMDHGIFHIQCQTEDCTIAYVSREMLVTNTetGEEHTVTHLQYVAWPDHGVPDDSSDFLEFV 825
Cdd:cd14547   75 LTEA-KEKCAQYWPEEEN-ETYGDFEVTVQSVKETDGYTVRKLTLKYG--GEKRYLKHYWYTSWPDHKTPEAAQPLLSLV 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218505829 826 KYVRSLRVDGE---PALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFV 894
Cdd:cd14547  151 QEVEEARQTEPhrgPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFV 222
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 31-222 9.18e-57

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: 194.05  E-value: 9.18e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829    31 CSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPVDSPRWLEASKPLRKQLKGGFPCTLHFRVRYF 110
Cdd:smart00295   2 LKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRHWLDPAKTLLDQDVKSEPLTLYFRVKFY 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829   111 IPDPNTLQQEQTRH-LYFLQLKMDVCEGRLTCPLNSAVVLASYAVQSHFGDFNSSIH-HPGYLADSQFIPDQ------ND 182
Cdd:smart00295  82 PPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQlldsrkLK 161

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 218505829   183 DFLSKVESLHEQHSGLKQSEAESCYINIARTLDFYGVELH 222
Cdd:smart00295 162 EWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
PDZ_PTPN3-4-like cd06706
PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein ...
 506-595 1.93e-56

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: 188.67  E-value: 1.93e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 506 GYLVLIRITPDEEGRFGFNLKGGVDQKMPLVVSRINPESPADTCMPKLNEGDQIVLINGRDISEHTHDQVVMFIKASRES 585
Cdd:cd06706    1 DGLVLIRMKPDENGRFGFNVKGGVDQKMPVIVSRVAPGTPADLCIPRLNEGDQVLLINGRDISEHTHDQVVMFIKASRER 80

                         90
                 ....*....|
gi 218505829 586 HSRELALVIR 595
Cdd:cd06706   81 HSGELVLLVR 90
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 674-894 3.46e-56

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: 193.60  E-value: 3.46e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 674 NRYKDVLPYDTTRVLLQGNE-----DYINASYvnmeMPAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTE 748
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDddpcsDYINASY----IPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 749 RGRTKCHQYWPDPPDIMDHGIFHIQCQTEDCTIAYVSREMLVTNTETGEEH-TVTHLQYVAWPDHGVPDDSSDFLEFVKY 827
Cdd:cd14617   77 KGRVKCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPrLVRHFHYTVWPDHGVPETTQSLIQFVRT 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 828 VRSL--RVDGE-PALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFV 894
Cdd:cd14617  157 VRDYinRTPGSgPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYL 226
FERM_C_PTPN4_PTPN3_like cd13189
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and ...
 216-309 3.46e-56

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: 188.29  E-value: 3.46e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 216 FYGVELHGGRDLHNLDLMIGIASAGIAVYRKYICTSFYPWVNILKISFKRKKFFIHQRQKQAESREHIVAFNMLNYRSCK 295
Cdd:cd13189    1 LYGVELHSARDSNNLELQIGVSSAGILVFQNGIRINTFPWSKIVKISFKRKQFFIQLRREPNESRDTILGFNMLSYRACK 80

                         90
                 ....*....|....
gi 218505829 296 NLWKSCVEHHSFFQ 309
Cdd:cd13189   81 NLWKSCVEHHTFFR 94
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 695-894 7.91e-55

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 188.71  E-value: 7.91e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 695 YINASYVnmemPAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDpPDIMDHGIFHIQC 774
Cdd:cd14549    1 YINANYV----DGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPK-EGTETYGNIQVTL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 775 QTEDCTIAYVSREMLVTNTE------TGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVDGE-PALVHCSAGIG 847
Cdd:cd14549   76 LSTEVLATYTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAgPIVVHCSAGVG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 218505829 848 RTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFV 894
Cdd:cd14549  156 RTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFI 202
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 665-899 9.31e-55

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: 189.66  E-value: 9.31e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 665 AKLPQNLDKNRYKDVLPYDTTRVLLQ---GNE--DYINASYVNmempAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSL 739
Cdd:cd14554    1 ANLPCNKFKNRLVNILPYESTRVCLQpirGVEgsDYINASFID----GYRQRGAYIATQGPLAETTEDFWRMLWEHNSTI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 740 VVMLTTLTERGRTKCHQYWPDPPDIMdHGIFHIQCQTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSS 819
Cdd:cd14554   77 IVMLTKLREMGREKCHQYWPAERSAR-YQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 820 DFLEFVKYVRSLRV----DGePALVHCSAGIGRTGVLVTMETAMcliERNLPVYPLDI---VRKMRDQRAMMVQTSSQYK 892
Cdd:cd14554  156 GFIDFIGQVHKTKEqfgqEG-PITVHCSAGVGRTGVFITLSIVL---ERMRYEGVVDVfqtVKLLRTQRPAMVQTEDQYQ 231


                 ....*..
gi 218505829 893 FVCEAIL 899
Cdd:cd14554  232 FCYRAAL 238
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 665-894 2.73e-54

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: 188.94  E-value: 2.73e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 665 AKLPQNLDKNRYKDVLPYDTTRVLL-----QGNEDYINASYVnmemPAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSL 739
Cdd:cd14614    7 ADLPVNRCKNRYTNILPYDFSRVKLvsmheEEGSDYINANYI----PGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 740 VVMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQCQTEDCTIAYVSREMLVTNTEtgEEHTVTHLQYVAWPDHGVP--DD 817
Cdd:cd14614   83 IVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYAD--EVQDVMHFNYTAWPDHGVPtaNA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 218505829 818 SSDFLEFVKYVRSLRVDGE-PALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFV 894
Cdd:cd14614  161 AESILQFVQMVRQQAVKSKgPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFI 238
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 668-903 4.44e-54

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 188.94  E-value: 4.44e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 668 PQNLDKNRYKDVLPYDTTRVLLQGNE------DYINASYV-NMEMPAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLV 740
Cdd:cd14606   16 PENKSKNRYKNILPFDHSRVILQGRDsnipgsDYINANYVkNQLLGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 741 VMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQCQTEDCTIAYVSREMLVTNTETGEE-HTVTHLQYVAWPDHGVPDDSS 819
Cdd:cd14606   96 VMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELiREIWHYQYLSWPDHGVPSEPG 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 820 DFLEFVKYV----RSLRVDGePALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDI---VRKMRDQRAMMVQTSSQYK 892
Cdd:cd14606  176 GVLSFLDQInqrqESLPHAG-PIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIqktIQMVRAQRSGMVQTEAQYK 254

                        250
                 ....*....|.
gi 218505829 893 FVCEAILRVYE 903
Cdd:cd14606  255 FIYVAIAQFIE 265
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 669-898 1.05e-52

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: 184.84  E-value: 1.05e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 669 QNLDKNRYKDVLPYDTTRVLLQG---NE---DYINASYVNMEMPA----ANLVNKYIATQGPLPNTCAQFWQVVWDQKLS 738
Cdd:cd14605    1 ENKNKNRYKNILPFDHTRVVLHDgdpNEpvsDYINANIIMPEFETkcnnSKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 739 LVVMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQCQTEDCTIAYVSREMLVTNTETGE-EHTVTHLQYVAWPDHGVPDD 817
Cdd:cd14605   81 VIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGNtERTVWQYHFRTWPDHGVPSD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 818 SS---DFLEFVKYVRSLRVDGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDI---VRKMRDQRAMMVQTSSQY 891
Cdd:cd14605  161 PGgvlDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVpktIQMVRSQRSGMVQTEAQY 240


                 ....*..
gi 218505829 892 KFVCEAI 898
Cdd:cd14605  241 RFIYMAV 247
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 648-899 3.00e-52

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: 184.08  E-value: 3.00e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 648 IQFEQLYRK-KPGLAVSF--AKLPQNLDKNRYKDVLPYDTTRVLLQG-----NEDYINASYVNmempAANLVNKYIATQG 719
Cdd:cd14626   16 LKFSQEYESiDPGQQFTWenSNLEVNKPKNRYANVIAYDHSRVILTSvdgvpGSDYINANYID----GYRKQNAYIATQG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 720 PLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPdPPDIMDHGIFHIQCQTEDCTIAYVSREMLVTNTETGEEH 799
Cdd:cd14626   92 PLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWP-IRGTETYGMIQVTLLDTVELATYSVRTFALYKNGSSEKR 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 800 TVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLR-VDGEPALVHCSAGIGRTGVLVTMETamcLIERNLPVYPLDI---VR 875
Cdd:cd14626  171 EVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNpPDAGPMVVHCSAGVGRTGCFIVIDA---MLERMKHEKTVDIyghVT 247

                        250       260
                 ....*....|....*....|....
gi 218505829 876 KMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd14626  248 CMRSQRNYMVQTEDQYIFIHEALL 271
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 654-906 9.24e-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: 183.60  E-value: 9.24e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 654 YRKKPGLAVSFAKLPQNLDKNRYKDVLPYDTTRVLL-----QGNEDYINASYVN-MEMPAAnlvnkYIATQGPLPNTCAQ 727
Cdd:cd14604   41 YRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLtlktsSQDSDYINANFIKgVYGPKA-----YIATQGPLANTVID 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 728 FWQVVWDQKLSLVVMLTTLTERGRTKCHQYWP---DPPdiMDHGIFHIQCQTEDCTIAYVSREMLVTNTEtgEEHTVTHL 804
Cdd:cd14604  116 FWRMIWEYNVAIIVMACREFEMGRKKCERYWPlygEEP--MTFGPFRISCEAEQARTDYFIRTLLLEFQN--ETRRLYQF 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 805 QYVAWPDHGVPDDSSDFLEFVKYVRSLRV-DGEPALVHCSAGIGRTGVLVTMETAMCL-----IERNLPVYPLdiVRKMR 878
Cdd:cd14604  192 HYVNWPDHDVPSSFDSILDMISLMRKYQEhEDVPICIHCSAGCGRTGAICAIDYTWNLlkagkIPEEFNVFNL--IQEMR 269

                        250       260
                 ....*....|....*....|....*...
gi 218505829 879 DQRAMMVQTSSQYKFVCEAILRVYEEGL 906
Cdd:cd14604  270 TQRHSAVQTKEQYELVHRAIAQLFEKQL 297
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 673-902 2.18e-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: 180.04  E-value: 2.18e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 673 KNRYKDVLPYDTTRVLLQ-----GNEDYINASYVN-MEMPAAnlvnkYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTL 746
Cdd:cd14602    1 KNRYKDILPYDHSRVELSlitsdEDSDYINANFIKgVYGPRA-----YIATQGPLSTTLLDFWRMIWEYSVLIIVMACME 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 747 TERGRTKCHQYWPDP-PDIMDHGIFHIQCQTEDCTIAYVSREMLVTNTEtgEEHTVTHLQYVAWPDHGVPDDSSDFLEFV 825
Cdd:cd14602   76 FEMGKKKCERYWAEPgEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNS--ETRTIYQFHYKNWPDHDVPSSIDPILELI 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 826 KYVRSLRVDGE-PALVHCSAGIGRTGVLVTME-TAMCL----IERNLPVYplDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd14602  154 WDVRCYQEDDSvPICIHCSAGCGRTGVICAIDyTWMLLkdgiIPENFSVF--SLIQEMRTQRPSLVQTKEQYELVYNAVI 231


                 ...
gi 218505829 900 RVY 902
Cdd:cd14602  232 ELF 234
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 674-899 2.41e-51

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: 180.14  E-value: 2.41e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 674 NRYKDVLPYDTTRVLL-----QGNEDYINASYvnmeMPAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTE 748
Cdd:cd14618    1 NRYPHVLPYDHSRVRLsqlggEPHSDYINANF----IPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGME 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 749 RGRTKCHQYWPDPPDIMDHGIFHIQCQTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYV 828
Cdd:cd14618   77 NGRVLCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELV 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 218505829 829 R---SLRVDGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd14618  157 RehvQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 676-899 1.13e-50

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: 178.21  E-value: 1.13e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 676 YKDVLPYDTTRVLL---QGN--EDYINASYVNmempAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERG 750
Cdd:cd14620    1 YPNILPYDHSRVILsqlDGIpcSDYINASYID----GYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 751 RTKCHQYWPdppdimDHGIF---HIQCQTEDCTIA--YVSREMLVTNTETGE---EHTVTHLQYVAWPDHGVPDDSSDFL 822
Cdd:cd14620   77 EEKCYQYWP------DQGCWtygNIRVAVEDCVVLvdYTIRKFCIQPQLPDGckaPRLVTQLHFTSWPDFGVPFTPIGML 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 218505829 823 EFVKYVRSLR-VDGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd14620  151 KFLKKVKSVNpVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 695-900 2.59e-50

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: 176.70  E-value: 2.59e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 695 YINASYVNMEMPAANLvnKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWP---DPPDIMDHGIFH 771
Cdd:cd14598    1 YINASHIKVTVGGKEW--DYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgSRHNTVTYGRFK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 772 IQCQTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLR------VDGE----PALVH 841
Cdd:cd14598   79 ITTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRrhtnstIDPKspnpPVLVH 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218505829 842 CSAGIGRTGVLVTMETAMCLIERNlpvYPLDIVR---KMRDQRAMMVQTSSQYKFVCEAILR 900
Cdd:cd14598  159 CSAGVGRTGVVILSEIMIACLEHN---EMLDIPRvldMLRQQRMMMVQTLSQYTFVYKVLIQ 217
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 648-899 2.67e-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: 179.16  E-value: 2.67e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 648 IQFEQLYRK-KPGLAVSF--AKLPQNLDKNRYKDVLPYDTTRVLLQGNE-----DYINASYVNmempAANLVNKYIATQG 719
Cdd:cd14624   22 LKFSQEYESiDPGQQFTWehSNLEVNKPKNRYANVIAYDHSRVLLSAIEgipgsDYINANYID----GYRKQNAYIATQG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 720 PLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDpPDIMDHGIFHIQCQTEDCTIAYVSREMLVTNTETGEEH 799
Cdd:cd14624   98 ALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPS-RGTETYGLIQVTLLDTVELATYCVRTFALYKNGSSEKR 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 800 TVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLR-VDGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMR 878
Cdd:cd14624  177 EVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNpPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMR 256

                        250       260
                 ....*....|....*....|.
gi 218505829 879 DQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd14624  257 AQRNYMVQTEDQYIFIHDALL 277
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 654-898 8.85e-50

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: 177.56  E-value: 8.85e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 654 YRKKPGlAVSFAKLPQNLDKNRYKDVLPYDTTRVLLQG-----NEDYINASYVnMEMPAANlvNKYIATQGPLPNTCAQF 728
Cdd:cd14610   29 YQAEPN-ATNVAQREENVQKNRSLAVLPYDHSRIILKAenshsHSDYINASPI-MDHDPRN--PAYIATQGPLPATVADF 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 729 WQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDIMDHgIF-------HIQCqtEDctiaYVSREMLVTNTETGEEHTV 801
Cdd:cd14610  105 WQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYH-IYevnlvseHIWC--ED----FLVRSFYLKNLQTNETRTV 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 802 THLQYVAWPDHGVPDDSSDFLEFVKYV-RSLRVDGEPALVHCSAGIGRTGVLVTMEtaMCLIERNLPVYPLDI---VRKM 877
Cdd:cd14610  178 TQFHFLSWNDQGVPASTRSLLDFRRKVnKCYRGRSCPIIVHCSDGAGRSGTYILID--MVLNKMAKGAKEIDIaatLEHL 255

                        250       260
                 ....*....|....*....|.
gi 218505829 878 RDQRAMMVQTSSQYKFVCEAI 898
Cdd:cd14610  256 RDQRPGMVQTKEQFEFALTAV 276
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 665-899 8.98e-50

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: 177.59  E-value: 8.98e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 665 AKLPQNLDKNRYKDVLPYDTTRVLLQGNE-----DYINASYVNmempAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSL 739
Cdd:cd14625   42 SNLEVNKPKNRYANVIAYDHSRVILQPIEgimgsDYINANYID----GYRKQNAYIATQGPLPETFGDFWRMVWEQRSAT 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 740 VVMLTTLTERGRTKCHQYWPDpPDIMDHGIFHIQCQTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSS 819
Cdd:cd14625  118 VVMMTKLEEKSRIKCDQYWPS-RGTETYGMIQVTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPT 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 820 DFLEFVKYVRSLR-VDGEPALVHCSAGIGRTGVLVTMETamcLIERNLPVYPLDI---VRKMRDQRAMMVQTSSQYKFVC 895
Cdd:cd14625  197 PFLAFLRRVKTCNpPDAGPIVVHCSAGVGRTGCFIVIDA---MLERIKHEKTVDIyghVTLMRSQRNYMVQTEDQYSFIH 273


                 ....
gi 218505829 896 EAIL 899
Cdd:cd14625  274 DALL 277
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 665-899 1.52e-49

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type tyrosine-protein phosphatase-like D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 177.23  E-value: 1.52e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 665 AKLPQNLDKNRYKDVLPYDTTRVLLQ---GNE--DYINASYVNmempAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSL 739
Cdd:cd14628   47 ANLPCNKFKNRLVNIMPYESTRVCLQpirGVEgsDYINASFID----GYRQQKAYIATQGPLAETTEDFWRMLWEHNSTI 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 740 VVMLTTLTERGRTKCHQYWPDPPDiMDHGIFHIQCQTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSS 819
Cdd:cd14628  123 VVMLTKLREMGREKCHQYWPAERS-ARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 820 DFLEFVKYVRSLR----VDGePALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVC 895
Cdd:cd14628  202 GFIDFIGQVHKTKeqfgQDG-PISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCY 280


                 ....
gi 218505829 896 EAIL 899
Cdd:cd14628  281 RAAL 284
FERM_F1_PTPN3 cd17193
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 28-111 1.77e-49

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: 169.26  E-value: 1.77e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  28 EVICSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPVDSPRWLEASKPLRKQLKGGFPCTLHFRV 107
Cdd:cd17193    1 EVICNVHFLDGSVQSFKVNKQDTGQVLLDMAYNHLGLTEREYFGLQHNEDSVDSPRWLEPSKPIRKQLKGGFPCSLHFRV 80


                 ....
gi 218505829 108 RYFI 111
Cdd:cd17193   81 RFFI 84
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 665-899 2.05e-49

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 176.85  E-value: 2.05e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 665 AKLPQNLDKNRYKDVLPYDTTRVLLQ---GNE--DYINASYVNmempAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSL 739
Cdd:cd14627   48 ANLPCNKFKNRLVNIMPYETTRVCLQpirGVEgsDYINASFID----GYRQQKAYIATQGPLAETTEDFWRMLWENNSTI 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 740 VVMLTTLTERGRTKCHQYWPDPPDiMDHGIFHIQCQTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSS 819
Cdd:cd14627  124 VVMLTKLREMGREKCHQYWPAERS-ARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 820 DFLEFVKYVRSLR----VDGePALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVC 895
Cdd:cd14627  203 GFIDFIGQVHKTKeqfgQDG-PISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCY 281


                 ....
gi 218505829 896 EAIL 899
Cdd:cd14627  282 QAAL 285
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 674-896 2.71e-49

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: 173.94  E-value: 2.71e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 674 NRYKDVLPYDTTRVLLQGN-----EDYINASYVNMEMpaanLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTE 748
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADagvpgSDYINASYISGYL----CPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 749 RGRTKCHQYWP-DPPDIMDHGIFHIQCQTEDCTIAYVSREMLVtnTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKY 827
Cdd:cd14616   77 KGRIRCHQYWPeDNKPVTVFGDIVITKLMEDVQIDWTIRDLKI--ERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKL 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 828 VRSLRV-DGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCE 896
Cdd:cd14616  155 VRASRAhDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 649-899 6.09e-49

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: 174.84  E-value: 6.09e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 649 QFEQLYRKKPGLAVS--FAKLPQNLDKNRYKDVLPYDTTRVLLQ-------GNEDYINASYVNmempAANLVNKYIATQG 719
Cdd:cd17667    4 DFEEVQRCTADMNITaeHSNHPDNKHKNRYINILAYDHSRVKLRplpgkdsKHSDYINANYVD----GYNKAKAYIATQG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 720 PLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDpPDIMDHGIFHIQCQTEDCTIAYVSREMLVTNTETGE-- 797
Cdd:cd17667   80 PLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPT-ENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKgq 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 798 ---------EHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRV-DGEPALVHCSAGIGRTGVLVTMETAMCLIERNLP 867
Cdd:cd17667  159 kgnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTpEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKST 238

                        250       260       270
                 ....*....|....*....|....*....|..
gi 218505829 868 VYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd17667  239 VNVLGFLKHIRTQRNYLVQTEEQYIFIHDALL 270
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 695-898 4.64e-48

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: 169.93  E-value: 4.64e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 695 YINASYV---NMEMPAanlvnkYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDIMdHGIF- 770
Cdd:cd14546    1 YINASTIydhDPRNPA------YIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEV-YHIYe 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 771 ------HIQCqtEDctiaYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYV-RSLRVDGEPALVHCS 843
Cdd:cd14546   74 vhlvseHIWC--DD----YLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVnKSYRGRSCPIVVHCS 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 218505829 844 AGIGRTGVLVTMEtaMCLIERNLPVYPLDI---VRKMRDQRAMMVQTSSQYKFVCEAI 898
Cdd:cd14546  148 DGAGRTGTYILID--MVLNRMAKGAKEIDIaatLEHLRDQRPGMVKTKDQFEFVLTAV 203
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 654-898 4.82e-48

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: 172.53  E-value: 4.82e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 654 YRKKPGlAVSFAKLPQNLDKNRYKDVLPYDTTRVLLQ-----GNEDYINASYV---NMEMPAanlvnkYIATQGPLPNTC 725
Cdd:cd14609   27 YQAEPN-TCSTAQGEANVKKNRNPDFVPYDHARIKLKaesnpSRSDYINASPIiehDPRMPA------YIATQGPLSHTI 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 726 AQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDIMDHgIF-------HIQCqtEDctiaYVSREMLVTNTETGEE 798
Cdd:cd14609  100 ADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYH-IYevnlvseHIWC--ED----FLVRSFYLKNVQTQET 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 799 HTVTHLQYVAWPDHGVPDDSSDFLEFVKYV-RSLRVDGEPALVHCSAGIGRTGVLVTMEtaMCLIERNLPVYPLDI---V 874
Cdd:cd14609  173 RTLTQFHFLSWPAEGIPSSTRPLLDFRRKVnKCYRGRSCPIIVHCSDGAGRTGTYILID--MVLNRMAKGVKEIDIaatL 250

                        250       260
                 ....*....|....*....|....
gi 218505829 875 RKMRDQRAMMVQTSSQYKFVCEAI 898
Cdd:cd14609  251 EHVRDQRPGMVRTKDQFEFALTAV 274
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 695-894 1.08e-47

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: 168.37  E-value: 1.08e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 695 YINASYVnmEMPAANLVnkYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDP-PDIMDHGIFHIQ 773
Cdd:cd14542    1 YINANFI--KGVSGSKA--YIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEgEEQLQFGPFKIS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 774 CQTED-CTIAYVSREMLVTNTEtgEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVDGE-PALVHCSAGIGRTGV 851
Cdd:cd14542   77 LEKEKrVGPDFLIRTLKVTFQK--ESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDvPICVHCSAGCGRTGT 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 218505829 852 LVTMETAMCL-----IERNLPVYplDIVRKMRDQRAMMVQTSSQYKFV 894
Cdd:cd14542  155 ICAIDYVWNLlktgkIPEEFSLF--DLVREMRKQRPAMVQTKEQYELV 200
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 665-899 2.38e-47

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: 170.68  E-value: 2.38e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 665 AKLPQNLDKNRYKDVLPYDTTRVLLQ---GNE--DYINASYVNmempAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSL 739
Cdd:cd14629   48 ANLPCNKFKNRLVNIMPYELTRVCLQpirGVEgsDYINASFID----GYRQQKAYIATQGPLAETTEDFWRMLWEHNSTI 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 740 VVMLTTLTERGRTKCHQYWPDPPDiMDHGIFHIQCQTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSS 819
Cdd:cd14629  124 VVMLTKLREMGREKCHQYWPAERS-ARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGE 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 820 DFLEFVKYVRSLR----VDGePALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVC 895
Cdd:cd14629  203 GFIDFIGQVHKTKeqfgQDG-PITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCY 281


                 ....
gi 218505829 896 EAIL 899
Cdd:cd14629  282 RAAL 285
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 695-894 1.36e-46

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: 165.39  E-value: 1.36e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 695 YINASYVN-MEMPaanlvNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPP-DIMDHGIFHI 772
Cdd:cd14557    1 YINASYIDgFKEP-----RKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEeGSRAFGDVVV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 773 QCQTEDCTIAYVSREMLVTNT-ETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVDGE-PALVHCSAGIGRTG 850
Cdd:cd14557   76 KINEEKICPDYIIRKLNINNKkEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSgPIVVHCSAGVGRTG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 218505829 851 VLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFV 894
Cdd:cd14557  156 TYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILI 199
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 669-899 2.89e-46

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: 165.97  E-value: 2.89e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 669 QNLDKNRYKDVLPYDTTRVLLQGNE-----DYINASYVNmempAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVML 743
Cdd:cd14630    2 ENRNKNRYGNIISYDHSRVRLQLLDgdphsDYINANYID----GYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 744 TTLTERGRTKCHQYWPDPPDImdHGIFHIQCQTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLE 823
Cdd:cd14630   78 TNLVEVGRVKCVRYWPDDTEV--YGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLG 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 218505829 824 FVKYVRSLR-VDGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd14630  156 FVRQVKFLNpPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAIL 232
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 667-894 3.85e-46

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


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 165.78  E-value: 3.85e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 667 LPQNLDKNRYKDVLPYDTTRVLLQG------NEDYINASYVnmeMPAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLV 740
Cdd:cd14612   12 IPGHASKDRYKTILPNPQSRVCLRRagsqeeEGSYINANYI---RGYDGKEKAYIATQGPMLNTVSDFWEMVWQEECPII 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 741 VMLTTLTERgRTKCHQYWPDPPDimDHGIFHIQCQTEDCTIAYVSREMLVTNteTGEEHTVTHLQYVAWPDHGVPDDSSD 820
Cdd:cd14612   89 VMITKLKEK-KEKCVHYWPEKEG--TYGRFEIRVQDMKECDGYTIRDLTIQL--EEESRSVKHYWFSSWPDHQTPESAGP 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 218505829 821 FLEFVKYVRSLRVDGE---PALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFV 894
Cdd:cd14612  164 LLRLVAEVEESRQTAAspgPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 695-899 2.02e-45

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: 162.39  E-value: 2.02e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 695 YINASYVNmempAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDImdHGIFHIQC 774
Cdd:cd14555    1 YINANYID----GYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEV--YGDIKVTL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 775 QTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLR-VDGEPALVHCSAGIGRTGVLV 853
Cdd:cd14555   75 VETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNpPSAGPIVVHCSAGAGRTGCYI 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 218505829 854 TMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd14555  155 VIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 695-893 2.26e-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: 2.26e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 695 YINASYVNmemPAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWP-DPPDIMDHGIFHIQ 773
Cdd:cd14539    1 YINASLIE---DLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPtERGQALVYGAITVS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 774 CQTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRS--LRVDGE--PALVHCSAGIGRT 849
Cdd:cd14539   78 LQSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHShyLQQRSLqtPIVVHCSSGVGRT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 218505829 850 GVLVTMETAMCLIE--RNLPVYPlDIVRKMRDQRAMMVQTSSQYKF 893
Cdd:cd14539  158 GAFCLLYAAVQEIEagNGIPDLP-QLVRKMRQQRKYMLQEKEHLKF 202
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 695-894 4.24e-45

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: 161.23  E-value: 4.24e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 695 YINASYVNmempAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPdppdimDHGIFH--- 771
Cdd:cd14551    1 YINASYID----GYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP------DQGCWTygn 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 772 IQCQTEDCT--IAYVSREMLV--TNTETGEE--HTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLR-VDGEPALVHCSA 844
Cdd:cd14551   71 LRVRVEDTVvlVDYTTRKFCIqkVNRGIGEKrvRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANpPRAGPIVVHCSA 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 218505829 845 GIGRTGVLVTMETAMCLI--ERNLPVYplDIVRKMRDQRAMMVQTSSQYKFV 894
Cdd:cd14551  151 GVGRTGTFIVIDAMLDMMhaEGKVDVF--GFVSRIRQQRSQMVQTDMQYVFI 200
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 665-899 7.50e-45

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: 162.90  E-value: 7.50e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 665 AKLPQNLDKNRYKDVLPYDTTRVLLQ-----GNEDYINASYVNmempAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSL 739
Cdd:cd14633   35 AKKDENRMKNRYGNIIAYDHSRVRLQpiegeTSSDYINGNYID----GYHRPNHYIATQGPMQETIYDFWRMVWHENTAS 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 740 VVMLTTLTERGRTKCHQYWPDPPDIM-DHGIFHIQCQTedcTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDS 818
Cdd:cd14633  111 IIMVTNLVEVGRVKCCKYWPDDTEIYkDIKVTLIETEL---LAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHA 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 819 SDFLEFVKYVRSLR-VDGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEA 897
Cdd:cd14633  188 TGLLGFVRQVKSKSpPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDA 267


                 ..
gi 218505829 898 IL 899
Cdd:cd14633  268 IL 269
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 665-905 1.63e-43

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: 160.19  E-value: 1.63e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 665 AKLPQNLDKNRYKDVLPYDTTRVLLQGNE-----DYINASYVNmempAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSL 739
Cdd:cd14621   47 ASKEENKEKNRYVNILPYDHSRVHLTPVEgvpdsDYINASFIN----GYQEKNKFIAAQGPKEETVNDFWRMIWEQNTAT 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 740 VVMLTTLTERGRTKCHQYWPDpPDIMDHGifHIQCQTEDCTIA--YVSREMLVTN----TETGEEHTVTHLQYVAWPDHG 813
Cdd:cd14621  123 IVMVTNLKERKECKCAQYWPD-QGCWTYG--NIRVSVEDVTVLvdYTVRKFCIQQvgdvTNKKPQRLITQFHFTSWPDFG 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 814 VPDDSSDFLEFVKYVRSLRVD-GEPALVHCSAGIGRTGVLVTMETAMCLI--ERNLPVYplDIVRKMRDQRAMMVQTSSQ 890
Cdd:cd14621  200 VPFTPIGMLKFLKKVKNCNPQyAGAIVVHCSAGVGRTGTFIVIDAMLDMMhaERKVDVY--GFVSRIRAQRCQMVQTDMQ 277

                        250
                 ....*....|....*
gi 218505829 891 YKFVCEAILRVYEEG 905
Cdd:cd14621  278 YVFIYQALLEHYLYG 292
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 669-902 1.02e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 157.86  E-value: 1.02e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 669 QNLDKNRYKDVLPYDTTRVLL---QGNEDYINASYVNmempAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTT 745
Cdd:PHA02742  51 KNMKKCRYPDAPCFDRNRVILkieDGGDDFINASYVD----GHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITK 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 746 LTERGRTKCHQYW-PDPPDIMDHGIFHIQCQTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEF 824
Cdd:PHA02742 127 IMEDGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDF 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 825 VKYVRSL------------RVDGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYK 892
Cdd:PHA02742 207 VLAVREAdlkadvdikgenIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYI 286

                        250
                 ....*....|
gi 218505829 893 FvCEAILRVY 902
Cdd:PHA02742 287 F-CYFIVLIF 295
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 695-898 4.56e-42

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 152.42  E-value: 4.56e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 695 YINASYVNmempAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDpPDIMDHGIFHIQC 774
Cdd:cd14552    1 YINASFID----GYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPE-DGSVSSGDITVEL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 775 QTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLR--VDGEPALVHCSAGIGRTGVL 852
Cdd:cd14552   76 KDQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQqqSGNHPITVHCSAGAGRTGTF 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 218505829 853 VTMETamcLIERNLPVYPLDI---VRKMRDQRAMMVQTSSQYKFVCEAI 898
Cdd:cd14552  156 CALST---VLERVKAEGVLDVfqvVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 695-899 4.89e-42

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


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 152.83  E-value: 4.89e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 695 YINASYVNmempAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPdPPDIMDHGIFHIQC 774
Cdd:cd17668    1 YINANYVD----GYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-ADGSEEYGNFLVTQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 775 QTEDCTIAYVSREMLVTNTETGE--------EHTVTHLQYVAWPDHGVPDDSSDFLEFV-KYVRSLRVDGEPALVHCSAG 845
Cdd:cd17668   76 KSVQVLAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYTLPVLTFVrKASYAKRHAVGPVVVHCSAG 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 218505829 846 IGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd17668  156 VGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 686-899 7.88e-42

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: 152.48  E-value: 7.88e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 686 RVLLQGNE-----DYINASYVN-MEMPAanlvnKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWP 759
Cdd:cd14631    1 RVILQPVEddpssDYINANYIDgYQRPS-----HYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 760 DPPDImdHGIFHIQCQTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVR-SLRVDGEPA 838
Cdd:cd14631   76 DDTEV--YGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKlSNPPSAGPI 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 218505829 839 LVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd14631  154 VVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 695-899 2.58e-41

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: 150.59  E-value: 2.58e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 695 YINASYVNmempAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDImdHGIFHIQC 774
Cdd:cd14632    1 YINANYID----GYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDT--YGDIKITL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 775 QTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVR-SLRVDGEPALVHCSAGIGRTGVLV 853
Cdd:cd14632   75 LKTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKaSTPPDAGPVVVHCSAGAGRTGCYI 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 218505829 854 TMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd14632  155 VLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 675-893 3.54e-41

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 150.97  E-value: 3.54e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 675 RYKDVLPYDTTRVLL-----QGNEDYINASYVNmempAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTER 749
Cdd:cd14623    1 RVLQIIPYEFNRVIIpvkrgEENTDYVNASFID----GYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEER 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 750 GRTKCHQYWPDpPDIMDHGIFHIQCQTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVR 829
Cdd:cd14623   77 GQEKCAQYWPS-DGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQ 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 218505829 830 SLRVDG--EPALVHCSAGIGRTGVLVTMETamcLIERNLPVYPLDI---VRKMRDQRAMMVQTSSQYKF 893
Cdd:cd14623  156 KQQQQSgnHPITVHCSAGAGRTGTFCALST---VLERVKAEGILDVfqtVKSLRLQRPHMVQTLEQYEF 221
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 673-894 1.07e-40

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


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 150.78  E-value: 1.07e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 673 KNRYKDVLPYDTTRVLLQGNED------YINASYVNMEMPAANLvnkYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTL 746
Cdd:cd14613   28 KNRYKTILPNPHSRVCLTSPDQddplssYINANYIRGYGGEEKV---YIATQGPTVNTVGDFWRMVWQERSPIIVMITNI 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 747 TERGRtKCHQYWPDPPDIMDhGIfHIQCQTEDCTIAYVSRemLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVK 826
Cdd:cd14613  105 EEMNE-KCTEYWPEEQVTYE-GI-EITVKQVIHADDYRLR--LITLKSGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQ 179

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 218505829 827 YVRSLRVDGE----PALVHCSAGIGRTGVLVTmeTAMCLIE-RNLPVypLDIVR---KMRDQRAMMVQTSSQYKFV 894
Cdd:cd14613  180 EVEEARQQAEpncgPVIVHCSAGIGRTGCFIA--TSICCKQlRNEGV--VDILRttcQLRLDRGGMIQTCEQYQFV 251
PHA02738 PHA02738
hypothetical protein; Provisional
 663-900 2.08e-40

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 152.00  E-value: 2.08e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 663 SFAKLPQNLDKNRYKDVLPYDTTRVLL---QGNEDYINASYVNmempAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSL 739
Cdd:PHA02738  42 TFNAEKKNRKLNRYLDAVCFDHSRVILpaeRNRGDYINANYVD----GFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQI 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 740 VVMLTTLTERGRTKCHQYWPD-PPDIMDHGIFHIQCQTEDCTIAYVSREMLVTNTeTGEEHTVTHLQYVAWPDHGVPDDS 818
Cdd:PHA02738 118 IVMLCKKKENGREKCFPYWSDvEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDG-TSATQTVTHFNFTAWPDHDVPKNT 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 819 SDFLEFVKYVRSL--------------RVDGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMM 884
Cdd:PHA02738 197 SEFLNFVLEVRQCqkelaqeslqighnRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYS 276

                        250
                 ....*....|....*.
gi 218505829 885 VQTSSQYKFVCEAILR 900
Cdd:PHA02738 277 LFIPFQYFFCYRAVKR 292
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 695-893 3.11e-40

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


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 147.61  E-value: 3.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 695 YINASYVnmEMPAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRT-KCHQYWPDPPDI-MDHGIFHI 772
Cdd:cd17658    1 YINASLV--ETPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEENEsREFGRISV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 773 QCQTEDCTIAYVSREMLVTNTETGEEH--TVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVDGEPALVHCSAGIGRTG 850
Cdd:cd17658   79 TNKKLKHSQHSITLRVLEVQYIESEEPplSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPPSAGPIVVHCSAGIGRTG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 218505829 851 VLVTMETAmclIERNLP--VYPLDI---VRKMRDQRAMMVQTSSQYKF 893
Cdd:cd17658  159 AYCTIHNT---IRRILEgdMSAVDLsktVRKFRSQRIGMVQTQDQYIF 203
FERM_F1_PTPN3_like cd17100
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 28-111 4.43e-39

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: 139.75  E-value: 4.43e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  28 EVICSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDP--VDSPRWLEASKPLRKQLKGGFPCTLHF 105
Cdd:cd17100    1 EVRCIVHFLDDTEQTFEVEKRDKGQVLLDKVFNHLELVEKDYFGLQFSDDSpaTDSMRWLDPLKPIRKQIKGGPPYYLNF 80


                 ....*.
gi 218505829 106 RVRYFI 111
Cdd:cd17100   81 RVKFYV 86
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 673-894 1.73e-38

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: 143.13  E-value: 1.73e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 673 KNRYKDVLPYDTTRVLLQ-GNEDYINASYVNmempaANLVNKY-------IATQGPLPNTCAQFWQVVWDQKLSLVVMLT 744
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKpKNSNDSLSTYIN-----ANYIRGYggkekafIATQGPMINTVNDFWQMVWQEDSPVIVMIT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 745 TLTERGRtKCHQYWPDPPDImdHGIFHIQCQTEDCTIAYVSREMLVTNTetGEEHTVTHLQYVAWPDHGVPDDSSDFLEF 824
Cdd:cd14611   77 KLKEKNE-KCVLYWPEKRGI--YGKVEVLVNSVKECDNYTIRNLTLKQG--SQSRSVKHYWYTSWPDHKTPDSAQPLLQL 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 218505829 825 VKYVRSLRVDGE---PALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFV 894
Cdd:cd14611  152 MLDVEEDRLASPgrgPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFV 224
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 659-894 8.81e-38

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 143.99  E-value: 8.81e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 659 GLAVSFAKlPQNLDKNRYKDVLPYDTTRVLLQ----GNEDYINASYVN-MEMPaanlvNKYIATQGPLPNTCAQFWQVVW 733
Cdd:PHA02747  41 GLIANFEK-PENQPKNRYWDIPCWDHNRVILDsgggSTSDYIHANWIDgFEDD-----KKFIATQGPFAETCADFWKAVW 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 734 DQKLSLVVMLT-TLTERGRTKCHQYW-PDPPDIMDHGIFHIQCQTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPD 811
Cdd:PHA02747 115 QEHCSIIVMLTpTKGTNGEEKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQCSEWFE 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 812 HGVPDDSSDFLEFVKYV-RSLRVDGE----------PALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQ 880
Cdd:PHA02747 195 DETPSDHPDFIKFIKIIdINRKKSGKlfnpkdallcPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQ 274

                        250
                 ....*....|....
gi 218505829 881 RAMMVQTSSQYKFV 894
Cdd:PHA02747 275 RHAGIMNFDDYLFI 288
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 694-893 4.74e-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: 138.21  E-value: 4.74e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 694 DYINASYVNmempAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDImDHGIFHIQ 773
Cdd:cd14622    1 DYINASFID----GYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSV-THGEITIE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 774 CQTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYV--RSLRVDGEPALVHCSAGIGRTGV 851
Cdd:cd14622   76 IKNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVqkQQQQTGNHPIVVHCSAGAGRTGT 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 218505829 852 LVTMETamcLIERNLPVYPLDI---VRKMRDQRAMMVQTSSQYKF 893
Cdd:cd14622  156 FIALSN---ILERVKAEGLLDVfqtVKSLRLQRPHMVQTLEQYEF 197
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 695-893 5.94e-36

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: 135.21  E-value: 5.94e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 695 YINASYVNMEMPAANLvnkyIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDppDIMDHGIFHIQC 774
Cdd:cd14558    1 YINASFIDGYWGPKSL----IATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGD--EKKTYGDIEVEL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 775 QTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVDGE-------PALVHCSAGIG 847
Cdd:cd14558   75 KDTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNskhgrsvPIVVHCSDGSS 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 218505829 848 RTGVLV----TMETAMclIERNLPVypLDIVRKMRDQRAMMVQTSSQYKF 893
Cdd:cd14558  155 RTGIFCalwnLLESAE--TEKVVDV--FQVVKALRKQRPGMVSTLEQYQF 200
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 695-896 1.74e-35

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: 133.69  E-value: 1.74e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 695 YINASYVN-MEMPAAnlvnkYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTkCHQYWPDPpDIMDHGIFHIQ 773
Cdd:cd14556    1 YINAALLDsYKQPAA-----FIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQS-CPQYWPDE-GSGTYGPIQVE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 774 CQTEDCTIAYVSREMLVTNTETGEE--HTVTHLQYVAWPDHG-VPDDSSDFLEFVKYVRSLR--VDGEPALVHCSAGIGR 848
Cdd:cd14556   74 FVSTTIDEDVISRIFRLQNTTRPQEgyRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQeqSGEGPIVVHCLNGVGR 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 218505829 849 TGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCE 896
Cdd:cd14556  154 SGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
800-899 1.09e-34

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 127.86  E-value: 1.09e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829   800 TVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVDGE---PALVHCSAGIGRTGVLVTMETAMCLIE-RNLPVYPLDIVR 875
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssgPVVVHCSAGVGRTGTFVAIDILLQQLEaEAGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....
gi 218505829   876 KMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALL 104
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 800-899 1.09e-34

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: 127.86  E-value: 1.09e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829   800 TVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVDGE---PALVHCSAGIGRTGVLVTMETAMCLIE-RNLPVYPLDIVR 875
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssgPVVVHCSAGVGRTGTFVAIDILLQQLEaEAGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....
gi 218505829   876 KMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALL 104
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 112-222 1.52e-33

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 125.07  E-value: 1.52e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  112 PDPNTLQQEQTRHLYFLQLKMDVCEGRLTCPLNSAVVLASYAVQSHFGDFNSSIHHPGYLADSQFIPDQN------DDFL 185
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLlrkmksKELE 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 218505829  186 SKVESLHEQHSGLKQSEAESCYINIARTLDFYGVELH 222
Cdd:pfam00373  81 KRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
666-891 1.54e-33

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 130.60  E-value: 1.54e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 666 KLPQNLDKNRYKDVLPYDTTRVllQGNEDYINASYVNMEMPaanlvNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTT 745
Cdd:COG5599   38 QNINGSPLNRFRDIQPYKETAL--RANLGYLNANYIQVIGN-----HRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLAS 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 746 LTE--RGRTKCHQYWPDPPDIMDHGIFHIQCQTEDCTIAYVSREMLVTNTETGEEHT-VTHLQYVAWPDHGVPdDSSDFL 822
Cdd:COG5599  111 DDEisKPKVKMPVYFRQDGEYGKYEVSSELTESIQLRDGIEARTYVLTIKGTGQKKIeIPVLHVKNWPDHGAI-SAEALK 189

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 218505829 823 EFVKYV----RSLRVDGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYP--LDIVRKMRDQRAM-MVQTSSQY 891
Cdd:COG5599  190 NLADLIdkkeKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVQITLsvEEIVIDMRTSRNGgMVQTSEQL 265
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 668-900 1.56e-33

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 132.07  E-value: 1.56e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 668 PQNLDKNRYKDVLPYDTTRVLLQG------------------------NEDYINASYVNmempAANLVNKYIATQGPLPN 723
Cdd:PHA02746  49 KENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkievtsednAENYIHANFVD----GFKEANKFICAQGPKED 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 724 TCAQFWQVVWDQKLSLVVMLTTlTERGRTKCHQYWPDPPDI-MDHGIFHIQCQTEDCTIAYVSREMLVTNTETGEEHTVT 802
Cdd:PHA02746 125 TSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWTKEEDSeLAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIH 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 803 HLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVD-----------GEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPL 871
Cdd:PHA02746 204 HFWFPDWPDNGIPTGMAEFLELINKVNEEQAElikqadndpqtLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLG 283

                        250       260
                 ....*....|....*....|....*....
gi 218505829 872 DIVRKMRDQRAMMVQTSSQYKFvCEAILR 900
Cdd:PHA02746 284 EIVLKIRKQRHSSVFLPEQYAF-CYKALK 311
FERM_F1_PTPN4 cd17194
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 28-111 5.45e-33

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: 122.33  E-value: 5.45e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  28 EVICSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPVDSPRWLEASKPLRKQLKGGFPCTLHFRV 107
Cdd:cd17194    1 EVVCNILLLDNTVQAFKVNKHDQGQVLLDLVFKHLDLTERDYFGLQLADDSTDNPRWLDPNKPIRKQLKRGSPHNLNFRV 80


                 ....
gi 218505829 108 RYFI 111
Cdd:cd17194   81 KFFV 84
FERM_C pfam09380
FERM C-terminal PH-like domain;
226-312 2.82e-30

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 114.27  E-value: 2.82e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  226 DLHNLDLMIGIASAGIAVYRKYICTS-FYPWVNILKISFKRKKFFIHQRQKqaeSREHIVAFNMLNYRSCKNLWKSCVEH 304
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKILnLFPWREIRKISFKRKKFLIKLRDK---SSEETLGFYTESSRACKYLWKLCVEQ 77


                  ....*...
gi 218505829  305 HSFFQAKK 312
Cdd:pfam09380  78 HTFFRLRR 85
FERM_C_4_1_family cd13184
FERM domain C-lobe of Protein 4.1 family; The protein 4.1 family includes four well-defined ...
 217-308 7.07e-30

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: 113.57  E-value: 7.07e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 217 YGVELHGGRDLHNLDLMIGIASAGIAVYRKYICTSFYPWVNILKISFKRKKFFIHQRQKQAESREHIVAFNMLNYRSCKN 296
Cdd:cd13184    1 YGVDLHPAKDSEGVDIMLGVCSSGLLVYRDRLRINRFAWPKVLKISYKRNNFYIKIRPGEFEQYETTIGFKLPNHRAAKR 80

                         90
                 ....*....|..
gi 218505829 297 LWKSCVEHHSFF 308
Cdd:cd13184   81 LWKVCVEHHTFF 92
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 122-214 1.31e-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: 107.33  E-value: 1.31e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 122 TRHLYFLQLKMDVCEGRLTCPLNSAVVLASYAVQSHFGDFNSSIHHPGYLADSQFIPDQ------NDDFLSKVESLHEQH 195
Cdd:cd14473    1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLSLKRFLPKQllkqrkPEEWEKRIVELHKKL 80

                         90
                 ....*....|....*....
gi 218505829 196 SGLKQSEAESCYINIARTL 214
Cdd:cd14473   81 RGLSPAEAKLKYLKIARKL 99
FERM_C_FARP1-like cd13193
FERM domain C-lobe of FERM, RhoGEF and pleckstrin domain-containing protein 1 and related ...
 210-322 7.49e-26

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: 103.19  E-value: 7.49e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 210 IARTLDFYGVELHGGRDLHNLDLMIGIASAGIAVYRKYICTSFYPWVNILKISFKRKKFFIHQRQKQAESREHIVAFNML 289
Cdd:cd13193    2 TARRCELYGIRLHPAKDREGVKLNLAVAHMGILVFQGFTKINTFSWAKIRKLSFKRKRFLIKLHPEAYGSYKDTVEFSFE 81

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 218505829 290 NYRSCKNLWKSCVEHHSFFQAKKL--LPQEKNVLS 322
Cdd:cd13193   82 SRNECKSFWKKCIEHHAFFRCSEVpkPPSPKLRLF 116
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 695-899 2.68e-24

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: 101.64  E-value: 2.68e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 695 YINASYVNM-EMPAAnlvnkYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTerGRTKCHQYWPDPPDIMdHGIFHIQ 773
Cdd:cd14634    1 YINAALMDShKQPAA-----FIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMD--AAQLCMQYWPEKTSCC-YGPIQVE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 774 CQTEDCTIAYVSREMLVTNTETGEE--HTVTHLQYVAWPDH-GVPDDSSDFLEFVKYVRSL--RVDGEPA--LVHCSAGI 846
Cdd:cd14634   73 FVSADIDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWqeQYDGREGrtVVHCLNGG 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 218505829 847 GRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd14634  153 GRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVAL 205
FERM_C_NBL4_NBL5 cd13186
FERM domain C-lobe of Novel band 4.1-like protein 4 and 5 (NBL4 and 5); NBL4 (also called ...
 218-308 8.07e-22

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: 90.42  E-value: 8.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 218 GVELHGGRDLHNLDLMIGIASAGIAVYRKYICTSFYPWVNILKISFKRKKFFIHQRQKQAESREHIVAFNMLNYRSCKNL 297
Cdd:cd13186    1 GVDLHPVKGEDGNEYFLGLTPTGILVFENKTKIGLFFWPRITKLDFKGKKLKLVVKEKDDQEQEHTFVFRLPNKKACKHL 80

                         90
                 ....*....|.
gi 218505829 298 WKSCVEHHSFF 308
Cdd:cd13186   81 WKCAVEHHAFF 91
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 695-893 1.27e-21

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: 93.94  E-value: 1.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 695 YINASYVN-MEMPAAnlvnkYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLT-ERGrtkCHQYWPDpPDIMDHGIFHI 772
Cdd:cd14636    1 YINAALMDsYRQPAA-----FIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDlAQG---CPQYWPE-EGMLRYGPIQV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 773 QCQ--TEDCTIayVSREMLVTNTETGEEH--TVTHLQYVAWPDH-GVPDDSSDFLEFVKYVRSLRVDGEPA----LVHCS 843
Cdd:cd14636   72 ECMscSMDCDV--ISRIFRICNLTRPQEGylMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECDEGegrtIIHCL 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 218505829 844 AGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKF 893
Cdd:cd14636  150 NGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRF 199
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 695-899 5.29e-21

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: 92.28  E-value: 5.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 695 YINASYVNMEMPAANlvnkYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRT-KCHQYWPDpPDIMDHGIFHIQ 773
Cdd:cd14637    1 YINAALTDSYTRSAA----FIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPE-PGLQQYGPMEVE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 774 CQTEDCTIAYVSREMLVTN-TETGEEH-TVTHLQYVAW-PDHGVPDDSSDFLEFVKYV-RSLRVDGE-PALVHCSAGIGR 848
Cdd:cd14637   76 FVSGSADEDIVTRLFRVQNiTRLQEGHlMVRHFQFLRWsAYRDTPDSKKAFLHLLASVeKWQRESGEgRTVVHCLNGGGR 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 218505829 849 TGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd14637  156 SGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
 31-109 1.07e-19

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


Pssm-ID: 340464  Cd Length: 80  Bit Score: 84.18  E-value: 1.07e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 218505829  31 CSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHgDDPVDSPRWLEASKPLRKQLKGGFPCTLHFRVRY 109
Cdd:cd01765    3 CRVRLLDGTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFY-EDNDGQKHWLDLDKKISKQLKRSGPYQFYFRVKF 80
FERM_C_FRMD3_FRMD5 cd13192
FERM domain C-lobe of FERM domain-containing protein 3 and 5 (FRMD3 and 5); FRMD3 (also called ...
 203-308 2.42e-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: 83.98  E-value: 2.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 203 AESCYINIARTLDFYGVELHGGRDLHNLDLMIGIASAGIAVYRKYICTSFYPWVNILKISFKRKKFFIHQRQKqaESREH 282
Cdd:cd13192    1 AEDNFLRKAATLETYGVDPHPVKDHRGNQLYLGFTHTGIVTFQGGKRVHHFRWNDITKFNYEGKMFILHVMQK--EEKKH 78

                         90       100
                 ....*....|....*....|....*.
gi 218505829 283 IVAFNMLNYRSCKNLWKSCVEHHSFF 308
Cdd:cd13192   79 TLGFKCPTPAACKHLWKCAVEQQAFY 104
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 695-845 4.22e-19

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 86.22  E-value: 4.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 695 YINASYVNmempAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGrtKCHQYWPDPPDIMDHGIFHIQC 774
Cdd:cd14550    1 YINASYLQ----GYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPLECETFKVTL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 775 QTED-----CTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPddSSDFLEFVKYVRSLRVDGE-PALVH-----CS 843
Cdd:cd14550   75 SGEDhsclsNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSP--IHTVFELINTVQEWAQQRDgPIVVHdryggVQ 152


                 ..
gi 218505829 844 AG 845
Cdd:cd14550  153 AA 154
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 510-595 6.07e-19

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: 81.82  E-value: 6.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 510 LIRITPDEEGRFGFNLKGGVDQKMPLVVSRINPESPADTCMpKLNEGDQIVLINGRDISEHTHDQVVMFIKASreshSRE 589
Cdd:cd00136    1 TVTLEKDPGGGLGFSIRGGKDGGGGIFVSRVEPGGPAARDG-RLRVGDRILEVNGVSLEGLTHEEAVELLKSA----GGE 75


                 ....*.
gi 218505829 590 LALVIR 595
Cdd:cd00136   76 VTLTVR 81
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 510-595 1.14e-18

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 81.17  E-value: 1.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  510 LIRITPDEEGRFGFNLKGGVDQK-MPLVVSRINPESPADTcmPKLNEGDQIVLINGRDISEHTHDQVVMFIKASREshsr 588
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKGGSDQGdPGIFVSEVLPGGAAEA--GGLKVGDRILSINGQDVENMTHEEAVLALKGSGG---- 74


                  ....*..
gi 218505829  589 ELALVIR 595
Cdd:pfam00595  75 KVTLTIL 81
FERM_F1_EPB41L5_like cd17108
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 29-110 6.06e-18

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: 79.32  E-value: 6.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  29 VICSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHgDDPVDSPRWLEASKPLRKQLKGGFPCTLHFRVR 108
Cdd:cd17108    1 IQCKVILLDGTDLSIELPKKAKGQELYEQVFYHLDLIEKDYFGLQF-MDAAQVQHWLDPTKKIKKQVKIGPPYTLRFRVK 79


                 ..
gi 218505829 109 YF 110
Cdd:cd17108   80 FY 81
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 695-899 1.68e-17

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: 82.04  E-value: 1.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 695 YINASYVN-MEMPAAnlvnkYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTErgRTKCHQYWPDpPDIMDHGIFHIQ 773
Cdd:cd14635    1 YINAALMDsYKQPSA-----FIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDP--AQLCPQYWPE-NGVHRHGPIQVE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 774 CQTEDCTIAYVSREMLVTNTETGEE--HTVTHLQYVAWPDH-GVPDDSSDFLEFVKYVRSLRVD---GE-PALVHCSAGI 846
Cdd:cd14635   73 FVSADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEyngGEgRTVVHCLNGG 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 218505829 847 GRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd14635  153 GRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
758-896 2.07e-17

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 79.63  E-value: 2.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 758 WPDPPDIMDHGIFHIQCQTEDCtiayvsrEMLVtntETGEEHTVTHLqYVAWPDHGVPDDSsDFLEFVKYVRSLRVDGEP 837
Cdd:COG2453   15 GGGEADLKREGIDAVVSLTEEE-------ELLL---GLLEEAGLEYL-HLPIPDFGAPDDE-QLQEAVDFIDEALREGKK 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 218505829 838 ALVHCSAGIGRTGVLVtmetAMCLIERNLPvyPLDIVRKMRDQRAMMVQTSSQYKFVCE 896
Cdd:COG2453   83 VLVHCRGGIGRTGTVA----AAYLVLLGLS--AEEALARVRAARPGAVETPAQRAFLER 135
FERM_N pfam09379
FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the ...
 33-96 3.06e-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: 76.47  E-value: 3.06e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 218505829   33 IRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPvDSPRWLEASKPLRKQLK 96
Cdd:pfam09379   1 VRLLDGTVLEFDVQPKATGQVLLDQVCNHLNLKEKDYFGLQFLDDN-GEHRWLDLSKRLSKQAP 63
FERM_F1_FRMD3 cd17102
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 31-110 1.81e-16

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: 74.97  E-value: 1.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  31 CSIRFLDG---LVQTFKvnKQDLGQSLLDMAYGHLGVTEKEYFGLQHgDDPVDSPRWLEASKPLRKQLKGGFPCTLHFRV 107
Cdd:cd17102    3 CTIRLLDDsevICCEFK--KDTKGQFLLDYVCNYLNLLEKDYFGLRY-VDTEKQRHWLDPNKSIYKQLKGVPPYVLCFRV 79


                 ...
gi 218505829 108 RYF 110
Cdd:cd17102   80 KFY 82
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 670-902 2.97e-16

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 80.40  E-value: 2.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 670 NLDKNRYKD------VLPYDTTRVLLQGNEDYINASYVNmempAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVML 743
Cdd:PHA02740  47 AQAENKAKDenlalhITRLLHRRIKLFNDEKVLDARFVD----GYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLI 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 744 TTLTERgrtKCH-QYWP-DPPDIMDHGIFHIQcQTEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDF 821
Cdd:PHA02740 123 SRHADK---KCFnQFWSlKEGCVITSDKFQIE-TLEIIIKPHFNLTLLSLTDKFGQAQKISHFQYTAWPADGFSHDPDAF 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 822 LEFVKYVRSLRVDGE---------PALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYK 892
Cdd:PHA02740 199 IDFFCNIDDLCADLEkhkadgkiaPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYV 278

                        250
                 ....*....|
gi 218505829 893 FvCEAILRVY 902
Cdd:PHA02740 279 F-CYHLIAAY 287
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 508-597 4.30e-16

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: 73.95  E-value: 4.30e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829   508 LVLIRITPDEEGrFGFNLKGGVDQKMPLVVSRINPESPADTCmpKLNEGDQIVLINGRDISEHTHDQVVMFIKASREShs 587
Cdd:smart00228   2 PRLVELEKGGGG-LGFSLVGGKDEGGGVVVSSVVPGSPAAKA--GLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGK-- 76

                           90
                   ....*....|
gi 218505829   588 reLALVIRRK 597
Cdd:smart00228  77 --VTLTVLRG 84
PDZ_ZASP52-like cd23068
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ...
 521-596 3.02e-15

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: 71.41  E-value: 3.02e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 218505829 521 FGFNLKGGVDQKMPLVVSRINPESPADTCmpKLNEGDQIVLINGRDISEHTHDQVVMFIKASreshSRELALVIRR 596
Cdd:cd23068   13 WGFRLQGGADFGQPLSIQKVNPGSPADKA--GLRRGDVILRINGTDTSNLTHKQAQDLIKRA----GNDLQLTVQR 82
FERM_F1_EPB41L4B cd17204
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 31-110 5.95e-15

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: 70.62  E-value: 5.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  31 CSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDdPVDSPRWLEASKPLRKQLKGGFPCTLHFRVRYF 110
Cdd:cd17204    3 CRVLLLDGTDVSVELPKHAKGQDLFDQIVYHLDLVETDYFGLQFMD-AAQVAHWLDHTKPIKKQIKIGPPYTLHFRIKYY 81
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 695-899 3.58e-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: 72.33  E-value: 3.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 695 YINASYVNmempAANLVNKYIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRTKChQYWPDPPDIMDHGIFHIQC 774
Cdd:cd17669    1 YINASYIM----GYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKDEPINCETFKVTL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 775 QTEDCTIAYVSREMLVTN-----TETGEEHTVTHLQYVAWPDhgvPDDS-SDFLEFVKYVR--SLRVDGePALVHCSAGI 846
Cdd:cd17669   76 IAEEHKCLSNEEKLIIQDfileaTQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISIIKeeAANRDG-PMIVHDEHGG 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 218505829 847 GRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd17669  152 VTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 695-899 3.58e-14

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: 72.40  E-value: 3.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 695 YINASYVNMEMPAanlvNKYIATQGPLPNTCAQFWQVVWDQKLSLVVML---TTLTERGRTkchqYWPDPPDIMDHGIFH 771
Cdd:cd17670    1 YINASYIMGYYRS----NEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQGLAEDEFV----YWPSREESMNCEAFT 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 772 IQCQTEDcTIAYVSREMLVTN------TETGEEHTVTHLQYVAWPDHGVPDDSSdfLEFVKYVR--SLRVDGePALVHCS 843
Cdd:cd17670   73 VTLISKD-RLCLSNEEQIIIHdfileaTQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKeeALTRDG-PTIVHDE 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 218505829 844 AGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd17670  149 FGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PDZ_syntrophin-like cd06801
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 511-582 8.36e-14

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: 67.60  E-value: 8.36e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218505829 511 IRITPDEEGRFGFNLKGGVDQKMPLVVSRINPESPADTCmPKLNEGDQIVLINGRDISEHTHDQVVMFIKAS 582
Cdd:cd06801    3 VRVVKQDVGGLGISIKGGAEHKMPILISKIFKGQAADQT-GQLFVGDAILSVNGENLEDATHDEAVQALKNA 73
PDZ_PDLIM-like cd06753
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 521-596 1.43e-13

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: 66.78  E-value: 1.43e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 218505829 521 FGFNLKGGVDQKMPLVVSRINPESPADTCmpKLNEGDQIVLINGRDISEHTHDQVVMFIKASreshSRELALVIRR 596
Cdd:cd06753   10 WGFRLQGGKDFNQPLTISRVTPGGKAAQA--NLRPGDVILAINGESTEGMTHLEAQNKIKAA----TGSLSLTLER 79
FERM_F1_EPB41L5 cd17205
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 27-110 2.09e-13

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: 66.60  E-value: 2.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  27 SEVICSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDpVDSPRWLEASKPLRKQLKGGFPCTLHFR 106
Cdd:cd17205    1 SIITCRVSLLDGTDVSVDLPKKAKGQELFEQIMYHLDLIEKDYFGLRFMDS-AQVAHWLDVTKSIKKQVKIGPPYCLHLR 79


                 ....
gi 218505829 107 VRYF 110
Cdd:cd17205   80 VKFY 83
FERM_F1_EPB41L1 cd17201
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 29-113 3.51e-13

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: 65.68  E-value: 3.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  29 VICSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDdpVDSPR-WLEASKPLRKQLKGGfPCTLHFRV 107
Cdd:cd17201    2 AICKVTLLDGSEYECEVEKHARGQVLFDTVCEHLNLLEKDYFGLTFCD--TESQKnWLDPSKEIKKQIRSG-PWHFAFTV 78


                 ....*.
gi 218505829 108 RYFIPD 113
Cdd:cd17201   79 KFYPPD 84
FERM_F1_MYLIP cd17104
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in E3 ...
 29-110 4.20e-13

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: 65.37  E-value: 4.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  29 VICSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHgDDPVDSPRWLEASKPLRKQLKGGFPCTLHFRVR 108
Cdd:cd17104    1 MLCLVSQPDSVVIEVEVDPKANGQECLDKVCQKLGIIEKDYFGLQY-TGPKGERLWLNLRNRISRQLPGPPPYRLRLRVK 79


                 ..
gi 218505829 109 YF 110
Cdd:cd17104   80 FF 81
FERM_F1_EPB41L3 cd17203
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 31-113 4.80e-13

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: 65.35  E-value: 4.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  31 CSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPvDSPRWLEASKPLRKQLKGGfPCTLHFRVRYF 110
Cdd:cd17203    4 CKVTLLDGSEYTCEVEKRSKGQVLFDKVCEHLNLLEKDYFGLTYRDSE-NQKNWLDPAKEIKKQIRSG-AWQFSFNVKFY 81


                 ...
gi 218505829 111 IPD 113
Cdd:cd17203   82 PPD 84
FERM_F1_FARP1_like cd17098
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, RhoGEF and ...
 31-114 6.41e-13

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


Pssm-ID: 340618  Cd Length: 85  Bit Score: 64.93  E-value: 6.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  31 CSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHgDDPVDSPRWLEASKPLRKQLKGGFPCTLHFRVRYF 110
Cdd:cd17098    3 VKVQMLDDTVHIFQVQQKALGEVLFDQVCKHLNLLESDYFGLEF-TDPEGNKCWLDPEKPILRQVKRPKDVVFKFVVKFY 81


                 ....
gi 218505829 111 IPDP 114
Cdd:cd17098   82 TPDP 85
FERM_F1_FRMD7 cd17188
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 33-114 9.05e-13

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: 64.44  E-value: 9.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  33 IRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGL----QHGddpvdSPRWLEASKPLRKQLKGGFPCTLHFRVR 108
Cdd:cd17188    6 VQFLDDSQKVFVVDQKSTGKDLFNMSCSHLNLVEKEYFGLefrnHAG-----NNVWLELLKPITKQIKNPKELIFKFTVK 80


                 ....*.
gi 218505829 109 YFIPDP 114
Cdd:cd17188   81 FFPVDP 86
FERM_F1_EPB41L cd17106
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 29-113 1.93e-12

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


Pssm-ID: 340626  Cd Length: 84  Bit Score: 63.61  E-value: 1.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  29 VICSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHgDDPVDSPRWLEASKPLRKQLKGGfPCTLHFRVR 108
Cdd:cd17106    2 QQCKVLLLDGTEYTCEVEKRAKGQVLFDKVCEHLNLLEKDYFGLTY-RDAQDQKNWLDPAKEIKKQIRSG-PWLFSFNVK 79


                 ....*
gi 218505829 109 YFIPD 113
Cdd:cd17106   80 FYPPD 84
FERM_F1_EPB41 cd17105
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 31-113 2.90e-12

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


Pssm-ID: 340625  Cd Length: 83  Bit Score: 62.91  E-value: 2.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  31 CSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPVdSPRWLEASKPLRKQLKGGfPCTLHFRVRYF 110
Cdd:cd17105    3 CKVSLLDDTVYECEVEKHAKGQDLFKKVCEHLNLLEEDYFGLAIWDSPT-SKTWLDPAKEIKKQVHGG-PWEFTFNVKFY 80


                 ...
gi 218505829 111 IPD 113
Cdd:cd17105   81 PPD 83
FERM_F1_EPB41L4A cd17107
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 27-113 1.74e-11

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: 61.20  E-value: 1.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  27 SEVICSIRFLDGLVQTFKVNKQDL----GQSLLDMAYGHLGVTEKEYFGLQHGDDPvDSPRWLEASKPLRKQLKG-GFPC 101
Cdd:cd17107    1 EEFYCEIVLLDESELILTIQQDGIksskGSVVLDVVFQHLNLLETDYFGLRYIDRQ-HQTHWLDPAKTLSEQLKLiGPPY 79

                         90
                 ....*....|..
gi 218505829 102 TLHFRVRYFIPD 113
Cdd:cd17107   80 TLYFGVKFYAED 91
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 674-892 1.81e-11

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: 64.73  E-value: 1.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 674 NRYKDVlpydTTRVLLQGNEDyINASYVNM-EMPAAnlvnkyIATQGPLPNTCAQFWQVVWDQKLSLVVMLTTLTERGRT 752
Cdd:cd14559    1 NRFTNI----QTRVSTPVGKN-LNANRVQIgNKNVA------IACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRK 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 753 KCHQYWpdppdIMDHGIFHIQCQTEDCTIAYVSREMLV-----TNTETGEEHTVTHLQYVAWPDHGvPDDSSDFLEFVKY 827
Cdd:cd14559   70 GLPPYF-----RQSGTYGSVTVKSKKTGKDELVDGLKAdmynlKITDGNKTITIPVVHVTNWPDHT-AISSEGLKELADL 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 828 VRSLRVDGEPAL-----------------VHCSAGIGRTGVLVtmeTAMCLIERNLPVYPLDIVRKMRDQR-AMMVQTSS 889
Cdd:cd14559  144 VNKSAEEKRNFYkskgssaindknkllpvIHCRAGVGRTGQLA---AAMELNKSPNNLSVEDIVSDMRTSRnGKMVQKDE 220


                 ...
gi 218505829 890 QYK 892
Cdd:cd14559  221 QLD 223
FERM_F1_EPB41L2 cd17202
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 29-113 8.52e-11

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: 58.83  E-value: 8.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  29 VICSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPvDSPRWLEASKPLRKQLKgGFPCTLHFRVR 108
Cdd:cd17202    2 VLCKVTLLDGTEYSCDLEKRAKGQVLFDKVCEHLNLLEKDYFGLLYQVSA-NQKNWLDSTKEIKRQIR-RLPWLFTFNVK 79


                 ....*
gi 218505829 109 YFIPD 113
Cdd:cd17202   80 FYPPD 84
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 820-896 1.63e-10

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: 58.90  E-value: 1.63e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 218505829 820 DFLEFVKYVRSLRVDGEPALVHCSAGIGRTGVLVTMetaMCLIERNLPVYplDIVRKMRDQR-AMMVQTSSQYKFVCE 896
Cdd:cd14494   41 MVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVAC---YLVLLGGMSAE--EAVRIVRLIRpGGIPQTIEQLDFLIK 113
FERM_F1_FARP2 cd17190
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 31-114 1.85e-10

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


Pssm-ID: 340710  Cd Length: 85  Bit Score: 57.88  E-value: 1.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  31 CSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHgDDPVDSPRWLEASKPLRKQLKGGFPCTLHFRVRYF 110
Cdd:cd17190    3 LRVKLLDNTTEPLEIEPKADGQALLSQVFKRLNLVESDYFGLEF-QNSQSNWIWLEPMKLIVKQVRRPKNTKLRLAVKFF 81


                 ....
gi 218505829 111 IPDP 114
Cdd:cd17190   82 PPDP 85
PDZ_SYNJ2BP-like cd06709
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ...
 511-584 3.57e-10

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: 57.30  E-value: 3.57e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 218505829 511 IRITPDEEGrFGFNLKGGVDQK-MP----LVVSRINPESPADTcMPKLNEGDQIVLINGRDISEHTHDQVVMFIKASRE 584
Cdd:cd06709    3 ITLKRGPSG-LGFNIVGGTDQPyIPndsgIYVAKIKEDGAAAI-DGRLQEGDKILEINGQSLENLTHQDAVELFRNAGE 79
PDZ4_MAGI-1_3-like cd06734
PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 515-582 3.61e-10

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: 57.24  E-value: 3.61e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 218505829 515 PDEEGrFGFNLKGGVDQKMPLVVSRINPESPADTCmPKLNEGDQIVLINGRDISEHTHDQVVMFIKAS 582
Cdd:cd06734    9 RENEG-FGFVIISSVNKKSGSKIGRIIPGSPADRC-GQLKVGDRILAVNGISILNLSHGDIVNLIKDS 74
PDZ_SYNPO2-like cd10820
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related ...
 521-582 4.38e-10

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: 56.55  E-value: 4.38e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218505829 521 FGFNLKGGVDQKMPLVVSRINPESPAdtCMPKLNEGDQIVLINGRDISEHTHDQVVMFIKAS 582
Cdd:cd10820   10 WGFRLQGGSEQKKPLQVAKIRKKSKA--ALAGLCEGDELLSINGKPCADLSHSEAMDLIDSS 69
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 810-894 4.86e-10

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: 59.20  E-value: 4.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 810 PDHGVPDDSSDFLEFVKYVRSLRVDGEPALVHCSAGIGRTGVLVtmetAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSS 889
Cdd:cd14505   81 PDGGVPSDIAQWQELLEELLSALENGKKVLIHCKGGLGRTGLIA----ACLLLELGDTLDPEQAIAAVRALRPGAIQTPK 156


                 ....*
gi 218505829 890 QYKFV 894
Cdd:cd14505  157 QENFL 161
PDZ_Lin-7-like cd06796
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 510-595 5.52e-10

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: 56.68  E-value: 5.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 510 LIRITPDEEGrFGFNLKGGVDQKMPLVVSRINPESPADTcMPKLNEGDQIVLINGRDISEHTHDQVVMFIKASREShsre 589
Cdd:cd06796    4 VVELPKTEEG-LGFNVMGGKEQNSPIYISRIIPGGVADR-HGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGS---- 77


                 ....*.
gi 218505829 590 LALVIR 595
Cdd:cd06796   78 VKLVVR 83
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 510-582 1.02e-09

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: 55.52  E-value: 1.02e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 218505829 510 LIRITPDEEGrFGFNL---KGGVDQkmplVVSRINPESPADTCmpKLNEGDQIVLINGRDISEHTHDQVVMFIKAS 582
Cdd:cd06768    2 LCHLVKGPEG-YGFNLhaeKGRPGH----FIREVDPGSPAERA--GLKDGDRLVEVNGENVEGESHEQVVEKIKAS 70
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 508-584 1.84e-09

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: 55.34  E-value: 1.84e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 218505829 508 LVLIRITPDEEGRFGFNLKGGVDQKMPLVVSRINPESPADTcmPKLNEGDQIVLINGRDISEHTHDQVVMFIKASRE 584
Cdd:cd06737    2 LRLVRLDRRGPESLGFSVRGGLEHGCGLFVSHVSPGSQADN--KGLRVGDEIVRINGYSISQCTHEEVINLIKTKKT 76
PDZ5_MAGI-1_3-like cd06735
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 521-596 1.89e-09

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: 55.28  E-value: 1.89e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 218505829 521 FGFNLKGGVD-QKMPLVVSRINPESPADTCmPKLNEGDQIVLINGRDISEHTHDQVVMFIKasreSHSRELALVIRR 596
Cdd:cd06735   13 FGFSIRGGREyNNMPLYVLRLAEDGPAQRD-GRLRVGDQILEINGESTQGMTHAQAIELIR----SGGSVVRLLLRR 84
FERM_F1_PTPN14_like cd17099
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 32-110 2.34e-09

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: 54.93  E-value: 2.34e-09
                         10        20        30        40        50        60        70        80
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gi 218505829  32 SIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPvDSPRWLEASKPLRKQL-KGGFPCTLHFRVRYF 110
Cdd:cd17099    7 RIQLLDNTVLECTLSPESTGQDCLEYVAQRLELREIEYFGLRYVNKK-GQLRWVDLEKPLKKQLdKHAHEPLLYFGVMFY 85
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 218-308 2.59e-09

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: 55.07  E-value: 2.59e-09
                         10        20        30        40        50        60        70        80
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gi 218505829 218 GVELHGGRDL--HNLDLMIGIASAGIAVY----RKYICTsfYPWVNILKISFKRKKFF-IHQRQKQAESrehIVAFNMLN 290
Cdd:cd00836    1 GVEFFPVKDKskKGSPIILGVNPEGISVYdeltGQPLVL--FPWPNIKKISFSGAKKFtIVVADEDKQS---KLLFQTPS 75

                         90
                 ....*....|....*...
gi 218505829 291 yRSCKNLWKSCVEHHSFF 308
Cdd:cd00836   76 -RQAKEIWKLIVGYHRFL 92
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 766-894 2.96e-09

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: 56.52  E-value: 2.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 766 DHGIFHIQCQTEDCTIAYVSREMLVTNTetgeehtvtHLQYvawPDHGVPDDSS--DFLEFVKYVRSLrvdGEPALVHCS 843
Cdd:cd14504   26 ENGIRHVVTLTEEPPPEHSDTCPGLRYH---------HIPI---EDYTPPTLEQidEFLDIVEEANAK---NEAVLVHCL 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 218505829 844 AGIGRTGvlvTMetAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFV 894
Cdd:cd14504   91 AGKGRTG---TM--LACYLVKTGKISAVDAINEIRRIRPGSIETSEQEKFV 136
PDZ_rhophilin-like cd06712
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 511-584 2.20e-08

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: 51.82  E-value: 2.20e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 218505829 511 IRITPdEEGRFGFNLKGGVdqkmPLVVSRINPESPADTCmpKLNEGDQIVLINGRDISEHTHDQVVMFIKASRE 584
Cdd:cd06712    4 VHLTK-EEGGFGFTLRGDS----PVQVASVDPGSCAAEA--GLKEGDYIVSVGGVDCKWSKHSEVVKLLKSAGE 70
PDZ_shroom2_3_4-like cd06750
PDZ domain of shroom2, shroom3, shroom4, and related domains; PDZ (PSD-95 (Postsynaptic ...
 522-596 3.73e-08

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: 51.18  E-value: 3.73e-08
                         10        20        30        40        50        60        70
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gi 218505829 522 GFNLKGGVDQKMPLVVSRINPESPADTCmPKLNEGDQIVLINGRDISEhTHDQVVMFIKASReshsRELALVIRR 596
Cdd:cd06750   14 GFTLKGGLEHGEPLVISKIEEGGKAASV-GKLQVGDEVVNINGVPLSG-SRQEAIQLVKGSH----KTLKLVVRR 82
PDZ_PDZD11-like cd06752
PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic ...
 509-588 4.25e-08

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: 51.16  E-value: 4.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 509 VLIRITPDEEgrFGFNLKGGVDQKMPLVVSRINPESPADTCmpKLNEGDQIVLINGRDISEHTHDQVVMFIKASRESHSR 588
Cdd:cd06752    3 VVLKRPPGEQ--LGFNIRGGKASGLGIFISKVIPDSDAHRL--GLKEGDQILSVNGVDFEDIEHSEAVKVLKTAREIQMR 78
FERM_F1_FRMD4 cd17103
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 31-112 5.61e-08

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: 51.13  E-value: 5.61e-08
                         10        20        30        40        50        60        70        80
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gi 218505829  31 CSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPvDSPRWLEASKPL------RKQLKGgfPCTLH 104
Cdd:cd17103    5 CQVVLLDDRRLEILVQPKLLAGDLLDLVASHFNLKEKEYFGLAYEDET-GHYNWLQLDKRVldhefpKKWSSG--PLVLH 81


                 ....*...
gi 218505829 105 FRVRYFIP 112
Cdd:cd17103   82 FAVKFYVE 89
FERM_F1_ERM_like cd17097
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 43-110 8.13e-08

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


Pssm-ID: 340617  Cd Length: 83  Bit Score: 50.36  E-value: 8.13e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 218505829  43 FKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHgDDPVDSPRWLEASKPLRKQLKG-GFPCTLHFRVRYF 110
Cdd:cd17097   14 FSIKPKAKGRELFDLVCRTIGLRETWYFGLQY-ENKKGRVAWLKPDKKVLTQDVSkNNTLKFFFLVKFY 81
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 808-896 8.16e-08

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: 53.51  E-value: 8.16e-08
                         10        20        30        40        50        60        70        80
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gi 218505829 808 AWPDHGVPddSSDF-LEFVKYVRSLRVDGEPALVHCSAGIGRTGVLVTmetamCLIERNLPVYPLDIVRKMRDQRAMMVQ 886
Cdd:cd14506   83 GWKDYGVP--SLTTiLDIVKVMAFALQEGGKVAVHCHAGLGRTGVLIA-----CYLVYALRMSADQAIRLVRSKRPNSIQ 155

                         90
                 ....*....|
gi 218505829 887 TSSQYKFVCE 896
Cdd:cd14506  156 TRGQVLCVRE 165
PDZ_RGS12-like cd06710
PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 ...
 521-583 1.77e-07

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: 49.17  E-value: 1.77e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 218505829 521 FGFNLKGgvdqKMPLVVSRINPESPADTCmpKLNEGDQIVLINGRDISEHTHDQVVMFIKASR 583
Cdd:cd06710   12 YGFTISG----QAPCVLSCVVRGSPADVA--GLKAGDQILAVNGINVSKASHEDVVKLIGKCT 68
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 217-308 3.37e-07

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: 48.82  E-value: 3.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 217 YGVELHGGRDLHNLDLMIGIASAGIAVYRKY-ICTSFYPWVNILKISFkRKKFFihqRQKQAESREHIVaFNMLNYRSCK 295
Cdd:cd13188    1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNgRPPVFFRWEDIKNVIN-HKRTF---SIECQNSEETVQ-FQFEDAETAK 75

                         90
                 ....*....|...
gi 218505829 296 NLWKSCVEHHSFF 308
Cdd:cd13188   76 YVWKLCVLQHKFY 88
FERM_F1_FARP1 cd17189
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 33-113 4.07e-07

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: 48.65  E-value: 4.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  33 IRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPvDSPRWLEASKPLRKQLKGGFPCTLHFRVRYFIP 112
Cdd:cd17189    5 VQMLDDTQEVFEVPQRAPGKVLLDAVCSHLNLVEGDYFGLEFQDHR-KVMVWLDLLKPIVKQIRRPKHVVLRFVVKFFPP 83


                 .
gi 218505829 113 D 113
Cdd:cd17189   84 D 84
PDZ_TAX1BP3-like cd10822
PDZ domain of tax1-binding protein 3 (TAX1BP3), and related domains; PDZ (PSD-95 (Postsynaptic ...
 520-584 5.40e-07

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: 48.49  E-value: 5.40e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 218505829 520 RFGFNLKGGVDQ---KMP-------LVVSRINPESPADTCmpKLNEGDQIVLINGRDISEHTHDQVVMFIKASRE 584
Cdd:cd10822   14 ILGFSIGGGIDQdpsKNPfsytdkgIYVTRVSEGGPAEKA--GLQVGDKILQVNGWDMTMVTHKQAVKRLTKKKP 86
PDZ1-PDZRN4-like cd06715
PDZ domain 1 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 517-584 6.82e-07

PDZ domain 1 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 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: 467199 [Multi-domain]  Cd Length: 92  Bit Score: 48.16  E-value: 6.82e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 218505829 517 EEGRFGFNLKGG----VDQKMP----LVVSRINPESPADTCMpKLNEGDQIVLINGRDISEHTHDQVVMFIKASRE 584
Cdd:cd06715   10 ENGSLGFNIIGGrpceNNQEGSssegIYVSKIVENGPAADEG-GLQVHDRIIEVNGKDLSKATHEEAVEAFRTAKE 84
FERM_F1_FRMD4B cd17200
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 31-111 6.87e-07

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


Pssm-ID: 340720  Cd Length: 89  Bit Score: 47.96  E-value: 6.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  31 CSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPVDSpRWLEAS-KPLRKQL-KGGFPCTLHFRVR 108
Cdd:cd17200    5 CQVHLLDDRKLELLVQPKLLSRELLDLVASHFNLKEKEYFGITFIDDTGQS-NWLQLDhRVLDHDLpKKSGPVTLYFAVR 83


                 ...
gi 218505829 109 YFI 111
Cdd:cd17200   84 FYI 86
PDZ1_MAGI-1_3-like cd06731
PDZ domain 1 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 521-578 8.02e-07

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: 47.59  E-value: 8.02e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 218505829 521 FGFNLKGGVDQKMPLVVSRINPESPADTcMPKLNEGDQIVLINGRDISEHTHDQVV-MF 578
Cdd:cd06731   13 FGFTIIGGDEPDEFLQIKSVVPDGPAAL-DGKLRTGDVLVSVNDTCVLGYTHADVVkLF 70
PDZ4_GRIP1-2-like cd06686
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 513-583 1.51e-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: 47.34  E-value: 1.51e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 218505829 513 ITPDEEGRFGFNLKGGVDQKMPL----VVSRINPESPADTCmPKLNEGDQIVLINGRDISEHTHDQVVMFIKASR 583
Cdd:cd06686   12 LRGDPLKGFGIQLQGGVFATETLssppLISFIEPDSPAERC-GVLQVGDRVLSINGIPTEDRTLEEANQLLRDSA 85
PDZ3_Dlg1-2-4-like cd06795
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 522-582 1.71e-06

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: 46.96  E-value: 1.71e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 218505829 522 GFNLKGGVDQKmPLVVSRINPESPADTCmPKLNEGDQIVLINGRDISEHTHDQVVMFIKAS 582
Cdd:cd06795   15 GFNIVGGEDGE-GIFISFILAGGPADLS-GELRRGDQILSVNGVDLRNATHEQAAAALKNA 73
PDZ2_L-delphilin-like cd06744
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
 519-582 1.92e-06

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


Pssm-ID: 467226 [Multi-domain]  Cd Length: 75  Bit Score: 46.11  E-value: 1.92e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 218505829 519 GRFGFNLKGgvdqKMPLVVSRINPESPADTCmpKLNEGDQIVLINGRDISEHTHDQVVMFIKAS 582
Cdd:cd06744    9 GSFGFTLRG----HAPVYIESVDPGSAAERA--GLKPGDRILFLNGLDVRNCSHDKVVSLLQGS 66
PDZ2_FL-whirlin cd06741
PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 517-584 2.77e-06

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: 46.10  E-value: 2.77e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 218505829 517 EEGR-FGFNLKGGVDQKMPLVVSRINPESPADTCMPKLneGDQIVLINGRDISEHTHDQVVMFIKASRE 584
Cdd:cd06741    9 EDGQsLGLMIRGGAEYGLGIYVTGVDPGSVAENAGLKV--GDQILEVNGRSFLDITHDEAVKILKSSKH 75
FERM_F1_PTPN21 cd17192
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 26-112 3.01e-06

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


Pssm-ID: 340712  Cd Length: 87  Bit Score: 46.17  E-value: 3.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  26 RSEVICSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPvDSPRWLEASKPLRKQL-KGGFPCTLH 104
Cdd:cd17192    1 KSCLVARIQLLNNEFVEFTLSVESTGQECLEAVAQRLELREITYFSLWYYNKQ-NQQRWVDLEKPLKKQLdKYALEPTVY 79


                 ....*...
gi 218505829 105 FRVRYFIP 112
Cdd:cd17192   80 FGVVFYVP 87
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 508-583 3.96e-06

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: 45.82  E-value: 3.96e-06
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gi 218505829 508 LVLIRITPDEEGrFGFNLKGGVDQKMPLVVSRINPESPADTcmPKLNEGDQIVLINGRDISEHTHDQVVMFIKASR 583
Cdd:cd06740    3 QVTLKRSKSHEG-LGFSIRGGAEHGVGIYVSLVEPGSLAEK--EGLRVGDQILRVNDVSFEKVTHAEAVKILRVSK 75
PDZ2_Scribble-like cd06703
PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 507-598 4.68e-06

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


Pssm-ID: 467187 [Multi-domain]  Cd Length: 92  Bit Score: 45.71  E-value: 4.68e-06
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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 507 YLVLIRitpDEEGrFGFNLKGGV------DQKMPLVVSRINPESPADTcMPKLNEGDQIVLINGRDISEHTHDQVVMFIK 580
Cdd:cd06703    4 TTTLIR---DGKG-LGFSIAGGKgstpfrDGDEGIFISRITEGGAADR-DGKLQVGDRVLSINGVDVTEARHDQAVALLT 78

                         90
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gi 218505829 581 asreSHSRELALVIRRKA 598
Cdd:cd06703   79 ----SSSPTITLVVEREA 92
PDZ_FRMPD1_3_4-like cd06769
PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related ...
 511-585 5.47e-06

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: 44.93  E-value: 5.47e-06
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gi 218505829 511 IRITPDEEGRFGFNLKGgvdqKMPLVVSRINPESPADTcmpKLNEGDQIVLINGRDISEHTHDQVVMFIKASRES 585
Cdd:cd06769    2 VEIQRDAVLGFGFVAGS----ERPVVVRSVTPGGPSEG---KLLPGDQILKINNEPVEDLPRERVIDLIRECKDS 69
PDZ1_INAD-like cd23063
PDZ domain 1 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 513-580 5.59e-06

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: 45.20  E-value: 5.59e-06
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gi 218505829 513 ITPDEEGRFGFNLKGG-VDQKMPLVVS-----RINPESPADTCmPKLNEGDQIVLINGRDISEHTHDQVVMFIK 580
Cdd:cd23063    4 IEKTEKKSFGICIVRGeVKVSPNTKTTgifikGIIPDSPAHKC-GRLKVGDRILSVNGNDVRNSTEQAAIDLIK 76
PDZ1_PDZD7-like cd10833
PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 511-596 8.60e-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: 44.73  E-value: 8.60e-06
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gi 218505829 511 IRITPDEEGRFGFNLKGGVDQKMPLVVSRINPESPADtcMPKLNEGDQIVLINGRDISEHTHDQVVMFIKASreshSReL 590
Cdd:cd10833    4 VTVEKSPDGSLGFSVRGGSEHGLGIFVSKVEEGSAAE--RAGLCVGDKITEVNGVSLENITMSSAVKVLTGS----NR-L 76


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gi 218505829 591 ALVIRR 596
Cdd:cd10833   77 RMVVRR 82
PDZ_SNX27-like cd23070
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density ...
 510-582 1.01e-05

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: 44.71  E-value: 1.01e-05
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gi 218505829 510 LIRITPDEEGrFGFNLKGGVDQKMPL------------VVSRINPESPADtcMPKLNEGDQIVLINGRDISEHTHDQVVM 577
Cdd:cd23070    2 VVTIVKSETG-FGFNVRGQVSEGGQLrsingelyaplqHVSAVLEGGAAD--KAGVRKGDRILEVNGVNVEGATHKQVVD 78


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gi 218505829 578 FIKAS 582
Cdd:cd23070   79 LIKSG 83
PDZ_GOPC-like cd06800
PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and ...
 516-576 1.35e-05

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: 44.28  E-value: 1.35e-05
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gi 218505829 516 DEEGrFGFNLKGGVDQKMPLVVSRINPESPADTCmPKLNEGDQIVLINGRDISEHTHDQVV 576
Cdd:cd06800    9 PHEG-LGISITGGKEHGVPILISEIHEGQPADRC-GGLYVGDAILSVNGIDLRDAKHKEAV 67
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 801-881 1.42e-05

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: 46.06  E-value: 1.42e-05
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gi 218505829 801 VTHLQYvawPDHGVPDDS--SDFLEFVKYV-RSLRVDGEPALVHCSAGIGRTGVLVtmetAMCLIERNLPvyPLDIVRKM 877
Cdd:cd14500   61 VHDWPF---DDGSPPPDDvvDDWLDLLKTRfKEEGKPGACIAVHCVAGLGRAPVLV----AIALIELGMK--PEDAVEFI 131


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gi 218505829 878 RDQR 881
Cdd:cd14500  132 RKKR 135
PDZ2_GRIP1-2-like cd06681
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 517-594 2.09e-05

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: 43.76  E-value: 2.09e-05
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gi 218505829 517 EEGRFGFNLKGGVDQKM----PLVVSRINPESPADtCMPKLNEGDQIVLINGRDISEHTHDQVVMFIKASreshSRELAL 592
Cdd:cd06681   10 EGNSFGFVIRGGAHEDRnksrPLTVTHVRPGGPAD-REGTIKPGDRLLSVDGISLHGATHAEAMSILKQC----GQEATL 84


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gi 218505829 593 VI 594
Cdd:cd06681   85 LI 86
PDZ_tamalin_CYTIP-like cd06713
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ ...
 508-582 2.49e-05

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: 43.77  E-value: 2.49e-05
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gi 218505829 508 LVLIRitpDEEGRFGFNL-------KGGVDQKMPLVVSRINPESPADTCmpKLNEGDQIVLINGRDISEHTHDQVVMFIK 580
Cdd:cd06713    6 IILEK---QDNETFGFEIqtyglhhKNSNEVEMCTYVCRVHEDSPAYLA--GLTAGDVILSVNGVSVEGASHQEIVELIR 80


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gi 218505829 581 AS 582
Cdd:cd06713   81 SS 82
PDZ3_MAGI-1_3-like cd06733
PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 517-596 3.07e-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: 43.37  E-value: 3.07e-05
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gi 218505829 517 EEGRFGFNLKGGVDQKMPLVVSRINPESPADTcMPKLNEGDQIVLINGRDISEHTHDQVVMFIKASreSHSRELALVIRR 596
Cdd:cd06733    9 QETGFGFRILGGTEEGSQVSIGAIVPGGAADL-DGRLRTGDELLSVDGVNVVGASHHKVVDLMGNA--ARNGQVNLTVRR 85
FERM_C_PTPH13 cd13187
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many ...
 228-307 3.41e-05

FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many functions of PTPN13 (also called PTPL1, PTP-BAS, hPTP1E, FAP1, or PTPL1). Mice lacking PTPN13 activity have abnormal regulation of signal transducer and activator of transcription signaling in their T cells, mild impairment of motor nerve repair, and a significant reduction in the growth of retinal glia cultures. It also plays a role in adipocyte differentiation. PTPN13 contains a kinase non-catalytic C-lobe domain (KIND), a FERM domain with two potential phosphatidylinositol 4,5-biphosphate [PtdIns(4,5)P2]-binding motifs, 5 PDZ domains, and a carboxy-terminal catalytic domain. There is an nteraction between the FERM domain of PTPL1 and PtdIns(4,5)P2 which is thought to regulate the membrane localization of PTPN13. PDZ are protein/protein interaction domains so there is the potential for numerous partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated PTPL1 substrates. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270008  Cd Length: 103  Bit Score: 43.47  E-value: 3.41e-05
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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 228 HNLDLMIGIASAGIAVYRKY----ICTSFYPWVNILKISFKRKKFFIHQRQKQAEsrEHIvaFNMLNYRSCKNLWKSCVE 303
Cdd:cd13187   14 STLSLWLGICSRGIIIYEEKngarTPVLRFPWRETQKISFDKKKFTIESRGGSGI--KHT--FYTDSYKKSQYLLQLCSA 89


                 ....
gi 218505829 304 HHSF 307
Cdd:cd13187   90 QHKF 93
FERM_C_MYLIP_IDOL cd13195
FERM domain C-lobe of E3 ubiquitin ligase myosin regulatory light chain-interacting protein ...
 217-333 4.06e-05

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: 43.78  E-value: 4.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 217 YGVELHGGRDLHNLDLMIGIASAGIAVYRK-YICTSFYPWVNILKISFKRKKFFIHQRQKQAESRehIVAFNMLNYRSCK 295
Cdd:cd13195    1 YGVEFFEVRNIEGQKLLIGVGPHGITICNDdFEVIERIPYTAIQMATSSGRVFTLTYLSDDGSVK--VLEFKLPSTRAAS 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 218505829 296 NLWKSCVEHHSFFQAKKLlpqEKNVLSQYwtlgSRNPK 333
Cdd:cd13195   79 GLYRAITEKHAFYRCETV---RSAVTDQF----SRDLK 109
PDZ2_PDZD7-like cd10834
PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 522-595 4.80e-05

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: 42.76  E-value: 4.80e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 218505829 522 GFNLKGGVDQKMPLVVSRINPESPADTcmPKLNEGDQIVLINGRDISEHTHDQVVMFIKasreSHSReLALVIR 595
Cdd:cd10834   16 GFNIRGGSEYGLGIYVSKVDPGGLAEQ--NGIKVGDQILAVNGVSFEDITHSKAVEVLK----SQTH-LMLTIK 82
FERM_F1_PTPN14 cd17191
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 30-112 7.06e-05

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


Pssm-ID: 340711  Cd Length: 87  Bit Score: 42.34  E-value: 7.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  30 ICSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHgDDPVDSPRWLEASKPLRKQL-KGGFPCTLHFRVR 108
Cdd:cd17191    5 VTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWF-LSKSQQARWVELEKPLKKQLdKFANEPLLFFGVM 83


                 ....
gi 218505829 109 YFIP 112
Cdd:cd17191   84 FYVP 87
PDZ_densin_erbin-like cd06749
PDZ domain of densin, erbin, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 507-596 7.41e-05

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: 42.31  E-value: 7.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 507 YLVLIRITPDeegrFGFNLKGGVDQK--------MPLVVSRINPESPADTCmpkLNEGDQIVLINGRDISEHTHDQVVMF 578
Cdd:cd06749    1 IRVRIEKNPG----LGFSISGGIGSQgnpfrpddDGIFVTKVQPDGPASKL---LQPGDKILEVNGYDFVNIEHGQAVSL 73

                         90
                 ....*....|....*...
gi 218505829 579 IKasreSHSRELALVIRR 596
Cdd:cd06749   74 LK----SFQNTVDLVVER 87
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 515-596 7.85e-05

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: 42.24  E-value: 7.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 515 PDEEGRFGFNLKGGVD-------QKMPLV-VSRINPESPADTCMpkLNEGDQIVLINGRDISEHTHDQVVMFIKASresh 586
Cdd:cd06702    6 VKAGGPLGLSIVGGSDhsshpfgVDEPGIfISKVIPDGAAAKSG--LRIGDRILSVNGKDLRHATHQEAVSALLSP---- 79

                         90
                 ....*....|
gi 218505829 587 SRELALVIRR 596
Cdd:cd06702   80 GQEIKLLVRH 89
PDZ2-PTPN13_FRMPD2-like cd06792
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ...
 519-596 9.03e-05

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: 41.81  E-value: 9.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 519 GRFGFNLKGGVDQKMPL---VVSRINPESPADtCMPKLNEGDQIVLINGRDISEHTHDQVVMFIKASREshsrELALVIR 595
Cdd:cd06792   12 GSLGISVTGGINTSVRHggiYVKSLVPGGAAE-QDGRIQKGDRLLEVNGVSLEGVTHKQAVECLKNAGQ----VVTLVLE 86


                 .
gi 218505829 596 R 596
Cdd:cd06792   87 R 87
FERM_C_ERM cd13194
FERM domain C-lobe/F3 of the ERM family; The ERM family includes ezrin, radixin, moesin and ...
 217-308 1.05e-04

FERM domain C-lobe/F3 of the ERM family; The ERM family includes ezrin, radixin, moesin and merlin. They are composed of a N-terminal FERM (ERM) domain (also called N-ERMAD (N-terminal ERM association domain)), a coiled coil region (CRR), and a C-terminal domain CERMAD (C-terminal ERM association domain) which has an F-actin-binding site (ABD). Two actin-binding sites have been identified in the middle and N-terminal domains. Merlin is structurally similar to the ERM proteins, but instead of an actin-binding domain (ABD), it contains a C-terminal domain (CTD), just like the proteins from the 4.1 family. Activated ezrin, radixin and moesin are thought to be involved in the linking of actin filaments to CD43, CD44, ICAM1-3 cell adhesion molecules, various membrane channels and receptors, such as the Na+/H+ exchanger-3 (NHE3), cystic fibrosis transmembrane conductance regulator (CFTR), and the beta2-adrenergic receptor. The ERM proteins exist in two states, a dormant state in which the FERM domain binds to its own C-terminal tail and thereby precludes binding of some partner proteins, and an activated state, in which the FERM domain binds to one of many membrane binding proteins and the C-terminal tail binds to F-actin. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain of ERM is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270015  Cd Length: 97  Bit Score: 41.87  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 217 YGVELHGGRDLHNLDLMIGIASAGIAVYR---KYICTSFYPWVNILKISFKRKKFFIhqrqKQAESREHIVAFNMLNYRS 293
Cdd:cd13194    2 YGVNYFEIKNKKGTDLWLGVDALGLNIYEpdnKLTPKIGFPWSEIRNISFNDKKFVI----KPIDKKAPDFVFYSPRLRI 77

                         90
                 ....*....|....*
gi 218505829 294 CKNLWKSCVEHHSFF 308
Cdd:cd13194   78 NKRILDLCMGNHELY 92
PDZ_SHANK1_3-like cd06746
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ...
 521-582 1.05e-04

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


Pssm-ID: 467228 [Multi-domain]  Cd Length: 101  Bit Score: 42.20  E-value: 1.05e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 218505829 521 FGFNLKGG--VDQKMPLVVS----------RINPESPADtcMPKLNEGDQIVLINGRDISEHTHDQVVMFIKAS 582
Cdd:cd06746   18 FGFVLRGAkaVGPILEFTPTpafpalqyleSVDPGGVAD--KAGLKKGDFLLEINGEDVVKASHEQVVNLIRQS 89
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 495-600 1.19e-04

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


Pssm-ID: 440556 [Multi-domain]  Cd Length: 341  Bit Score: 45.25  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 495 QYYCDKSDDGDGYLVLIR-------------ITPDEEGRFGFNLKG-----GVDQKMP---LVVSRINPESPADTcmPKL 553
Cdd:COG0793   12 DNYVDEYDDRDLAEGALNgmlgelgdphsyyLDPEEYEDFQESTSGefgglGAELGEEdgkVVVVSVIPGSPAEK--AGI 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 218505829 554 NEGDQIVLINGRDISEHTHDQVVMFIKA----------SRESHSRELALVIRRKAVR 600
Cdd:COG0793   90 KPGDIILAIDGKSVAGLTLDDAVKLLRGkagtkvtltiKRPGEGEPITVTLTRAEIK 146
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 ...
 516-596 1.39e-04

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: 41.48  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 516 DEEGRFGFNLKGGVDQKM-PLVVSRINPESPADTcMPKLNEGDQIVLINGRDISEHTHDQVVMFIKASReshSRELALVI 594
Cdd:cd06762    9 EEGSGLGFSLAGGSDLENkSITVHRVFPSGLAAQ-EGTIQKGDRILSINGKSLKGVTHGDALSVLKQAR---LPKVAVVV 84


                 ..
gi 218505829 595 RR 596
Cdd:cd06762   85 IR 86
PRK15375 PRK15375
type III secretion system effector GTPase-activating protein SptP;
797-891 1.46e-04

type III secretion system effector GTPase-activating protein SptP;


Pssm-ID: 185273 [Multi-domain]  Cd Length: 535  Bit Score: 45.56  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 797 EEHTVTHLQYVAWPDHGvPDDSSDFLEFV-KYVRSLRVDGEPA---------LVHCSAGIGRTGvlvTMETAMCLieRNL 866
Cdd:PRK15375 419 KRYTIPVLHVKNWPDHQ-PLPSTDQLEYLaDRVKNSNQNGAPGrsssdkhlpMIHCLGGVGRTG---TMAAALVL--KDN 492

                         90       100
                 ....*....|....*....|....*..
gi 218505829 867 PVYPLDIVR-KMRDQR-AMMVQTSSQY 891
Cdd:PRK15375 493 PHSNLEQVRaDFRNSRnNRMLEDASQF 519
PDZ7_MUPP1-PD6_PATJ-like cd06671
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ...
 540-582 1.52e-04

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: 41.54  E-value: 1.52e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 218505829 540 INPESPADTCmPKLNEGDQIVLINGRDISEHTHDQVVMFIKAS 582
Cdd:cd06671   43 VLEDSPAGRN-GTLKTGDRILEVNGVDLRNATHEEAVEAIRNA 84
PDZ4_PTPN13-like cd06696
PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 517-596 1.94e-04

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


Pssm-ID: 467182 [Multi-domain]  Cd Length: 85  Bit Score: 40.75  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 517 EEGRFGFNLKGGVDQKMPLVVSRINPESPADTcmpKLNEGDQIVLINGRDISEHTHDQVVMFIKASreshSRELALVIRR 596
Cdd:cd06696   12 EKGSLGFTVTKGKDDNGCYIHDIVQDPAKSDG---RLRPGDRLIMVNGVDVTNMSHTEAVSLLRAA----PKEVTLVLGR 84
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 802-863 5.25e-04

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa TpbA; This subfamily contains bacterial protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DUSPs) related to Pseudomonas aeruginosa TpbA, a DUSP that negatively regulates biofilm formation by converting extracellular quorum sensing signals and to Mycobacterium tuberculosis PtpB, a PTP virulence factor that attenuates host immune defenses by interfering with signal transduction pathways in macrophages. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides, while DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and PTPs.


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 41.59  E-value: 5.25e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218505829 802 THLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVDGePALVHCSAGIGRTGVLVtmetAMCLIE 863
Cdd:cd14529   57 DGVKYVNLPLSATRPTESDVQSFLLIMDLKLAPG-PVLIHCKHGKDRTGLVS----ALYRIV 113
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 809-881 5.64e-04

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 41.55  E-value: 5.64e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 218505829 809 WP--DHGVPDDS--SDFLEFVKYVRSLRVDGEPAL-VHCSAGIGRTGVLVtmetAMCLIERNlPVYPLDIVRKMRDQR 881
Cdd:PTZ00242  67 WPfdDGAPPPKAviDNWLRLLDQEFAKQSTPPETIaVHCVAGLGRAPILV----ALALVEYG-GMEPLDAVGFVREKR 139
PDZ2_harmonin cd06738
PDZ domain 2 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 522-595 6.44e-04

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: 39.23  E-value: 6.44e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 218505829 522 GFNLKGGVDQKMPLVVSRINPESPADTCmpKLNEGDQIVLINGRDISEHTHDQVVMFIKAsreshSRELALVIR 595
Cdd:cd06738   16 GCSISSGPTQKPGIFISNVKPGSLAEEV--GLEVGDQIVEVNGTSFTNVDHKEAVMALKS-----SRHLTITVR 82
PDZ_RapGEF2_RapGEF6-like cd06755
PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange ...
 515-582 7.49e-04

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: 39.17  E-value: 7.49e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 218505829 515 PDEEGRFGFNLKGGVDQKMPLVVSRINPESPADTCmpKLNEGDQIVLINGRDISEHTHDQVVMFIKAS 582
Cdd:cd06755    8 PSRESPLHFSLLGGSEKGFGIFVSKVEKGSKAAEA--GLKRGDQILEVNGQNFENITLKKALEILRNN 73
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 536-596 7.83e-04

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


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 38.28  E-value: 7.83e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 218505829  536 VVSRINPESPADTCmpKLNEGDQIVLINGRDIseHTHDQVVMFIkasRESHSRELALVIRR 596
Cdd:pfam17820   1 VVTAVVPGSPAERA--GLRVGDVILAVNGKPV--RSLEDVARLL---QGSAGESVTLTVRR 54
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
 779-862 8.91e-04

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: 40.76  E-value: 8.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  779 CTIAYVSREMLVTNTETGEEHTVTH--LQY--VAWPDHGVPDDSsDFLEFVKYVRSLRVDgePALV-HCSAGIGRTgvlv 853
Cdd:pfam14566  74 LTVVDVWESDVQTPEEVYERLKAEGpgVDYrrIPITDEKAPLEE-DFDALISIVKDAPED--TALVfNCQMGRGRT---- 146

                          90
                  ....*....|..
gi 218505829  854 TmeTAM---CLI 862
Cdd:pfam14566 147 T--TAMviaDLV 156
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 771-854 1.03e-03

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


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 39.94  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  771 HIQCQTEDCTIAYVSREMLVTNTETGeehtvtHLQYVAWPDHGVPDD--SSDFLEFVKYVRSLRVDGEPALVHCSAGIGR 848
Cdd:pfam00782   9 ASDAFLSKLGITAVINVTREVDLYNS------GILYLRIPVEDNHETniSKYLEEAVEFIDDARQKGGKVLVHCQAGISR 82


                  ....*.
gi 218505829  849 TGVLVT 854
Cdd:pfam00782  83 SATLII 88
FERM_C_FRMD4A_FRMD4B cd13191
FERM domain C-lobe of FERM domain-containing protein 4A and 4B (FRMD4A and 4B); FRMD4A is part ...
 218-312 1.12e-03

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: 39.64  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 218 GVELHGGRDLHNLDLMIGIASAGIAVYR---KYICTSFYPWVNILKISFKRKKFFIH---QRQKQAESREHIVAFNML-- 289
Cdd:cd13191    1 GVHYYEVKDKNGIPWWLGVSYKGIGQYDlqdKVKPRKFFQWKQLENLYFRDRKFSIEvrdPRRNSHRSRRTFQSSSVSvh 80

                         90       100
                 ....*....|....*....|....*...
gi 218505829 290 -----NYRSCKNLWKSCVEHHSFFQAKK 312
Cdd:cd13191   81 vwygqTPALCKTIWSMAIAQHQFYLDRK 108
Y_phosphatase3 pfam13350
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
 806-853 1.30e-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: 41.46  E-value: 1.30e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 218505829  806 YVAWPDHGVPddssdflEFVKYVRSLRVDGEPALVHCSAGIGRTGVLV 853
Cdd:pfam13350 107 YRDMVTSARA-------AYRALFEALADNDGPVLFHCTAGKDRTGVAA 147
PDZ1_LNX1_2-like cd06677
PDZ domain 1 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 512-580 1.42e-03

PDZ domain 1 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of LNX1 (also known as PDZ domain-containing RING finger protein 2, PDZRN2) and LNX2 (also known as PDZ domain-containing RING finger protein 1, PDZRN1), and related domains. LNX1 and LNX2 are Ring (Really Interesting New Gene) finger and PDZ domain-containing E3 ubiquitin ligases that bind to the cell fate determinant protein NUMB and mediate its ubiquitination. LNX1 can ubiquitinate a number of other ligands including PPFIA1, KLHL11, KIF7 and ERC2. LNX1 and LNX2 each have four PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This LNX family 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: 467165 [Multi-domain]  Cd Length: 89  Bit Score: 38.77  E-value: 1.42e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218505829 512 RITPDEEgrFGFNLKGGVDQkmPL---VVSRINPESPADTcMPKLNEGDQIVLINGRDISEHTHDQVVMFIK 580
Cdd:cd06677   10 RSDPYEE--LGISIVGGNDT--PLiniVIQEVYRDGVIAR-DGRLLPGDQILEVNGVDISNVTHSQARSVLR 76
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
760-885 1.49e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 39.96  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829   760 DPPDIMDHGIFH-IQCQTEDCTIAYVSREMLVTnteTGEEHTVTHLqyvawpdhgvpddSSDFLEFVKYVRSLRVDGEPA 838
Cdd:smart00195  18 NLALLKKLGITHvINVTNEVPNYNGSDFTYLGV---PIDDNTETKI-------------SPYFPEAVEFIEDAESKGGKV 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 218505829   839 LVHCSAGIGRTGVLVtmeTAMCLIERNLPVYplDIVRKMRDQRAMMV 885
Cdd:smart00195  82 LVHCQAGVSRSATLI---IAYLMKTRNMSLN--DAYDFVKDRRPIIS 123
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 528-596 1.65e-03

Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, protein turnover, chaperones, Transcription];


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 41.61  E-value: 1.65e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 218505829 528 GVDQKMPLVVSRINPESPADTCmpKLNEGDQIVLINGRDIseHTHDQVVMFIKASREshsRELALVIRR 596
Cdd:COG0750  123 GVPVLTPPVVGEVVPGSPAAKA--GLQPGDRIVAINGQPV--TSWDDLVDIIRASPG---KPLTLTVER 184
FERM_F1_FRMD4A cd17199
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 31-111 1.82e-03

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


Pssm-ID: 340719  Cd Length: 89  Bit Score: 38.41  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829  31 CSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDpVDSPRWLEASKPLRKQ--LKGGFPCTLHFRVR 108
Cdd:cd17199    5 CQVHLLDDRKLELLVQPKLLAKELLDLVASHFNLKEKEYFGIAFTDE-TGHLNWLQLDRRVLEHdfPKKSGPVVLYFCVR 83


                 ...
gi 218505829 109 YFI 111
Cdd:cd17199   84 FYI 86
PDZ12_MUPP1-like cd06675
PDZ domain 12 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 10 of protein-associated tight ...
 513-580 2.06e-03

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


Pssm-ID: 467163 [Multi-domain]  Cd Length: 86  Bit Score: 38.11  E-value: 2.06e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 218505829 513 ITPDEEGRFGFNLKGGVDQKM---PLVVSRINPESPADTCMpKLNEGDQIVLINGRDISEHTHDQVVMFIK 580
Cdd:cd06675    5 IKRGPQDSLGISIAGGVGSPLgdvPVFIAMIQPNGVAAQTG-KLKVGDRIVSINGQSTDGLTHSEAVNLLK 74
PDZ_CNK1_2_3-like cd06748
PDZ domain of connector enhancer of kinase suppressor of ras 1 (CNK1), CNK2, CNK3, and related ...
 509-595 2.12e-03

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


Pssm-ID: 467230 [Multi-domain]  Cd Length: 81  Bit Score: 37.97  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 509 VLIRITPDEEgrFGFNLKG---GVDqkmplVVSRINPESPADTCMpKLNEGDQIVLINGRDISEHTHDQVVmfiKASRES 585
Cdd:cd06748    4 QLTNKKPEEG--LGLEIKStynGLH-----VITGTKENSPADRCG-KIHAGDEVIQVNYQTVVGWQLKNLV---RALRED 72

                         90
                 ....*....|
gi 218505829 586 hSRELALVIR 595
Cdd:cd06748   73 -PHGVTLTLK 81
PTPLP-like cd14495
Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily ...
 785-892 2.25e-03

Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily contains the tandem protein tyrosine phosphatase (PTP)-like domains of protein tyrosine phosphatase-like phytases (PTPLPs) and similar domains including the PTP domain of Pseudomonas syringae tyrosine-protein phosphatase hopPtoD2. PTPLPs, also known as cysteine phytases, are one of four known classes of phytases, enzymes that degrade phytate (inositol hexakisphosphate [InsP(6)]) to less-phosphorylated myo-inositol derivatives. Phytate is the most abundant cellular inositol phosphate and plays important roles in a broad scope of cellular processes, including DNA repair, RNA processing and export, development, apoptosis, and pathogenicity. PTPLPs adopt a PTP fold, including the active-site signature sequence (CX5R(S/T)) and utilize a classical PTP reaction mechanism. However, these enzymes display no catalytic activity against classical PTP substrates due to several unique structural features that confer specificity for myo-inositol polyphosphates.


Pssm-ID: 350345  Cd Length: 278  Bit Score: 40.82  E-value: 2.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 785 SREMLVTNTETgEEHTVTH--LQYV--AWPDHGVPDDSS-DflEFVKYVRSLrvdgePA----LVHCSAGIGRTgvlvTM 855
Cdd:cd14495  135 PKTVKVESVRT-EEELVKKkgAHYVriAATDHVWPDDEEiD--AFVAFYRSL-----PAdawlHFHCRAGKGRT----TT 202

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 218505829 856 ETAMCLIERNLPVYPL-DIVRKMR----DQRAMMVQTSSQYK 892
Cdd:cd14495  203 FMVMYDMLKNPKDVSFdDIIARQYliggNYLAYEVDKDKNWK 244
PDZ1_ZO1-like cd06727
PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 521-596 2.60e-03

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


Pssm-ID: 467209 [Multi-domain]  Cd Length: 87  Bit Score: 37.64  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 521 FGFNLKGGVDQKMP------LVVSRINPESPADTcmpKLNEGDQIVLINGRDISEHTHDQVVMFIKASREshsrELALVI 594
Cdd:cd06727   13 FGIAVSGGRDNPHFqsgdtsIVISDVLKGGPAEG---KLQENDRVVSVNGVSMENVEHSFAVQILRKCGK----TANITV 85


                 ..
gi 218505829 595 RR 596
Cdd:cd06727   86 KR 87
PDZ4_LNX1_2-like cd06680
PDZ domain 4 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 519-583 2.86e-03

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


Pssm-ID: 467168 [Multi-domain]  Cd Length: 89  Bit Score: 37.71  E-value: 2.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 218505829 519 GRFGFNLKGGVDQ---KMPLVVSRINPESPADTcMPKLNEGDQIVLINGRDISEHTHDQVVMFIKASR 583
Cdd:cd06680   11 GSLGFSIVGGYEEshgNQPFFVKSIVPGTPAYN-DGRLKCGDIILAVNGVSTVGMSHAALVPLLKEQR 77
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 810-894 3.37e-03

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase/transmembrane phosphatase with tensin homology; Voltage-sensitive phosphatase (VSP) proteins comprise a family of phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. This family is conserved in deuterostomes; VSP was first identified as a sperm flagellar plasma membrane protein in Ciona intestinalis. Gene duplication events in primates resulted in the presence of paralogs, transmembrane phosphatase with tensin homology (TPTE) and TPTE2, that retain protein domain architecture but, in the case of TPTE, have lost catalytic activity. TPTE, also called cancer/testis antigen 44 (CT44), may play a role in the signal transduction pathways of the endocrine or spermatogenic function of the testis. TPTE2, also called TPTE and PTEN homologous inositol lipid phosphatase (TPIP), occurs in several differentially spliced forms; TPIP alpha displays phosphoinositide 3-phosphatase activity and is localized on the endoplasmic reticulum, while TPIP beta is cytosolic and lacks detectable phosphatase activity. VSP/TPTE proteins contain an N-terminal voltage sensor consisting of four transmembrane segments, a protein tyrosine phosphatase (PTP)-like phosphoinositide phosphatase catalytic domain, followed by a regulatory C2 domain.


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 39.27  E-value: 3.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 810 PDHGVPDdSSDFLEFVKYVRS-LRVDGEPAL-VHCSAGIGRTGVLVT---METAMCL-IERNLPVYPLDIVRKMRDQRAM 883
Cdd:cd14510   82 DDHNVPT-LDEMLSFTAEVREwMAADPKNVVaIHCKGGKGRTGTMVCawlIYSGQFEsAKEALEYFGERRTDKSVSSKFQ 160

                         90
                 ....*....|.
gi 218505829 884 MVQTSSQYKFV 894
Cdd:cd14510  161 GVETPSQSRYV 171
PDZ2-PDZRN4-like cd06716
PDZ domain 2 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 537-596 4.26e-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: 37.25  E-value: 4.26e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 537 VSRINPESPADTcMPKLNEGDQIVLINGRDIseHTHDQVVMFIKASREShsreLALVIRR 596
Cdd:cd06716   35 VSEVDPNSIAAK-DGRIREGDQILQINGVDV--QNREEAIALLSEEEKS----ITLLVAR 87
PDZ5_DrPTPN13-like cd23060
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ...
 511-583 4.31e-03

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


Pssm-ID: 467273 [Multi-domain]  Cd Length: 80  Bit Score: 36.94  E-value: 4.31e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 218505829 511 IRITPDEEGRFGFNLKGGvDQKMPLVVSRINPESPADTcMPKLNEGDQIVLINGRDISEHTHDQVVMFIKASR 583
Cdd:cd23060    2 IELEKPANGGLGFSLVGG-EGGSGIFVKSISPGGVADR-DGRLQVGDRLLQVNGESVIGLSHSKAVNILRKAK 72
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 766-848 5.04e-03

dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in typical and atypical dual-specificity phosphatases (DUSPs), which function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). Typical DUSPs, also called mitogen-activated protein kinase (MAPK) phosphatases (MKPs), deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain. Atypical DUSPs contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. Also included in this family are dual specificity phosphatase-like domains of catalytically inactive members such as serine/threonine/tyrosine-interacting protein (STYX) and serine/threonine/tyrosine interacting like 1 (STYXL1), as well as active phosphatases with substrates that are not phosphoproteins such as PTP localized to the mitochondrion 1 (PTPMT1), which is a lipid phosphatase, and laforin, which is a glycogen phosphatase.


Pssm-ID: 350348 [Multi-domain]  Cd Length: 135  Bit Score: 38.30  E-value: 5.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218505829 766 DHGIFHI-QCQTEDCTIAYvsremlvtntetgeEHTVTHLQyVAWPDHGVPDDSSDFLEFVKYVRSLRVDGEPALVHCSA 844
Cdd:cd14498   24 KLGITHIlNVAGEPPPNKF--------------PDGIKYLR-IPIEDSPDEDILSHFEEAIEFIEEALKKGGKVLVHCQA 88


                 ....
gi 218505829 845 GIGR 848
Cdd:cd14498   89 GVSR 92
PDZ7_PDZD2-PDZ4_hPro-IL-16-like cd06763
PDZ domain 7 of PDZ domain containing 2 (PDZD2), PDZ domain 4 of human pro-interleukin-16 ...
 522-581 5.46e-03

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


Pssm-ID: 467244 [Multi-domain]  Cd Length: 86  Bit Score: 36.82  E-value: 5.46e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 218505829 522 GFNLKGGVDQKM---PLVVSRINPESPADTCMPkLNEGDQIVLINGRDISEHTHDQVVMFIKA 581
Cdd:cd06763   14 GFSLEGGKGSPLgdrPLTIKRIFKGGAAEQSGV-LQVGDEILQINGTSLQGLTRFEAWNIIKS 75
DSP_MKP_classI cd14565
dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; ...
 798-849 5.75e-03

dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs and function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III). Class I MKPs consist of DUSP1/MKP-1, DUSP2 (PAC1), DUSP4/MKP-2 and DUSP5. They are all mitogen- and stress-inducible nuclear MKPs. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350413 [Multi-domain]  Cd Length: 138  Bit Score: 38.14  E-value: 5.75e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 218505829 798 EHTVTHLQYVAWP--DHGVPDDSSDFLEFVKYVRSLRVDGEPALVHCSAGIGRT 849
Cdd:cd14565   39 NHFEDHFQYKSIPveDSHNADISSWFEEAIGFIDKVKASGGRVLVHCQAGISRS 92
DSP_DUSP4 cd14640
dual specificity phosphatase domain of dual specificity protein phosphatase 4; Dual ...
 799-852 7.90e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 4; Dual specificity protein phosphatase 4 (DUSP4), also called mitogen-activated protein kinase (MAPK) phosphatase 2 (MKP-2), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other 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. DUSP4 regulates either ERK or c-JUN N-terminal kinase (JNK), depending on the cell type. It dephosphorylates nuclear JNK and induces apoptosis in diffuse large B cell lymphoma (DLBCL) cells. It acts as a negative regulator of macrophage M1 activation and inhibits inflammation during macrophage-adipocyte interaction. It has been linked to different aspects of cancer: it may have a role in the development of ovarian cancers, oesophagogastric rib metastasis, and pancreatic tumours; it may also be a candidate tumor suppressor gene, with its deletion implicated in breast cancer, prostate cancer, and gliomas. DUSP4/MKP-2 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: 350488 [Multi-domain]  Cd Length: 141  Bit Score: 37.71  E-value: 7.90e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 218505829 799 HTVTHLQYVAWP--DHGVPDDSSDFLEFVKYVRSLRVDGEPALVHCSAGIGRTGVL 852
Cdd:cd14640   40 HFEGHYQYKCIPveDNHKADISSWFMEAIEYIDSVKDCNGRVLVHCQAGISRSATI 95
 
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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