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Conserved domains on  [gi|1958779398|ref|XP_038966966|]
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tyrosine-protein phosphatase non-receptor type 3 isoform X3 [Rattus norvegicus]

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: 604.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 631 EGSMELLKKGLESGTVLIQFEQLYRKKPGLAVTFAKLPQNLDKNRYKDVLPYDTTRVLLQGNEDYINASYVNMEIPAANL 710
Cdd:cd14600     1 EESMAQLKKGLESGTVLIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQGNEDYINASYVNMEIPSANI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 711 VNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQCQAEDCTIAYVSREMLV 790
Cdd:cd14600    81 VNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 791 TNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVGGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYP 870
Cdd:cd14600   161 TNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYP 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958779398 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 ...
 30-222 1.23e-56

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: 193.67  E-value: 1.23e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398   30 TCSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPVDSPRWLEASKPLRKQLKGGLPCILHFRVRY 109
Cdd:smart00295   1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRHWLDPAKTLLDQDVKSEPLTLYFRVKF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  110 FIPDPNTLQQEQTRH-LYFLQLKMDVCEGRLTCPLNSAVVLASYAVQSHIGDFNSSIH-HPGYLADSQFIPDQ------N 181
Cdd:smart00295  81 YPPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQlldsrkL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1958779398  182 DDFLSKVESLHEQHSGLKQSEAESCYINIARTLDFYGVELH 222
Cdd:smart00295 161 KEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
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 1958779398 216 FYGVELHGGRDLHNLDLMIGIASAGIAVYRKYICTSFYPWVNILKISFKRKKFFIHQRQKQAESREHIVAFNMLNYRSCK 295
Cdd:cd13189     1 LYGVELHSARDSNNLELQIGVSSAGILVFQNGIRINTFPWSKIVKISFKRKQFFIQLRREPNESRDTILGFNMLSYRACK 80

                          90
                  ....*....|....
gi 1958779398 296 NLWKSCVEHHSFFQ 309
Cdd:cd13189    81 NLWKSCVEHHTFFR 94
PDZ_PTPN3-4-like cd06706
PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein ...
 506-595 6.69e-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: 187.13  E-value: 6.69e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 506 GYLVLIRITPDKEGRFGFNLKGGVDQKMPLVVSRINPESPADTCMPKLNEGDQIVLINGRDISEHTHDQVVMFIKASRES 585
Cdd:cd06706     1 DGLVLIRMKPDENGRFGFNVKGGVDQKMPVIVSRVAPGTPADLCIPRLNEGDQVLLINGRDISEHTHDQVVMFIKASRER 80

                          90
                  ....*....|
gi 1958779398 586 HSRELALVIR 595
Cdd:cd06706    81 HSGELVLLVR 90
 
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: 604.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 631 EGSMELLKKGLESGTVLIQFEQLYRKKPGLAVTFAKLPQNLDKNRYKDVLPYDTTRVLLQGNEDYINASYVNMEIPAANL 710
Cdd:cd14600     1 EESMAQLKKGLESGTVLIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQGNEDYINASYVNMEIPSANI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 711 VNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQCQAEDCTIAYVSREMLV 790
Cdd:cd14600    81 VNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 791 TNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVGGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYP 870
Cdd:cd14600   161 TNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYP 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958779398 871 LDIVRKMRDQRAMMVQTSSQYKFVCEAILRVYEE 904
Cdd:cd14600   241 LDIVRKMRDQRAMMVQTSSQYKFVCEAILRVYEE 274
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
649-900 1.61e-107

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 332.32  E-value: 1.61e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  649 QFEQLYRKKPG-LAVTFAKLPQNLDKNRYKDVLPYDTTRVLLQGNE----DYINASYVNMEipaaNLVNKYIATQGPLPH 723
Cdd:smart00194   5 EFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPgegsDYINASYIDGP----NGPKAYIATQGPLPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  724 TCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDI-MDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEHTVT 802
Cdd:smart00194  81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEpLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  803 HLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVGGE-PALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQR 881
Cdd:smart00194 161 HYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTgPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQR 240

                          250
                   ....*....|....*....
gi 1958779398  882 AMMVQTSSQYKFVCEAILR 900
Cdd:smart00194 241 PGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
670-899 3.07e-103

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 320.34  E-value: 3.07e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 670 NLDKNRYKDVLPYDTTRVLLQ---GNEDYINASYVNMEipaaNLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTL 746
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTgdpGPSDYINASYIDGY----KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 747 TERGRTKCHQYWPDPP-DIMDHGIFHIQCQAE-DCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEF 824
Cdd:pfam00102  77 EEKGREKCAQYWPEEEgESLEYGDFTVTLKKEkEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDL 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958779398 825 VKYVRSLRVGGE--PALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:pfam00102 157 LRKVRKSSLDGRsgPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 30-222 1.23e-56

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: 193.67  E-value: 1.23e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398   30 TCSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPVDSPRWLEASKPLRKQLKGGLPCILHFRVRY 109
Cdd:smart00295   1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRHWLDPAKTLLDQDVKSEPLTLYFRVKF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  110 FIPDPNTLQQEQTRH-LYFLQLKMDVCEGRLTCPLNSAVVLASYAVQSHIGDFNSSIH-HPGYLADSQFIPDQ------N 181
Cdd:smart00295  81 YPPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQlldsrkL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1958779398  182 DDFLSKVESLHEQHSGLKQSEAESCYINIARTLDFYGVELH 222
Cdd:smart00295 161 KEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
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 1958779398 216 FYGVELHGGRDLHNLDLMIGIASAGIAVYRKYICTSFYPWVNILKISFKRKKFFIHQRQKQAESREHIVAFNMLNYRSCK 295
Cdd:cd13189     1 LYGVELHSARDSNNLELQIGVSSAGILVFQNGIRINTFPWSKIVKISFKRKQFFIQLRREPNESRDTILGFNMLSYRACK 80

                          90
                  ....*....|....
gi 1958779398 296 NLWKSCVEHHSFFQ 309
Cdd:cd13189    81 NLWKSCVEHHTFFR 94
PDZ_PTPN3-4-like cd06706
PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein ...
 506-595 6.69e-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: 187.13  E-value: 6.69e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 506 GYLVLIRITPDKEGRFGFNLKGGVDQKMPLVVSRINPESPADTCMPKLNEGDQIVLINGRDISEHTHDQVVMFIKASRES 585
Cdd:cd06706     1 DGLVLIRMKPDENGRFGFNVKGGVDQKMPVIVSRVAPGTPADLCIPRLNEGDQVLLINGRDISEHTHDQVVMFIKASRER 80

                          90
                  ....*....|
gi 1958779398 586 HSRELALVIR 595
Cdd:cd06706    81 HSGELVLLVR 90
FERM_F1_PTPN3 cd17193
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 28-111 4.50e-47

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: 162.33  E-value: 4.50e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  28 EVTCSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPVDSPRWLEASKPLRKQLKGGLPCILHFRV 107
Cdd:cd17193     1 EVICNVHFLDGSVQSFKVNKQDTGQVLLDMAYNHLGLTEREYFGLQHNEDSVDSPRWLEPSKPIRKQLKGGFPCSLHFRV 80


                  ....
gi 1958779398 108 RYFI 111
Cdd:cd17193    81 RFFI 84
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 669-902 8.79e-43

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 158.24  E-value: 8.79e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 669 QNLDKNRYKDVLPYDTTRVLL---QGNEDYINASYVNmeipAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTT 745
Cdd:PHA02742   51 KNMKKCRYPDAPCFDRNRVILkieDGGDDFINASYVD----GHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITK 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 746 LTERGRTKCHQYW-PDPPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEF 824
Cdd:PHA02742  127 IMEDGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDF 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 825 VKYVRSL------------RVGGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYK 892
Cdd:PHA02742  207 VLAVREAdlkadvdikgenIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYI 286

                         250
                  ....*....|
gi 1958779398 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 4.61e-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: 123.53  E-value: 4.61e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 112 PDPNTLQQEQTRHLYFLQLKMDVCEGRLTCPLNSAVVLASYAVQSHIGDFNSSIHHPGYLADSQFIPDQN------DDFL 185
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLlrkmksKELE 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958779398 186 SKVESLHEQHSGLKQSEAESCYINIARTLDFYGVELH 222
Cdd:pfam00373  81 KRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
663-891 1.52e-31

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 124.82  E-value: 1.52e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 663 TFAKLPQNLDKNRYKDVLPYDTTRVllQGNEDYINASYVNMEIPaanlvNKYIATQGPLPHTCAQFWQVVWDQKLSLVVM 742
Cdd:COG5599    35 QYLQNINGSPLNRFRDIQPYKETAL--RANLGYLNANYIQVIGN-----HRYIATQYPLEEQLEDFFQMLFDNNTPVLVV 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 743 LTTLTE--RGRTKCHQYWPDPPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEHT-VTHLQYVAWPDHGVPdDSS 819
Cdd:COG5599   108 LASDDEisKPKVKMPVYFRQDGEYGKYEVSSELTESIQLRDGIEARTYVLTIKGTGQKKIeIPVLHVKNWPDHGAI-SAE 186

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958779398 820 DFLEFVKYV----RSLRVGGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYP--LDIVRKMRDQRAM-MVQTSSQY 891
Cdd:COG5599   187 ALKNLADLIdkkeKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVQITLsvEEIVIDMRTSRNGgMVQTSEQL 265
FERM_C pfam09380
FERM C-terminal PH-like domain;
226-312 3.05e-30

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 114.27  E-value: 3.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 226 DLHNLDLMIGIASAGIAVYRKYICTS-FYPWVNILKISFKRKKFFIHQRQKqaeSREHIVAFNMLNYRSCKNLWKSCVEH 304
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKILnLFPWREIRKISFKRKKFLIKLRDK---SSEETLGFYTESSRACKYLWKLCVEQ 77


                  ....*...
gi 1958779398 305 HSFFQAKK 312
Cdd:pfam09380  78 HTFFRLRR 85
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 510-595 8.14e-19

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 81.56  E-value: 8.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 510 LIRITPDKEGRFGFNLKGGVDQK-MPLVVSRINPESPADTcmPKLNEGDQIVLINGRDISEHTHDQVVMFIKASREshsr 588
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKGGSDQGdPGIFVSEVLPGGAAEA--GGLKVGDRILSINGQDVENMTHEEAVLALKGSGG---- 74


                  ....*..
gi 1958779398 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 6.79e-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: 73.57  E-value: 6.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  508 LVLIRITPDKEGrFGFNLKGGVDQKMPLVVSRINPESPADTCmpKLNEGDQIVLINGRDISEHTHDQVVMFIKASREShs 587
Cdd:smart00228   2 PRLVELEKGGGG-LGFSLVGGKDEGGGVVVSSVVPGSPAAKA--GLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGK-- 76

                           90
                   ....*....|
gi 1958779398  588 reLALVIRRK 597
Cdd:smart00228  77 --VTLTVLRG 84
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 535-600 1.94e-04

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


Pssm-ID: 440556 [Multi-domain]  Cd Length: 341  Bit Score: 44.48  E-value: 1.94e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958779398 535 LVVSRINPESPADTcmPKLNEGDQIVLINGRDISEHTHDQVVMFIKA----------SRESHSRELALVIRRKAVR 600
Cdd:COG0793    73 VVVVSVIPGSPAEK--AGIKPGDIILAIDGKSVAGLTLDDAVKLLRGkagtkvtltiKRPGEGEPITVTLTRAEIK 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: 604.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 631 EGSMELLKKGLESGTVLIQFEQLYRKKPGLAVTFAKLPQNLDKNRYKDVLPYDTTRVLLQGNEDYINASYVNMEIPAANL 710
Cdd:cd14600     1 EESMAQLKKGLESGTVLIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQGNEDYINASYVNMEIPSANI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 711 VNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQCQAEDCTIAYVSREMLV 790
Cdd:cd14600    81 VNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 791 TNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVGGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYP 870
Cdd:cd14600   161 TNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYP 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958779398 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 1.10e-152

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: 447.55  E-value: 1.10e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 694 DYINASYVNMEIPAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQ 773
Cdd:cd14541     1 DYINANYVNMEIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 774 CQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVG-GEPALVHCSAGIGRTGVL 852
Cdd:cd14541    81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGmVEPTVVHCSAGIGRTGVL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958779398 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 1.92e-121

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: 366.96  E-value: 1.92e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 694 DYINASYVNMEIPAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQ 773
Cdd:cd14601     1 DYINANYINMEIPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 774 CQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVGG-EPALVHCSAGIGRTGVL 852
Cdd:cd14601    81 CHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKdEPVVVHCSAGIGRTGVL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958779398 853 VTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAILRVYEE 904
Cdd:cd14601   161 ITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYEE 212
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
649-900 1.61e-107

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 332.32  E-value: 1.61e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  649 QFEQLYRKKPG-LAVTFAKLPQNLDKNRYKDVLPYDTTRVLLQGNE----DYINASYVNMEipaaNLVNKYIATQGPLPH 723
Cdd:smart00194   5 EFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPgegsDYINASYIDGP----NGPKAYIATQGPLPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  724 TCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDI-MDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEHTVT 802
Cdd:smart00194  81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEpLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  803 HLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVGGE-PALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQR 881
Cdd:smart00194 161 HYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTgPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQR 240

                          250
                   ....*....|....*....
gi 1958779398  882 AMMVQTSSQYKFVCEAILR 900
Cdd:smart00194 241 PGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
670-899 3.07e-103

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 320.34  E-value: 3.07e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 670 NLDKNRYKDVLPYDTTRVLLQ---GNEDYINASYVNMEipaaNLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTL 746
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTgdpGPSDYINASYIDGY----KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 747 TERGRTKCHQYWPDPP-DIMDHGIFHIQCQAE-DCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEF 824
Cdd:pfam00102  77 EEKGREKCAQYWPEEEgESLEYGDFTVTLKKEkEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDL 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958779398 825 VKYVRSLRVGGE--PALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:pfam00102 157 LRKVRKSSLDGRsgPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 695-896 1.27e-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: 259.14  E-value: 1.27e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 695 YINASYVNMEipaaNLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDI-MDHGIFHIQ 773
Cdd:cd00047     1 YINASYIDGY----RGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKpLEYGDITVT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 774 CQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVGGE-PALVHCSAGIGRTGVL 852
Cdd:cd00047    77 LVSEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNgPIVVHCSAGVGRTGTF 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1958779398 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 9.61e-72

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


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 235.35  E-value: 9.61e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 695 YINASYVNmeIPAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQC 774
Cdd:cd14538     1 YINASHIR--IPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLICGGRLEV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 775 QAEDCTI--AYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVGGePALVHCSAGIGRTGVL 852
Cdd:cd14538    79 SLEKYQSlqDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHNSG-PIVVHCSAGIGRTGVL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958779398 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 1.82e-71

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: 237.59  E-value: 1.82e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 635 ELLKKGLESGTVLIQFEQLYRKKPGLAVTFAKLPQNLDKNRYKDVLPYDTTRVLL----QGNEDYINASYVNMEIPAANL 710
Cdd:cd14599     3 KTLERKLEEGMVFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELvptkENNTGYINASHIKVTVGGEEW 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 711 vnKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWP---DPPDIMDHGIFHIQCQAEDCTIAYVSRE 787
Cdd:cd14599    83 --HYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPklgSKHSSATYGKFKVTTKFRTDSGCYATTG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 788 MLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLR-----------VGGEPALVHCSAGIGRTGVLVTME 856
Cdd:cd14599   161 LKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRrhtnsmldstkNCNPPIVVHCSAGVGRTGVVILTE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958779398 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 1.17e-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: 232.25  E-value: 1.17e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 649 QFEQLYRKKPGLAVTFAKLPQNLDKNRYKDVLPYDTTRVLLQ---GNE--DYINASYVNmeipAANLVNKYIATQGPLPH 723
Cdd:cd14543     8 EYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPkrnGDErtDYINANFMD----GYKQKNAYIATQGPLPK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 724 TCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWP-DPPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEHTVT 802
Cdd:cd14543    84 TYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPlEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVT 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 803 HLQYVAWPDHGVPDDSS---DFLEFVKYVRSLRV-----------GGEPALVHCSAGIGRTGVLVTMEtaMCLiERNLPV 868
Cdd:cd14543   164 HFQFTSWPDFGVPSSAAallDFLGEVRQQQALAVkamgdrwkghpPGPPIVVHCSAGIGRTGTFCTLD--ICL-SQLEDV 240

                         250       260
                  ....*....|....*....|....*...
gi 1958779398 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 1.56e-69

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: 230.49  E-value: 1.56e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 669 QNLDKNRYKDVLPYDTTRVLLQGNEDYINASYVNMEIPAANLVnkYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTE 748
Cdd:cd14597     2 ENRKKNRYKNILPYDTTRVPLGDEGGYINASFIKMPVGDEEFV--YIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 749 RGRTKCHQYWPDPPD--IMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVK 826
Cdd:cd14597    80 GGKIKCQRYWPEILGktTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLTFIS 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958779398 827 YVRSLRVGGePALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAILRV 901
Cdd:cd14597   160 YMRHIHKSG-PIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVILYV 233
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 695-894 7.17e-67

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: 222.12  E-value: 7.17e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 695 YINASYVNMEipaANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQC 774
Cdd:cd18533     1 YINASYITLP---GTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 775 QA--EDCTIAYVSREMLVTnTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVG---GEPALVHCSAGIGRT 849
Cdd:cd18533    78 VSeeENDDGGFIVREFELS-KEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSaslDPPIIVHCSAGVGRT 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958779398 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 2.65e-66

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: 221.07  E-value: 2.65e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 675 RYKDVLPYDTTRVLLQG-----NEDYINASYvnmeIPAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTER 749
Cdd:cd14548     1 RYTNILPYDHSRVKLIPineeeGSDYINANY----IPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 750 GRTKCHQYWPDPPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTEtgEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVR 829
Cdd:cd14548    77 GRVKCDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERGD--EVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVR 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958779398 830 SLRV-GGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFV 894
Cdd:cd14548   155 DYIKqEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFL 220
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 695-901 8.12e-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: 214.24  E-value: 8.12e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 695 YINASYVNMEIPAANLvnKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPD---PPDIMDHGIFH 771
Cdd:cd14540     1 YINASHITATVGGKQR--FYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTlggEHDALTFGEYK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 772 IQCQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLR------VGGE----PALVH 841
Cdd:cd14540    79 VSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRrhtnqdVAGHnrnpPTLVH 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 842 CSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAILRV 901
Cdd:cd14540   159 CSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQY 218
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 695-901 2.31e-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: 212.69  E-value: 2.31e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 695 YINASYVNMEIPAANLVnkYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDI-MDHGIFHI- 772
Cdd:cd14596     1 YINASYITMPVGEEELF--YIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEpMELENYQLr 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 773 --QCQA-EDCTIayvsREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVGGePALVHCSAGIGRT 849
Cdd:cd14596    79 leNYQAlQYFII----RIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTG-PIVVHCSAGIGRA 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958779398 850 GVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAILRV 901
Cdd:cd14596   154 GVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEV 205
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 670-899 3.55e-63

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: 213.03  E-value: 3.55e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 670 NLDKNRYKDVLPYDTTRVLLQGNE-----DYINASYVNmeipAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLT 744
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEgvpgsDYINANYCD----GYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 745 TLTERGRTKCHQYWPDpPDIMDHGIfhIQCQAEDCT--IAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFL 822
Cdd:cd14553    79 KLEERSRVKCDQYWPT-RGTETYGL--IQVTLLDTVelATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 823 EFVKYVRSLR-VGGEPALVHCSAGIGRTGVLVTMEtamCLIERNLPVYPLDI---VRKMRDQRAMMVQTSSQYKFVCEAI 898
Cdd:cd14553   156 AFLRRVKACNpPDAGPIVVHCSAGVGRTGCFIVID---SMLERIKHEKTVDIyghVTCLRAQRNYMVQTEDQYIFIHDAL 232


                  .
gi 1958779398 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 1.08e-62

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: 211.67  E-value: 1.08e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 674 NRYKDVLPYDTTRVLL-----QGNEDYINASYvnmeIPAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTE 748
Cdd:cd14619     1 NRFRNVLPYDWSRVPLkpiheEPGSDYINANY----MPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCME 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 749 RGRTKCHQYWPDPPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYV 828
Cdd:cd14619    77 AGRVKCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLL 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958779398 829 RS---LRVGGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAILR 900
Cdd:cd14619   157 RQwldQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 671-893 1.68e-62

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: 211.10  E-value: 1.68e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 671 LDKNRYKDVLPYDTTRVLLQGNE-DYINASYVnmEIPAANlvNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTER 749
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQGDnDYINASLV--EVEEAK--RSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 750 GRTKCHQYWP---DPPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVK 826
Cdd:cd14545    77 GQIKCAQYWPqgeGNAMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQ 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958779398 827 YVR---SLRVGGEPALVHCSAGIGRTGVLVTMETAMCLIERN--LPVYPLDIVRKMRDQRAMMVQTSSQYKF 893
Cdd:cd14545   157 KVResgSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGnpSSVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 654-902 5.72e-62

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: 210.84  E-value: 5.72e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 654 YRKKPGLAVTFAKLPQNLDKNRYKDVLPYDTTRVLL-----QGNEDYINASYVNmeipAANLVNKYIATQGPLPHTCAQF 728
Cdd:cd14603    14 FKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILsllqeEGHSDYINANFIK----GVDGSRAYIATQGPLSHTVLDF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 729 WQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTETgEEHTVTHLQYVA 808
Cdd:cd14603    90 WRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTFQK-ESRSVSHFQYMA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 809 WPDHGVPDDSSDFLEFVKYVRSLR-VGGEPALVHCSAGIGRTGVLVTME--TAMCLIERNLPVYPL-DIVRKMRDQRAMM 884
Cdd:cd14603   169 WPDHGIPDSPDCMLAMIELARRLQgSGPEPLCVHCSAGCGRTGVICTVDyvRQLLLTQRIPPDFSIfDVVLEMRKQRPAA 248

                         250
                  ....*....|....*...
gi 1958779398 885 VQTSSQYKFVCEAILRVY 902
Cdd:cd14603   249 VQTEEQYEFLYHTVAQMF 266
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 670-898 6.27e-61

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: 207.32  E-value: 6.27e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 670 NLDKNRYKDVLPYDTTRVLLQGNE------DYINASYVNMEI--PAANLVNK-YIATQGPLPHTCAQFWQVVWDQKLSLV 740
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDpnvpgsDYINANYIRNENegPTTDENAKtYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 741 VMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGE-EHTVTHLQYVAWPDHGVPDDSS 819
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDpIREIWHYQYLSWPDHGVPSDPG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 820 ---DFLEFVKYVRSLRVGGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDI---VRKMRDQRAMMVQTSSQYKF 893
Cdd:cd14544   161 gvlNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIqktIQMVRSQRSGMVQTEAQYKF 240


                  ....*
gi 1958779398 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 2.75e-59

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: 203.27  E-value: 2.75e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 656 KKPGLAVTFAKLPQNLDKNRYKDVLPYDTTRVLLQGNE-DYINASYVNMEipaaNLVNKYIATQGPLPHTCAQFWQVVWD 734
Cdd:cd14607    10 ESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEnDYINASLVVIE----EAQRSYILTQGPLPNTCCHFWLMVWQ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 735 QKLSLVVMLTTLTERGRTKCHQYWPDPPDIM----DHGiFHIQCQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWP 810
Cdd:cd14607    86 QKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVlsfkETG-FSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 811 DHGVPDDSSDFLEFVKYVR---SLRVGGEPALVHCSAGIGRTGVLVTMETAMCLIERNLP--VYPLDIVRKMRDQRAMMV 885
Cdd:cd14607   165 DFGVPESPASFLNFLFKVResgSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDPdsVDIKQVLLDMRKYRMGLI 244

                         250
                  ....*....|...
gi 1958779398 886 QTSSQYKFVCEAI 898
Cdd:cd14607   245 QTPDQLRFSYMAV 257
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 650-899 1.92e-58

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: 201.41  E-value: 1.92e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 650 FEQLYRKKPGLAVTFAKLPQNLDKNRYKDVLPYDTTRVLL-QGNEDYINASYVNMEipaaNLVNKYIATQGPLPHTCAQF 728
Cdd:cd14608     5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLhQEDNDYINASLIKME----EAQRSYILTQGPLPNTCGHF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 729 WQVVWDQKLSLVVMLTTLTERGRTKCHQYWP---DPPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEHTVTHLQ 805
Cdd:cd14608    81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPqkeEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 806 YVAWPDHGVPDDSSDFLEFVKYVR---SLRVGGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVR---KMRD 879
Cdd:cd14608   161 YTTWPDFGVPESPASFLNFLFKVResgSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKvllEMRK 240

                         250       260
                  ....*....|....*....|
gi 1958779398 880 QRAMMVQTSSQYKFVCEAIL 899
Cdd:cd14608   241 FRMGLIQTADQLRFSYLAVI 260
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 674-894 9.18e-58

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: 197.62  E-value: 9.18e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 674 NRYKDVLPYDTTRVLLQGNED-----YINASYvnmeIPAANLVNK-YIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLT 747
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDdplssYINANY----IRGYDGEEKaYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 748 ERgRTKCHQYWPDPPDiMDHGIFHIQCQAEDCTIAYVSREMLVTNTetGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKY 827
Cdd:cd14547    77 EA-KEKCAQYWPEEEN-ETYGDFEVTVQSVKETDGYTVRKLTLKYG--GEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQE 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 828 VRSLR---VGGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFV 894
Cdd:cd14547   153 VEEARqtePHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFV 222
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 674-894 8.70e-57

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: 195.04  E-value: 8.70e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 674 NRYKDVLPYDTTRVLL----QGNEDYINASYvnmeIPAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTER 749
Cdd:cd14615     1 NRYNNVLPYDISRVKLsvqsHSTDDYINANY----MPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 750 GRTKCHQYWPD--PPDIMDHGIFHI-QCQAEDCTIayvsREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVK 826
Cdd:cd14615    77 GRTKCEEYWPSkqKKDYGDITVTMTsEIVLPEWTI----RDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRH 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958779398 827 YVR---SLRVGGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFV 894
Cdd:cd14615   153 LVReymKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 30-222 1.23e-56

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: 193.67  E-value: 1.23e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398   30 TCSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPVDSPRWLEASKPLRKQLKGGLPCILHFRVRY 109
Cdd:smart00295   1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRHWLDPAKTLLDQDVKSEPLTLYFRVKF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  110 FIPDPNTLQQEQTRH-LYFLQLKMDVCEGRLTCPLNSAVVLASYAVQSHIGDFNSSIH-HPGYLADSQFIPDQ------N 181
Cdd:smart00295  81 YPPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQlldsrkL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1958779398  182 DDFLSKVESLHEQHSGLKQSEAESCYINIARTLDFYGVELH 222
Cdd:smart00295 161 KEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
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 1958779398 216 FYGVELHGGRDLHNLDLMIGIASAGIAVYRKYICTSFYPWVNILKISFKRKKFFIHQRQKQAESREHIVAFNMLNYRSCK 295
Cdd:cd13189     1 LYGVELHSARDSNNLELQIGVSSAGILVFQNGIRINTFPWSKIVKISFKRKQFFIQLRREPNESRDTILGFNMLSYRACK 80

                          90
                  ....*....|....
gi 1958779398 296 NLWKSCVEHHSFFQ 309
Cdd:cd13189    81 NLWKSCVEHHTFFR 94
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 674-894 3.82e-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: 193.21  E-value: 3.82e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 674 NRYKDVLPYDTTRVLLQGNE-----DYINASYvnmeIPAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTE 748
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDddpcsDYINASY----IPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 749 RGRTKCHQYWPDPPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEH-TVTHLQYVAWPDHGVPDDSSDFLEFVKY 827
Cdd:cd14617    77 KGRVKCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPrLVRHFHYTVWPDHGVPETTQSLIQFVRT 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 828 VRSL---RVGGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFV 894
Cdd:cd14617   157 VRDYinrTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYL 226
PDZ_PTPN3-4-like cd06706
PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein ...
 506-595 6.69e-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: 187.13  E-value: 6.69e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 506 GYLVLIRITPDKEGRFGFNLKGGVDQKMPLVVSRINPESPADTCMPKLNEGDQIVLINGRDISEHTHDQVVMFIKASRES 585
Cdd:cd06706     1 DGLVLIRMKPDENGRFGFNVKGGVDQKMPVIVSRVAPGTPADLCIPRLNEGDQVLLINGRDISEHTHDQVVMFIKASRER 80

                          90
                  ....*....|
gi 1958779398 586 HSRELALVIR 595
Cdd:cd06706    81 HSGELVLLVR 90
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 665-899 2.62e-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: 191.20  E-value: 2.62e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 665 AKLPQNLDKNRYKDVLPYDTTRVLLQ---GNE--DYINASYvnmeIPAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSL 739
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQpirGVEgsDYINASF----IDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 740 VVMLTTLTERGRTKCHQYWPDPPDIMdHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSS 819
Cdd:cd14554    77 IVMLTKLREMGREKCHQYWPAERSAR-YQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 820 DFLEFVKYVRSLR--VGGE-PALVHCSAGIGRTGVLVTMETAMcliERNLPVYPLDI---VRKMRDQRAMMVQTSSQYKF 893
Cdd:cd14554   156 GFIDFIGQVHKTKeqFGQEgPITVHCSAGVGRTGVFITLSIVL---ERMRYEGVVDVfqtVKLLRTQRPAMVQTEDQYQF 232


                  ....*.
gi 1958779398 894 VCEAIL 899
Cdd:cd14554   233 CYRAAL 238
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 695-894 6.55e-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: 189.10  E-value: 6.55e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 695 YINASYVnmeiPAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDpPDIMDHGIFHIQC 774
Cdd:cd14549     1 YINANYV----DGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPK-EGTETYGNIQVTL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 775 QAEDCTIAYVSREMLVTNTE------TGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVGGE-PALVHCSAGIG 847
Cdd:cd14549    76 LSTEVLATYTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAgPIVVHCSAGVG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958779398 848 RTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFV 894
Cdd:cd14549   156 RTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFI 202
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 665-894 8.48e-55

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: 190.10  E-value: 8.48e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 665 AKLPQNLDKNRYKDVLPYDTTRVLL-----QGNEDYINASYvnmeIPAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSL 739
Cdd:cd14614     7 ADLPVNRCKNRYTNILPYDFSRVKLvsmheEEGSDYINANY----IPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 740 VVMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTEtgEEHTVTHLQYVAWPDHGVP--DD 817
Cdd:cd14614    83 IVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYAD--EVQDVMHFNYTAWPDHGVPtaNA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958779398 818 SSDFLEFVKYVRSLRVGGE-PALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFV 894
Cdd:cd14614   161 AESILQFVQMVRQQAVKSKgPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFI 238
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 668-903 6.21e-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: 188.55  E-value: 6.21e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 668 PQNLDKNRYKDVLPYDTTRVLLQGNE------DYINASYV-NMEIPAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLV 740
Cdd:cd14606    16 PENKSKNRYKNILPFDHSRVILQGRDsnipgsDYINANYVkNQLLGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 741 VMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEE-HTVTHLQYVAWPDHGVPDDSS 819
Cdd:cd14606    96 VMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELiREIWHYQYLSWPDHGVPSEPG 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 820 DFLEFVKYV----RSLRVGGePALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDI---VRKMRDQRAMMVQTSSQYK 892
Cdd:cd14606   176 GVLSFLDQInqrqESLPHAG-PIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIqktIQMVRAQRSGMVQTEAQYK 254

                         250
                  ....*....|.
gi 1958779398 893 FVCEAILRVYE 903
Cdd:cd14606   255 FIYVAIAQFIE 265
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 674-899 1.07e-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: 180.91  E-value: 1.07e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 674 NRYKDVLPYDTTRVLL-----QGNEDYINASYvnmeIPAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTE 748
Cdd:cd14618     1 NRYPHVLPYDHSRVRLsqlggEPHSDYINANF----IPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGME 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 749 RGRTKCHQYWPDPPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYV 828
Cdd:cd14618    77 NGRVLCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELV 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958779398 829 R---SLRVGGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd14618   157 RehvQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 648-899 1.39e-51

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: 182.16  E-value: 1.39e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 648 IQFEQLYRK-KPGLAVTF--AKLPQNLDKNRYKDVLPYDTTRVLLQG-----NEDYINASYVNmeipAANLVNKYIATQG 719
Cdd:cd14626    16 LKFSQEYESiDPGQQFTWenSNLEVNKPKNRYANVIAYDHSRVILTSvdgvpGSDYINANYID----GYRKQNAYIATQG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 720 PLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPdPPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEH 799
Cdd:cd14626    92 PLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWP-IRGTETYGMIQVTLLDTVELATYSVRTFALYKNGSSEKR 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 800 TVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLR-VGGEPALVHCSAGIGRTGVLVTMETamcLIERNLPVYPLDI---VR 875
Cdd:cd14626   171 EVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNpPDAGPMVVHCSAGVGRTGCFIVIDA---MLERMKHEKTVDIyghVT 247

                         250       260
                  ....*....|....*....|....
gi 1958779398 876 KMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd14626   248 CMRSQRNYMVQTEDQYIFIHEALL 271
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 669-898 1.71e-51

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: 181.37  E-value: 1.71e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 669 QNLDKNRYKDVLPYDTTRVLLQG---NE---DYINASYV--NMEIPAAN--LVNKYIATQGPLPHTCAQFWQVVWDQKLS 738
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVLHDgdpNEpvsDYINANIImpEFETKCNNskPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 739 LVVMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGE-EHTVTHLQYVAWPDHGVPDD 817
Cdd:cd14605    81 VIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGNtERTVWQYHFRTWPDHGVPSD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 818 SS---DFLEFVKYVRSLRVGGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDI---VRKMRDQRAMMVQTSSQY 891
Cdd:cd14605   161 PGgvlDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVpktIQMVRSQRSGMVQTEAQY 240


                  ....*..
gi 1958779398 892 KFVCEAI 898
Cdd:cd14605   241 RFIYMAV 247
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 654-906 9.42e-51

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: 180.51  E-value: 9.42e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 654 YRKKPGLAVTFAKLPQNLDKNRYKDVLPYDTTRVLL-----QGNEDYINASYvnmeIPAANLVNKYIATQGPLPHTCAQF 728
Cdd:cd14604    41 YRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLtlktsSQDSDYINANF----IKGVYGPKAYIATQGPLANTVIDF 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 729 WQVVWDQKLSLVVMLTTLTERGRTKCHQYWP---DPPdiMDHGIFHIQCQAEDCTIAYVSREMLVTNTEtgEEHTVTHLQ 805
Cdd:cd14604   117 WRMIWEYNVAIIVMACREFEMGRKKCERYWPlygEEP--MTFGPFRISCEAEQARTDYFIRTLLLEFQN--ETRRLYQFH 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 806 YVAWPDHGVPDDSSDFLEFVKYVRSLRVGGE-PALVHCSAGIGRTGVLVTMETAMCL-----IERNLPVYPLdiVRKMRD 879
Cdd:cd14604   193 YVNWPDHDVPSSFDSILDMISLMRKYQEHEDvPICIHCSAGCGRTGAICAIDYTWNLlkagkIPEEFNVFNL--IQEMRT 270

                         250       260
                  ....*....|....*....|....*..
gi 1958779398 880 QRAMMVQTSSQYKFVCEAILRVYEEGL 906
Cdd:cd14604   271 QRHSAVQTKEQYELVHRAIAQLFEKQL 297
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 676-899 1.29e-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: 177.83  E-value: 1.29e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 676 YKDVLPYDTTRVLL---QGN--EDYINASYVNmeipAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERG 750
Cdd:cd14620     1 YPNILPYDHSRVILsqlDGIpcSDYINASYID----GYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 751 RTKCHQYWPdppdimDHGIF---HIQCQAEDCTIA--YVSREMLVTNTETGE---EHTVTHLQYVAWPDHGVPDDSSDFL 822
Cdd:cd14620    77 EEKCYQYWP------DQGCWtygNIRVAVEDCVVLvdYTIRKFCIQPQLPDGckaPRLVTQLHFTSWPDFGVPFTPIGML 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958779398 823 EFVKYVRSLR-VGGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd14620   151 KFLKKVKSVNpVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 673-902 1.31e-50

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


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 178.11  E-value: 1.31e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 673 KNRYKDVLPYDTTRVLLQ-----GNEDYINASYVN-MEIPAAnlvnkYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTL 746
Cdd:cd14602     1 KNRYKDILPYDHSRVELSlitsdEDSDYINANFIKgVYGPRA-----YIATQGPLSTTLLDFWRMIWEYSVLIIVMACME 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 747 TERGRTKCHQYWPDP-PDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTEtgEEHTVTHLQYVAWPDHGVPDDSSDFLEFV 825
Cdd:cd14602    76 FEMGKKKCERYWAEPgEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNS--ETRTIYQFHYKNWPDHDVPSSIDPILELI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 826 KYVRSLRVGGE-PALVHCSAGIGRTGVLVTME-TAMCL----IERNLPVYplDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd14602   154 WDVRCYQEDDSvPICIHCSAGCGRTGVICAIDyTWMLLkdgiIPENFSVF--SLIQEMRTQRPSLVQTKEQYELVYNAVI 231


                  ...
gi 1958779398 900 RVY 902
Cdd:cd14602   232 ELF 234
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 665-899 8.31e-50

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: 178.00  E-value: 8.31e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 665 AKLPQNLDKNRYKDVLPYDTTRVLLQ---GNE--DYINASYVNmeipAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSL 739
Cdd:cd14628    47 ANLPCNKFKNRLVNIMPYESTRVCLQpirGVEgsDYINASFID----GYRQQKAYIATQGPLAETTEDFWRMLWEHNSTI 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 740 VVMLTTLTERGRTKCHQYWPDPPDiMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSS 819
Cdd:cd14628   123 VVMLTKLREMGREKCHQYWPAERS-ARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 820 DFLEFVKYVRSLR--VGGE-PALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCE 896
Cdd:cd14628   202 GFIDFIGQVHKTKeqFGQDgPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYR 281


                  ...
gi 1958779398 897 AIL 899
Cdd:cd14628   282 AAL 284
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 648-899 9.26e-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: 177.62  E-value: 9.26e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 648 IQFEQLYRK-KPGLAVTF--AKLPQNLDKNRYKDVLPYDTTRVLLQGNE-----DYINASYVNmeipAANLVNKYIATQG 719
Cdd:cd14624    22 LKFSQEYESiDPGQQFTWehSNLEVNKPKNRYANVIAYDHSRVLLSAIEgipgsDYINANYID----GYRKQNAYIATQG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 720 PLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDpPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEH 799
Cdd:cd14624    98 ALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPS-RGTETYGLIQVTLLDTVELATYCVRTFALYKNGSSEKR 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 800 TVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLR-VGGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMR 878
Cdd:cd14624   177 EVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNpPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMR 256

                         250       260
                  ....*....|....*....|.
gi 1958779398 879 DQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd14624   257 AQRNYMVQTEDQYIFIHDALL 277
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 665-899 9.74e-50

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: 177.62  E-value: 9.74e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 665 AKLPQNLDKNRYKDVLPYDTTRVLLQ---GNE--DYINASYVNmeipAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSL 739
Cdd:cd14627    48 ANLPCNKFKNRLVNIMPYETTRVCLQpirGVEgsDYINASFID----GYRQQKAYIATQGPLAETTEDFWRMLWENNSTI 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 740 VVMLTTLTERGRTKCHQYWPDPPDiMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSS 819
Cdd:cd14627   124 VVMLTKLREMGREKCHQYWPAERS-ARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 820 DFLEFVKYVRSLR--VGGE-PALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCE 896
Cdd:cd14627   203 GFIDFIGQVHKTKeqFGQDgPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQ 282


                  ...
gi 1958779398 897 AIL 899
Cdd:cd14627   283 AAL 285
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 695-900 1.69e-49

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: 174.39  E-value: 1.69e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 695 YINASYVNMEIPAANLvnKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWP---DPPDIMDHGIFH 771
Cdd:cd14598     1 YINASHIKVTVGGKEW--DYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgSRHNTVTYGRFK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 772 IQCQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLR----------VGGEPALVH 841
Cdd:cd14598    79 ITTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRrhtnstidpkSPNPPVLVH 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958779398 842 CSAGIGRTGVLVTMETAMCLIERNlpvYPLDIVR---KMRDQRAMMVQTSSQYKFVCEAILR 900
Cdd:cd14598   159 CSAGVGRTGVVILSEIMIACLEHN---EMLDIPRvldMLRQQRMMMVQTLSQYTFVYKVLIQ 217
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 654-898 2.80e-49

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: 176.02  E-value: 2.80e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 654 YRKKPGlAVTFAKLPQNLDKNRYKDVLPYDTTRVLLQG-----NEDYINASYVnMEIPAANlvNKYIATQGPLPHTCAQF 728
Cdd:cd14610    29 YQAEPN-ATNVAQREENVQKNRSLAVLPYDHSRIILKAenshsHSDYINASPI-MDHDPRN--PAYIATQGPLPATVADF 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 729 WQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDIMDHgIF-------HIQCqaEDctiaYVSREMLVTNTETGEEHTV 801
Cdd:cd14610   105 WQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYH-IYevnlvseHIWC--ED----FLVRSFYLKNLQTNETRTV 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 802 THLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVGGE-PALVHCSAGIGRTGVLVTMEtaMCLIERNLPVYPLDI---VRKM 877
Cdd:cd14610   178 TQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRScPIIVHCSDGAGRSGTYILID--MVLNKMAKGAKEIDIaatLEHL 255

                         250       260
                  ....*....|....*....|.
gi 1958779398 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 ...
 658-899 3.96e-49

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: 175.67  E-value: 3.96e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 658 PGLAVTF--AKLPQNLDKNRYKDVLPYDTTRVLLQGNE-----DYINASYVNmeipAANLVNKYIATQGPLPHTCAQFWQ 730
Cdd:cd14625    33 PGQQFTWehSNLEVNKPKNRYANVIAYDHSRVILQPIEgimgsDYINANYID----GYRKQNAYIATQGPLPETFGDFWR 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 731 VVWDQKLSLVVMLTTLTERGRTKCHQYWPDpPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWP 810
Cdd:cd14625   109 MVWEQRSATVVMMTKLEEKSRIKCDQYWPS-RGTETYGMIQVTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWP 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 811 DHGVPDDSSDFLEFVKYVRSLR-VGGEPALVHCSAGIGRTGVLVTMETamcLIERNLPVYPLDI---VRKMRDQRAMMVQ 886
Cdd:cd14625   188 DHGVPEYPTPFLAFLRRVKTCNpPDAGPIVVHCSAGVGRTGCFIVIDA---MLERIKHEKTVDIyghVTLMRSQRNYMVQ 264

                         250
                  ....*....|...
gi 1958779398 887 TSSQYKFVCEAIL 899
Cdd:cd14625   265 TEDQYSFIHDALL 277
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 674-896 1.07e-48

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: 172.40  E-value: 1.07e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 674 NRYKDVLPYDTTRVLLQGN-----EDYINASYVNMEIpaanLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTE 748
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADagvpgSDYINASYISGYL----CPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 749 RGRTKCHQYWP-DPPDIMDHGIFHIQCQAEDCTIAYVSREMLVtnTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKY 827
Cdd:cd14616    77 KGRIRCHQYWPeDNKPVTVFGDIVITKLMEDVQIDWTIRDLKI--ERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKL 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 828 VRSLRVGGE-PALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCE 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 1.80e-48

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: 173.30  E-value: 1.80e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 649 QFEQLYRKKPGLAVT--FAKLPQNLDKNRYKDVLPYDTTRVLLQ-------GNEDYINASYVNmeipAANLVNKYIATQG 719
Cdd:cd17667     4 DFEEVQRCTADMNITaeHSNHPDNKHKNRYINILAYDHSRVKLRplpgkdsKHSDYINANYVD----GYNKAKAYIATQG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 720 PLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDpPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGE-- 797
Cdd:cd17667    80 PLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPT-ENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKgq 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 798 ---------EHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVGGE-PALVHCSAGIGRTGVLVTMETAMCLIERNLP 867
Cdd:cd17667   159 kgnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMgPVLVHCSAGVGRTGTYIVIDSMLQQIKDKST 238

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958779398 868 VYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd17667   239 VNVLGFLKHIRTQRNYLVQTEEQYIFIHDALL 270
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 654-898 5.06e-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: 5.06e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 654 YRKKPGlAVTFAKLPQNLDKNRYKDVLPYDTTRVLLQ-----GNEDYINASYV---NMEIPAanlvnkYIATQGPLPHTC 725
Cdd:cd14609    27 YQAEPN-TCSTAQGEANVKKNRNPDFVPYDHARIKLKaesnpSRSDYINASPIiehDPRMPA------YIATQGPLSHTI 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 726 AQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDIMDHgIF-------HIQCqaEDctiaYVSREMLVTNTETGEE 798
Cdd:cd14609   100 ADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYH-IYevnlvseHIWC--ED----FLVRSFYLKNVQTQET 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 799 HTVTHLQYVAWPDHGVPDDSSDFLEFVKYV-RSLRVGGEPALVHCSAGIGRTGVLVTMEtaMCLIERNLPVYPLDI---V 874
Cdd:cd14609   173 RTLTQFHFLSWPAEGIPSSTRPLLDFRRKVnKCYRGRSCPIIVHCSDGAGRTGTYILID--MVLNRMAKGVKEIDIaatL 250

                         250       260
                  ....*....|....*....|....
gi 1958779398 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 5.91e-48

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: 169.14  E-value: 5.91e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 695 YINASYvnmeIPAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDP-PDIMDHGIFHIQ 773
Cdd:cd14542     1 YINANF----IKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEgEEQLQFGPFKIS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 774 CQAED-CTIAYVSREMLVTNTEtgEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVGGE-PALVHCSAGIGRTGV 851
Cdd:cd14542    77 LEKEKrVGPDFLIRTLKVTFQK--ESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDvPICVHCSAGCGRTGT 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958779398 852 LVTMETAMCL-----IERNLPVYplDIVRKMRDQRAMMVQTSSQYKFV 894
Cdd:cd14542   155 ICAIDYVWNLlktgkIPEEFSLF--DLVREMRKQRPAMVQTKEQYELV 200
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 695-898 8.02e-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: 169.16  E-value: 8.02e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 695 YINASYVNMEIPAANLvnkYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDIMdHGIF---- 770
Cdd:cd14546     1 YINASTIYDHDPRNPA---YIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEV-YHIYevhl 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 771 ---HIQCqaEDctiaYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYV-RSLRVGGEPALVHCSAGI 846
Cdd:cd14546    77 vseHIWC--DD----YLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVnKSYRGRSCPIVVHCSDGA 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958779398 847 GRTGVLVTMEtaMCLIERNLPVYPLDI---VRKMRDQRAMMVQTSSQYKFVCEAI 898
Cdd:cd14546   151 GRTGTYILID--MVLNRMAKGAKEIDIaatLEHLRDQRPGMVKTKDQFEFVLTAV 203
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 665-899 1.19e-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: 171.83  E-value: 1.19e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 665 AKLPQNLDKNRYKDVLPYDTTRVLLQ---GNE--DYINASYVNmeipAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSL 739
Cdd:cd14629    48 ANLPCNKFKNRLVNIMPYELTRVCLQpirGVEgsDYINASFID----GYRQQKAYIATQGPLAETTEDFWRMLWEHNSTI 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 740 VVMLTTLTERGRTKCHQYWPDPPDiMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSS 819
Cdd:cd14629   124 VVMLTKLREMGREKCHQYWPAERS-ARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGE 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 820 DFLEFVKYVRSLR--VGGE-PALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCE 896
Cdd:cd14629   203 GFIDFIGQVHKTKeqFGQDgPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYR 282


                  ...
gi 1958779398 897 AIL 899
Cdd:cd14629   283 AAL 285
FERM_F1_PTPN3 cd17193
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 28-111 4.50e-47

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: 162.33  E-value: 4.50e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  28 EVTCSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPVDSPRWLEASKPLRKQLKGGLPCILHFRV 107
Cdd:cd17193     1 EVICNVHFLDGSVQSFKVNKQDTGQVLLDMAYNHLGLTEREYFGLQHNEDSVDSPRWLEPSKPIRKQLKGGFPCSLHFRV 80


                  ....
gi 1958779398 108 RYFI 111
Cdd:cd17193    81 RFFI 84
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 695-894 1.86e-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: 165.00  E-value: 1.86e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 695 YINASYVN-MEIPaanlvNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPP-DIMDHGIFHI 772
Cdd:cd14557     1 YINASYIDgFKEP-----RKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEeGSRAFGDVVV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 773 QCQAEDCTIAYVSREMLVTNT-ETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLR-VGGEPALVHCSAGIGRTG 850
Cdd:cd14557    76 KINEEKICPDYIIRKLNINNKkEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNnFFSGPIVVHCSAGVGRTG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1958779398 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 2.16e-45

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: 163.27  E-value: 2.16e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 669 QNLDKNRYKDVLPYDTTRVLLQGNE-----DYINASYVNmeipAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVML 743
Cdd:cd14630     2 ENRNKNRYGNIISYDHSRVRLQLLDgdphsDYINANYID----GYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 744 TTLTERGRTKCHQYWPDPPDImdHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLE 823
Cdd:cd14630    78 TNLVEVGRVKCVRYWPDDTEV--YGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLG 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958779398 824 FVKYVRSLR-VGGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd14630   156 FVRQVKFLNpPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAIL 232
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 665-899 5.78e-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: 163.29  E-value: 5.78e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 665 AKLPQNLDKNRYKDVLPYDTTRVLLQ-----GNEDYINASYVNmeipAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSL 739
Cdd:cd14633    35 AKKDENRMKNRYGNIIAYDHSRVRLQpiegeTSSDYINGNYID----GYHRPNHYIATQGPMQETIYDFWRMVWHENTAS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 740 VVMLTTLTERGRTKCHQYWPDPPDI---MDHGIFHIQCQAEdctiaYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPD 816
Cdd:cd14633   111 IIMVTNLVEVGRVKCCKYWPDDTEIykdIKVTLIETELLAE-----YVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPY 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 817 DSSDFLEFVKYVRSLR-VGGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVC 895
Cdd:cd14633   186 HATGLLGFVRQVKSKSpPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIH 265


                  ....
gi 1958779398 896 EAIL 899
Cdd:cd14633   266 DAIL 269
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 667-894 5.96e-45

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


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 162.31  E-value: 5.96e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 667 LPQNLDKNRYKDVLPYDTTRVLLQG------NEDYINASYVNmeiPAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLV 740
Cdd:cd14612    12 IPGHASKDRYKTILPNPQSRVCLRRagsqeeEGSYINANYIR---GYDGKEKAYIATQGPMLNTVSDFWEMVWQEECPII 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 741 VMLTTLTERgRTKCHQYWPDPPDimDHGIFHIQCQ-AEDCTiAYVSREMLVTNteTGEEHTVTHLQYVAWPDHGVPDDSS 819
Cdd:cd14612    89 VMITKLKEK-KEKCVHYWPEKEG--TYGRFEIRVQdMKECD-GYTIRDLTIQL--EEESRSVKHYWFSSWPDHQTPESAG 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958779398 820 DFLEFVKYV-RSLRVGGE--PALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFV 894
Cdd:cd14612   163 PLLRLVAEVeESRQTAASpgPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 695-893 6.78e-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: 160.63  E-value: 6.78e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 695 YINASYVNmeiPAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWP-DPPDIMDHGIFHIQ 773
Cdd:cd14539     1 YINASLIE---DLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPtERGQALVYGAITVS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 774 CQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYV-------RSLRVggePALVHCSAGI 846
Cdd:cd14539    78 LQSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVhshylqqRSLQT---PIVVHCSSGV 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958779398 847 GRTGVLVTMETAMCLIE--RNLPVYPlDIVRKMRDQRAMMVQTSSQYKF 893
Cdd:cd14539   155 GRTGAFCLLYAAVQEIEagNGIPDLP-QLVRKMRQQRKYMLQEKEHLKF 202
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 695-899 7.46e-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: 160.47  E-value: 7.46e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 695 YINASYVNmeipAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDImdHGIFHIQC 774
Cdd:cd14555     1 YINANYID----GYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEV--YGDIKVTL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 775 QAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLR-VGGEPALVHCSAGIGRTGVLV 853
Cdd:cd14555    75 VETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNpPSAGPIVVHCSAGAGRTGCYI 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958779398 854 TMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd14555   155 VIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 695-894 1.69e-44

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: 159.69  E-value: 1.69e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 695 YINASYVNmeipAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPdppdimDHGIFH--- 771
Cdd:cd14551     1 YINASYID----GYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP------DQGCWTygn 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 772 IQCQAEDCT--IAYVSREMLV--TNTETGEE--HTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLR-VGGEPALVHCSA 844
Cdd:cd14551    71 LRVRVEDTVvlVDYTTRKFCIqkVNRGIGEKrvRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANpPRAGPIVVHCSA 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958779398 845 GIGRTGVLVTMETAMCLI--ERNLPVYplDIVRKMRDQRAMMVQTSSQYKFV 894
Cdd:cd14551   151 GVGRTGTFIVIDAMLDMMhaEGKVDVF--GFVSRIRQQRSQMVQTDMQYVFI 200
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 695-898 3.81e-44

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: 158.59  E-value: 3.81e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 695 YINASYVNmeipAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDpPDIMDHGIFHIQC 774
Cdd:cd14552     1 YINASFID----GYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPE-DGSVSSGDITVEL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 775 QAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLR--VGGEPALVHCSAGIGRTGVL 852
Cdd:cd14552    76 KDQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQqqSGNHPITVHCSAGAGRTGTF 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958779398 853 VTMETamcLIERNLPVYPLDI---VRKMRDQRAMMVQTSSQYKFVCEAI 898
Cdd:cd14552   156 CALST---VLERVKAEGVLDVfqvVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 665-905 1.44e-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: 1.44e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 665 AKLPQNLDKNRYKDVLPYDTTRVLLQGNE-----DYINASYVNmeipAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSL 739
Cdd:cd14621    47 ASKEENKEKNRYVNILPYDHSRVHLTPVEgvpdsDYINASFIN----GYQEKNKFIAAQGPKEETVNDFWRMIWEQNTAT 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 740 VVMLTTLTERGRTKCHQYWPDpPDIMDHGifHIQCQAEDCTIA--YVSREMLVTN----TETGEEHTVTHLQYVAWPDHG 813
Cdd:cd14621   123 IVMVTNLKERKECKCAQYWPD-QGCWTYG--NIRVSVEDVTVLvdYTVRKFCIQQvgdvTNKKPQRLITQFHFTSWPDFG 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 814 VPDDSSDFLEFVKYVRSLRVG-GEPALVHCSAGIGRTGVLVTMETAMCLI--ERNLPVYplDIVRKMRDQRAMMVQTSSQ 890
Cdd:cd14621   200 VPFTPIGMLKFLKKVKNCNPQyAGAIVVHCSAGVGRTGTFIVIDAMLDMMhaERKVDVY--GFVSRIRAQRCQMVQTDMQ 277

                         250
                  ....*....|....*
gi 1958779398 891 YKFVCEAILRVYEEG 905
Cdd:cd14621   278 YVFIYQALLEHYLYG 292
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 675-893 2.90e-43

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: 157.13  E-value: 2.90e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 675 RYKDVLPYDTTRVLL-----QGNEDYINASYVNmeipAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTER 749
Cdd:cd14623     1 RVLQIIPYEFNRVIIpvkrgEENTDYVNASFID----GYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEER 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 750 GRTKCHQYWPDpPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYV- 828
Cdd:cd14623    77 GQEKCAQYWPS-DGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVq 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958779398 829 -RSLRVGGEPALVHCSAGIGRTGVLVTMETamcLIERNLPVYPLDI---VRKMRDQRAMMVQTSSQYKF 893
Cdd:cd14623   156 kQQQQSGNHPITVHCSAGAGRTGTFCALST---VLERVKAEGILDVfqtVKSLRLQRPHMVQTLEQYEF 221
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 669-902 8.79e-43

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 158.24  E-value: 8.79e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 669 QNLDKNRYKDVLPYDTTRVLL---QGNEDYINASYVNmeipAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTT 745
Cdd:PHA02742   51 KNMKKCRYPDAPCFDRNRVILkieDGGDDFINASYVD----GHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITK 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 746 LTERGRTKCHQYW-PDPPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEF 824
Cdd:PHA02742  127 IMEDGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDF 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 825 VKYVRSL------------RVGGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYK 892
Cdd:PHA02742  207 VLAVREAdlkadvdikgenIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYI 286

                         250
                  ....*....|
gi 1958779398 893 FvCEAILRVY 902
Cdd:PHA02742  287 F-CYFIVLIF 295
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 686-899 2.74e-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: 153.64  E-value: 2.74e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 686 RVLLQGNE-----DYINASYVNmeipAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPD 760
Cdd:cd14631     1 RVILQPVEddpssDYINANYID----GYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 761 PPDImdHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVR-SLRVGGEPAL 839
Cdd:cd14631    77 DTEV--YGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKlSNPPSAGPIV 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 840 VHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd14631   155 VHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 695-899 3.35e-42

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


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 153.21  E-value: 3.35e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 695 YINASYVNmeipAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPdPPDIMDHGIFHIQC 774
Cdd:cd17668     1 YINANYVD----GYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-ADGSEEYGNFLVTQ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 775 QAEDCTIAYVSREMLVTNTETGE--------EHTVTHLQYVAWPDHGVPDDSSDFLEFVK---YVRSLRVGgePALVHCS 843
Cdd:cd17668    76 KSVQVLAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYTLPVLTFVRkasYAKRHAVG--PVVVHCS 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958779398 844 AGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd17668   154 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PHA02738 PHA02738
hypothetical protein; Provisional
 663-900 5.60e-41

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 153.54  E-value: 5.60e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 663 TFAKLPQNLDKNRYKDVLPYDTTRVLL---QGNEDYINASYVNmeipAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSL 739
Cdd:PHA02738   42 TFNAEKKNRKLNRYLDAVCFDHSRVILpaeRNRGDYINANYVD----GFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQI 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 740 VVMLTTLTERGRTKCHQYWPD-PPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTeTGEEHTVTHLQYVAWPDHGVPDDS 818
Cdd:PHA02738  118 IVMLCKKKENGREKCFPYWSDvEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDG-TSATQTVTHFNFTAWPDHDVPKNT 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 819 SDFLEFVKYVR---------SLRVGGE-----PALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMM 884
Cdd:PHA02738  197 SEFLNFVLEVRqcqkelaqeSLQIGHNrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYS 276

                         250
                  ....*....|....*.
gi 1958779398 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 1.50e-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: 148.38  E-value: 1.50e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 695 YINASYVnmEIPAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRT-KCHQYWPDPPDI-MDHGIFHI 772
Cdd:cd17658     1 YINASLV--ETPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEENEsREFGRISV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 773 QCQAEDCTIAYVSREMLVTNTETGEEH--TVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVGGEPALVHCSAGIGRTG 850
Cdd:cd17658    79 TNKKLKHSQHSITLRVLEVQYIESEEPplSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPPSAGPIVVHCSAGIGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958779398 851 VLVTMETAmclIERNLP--VYPLDI---VRKMRDQRAMMVQTSSQYKF 893
Cdd:cd17658   159 AYCTIHNT---IRRILEgdMSAVDLsktVRKFRSQRIGMVQTQDQYIF 203
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 695-899 5.45e-40

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: 146.73  E-value: 5.45e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 695 YINASYVNmeipAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDImdHGIFHIQC 774
Cdd:cd14632     1 YINANYID----GYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDT--YGDIKITL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 775 QAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVR-SLRVGGEPALVHCSAGIGRTGVLV 853
Cdd:cd14632    75 LKTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKaSTPPDAGPVVVHCSAGAGRTGCYI 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958779398 854 TMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd14632   155 VLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 673-894 1.12e-39

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


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 147.70  E-value: 1.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 673 KNRYKDVLPYDTTRVLLQGNED------YINASYVNmeiPAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTL 746
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTSPDQddplssYINANYIR---GYGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNI 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 747 TERGRtKCHQYWPDPPDIMDhGIfHIQCQAEDCTIAYVSRemLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVK 826
Cdd:cd14613   105 EEMNE-KCTEYWPEEQVTYE-GI-EITVKQVIHADDYRLR--LITLKSGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQ 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958779398 827 YVRSLRVGGE----PALVHCSAGIGRTGVLVTmeTAMCLIE-RNLPVypLDIVR---KMRDQRAMMVQTSSQYKFV 894
Cdd:cd14613   180 EVEEARQQAEpncgPVIVHCSAGIGRTGCFIA--TSICCKQlRNEGV--VDILRttcQLRLDRGGMIQTCEQYQFV 251
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 694-893 3.85e-39

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: 144.38  E-value: 3.85e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 694 DYINASYVNmeipAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDImDHGIFHIQ 773
Cdd:cd14622     1 DYINASFID----GYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSV-THGEITIE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 774 CQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYV--RSLRVGGEPALVHCSAGIGRTGV 851
Cdd:cd14622    76 IKNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVqkQQQQTGNHPIVVHCSAGAGRTGT 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1958779398 852 LVTMETamcLIERNLPVYPLDI---VRKMRDQRAMMVQTSSQYKF 893
Cdd:cd14622   156 FIALSN---ILERVKAEGLLDVfqtVKSLRLQRPHMVQTLEQYEF 197
FERM_F1_PTPN3_like cd17100
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 28-111 1.74e-38

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and similar proteins; This family includes two tyrosine-protein phosphatase non-receptors, PTPN3 and PTPN4, both of which belong to the non-transmembrane FERM-containing protein-tyrosine phosphatase (PTP) subfamily characterized by a conserved N-terminal FERM domain, a PDZ domain, and a C-terminal PTP catalytic domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340620  Cd Length: 86  Bit Score: 137.82  E-value: 1.74e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  28 EVTCSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDP--VDSPRWLEASKPLRKQLKGGLPCILHF 105
Cdd:cd17100     1 EVRCIVHFLDDTEQTFEVEKRDKGQVLLDKVFNHLELVEKDYFGLQFSDDSpaTDSMRWLDPLKPIRKQIKGGPPYYLNF 80


                  ....*.
gi 1958779398 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 7.15e-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: 141.59  E-value: 7.15e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 673 KNRYKDVLPYDTTRVLLQ-GNEDYINASYVNmeipaANLVNKY-------IATQGPLPHTCAQFWQVVWDQKLSLVVMLT 744
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKpKNSNDSLSTYIN-----ANYIRGYggkekafIATQGPMINTVNDFWQMVWQEDSPVIVMIT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 745 TLTERGRtKCHQYWPDPPDImdHGIFHIQCQAEDCTIAYVSREMLVTNTetGEEHTVTHLQYVAWPDHGVPDDSSDFLEF 824
Cdd:cd14611    77 KLKEKNE-KCVLYWPEKRGI--YGKVEVLVNSVKECDNYTIRNLTLKQG--SQSRSVKHYWYTSWPDHKTPDSAQPLLQL 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958779398 825 VKYVRSLRVGGE---PALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFV 894
Cdd:cd14611   152 MLDVEEDRLASPgrgPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFV 224
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 659-894 1.18e-36

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 140.52  E-value: 1.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 659 GLAVTFAKlPQNLDKNRYKDVLPYDTTRVLLQ----GNEDYINASYVN-MEIPaanlvNKYIATQGPLPHTCAQFWQVVW 733
Cdd:PHA02747   41 GLIANFEK-PENQPKNRYWDIPCWDHNRVILDsgggSTSDYIHANWIDgFEDD-----KKFIATQGPFAETCADFWKAVW 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 734 DQKLSLVVMLT-TLTERGRTKCHQYW-PDPPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPD 811
Cdd:PHA02747  115 QEHCSIIVMLTpTKGTNGEEKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQCSEWFE 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 812 HGVPDDSSDFLEFVKYV-RSLRVGGE----------PALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQ 880
Cdd:PHA02747  195 DETPSDHPDFIKFIKIIdINRKKSGKlfnpkdallcPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQ 274

                         250
                  ....*....|....
gi 1958779398 881 RAMMVQTSSQYKFV 894
Cdd:PHA02747  275 RHAGIMNFDDYLFI 288
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 695-893 4.51e-35

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: 132.52  E-value: 4.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 695 YINASYVNmeipaanlvnKY------IATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDppDIMDHG 768
Cdd:cd14558     1 YINASFID----------GYwgpkslIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGD--EKKTYG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 769 IFHIQCQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVR----SLRVGGE---PALVH 841
Cdd:cd14558    69 DIEVELKDTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKqklpYKNSKHGrsvPIVVH 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958779398 842 CSAGIGRTGVLV----TMETAMclIERNLPVypLDIVRKMRDQRAMMVQTSSQYKF 893
Cdd:cd14558   149 CSDGSSRTGIFCalwnLLESAE--TEKVVDV--FQVVKALRKQRPGMVSTLEQYQF 200
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 695-896 1.49e-34

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: 130.99  E-value: 1.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 695 YINASYVN-MEIPAAnlvnkYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTkCHQYWPDPpDIMDHGIFHIQ 773
Cdd:cd14556     1 YINAALLDsYKQPAA-----FIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQS-CPQYWPDE-GSGTYGPIQVE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 774 CQAEDCTIAYVSREMLVTNTETGEE--HTVTHLQYVAWPDHG-VPDDSSDFLEFVKYVRSLR--VGGEPALVHCSAGIGR 848
Cdd:cd14556    74 FVSTTIDEDVISRIFRLQNTTRPQEgyRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQeqSGEGPIVVHCLNGVGR 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958779398 849 TGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCE 896
Cdd:cd14556   154 SGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
800-899 1.93e-34

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 127.09  E-value: 1.93e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  800 TVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRV---GGEPALVHCSAGIGRTGVLVTMETAMCLIE-RNLPVYPLDIVR 875
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqseSSGPVVVHCSAGVGRTGTFVAIDILLQQLEaEAGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....
gi 1958779398  876 KMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALL 104
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 800-899 1.93e-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: 127.09  E-value: 1.93e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  800 TVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRV---GGEPALVHCSAGIGRTGVLVTMETAMCLIE-RNLPVYPLDIVR 875
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqseSSGPVVVHCSAGVGRTGTFVAIDILLQQLEaEAGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....
gi 1958779398  876 KMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALL 104
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 668-900 3.40e-33

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 130.92  E-value: 3.40e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 668 PQNLDKNRYKDVLPYDTTRVLLQG------------------------NEDYINASYVNmeipAANLVNKYIATQGPLPH 723
Cdd:PHA02746   49 KENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkievtsednAENYIHANFVD----GFKEANKFICAQGPKED 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 724 TCAQFWQVVWDQKLSLVVMLTTlTERGRTKCHQYWPDPPDI-MDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEHTVT 802
Cdd:PHA02746  125 TSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWTKEEDSeLAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIH 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 803 HLQYVAWPDHGVPDDSSDFLEFVKYVRSLR-----------VGGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPL 871
Cdd:PHA02746  204 HFWFPDWPDNGIPTGMAEFLELINKVNEEQaelikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLG 283

                         250       260
                  ....*....|....*....|....*....
gi 1958779398 872 DIVRKMRDQRAMMVQTSSQYKFvCEAILR 900
Cdd:PHA02746  284 EIVLKIRKQRHSSVFLPEQYAF-CYKALK 311
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 112-222 4.61e-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: 123.53  E-value: 4.61e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 112 PDPNTLQQEQTRHLYFLQLKMDVCEGRLTCPLNSAVVLASYAVQSHIGDFNSSIHHPGYLADSQFIPDQN------DDFL 185
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLlrkmksKELE 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958779398 186 SKVESLHEQHSGLKQSEAESCYINIARTLDFYGVELH 222
Cdd:pfam00373  81 KRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_F1_PTPN4 cd17194
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 28-111 2.98e-32

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: 120.02  E-value: 2.98e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  28 EVTCSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPVDSPRWLEASKPLRKQLKGGLPCILHFRV 107
Cdd:cd17194     1 EVVCNILLLDNTVQAFKVNKHDQGQVLLDLVFKHLDLTERDYFGLQLADDSTDNPRWLDPNKPIRKQLKRGSPHNLNFRV 80


                  ....
gi 1958779398 108 RYFI 111
Cdd:cd17194    81 KFFV 84
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
663-891 1.52e-31

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 124.82  E-value: 1.52e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 663 TFAKLPQNLDKNRYKDVLPYDTTRVllQGNEDYINASYVNMEIPaanlvNKYIATQGPLPHTCAQFWQVVWDQKLSLVVM 742
Cdd:COG5599    35 QYLQNINGSPLNRFRDIQPYKETAL--RANLGYLNANYIQVIGN-----HRYIATQYPLEEQLEDFFQMLFDNNTPVLVV 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 743 LTTLTE--RGRTKCHQYWPDPPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEHT-VTHLQYVAWPDHGVPdDSS 819
Cdd:COG5599   108 LASDDEisKPKVKMPVYFRQDGEYGKYEVSSELTESIQLRDGIEARTYVLTIKGTGQKKIeIPVLHVKNWPDHGAI-SAE 186

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958779398 820 DFLEFVKYV----RSLRVGGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYP--LDIVRKMRDQRAM-MVQTSSQY 891
Cdd:COG5599   187 ALKNLADLIdkkeKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVQITLsvEEIVIDMRTSRNGgMVQTSEQL 265
FERM_C pfam09380
FERM C-terminal PH-like domain;
226-312 3.05e-30

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 114.27  E-value: 3.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 226 DLHNLDLMIGIASAGIAVYRKYICTS-FYPWVNILKISFKRKKFFIHQRQKqaeSREHIVAFNMLNYRSCKNLWKSCVEH 304
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKILnLFPWREIRKISFKRKKFLIKLRDK---SSEETLGFYTESSRACKYLWKLCVEQ 77


                  ....*...
gi 1958779398 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 6.67e-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: 6.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 217 YGVELHGGRDLHNLDLMIGIASAGIAVYRKYICTSFYPWVNILKISFKRKKFFIHQRQKQAESREHIVAFNMLNYRSCKN 296
Cdd:cd13184     1 YGVDLHPAKDSEGVDIMLGVCSSGLLVYRDRLRINRFAWPKVLKISYKRNNFYIKIRPGEFEQYETTIGFKLPNHRAAKR 80

                          90
                  ....*....|..
gi 1958779398 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 6.04e-27

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


Pssm-ID: 271216  Cd Length: 99  Bit Score: 105.41  E-value: 6.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 122 TRHLYFLQLKMDVCEGRLTCPLNSAVVLASYAVQSHIGDFNSSIHHPGYLADSQFIPDQ------NDDFLSKVESLHEQH 195
Cdd:cd14473     1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLSLKRFLPKQllkqrkPEEWEKRIVELHKKL 80

                          90
                  ....*....|....*....
gi 1958779398 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 6.86e-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: 6.86e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 210 IARTLDFYGVELHGGRDLHNLDLMIGIASAGIAVYRKYICTSFYPWVNILKISFKRKKFFIHQRQKQAESREHIVAFNML 289
Cdd:cd13193     2 TARRCELYGIRLHPAKDREGVKLNLAVAHMGILVFQGFTKINTFSWAKIRKLSFKRKRFLIKLHPEAYGSYKDTVEFSFE 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958779398 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 3.04e-23

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: 98.55  E-value: 3.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 695 YINASYVNM-EIPAAnlvnkYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTerGRTKCHQYWPDPPDIMdHGIFHIQ 773
Cdd:cd14634     1 YINAALMDShKQPAA-----FIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMD--AAQLCMQYWPEKTSCC-YGPIQVE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 774 CQAEDCTIAYVSREMLVTNTETGEE--HTVTHLQYVAWPDH-GVPDDSSDFLEFVKYVRSLRV---GGE-PALVHCSAGI 846
Cdd:cd14634    73 FVSADIDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEqydGREgRTVVHCLNGG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958779398 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 1958779398 218 GVELHGGRDLHNLDLMIGIASAGIAVYRKYICTSFYPWVNILKISFKRKKFFIHQRQKQAESREHIVAFNMLNYRSCKNL 297
Cdd:cd13186     1 GVDLHPVKGEDGNEYFLGLTPTGILVFENKTKIGLFFWPRITKLDFKGKKLKLVVKEKDDQEQEHTFVFRLPNKKACKHL 80

                          90
                  ....*....|.
gi 1958779398 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 7.19e-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: 91.63  E-value: 7.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 695 YINASYVN-MEIPAAnlvnkYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLT-ERGrtkCHQYWPDPpDIMDHGIFHI 772
Cdd:cd14636     1 YINAALMDsYRQPAA-----FIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDlAQG---CPQYWPEE-GMLRYGPIQV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 773 QCQA--EDCTIayVSREMLVTNTETGEEH--TVTHLQYVAWPDH-GVPDDSSDFLEFV----KYVRSLRVGGEPALVHCS 843
Cdd:cd14636    72 ECMScsMDCDV--ISRIFRICNLTRPQEGylMVQQFQYLGWASHrEVPGSKRSFLKLIlqveKWQEECDEGEGRTIIHCL 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958779398 844 AGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKF 893
Cdd:cd14636   150 NGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRF 199
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
 29-109 1.12e-20

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


Pssm-ID: 340464  Cd Length: 80  Bit Score: 86.87  E-value: 1.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  29 VTCSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHgDDPVDSPRWLEASKPLRKQLKGGLPCILHFRVR 108
Cdd:cd01765     1 ISCRVRLLDGTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFY-EDNDGQKHWLDLDKKISKQLKRSGPYQFYFRVK 79


                  .
gi 1958779398 109 Y 109
Cdd:cd01765    80 F 80
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 695-899 2.38e-20

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: 90.35  E-value: 2.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 695 YINASYVNMEIPAANlvnkYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRT-KCHQYWPDpPDIMDHGIFHIQ 773
Cdd:cd14637     1 YINAALTDSYTRSAA----FIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPE-PGLQQYGPMEVE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 774 CQAEDCTIAYVSREMLVTN-TETGEEH-TVTHLQYVAW-PDHGVPDDSSDFLEFVKYVRSLR--VGGEPALVHCSAGIGR 848
Cdd:cd14637    76 FVSGSADEDIVTRLFRVQNiTRLQEGHlMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQreSGEGRTVVHCLNGGGR 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958779398 849 TGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd14637   156 SGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 695-845 1.70e-19

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


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 87.38  E-value: 1.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 695 YINASYVNmeipAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGrtKCHQYWPDPPDIMDHGIFHIQC 774
Cdd:cd14550     1 YINASYLQ----GYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPLECETFKVTL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 775 QAED-----CTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPddSSDFLEFVKYVRSL---RVGgePALVH----- 841
Cdd:cd14550    75 SGEDhsclsNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSP--IHTVFELINTVQEWaqqRDG--PIVVHdrygg 150


                  ....
gi 1958779398 842 CSAG 845
Cdd:cd14550   151 VQAA 154
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 2.50e-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: 2.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 203 AESCYINIARTLDFYGVELHGGRDLHNLDLMIGIASAGIAVYRKYICTSFYPWVNILKISFKRKKFFIHQRQKqaESREH 282
Cdd:cd13192     1 AEDNFLRKAATLETYGVDPHPVKDHRGNQLYLGFTHTGIVTFQGGKRVHHFRWNDITKFNYEGKMFILHVMQK--EEKKH 78

                          90       100
                  ....*....|....*....|....*.
gi 1958779398 283 IVAFNMLNYRSCKNLWKSCVEHHSFF 308
Cdd:cd13192    79 TLGFKCPTPAACKHLWKCAVEQQAFY 104
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 510-595 6.50e-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: 6.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 510 LIRITPDKEGRFGFNLKGGVDQKMPLVVSRINPESPADTCMpKLNEGDQIVLINGRDISEHTHDQVVMFIKASreshSRE 589
Cdd:cd00136     1 TVTLEKDPGGGLGFSIRGGKDGGGGIFVSRVEPGGPAARDG-RLRVGDRILEVNGVSLEGLTHEEAVELLKSA----GGE 75


                  ....*.
gi 1958779398 590 LALVIR 595
Cdd:cd00136    76 VTLTVR 81
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 510-595 8.14e-19

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 81.56  E-value: 8.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 510 LIRITPDKEGRFGFNLKGGVDQK-MPLVVSRINPESPADTcmPKLNEGDQIVLINGRDISEHTHDQVVMFIKASREshsr 588
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKGGSDQGdPGIFVSEVLPGGAAEA--GGLKVGDRILSINGQDVENMTHEEAVLALKGSGG---- 74


                  ....*..
gi 1958779398 589 ELALVIR 595
Cdd:pfam00595  75 KVTLTIL 81
FERM_N pfam09379
FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the ...
 33-96 2.69e-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: 76.86  E-value: 2.69e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958779398  33 IRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPvDSPRWLEASKPLRKQLK 96
Cdd:pfam09379   1 VRLLDGTVLEFDVQPKATGQVLLDQVCNHLNLKEKDYFGLQFLDDN-GEHRWLDLSKRLSKQAP 63
FERM_F1_EPB41L5_like cd17108
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 29-110 3.75e-17

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: 77.00  E-value: 3.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  29 VTCSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHgDDPVDSPRWLEASKPLRKQLKGGLPCILHFRVR 108
Cdd:cd17108     1 IQCKVILLDGTDLSIELPKKAKGQELYEQVFYHLDLIEKDYFGLQF-MDAAQVQHWLDPTKKIKKQVKIGPPYTLRFRVK 79


                  ..
gi 1958779398 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 4.77e-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: 80.50  E-value: 4.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 695 YINASYVN-MEIPAAnlvnkYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTErgRTKCHQYWPDpPDIMDHGIFHIQ 773
Cdd:cd14635     1 YINAALMDsYKQPSA-----FIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDP--AQLCPQYWPE-NGVHRHGPIQVE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 774 CQAEDCTIAYVSREMLVTNTETGEE--HTVTHLQYVAWPDH-GVPDDSSDFLEFVKYVRSLRV---GGE-PALVHCSAGI 846
Cdd:cd14635    73 FVSADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEeynGGEgRTVVHCLNGG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958779398 847 GRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd14635   153 GRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
758-896 1.23e-16

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 77.32  E-value: 1.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 758 WPDPPDIMDHGIFHIQCQAEDCtiayvsrEMLVtntETGEEHTVTHLqYVAWPDHGVPDDSsDFLEFVKYVRSLRVGGEP 837
Cdd:COG2453    15 GGGEADLKREGIDAVVSLTEEE-------ELLL---GLLEEAGLEYL-HLPIPDFGAPDDE-QLQEAVDFIDEALREGKK 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958779398 838 ALVHCSAGIGRTGVLVtmetAMCLIERNLPvyPLDIVRKMRDQRAMMVQTSSQYKFVCE 896
Cdd:COG2453    83 VLVHCRGGIGRTGTVA----AAYLVLLGLS--AEEALARVRAARPGAVETPAQRAFLER 135
FERM_F1_FRMD3 cd17102
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 31-110 3.90e-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: 74.20  E-value: 3.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  31 CSIRFLDG---LVQTFKvnKQDLGQSLLDMAYGHLGVTEKEYFGLQHgDDPVDSPRWLEASKPLRKQLKGGLPCILHFRV 107
Cdd:cd17102     3 CTIRLLDDsevICCEFK--KDTKGQFLLDYVCNYLNLLEKDYFGLRY-VDTEKQRHWLDPNKSIYKQLKGVPPYVLCFRV 79


                  ...
gi 1958779398 108 RYF 110
Cdd:cd17102    80 KFY 82
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 508-597 6.79e-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: 73.57  E-value: 6.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  508 LVLIRITPDKEGrFGFNLKGGVDQKMPLVVSRINPESPADTCmpKLNEGDQIVLINGRDISEHTHDQVVMFIKASREShs 587
Cdd:smart00228   2 PRLVELEKGGGG-LGFSLVGGKDEGGGVVVSSVVPGSPAAKA--GLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGK-- 76

                           90
                   ....*....|
gi 1958779398  588 reLALVIRRK 597
Cdd:smart00228  77 --VTLTVLRG 84
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 695-899 8.06e-16

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


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 76.96  E-value: 8.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 695 YINASYvnmeIPAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKChQYWPDPPDIMDHGIFHIQC 774
Cdd:cd17669     1 YINASY----IMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKDEPINCETFKVTL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 775 QAEDCTIAYVSREMLVTN-----TETGEEHTVTHLQYVAWPDHGVP-DDSSDFLEFVKYVRSLRVGgePALVHCSAGIGR 848
Cdd:cd17669    76 IAEEHKCLSNEEKLIIQDfileaTQDDYVLEVRHFQCPKWPNPDSPiSKTFELISIIKEEAANRDG--PMIVHDEHGGVT 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958779398 849 TGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd17669   154 AGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
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 1958779398 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 ...
 29-110 7.10e-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: 7.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  29 VTCSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDdPVDSPRWLEASKPLRKQLKGGLPCILHFRVR 108
Cdd:cd17204     1 LTCRVLLLDGTDVSVELPKHAKGQDLFDQIVYHLDLVETDYFGLQFMD-AAQVAHWLDHTKPIKKQIKIGPPYTLHFRIK 79


                  ..
gi 1958779398 109 YF 110
Cdd:cd17204    80 YY 81
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 695-899 7.30e-15

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


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 74.33  E-value: 7.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 695 YINASYvnmeIPAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVML---TTLTERGRTkchqYWPDPPDIMDhgifh 771
Cdd:cd17670     1 YINASY----IMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQGLAEDEFV----YWPSREESMN----- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 772 iqCQAedCTIAYVSREMLVTNTE------------TGEEHT--VTHLQYVAWPDHGVPDDSS-DFLEFVKYVRSLRVGge 836
Cdd:cd17670    68 --CEA--FTVTLISKDRLCLSNEeqiiihdfileaTQDDYVleVRHFQCPKWPNPDAPISSTfELINVIKEEALTRDG-- 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958779398 837 PALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 899
Cdd:cd17670   142 PTIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 670-902 1.09e-14

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 75.77  E-value: 1.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 670 NLDKNRYKD------VLPYDTTRVLLQGNEDYINASYVNmeipAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVML 743
Cdd:PHA02740   47 AQAENKAKDenlalhITRLLHRRIKLFNDEKVLDARFVD----GYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLI 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 744 TTLTERgrtKCH-QYWP-DPPDIMDHGIFHIQcQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDF 821
Cdd:PHA02740  123 SRHADK---KCFnQFWSlKEGCVITSDKFQIE-TLEIIIKPHFNLTLLSLTDKFGQAQKISHFQYTAWPADGFSHDPDAF 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 822 LEFVKYVRSLRVGGE---------PALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYK 892
Cdd:PHA02740  199 IDFFCNIDDLCADLEkhkadgkiaPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYV 278

                         250
                  ....*....|
gi 1958779398 893 FvCEAILRVY 902
Cdd:PHA02740  279 F-CYHLIAAY 287
FERM_F1_EPB41L5 cd17205
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 27-110 2.59e-14

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like 5 (EPB41L5); EPB41L5 is a mesenchymal-specific protein that is an integral component of the ARF6-based pathway. It is normally induced during epithelial-mesenchymal transition (EMT) by an EMT-related transcriptional factor, ZEB1, which drives ARF6-based invasion, metastasis and drug resistance. EPB41L5 also binds to paxillin to enhance integrin/paxillin association, and thus promotes focal adhesion dynamics. Moreover, EPB41L5 acts as a substrate for the E3 ubiquitin ligase Mind bomb 1 (Mib1), which is essential for activation of Notch signaling. EPB41L5 is a member of the band 4.1/Nbl4 (novel band 4.1-like protein 4) group of the FERM protein superfamily. It contains a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340725  Cd Length: 86  Bit Score: 68.91  E-value: 2.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  27 SEVTCSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDpVDSPRWLEASKPLRKQLKGGLPCILHFR 106
Cdd:cd17205     1 SIITCRVSLLDGTDVSVDLPKKAKGQELFEQIMYHLDLIEKDYFGLRFMDS-AQVAHWLDVTKSIKKQVKIGPPYCLHLR 79


                  ....
gi 1958779398 107 VRYF 110
Cdd:cd17205    80 VKFY 83
FERM_F1_FRMD7 cd17188
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 33-114 4.86e-14

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: 68.30  E-value: 4.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  33 IRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGL----QHGddpvdSPRWLEASKPLRKQLKGGLPCILHFRVR 108
Cdd:cd17188     6 VQFLDDSQKVFVVDQKSTGKDLFNMSCSHLNLVEKEYFGLefrnHAG-----NNVWLELLKPITKQIKNPKELIFKFTVK 80


                  ....*.
gi 1958779398 109 YFIPDP 114
Cdd:cd17188    81 FFPVDP 86
PDZ_syntrophin-like cd06801
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 511-582 6.06e-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: 67.98  E-value: 6.06e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958779398 511 IRITPDKEGRFGFNLKGGVDQKMPLVVSRINPESPADTCmPKLNEGDQIVLINGRDISEHTHDQVVMFIKAS 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 1958779398 521 FGFNLKGGVDQKMPLVVSRINPESPADTCmpKLNEGDQIVLINGRDISEHTHDQVVMFIKASreshSRELALVIRR 596
Cdd:cd06753    10 WGFRLQGGKDFNQPLTISRVTPGGKAAQA--NLRPGDVILAINGESTEGMTHLEAQNKIKAA----TGSLSLTLER 79
FERM_F1_FARP1_like cd17098
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, RhoGEF and ...
 29-114 2.05e-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: 66.47  E-value: 2.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  29 VTCSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHgDDPVDSPRWLEASKPLRKQLKGGLPCILHFRVR 108
Cdd:cd17098     1 LHVKVQMLDDTVHIFQVQQKALGEVLFDQVCKHLNLLESDYFGLEF-TDPEGNKCWLDPEKPILRQVKRPKDVVFKFVVK 79


                  ....*.
gi 1958779398 109 YFIPDP 114
Cdd:cd17098    80 FYTPDP 85
FERM_F1_MYLIP cd17104
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in E3 ...
 29-110 2.84e-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: 65.75  E-value: 2.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  29 VTCSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHgDDPVDSPRWLEASKPLRKQLKGGLPCILHFRVR 108
Cdd:cd17104     1 MLCLVSQPDSVVIEVEVDPKANGQECLDKVCQKLGIIEKDYFGLQY-TGPKGERLWLNLRNRISRQLPGPPPYRLRLRVK 79


                  ..
gi 1958779398 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 9.23e-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: 64.58  E-value: 9.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  31 CSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPvDSPRWLEASKPLRKQLKGGlPCILHFRVRYF 110
Cdd:cd17203     4 CKVTLLDGSEYTCEVEKRSKGQVLFDKVCEHLNLLEKDYFGLTYRDSE-NQKNWLDPAKEIKKQIRSG-AWQFSFNVKFY 81


                  ...
gi 1958779398 111 IPD 113
Cdd:cd17203    82 PPD 84
FERM_F1_EPB41L cd17106
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 29-113 1.97e-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: 1.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  29 VTCSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHgDDPVDSPRWLEASKPLRKQLKGGlPCILHFRVR 108
Cdd:cd17106     2 QQCKVLLLDGTEYTCEVEKRAKGQVLFDKVCEHLNLLEKDYFGLTY-RDAQDQKNWLDPAKEIKKQIRSG-PWLFSFNVK 79


                  ....*
gi 1958779398 109 YFIPD 113
Cdd:cd17106    80 FYPPD 84
FERM_F1_EPB41L1 cd17201
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 31-113 2.80e-12

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: 63.36  E-value: 2.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  31 CSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDdpVDSPR-WLEASKPLRKQLKGGlPCILHFRVRY 109
Cdd:cd17201     4 CKVTLLDGSEYECEVEKHARGQVLFDTVCEHLNLLEKDYFGLTFCD--TESQKnWLDPSKEIKKQIRSG-PWHFAFTVKF 80


                  ....
gi 1958779398 110 FIPD 113
Cdd:cd17201    81 YPPD 84
FERM_F1_EPB41 cd17105
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 31-113 5.68e-12

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


Pssm-ID: 340625  Cd Length: 83  Bit Score: 62.14  E-value: 5.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  31 CSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPVdSPRWLEASKPLRKQLKGGlPCILHFRVRYF 110
Cdd:cd17105     3 CKVSLLDDTVYECEVEKHAKGQDLFKKVCEHLNLLEEDYFGLAIWDSPT-SKTWLDPAKEIKKQVHGG-PWEFTFNVKFY 80


                  ...
gi 1958779398 111 IPD 113
Cdd:cd17105    81 PPD 83
FERM_F1_EPB41L2 cd17202
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 29-113 9.86e-12

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: 61.53  E-value: 9.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  29 VTCSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPvDSPRWLEASKPLRKQLKgGLPCILHFRVR 108
Cdd:cd17202     2 VLCKVTLLDGTEYSCDLEKRAKGQVLFDKVCEHLNLLEKDYFGLLYQVSA-NQKNWLDSTKEIKRQIR-RLPWLFTFNVK 79


                  ....*
gi 1958779398 109 YFIPD 113
Cdd:cd17202    80 FYPPD 84
FERM_F1_FARP2 cd17190
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 31-114 2.84e-11

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: 60.19  E-value: 2.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  31 CSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHgDDPVDSPRWLEASKPLRKQLKGGLPCILHFRVRYF 110
Cdd:cd17190     3 LRVKLLDNTTEPLEIEPKADGQALLSQVFKRLNLVESDYFGLEF-QNSQSNWIWLEPMKLIVKQVRRPKNTKLRLAVKFF 81


                  ....
gi 1958779398 111 IPDP 114
Cdd:cd17190    82 PPDP 85
FERM_F1_EPB41L4A cd17107
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 27-113 2.89e-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: 60.43  E-value: 2.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  27 SEVTCSIRFLDGLVQTFKVNKQDL----GQSLLDMAYGHLGVTEKEYFGLQHGDDPvDSPRWLEASKPLRKQLKG-GLPC 101
Cdd:cd17107     1 EEFYCEIVLLDESELILTIQQDGIksskGSVVLDVVFQHLNLLETDYFGLRYIDRQ-HQTHWLDPAKTLSEQLKLiGPPY 79

                          90
                  ....*....|..
gi 1958779398 102 ILHFRVRYFIPD 113
Cdd:cd17107    80 TLYFGVKFYAED 91
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 820-896 1.20e-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: 59.29  E-value: 1.20e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958779398 820 DFLEFVKYVRSLRVGGEPALVHCSAGIGRTGVLVTMetaMCLIERNLPVYplDIVRKMRDQR-AMMVQTSSQYKFVCE 896
Cdd:cd14494    41 MVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVAC---YLVLLGGMSAE--EAVRIVRLIRpGGIPQTIEQLDFLIK 113
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 674-892 1.34e-10

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: 62.42  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 674 NRYKDVlpydTTRVLLQGNEDyINASYV---NMEIpaanlvnkYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERG 750
Cdd:cd14559     1 NRFTNI----QTRVSTPVGKN-LNANRVqigNKNV--------AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQ 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 751 RTKCHQYWpdppdIMD--HGIFHIQCQAEDcTIAYVSREM----LVTNTETGEEHTVTHLQYVAWPDHGvPDDSSDFLEF 824
Cdd:cd14559    68 RKGLPPYF-----RQSgtYGSVTVKSKKTG-KDELVDGLKadmyNLKITDGNKTITIPVVHVTNWPDHT-AISSEGLKEL 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 825 VKYVRSLRVGGEPAL-----------------VHCSAGIGRTGVLVtmeTAMCLIERNLPVYPLDIVRKMRDQR-AMMVQ 886
Cdd:cd14559   141 ADLVNKSAEEKRNFYkskgssaindknkllpvIHCRAGVGRTGQLA---AAMELNKSPNNLSVEDIVSDMRTSRnGKMVQ 217


                  ....*.
gi 1958779398 887 TSSQYK 892
Cdd:cd14559   218 KDEQLD 223
PDZ_SYNJ2BP-like cd06709
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ...
 511-584 3.90e-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: 3.90e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958779398 511 IRITPDKEGrFGFNLKGGVDQK-MP----LVVSRINPESPADTcMPKLNEGDQIVLINGRDISEHTHDQVVMFIKASRE 584
Cdd:cd06709     3 ITLKRGPSG-LGFNIVGGTDQPyIPndsgIYVAKIKEDGAAAI-DGRLQEGDKILEINGQSLENLTHQDAVELFRNAGE 79
PDZ_SYNPO2-like cd10820
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related ...
 512-582 3.97e-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: 56.93  E-value: 3.97e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958779398 512 RITPDKEGRFGFNLKGGVDQKMPLVVSRINPESPAdtCMPKLNEGDQIVLINGRDISEHTHDQVVMFIKAS 582
Cdd:cd10820     1 CVTLTGGAPWGFRLQGGSEQKKPLQVAKIRKKSKA--ALAGLCEGDELLSINGKPCADLSHSEAMDLIDSS 69
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 4.13e-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: 56.85  E-value: 4.13e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958779398 515 PDKEGrFGFNLKGGVDQKMPLVVSRINPESPADTCmPKLNEGDQIVLINGRDISEHTHDQVVMFIKAS 582
Cdd:cd06734     9 RENEG-FGFVIISSVNKKSGSKIGRIIPGSPADRC-GQLKVGDRILAVNGISILNLSHGDIVNLIKDS 74
FERM_F1_PTPN14_like cd17099
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 32-110 5.63e-10

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: 56.47  E-value: 5.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  32 SIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPvDSPRWLEASKPLRKQL-KGGLPCILHFRVRYF 110
Cdd:cd17099     7 RIQLLDNTVLECTLSPESTGQDCLEYVAQRLELREIEYFGLRYVNKK-GQLRWVDLEKPLKKQLdKHAHEPLLYFGVMFY 85
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 810-894 8.98e-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: 58.43  E-value: 8.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 810 PDHGVPDDSSDFLEFVKYVRSLRVGGEPALVHCSAGIGRTGVLVtmetAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSS 889
Cdd:cd14505    81 PDGGVPSDIAQWQELLEELLSALENGKKVLIHCKGGLGRTGLIA----ACLLLELGDTLDPEQAIAAVRALRPGAIQTPK 156


                  ....*
gi 1958779398 890 QYKFV 894
Cdd:cd14505   157 QENFL 161
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 2.29e-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: 54.89  E-value: 2.29e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958779398 521 FGFNLKGGVD-QKMPLVVSRINPESPADTCmPKLNEGDQIVLINGRDISEHTHDQVVMFIKasreSHSRELALVIRR 596
Cdd:cd06735    13 FGFSIRGGREyNNMPLYVLRLAEDGPAQRD-GRLRVGDQILEINGESTQGMTHAQAIELIR----SGGSVVRLLLRR 84
PDZ_Lin-7-like cd06796
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 510-595 2.51e-09

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


Pssm-ID: 467258 [Multi-domain]  Cd Length: 86  Bit Score: 54.75  E-value: 2.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 510 LIRITPDKEGrFGFNLKGGVDQKMPLVVSRINPESPADTcMPKLNEGDQIVLINGRDISEHTHDQVVMFIKASREShsre 589
Cdd:cd06796     4 VVELPKTEEG-LGFNVMGGKEQNSPIYISRIIPGGVADR-HGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGS---- 77


                  ....*.
gi 1958779398 590 LALVIR 595
Cdd:cd06796    78 VKLVVR 83
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 218-308 2.89e-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: 2.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 218 GVELHGGRDL--HNLDLMIGIASAGIAVY----RKYICTsfYPWVNILKISFKRKKFF-IHQRQKQAESrehIVAFNMLN 290
Cdd:cd00836     1 GVEFFPVKDKskKGSPIILGVNPEGISVYdeltGQPLVL--FPWPNIKKISFSGAKKFtIVVADEDKQS---KLLFQTPS 75

                          90
                  ....*....|....*...
gi 1958779398 291 yRSCKNLWKSCVEHHSFF 308
Cdd:cd00836    76 -RQAKEIWKLIVGYHRFL 92
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 510-582 3.11e-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: 54.37  E-value: 3.11e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958779398 510 LIRITPDKEGrFGFNL---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 5.98e-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: 53.80  E-value: 5.98e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958779398 508 LVLIRITPDKEGRFGFNLKGGVDQKMPLVVSRINPESPADTcmPKLNEGDQIVLINGRDISEHTHDQVVMFIKASRE 584
Cdd:cd06737     2 LRLVRLDRRGPESLGFSVRGGLEHGCGLFVSHVSPGSQADN--KGLRVGDEIVRINGYSISQCTHEEVINLIKTKKT 76
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 789-894 1.99e-08

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: 53.82  E-value: 1.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 789 LVT-NTETGEEHTVTH--LQYVAWP--DHGVPDDSS--DFLEFVKYVRSLrvgGEPALVHCSAGIGRTGvlvTMetAMCL 861
Cdd:cd14504    32 VVTlTEEPPPEHSDTCpgLRYHHIPieDYTPPTLEQidEFLDIVEEANAK---NEAVLVHCLAGKGRTG---TM--LACY 103

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958779398 862 IERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFV 894
Cdd:cd14504   104 LVKTGKISAVDAINEIRRIRPGSIETSEQEKFV 136
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 808-896 2.62e-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: 55.05  E-value: 2.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 808 AWPDHGVPddSSDF-LEFVKYVRS-LRVGGEPAlVHCSAGIGRTGVLVTmetamCLIERNLPVYPLDIVRKMRDQRAMMV 885
Cdd:cd14506    83 GWKDYGVP--SLTTiLDIVKVMAFaLQEGGKVA-VHCHAGLGRTGVLIA-----CYLVYALRMSADQAIRLVRSKRPNSI 154

                          90
                  ....*....|.
gi 1958779398 886 QTSSQYKFVCE 896
Cdd:cd14506   155 QTRGQVLCVRE 165
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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958779398 522 GFNLKGGVDQKMPLVVSRINPESPADTCmPKLNEGDQIVLINGRDISEhTHDQVVMFIKASReshsRELALVIRR 596
Cdd:cd06750    14 GFTLKGGLEHGEPLVISKIEEGGKAASV-GKLQVGDEVVNINGVPLSG-SRQEAIQLVKGSH----KTLKLVVRR 82
FERM_F1_FRMD4 cd17103
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 31-112 5.51e-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: 5.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  31 CSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPvDSPRWLEASKPL------RKQLKGglPCILH 104
Cdd:cd17103     5 CQVVLLDDRRLEILVQPKLLAGDLLDLVASHFNLKEKEYFGLAYEDET-GHYNWLQLDKRVldhefpKKWSSG--PLVLH 81


                  ....*...
gi 1958779398 105 FRVRYFIP 112
Cdd:cd17103    82 FAVKFYVE 89
FERM_F1_FARP1 cd17189
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 29-113 7.15e-08

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF and pleckstrin domain-containing protein 1 (FARP1); FARP1, also termed chondrocyte-derived ezrin-like protein (CDEP), or pleckstrin homology (PH) domain-containing family C member 2 (PLEKHC2), is a neuronal activator of the RhoA GTPase. It promotes outgrowth of developing motor neuron dendrites. It also regulates excitatory synapse formation and morphology, as well as activates the GTPase Rac1 to promote F-actin assembly. As a novel downstream signaling partner of Rif, FARP1 is involved in the regulation of semaphorin signaling in neurons. FARP1 contains a FERM domain, a Dbl-homology (DH) domain and two pleckstrin homology (PH) domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340709  Cd Length: 85  Bit Score: 50.57  E-value: 7.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  29 VTCSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPvDSPRWLEASKPLRKQLKGGLPCILHFRVR 108
Cdd:cd17189     1 VPIKVQMLDDTQEVFEVPQRAPGKVLLDAVCSHLNLVEGDYFGLEFQDHR-KVMVWLDLLKPIVKQIRRPKHVVLRFVVK 79


                  ....*
gi 1958779398 109 YFIPD 113
Cdd:cd17189    80 FFPPD 84
PDZ_rhophilin-like cd06712
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 511-584 8.07e-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: 50.28  E-value: 8.07e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958779398 511 IRITPDkEGRFGFNLKGGVdqkmPLVVSRINPESPADTCmpKLNEGDQIVLINGRDISEHTHDQVVMFIKASRE 584
Cdd:cd06712     4 VHLTKE-EGGFGFTLRGDS----PVQVASVDPGSCAAEA--GLKEGDYIVSVGGVDCKWSKHSEVVKLLKSAGE 70
PDZ_PDZD11-like cd06752
PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic ...
 522-588 1.46e-07

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


Pssm-ID: 467234 [Multi-domain]  Cd Length: 83  Bit Score: 49.62  E-value: 1.46e-07
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gi 1958779398 522 GFNLKGGVDQKMPLVVSRINPESPADTCmpKLNEGDQIVLINGRDISEHTHDQVVMFIKASRESHSR 588
Cdd:cd06752    14 GFNIRGGKASGLGIFISKVIPDSDAHRL--GLKEGDQILSVNGVDFEDIEHSEAVKVLKTAREIQMR 78
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
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                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958779398 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 3.12e-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: 49.21  E-value: 3.12e-07
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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 217 YGVELHGGRDLHNLDLMIGIASAGIAVYRKY-ICTSFYPWVNILKISFkRKKFFihqRQKQAESREHIVaFNMLNYRSCK 295
Cdd:cd13188     1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNgRPPVFFRWEDIKNVIN-HKRTF---SIECQNSEETVQ-FQFEDAETAK 75

                          90
                  ....*....|...
gi 1958779398 296 NLWKSCVEHHSFF 308
Cdd:cd13188    76 YVWKLCVLQHKFY 88
PDZ1_MAGI-1_3-like cd06731
PDZ domain 1 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 510-578 5.07e-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: 48.36  E-value: 5.07e-07
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gi 1958779398 510 LIRITPDKEGR-FGFNLKGGVDQKMPLVVSRINPESPADTcMPKLNEGDQIVLINGRDISEHTHDQVV-MF 578
Cdd:cd06731     1 LIRTSLKKSARgFGFTIIGGDEPDEFLQIKSVVPDGPAAL-DGKLRTGDVLVSVNDTCVLGYTHADVVkLF 70
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
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gi 1958779398 520 RFGFNLKGGVDQ---KMP-------LVVSRINPESPADTCmpKLNEGDQIVLINGRDISEHTHDQVVMFIKASRE 584
Cdd:cd10822    14 ILGFSIGGGIDQdpsKNPfsytdkgIYVTRVSEGGPAEKA--GLQVGDKILQVNGWDMTMVTHKQAVKRLTKKKP 86
FERM_F1_ERM_like cd17097
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 43-110 1.16e-06

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


Pssm-ID: 340617  Cd Length: 83  Bit Score: 47.27  E-value: 1.16e-06
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gi 1958779398  43 FKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHgDDPVDSPRWLEASKPLRKQLKG-GLPCILHFRVRYF 110
Cdd:cd17097    14 FSIKPKAKGRELFDLVCRTIGLRETWYFGLQY-ENKKGRVAWLKPDKKVLTQDVSkNNTLKFFFLVKFY 81
PDZ4_GRIP1-2-like cd06686
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 513-583 1.69e-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: 1.69e-06
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gi 1958779398 513 ITPDKEGRFGFNLKGGVDQKMPL----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
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gi 1958779398 522 GFNLKGGVDQKmPLVVSRINPESPADTCmPKLNEGDQIVLINGRDISEHTHDQVVMFIKAS 582
Cdd:cd06795    15 GFNIVGGEDGE-GIFISFILAGGPADLS-GELRRGDQILSVNGVDLRNATHEQAAAALKNA 73
PDZ1-PDZRN4-like cd06715
PDZ domain 1 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 517-584 1.72e-06

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: 47.00  E-value: 1.72e-06
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gi 1958779398 517 KEGRFGFNLKGG----VDQKMP----LVVSRINPESPADTCMpKLNEGDQIVLINGRDISEHTHDQVVMFIKASRE 584
Cdd:cd06715    10 ENGSLGFNIIGGrpceNNQEGSssegIYVSKIVENGPAADEG-GLQVHDRIIEVNGKDLSKATHEEAVEAFRTAKE 84
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
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gi 1958779398 519 GRFGFNLKGgvdqKMPLVVSRINPESPADTCmpKLNEGDQIVLINGRDISEHTHDQVVMFIKAS 582
Cdd:cd06744     9 GSFGFTLRG----HAPVYIESVDPGSAAERA--GLKPGDRILFLNGLDVRNCSHDKVVSLLQGS 66
FERM_F1_FRMD4B cd17200
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 31-111 2.03e-06

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: 46.80  E-value: 2.03e-06
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gi 1958779398  31 CSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPVDSpRWLEAS-KPLRKQL-KGGLPCILHFRVR 108
Cdd:cd17200     5 CQVHLLDDRKLELLVQPKLLSRELLDLVASHFNLKEKEYFGITFIDDTGQS-NWLQLDhRVLDHDLpKKSGPVTLYFAVR 83


                  ...
gi 1958779398 109 YFI 111
Cdd:cd17200    84 FYI 86
PDZ2_FL-whirlin cd06741
PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 511-584 3.93e-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: 45.72  E-value: 3.93e-06
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gi 1958779398 511 IRITPDKEGRFGFNLKGGVDQKMPLVVSRINPESPADTCMPKLneGDQIVLINGRDISEHTHDQVVMFIKASRE 584
Cdd:cd06741     4 VNLVVEDGQSLGLMIRGGAEYGLGIYVTGVDPGSVAENAGLKV--GDQILEVNGRSFLDITHDEAVKILKSSKH 75
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 508-583 4.04e-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: 45.43  E-value: 4.04e-06
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gi 1958779398 508 LVLIRITPDKEGrFGFNLKGGVDQKMPLVVSRINPESPADTcmPKLNEGDQIVLINGRDISEHTHDQVVMFIKASR 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 7.85e-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: 44.94  E-value: 7.85e-06
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gi 1958779398 507 YLVLIRitpDKEGrFGFNLKGGV------DQKMPLVVSRINPESPADTcMPKLNEGDQIVLINGRDISEHTHDQVVMFIK 580
Cdd:cd06703     4 TTTLIR---DGKG-LGFSIAGGKgstpfrDGDEGIFISRITEGGAADR-DGKLQVGDRVLSINGVDVTEARHDQAVALLT 78

                          90
                  ....*....|....*...
gi 1958779398 581 asreSHSRELALVIRRKA 598
Cdd:cd06703    79 ----SSSPTITLVVEREA 92
PDZ2_GRIP1-2-like cd06681
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 511-594 7.95e-06

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: 44.92  E-value: 7.95e-06
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gi 1958779398 511 IRITPDKEGR-FGFNLKGGVDQKM----PLVVSRINPESPADtCMPKLNEGDQIVLINGRDISEHTHDQVVMFIKASres 585
Cdd:cd06681     3 VEVTLEKEGNsFGFVIRGGAHEDRnksrPLTVTHVRPGGPAD-REGTIKPGDRLLSVDGISLHGATHAEAMSILKQC--- 78


                  ....*....
gi 1958779398 586 hSRELALVI 594
Cdd:cd06681    79 -GQEATLLI 86
PDZ_FRMPD1_3_4-like cd06769
PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related ...
 511-585 1.12e-05

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: 44.16  E-value: 1.12e-05
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gi 1958779398 511 IRITPDKEGRFGFNLKGgvdqKMPLVVSRINPESPADTcmpKLNEGDQIVLINGRDISEHTHDQVVMFIKASRES 585
Cdd:cd06769     2 VEIQRDAVLGFGFVAGS----ERPVVVRSVTPGGPSEG---KLLPGDQILKINNEPVEDLPRERVIDLIRECKDS 69
PDZ1_PDZD7-like cd10833
PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 511-596 1.37e-05

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


Pssm-ID: 467269 [Multi-domain]  Cd Length: 84  Bit Score: 44.35  E-value: 1.37e-05
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gi 1958779398 511 IRITPDKEGRFGFNLKGGVDQKMPLVVSRINPESPADtcMPKLNEGDQIVLINGRDISEHTHDQVVMFIKASreshSReL 590
Cdd:cd10833     4 VTVEKSPDGSLGFSVRGGSEHGLGIFVSKVEEGSAAE--RAGLCVGDKITEVNGVSLENITMSSAVKVLTGS----NR-L 76


                  ....*.
gi 1958779398 591 ALVIRR 596
Cdd:cd10833    77 RMVVRR 82
FERM_F1_PTPN21 cd17192
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 26-112 1.41e-05

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: 44.24  E-value: 1.41e-05
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gi 1958779398  26 RSEVTCSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPvDSPRWLEASKPLRKQL-KGGLPCILH 104
Cdd:cd17192     1 KSCLVARIQLLNNEFVEFTLSVESTGQECLEAVAQRLELREITYFSLWYYNKQ-NQQRWVDLEKPLKKQLdKYALEPTVY 79


                  ....*...
gi 1958779398 105 FRVRYFIP 112
Cdd:cd17192    80 FGVVFYVP 87
PDZ_densin_erbin-like cd06749
PDZ domain of densin, erbin, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 511-596 1.57e-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: 44.24  E-value: 1.57e-05
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gi 1958779398 511 IRITPDKEGRFGFNLKGGVDQK--------MPLVVSRINPESPADTCmpkLNEGDQIVLINGRDISEHTHDQVVMFIKas 582
Cdd:cd06749     1 IRVRIEKNPGLGFSISGGIGSQgnpfrpddDGIFVTKVQPDGPASKL---LQPGDKILEVNGYDFVNIEHGQAVSLLK-- 75

                          90
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gi 1958779398 583 reSHSRELALVIRR 596
Cdd:cd06749    76 --SFQNTVDLVVER 87
PDZ2_PDZD7-like cd10834
PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 516-595 2.01e-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: 43.91  E-value: 2.01e-05
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gi 1958779398 516 DKEGRF-GFNLKGGVDQKMPLVVSRINPESPADTcmPKLNEGDQIVLINGRDISEHTHDQVVMFIKasreSHSReLALVI 594
Cdd:cd10834     9 TSDDYClGFNIRGGSEYGLGIYVSKVDPGGLAEQ--NGIKVGDQILAVNGVSFEDITHSKAVEVLK----SQTH-LMLTI 81


                  .
gi 1958779398 595 R 595
Cdd:cd10834    82 K 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 2.63e-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: 2.63e-05
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gi 1958779398 517 KEGRFGFNLKGGVDQKMPLVVSRINPESPADTcMPKLNEGDQIVLINGRDISEHTHDQVVMFIKASreSHSRELALVIRR 596
Cdd:cd06733     9 QETGFGFRILGGTEEGSQVSIGAIVPGGAADL-DGRLRTGDELLSVDGVNVVGASHHKVVDLMGNA--ARNGQVNLTVRR 85
PDZ1_INAD-like cd23063
PDZ domain 1 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 513-580 2.70e-05

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


Pssm-ID: 467276 [Multi-domain]  Cd Length: 87  Bit Score: 43.27  E-value: 2.70e-05
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gi 1958779398 513 ITPDKEGRFGFNLKGG-VDQKMPLVVS-----RINPESPADTCmPKLNEGDQIVLINGRDISEHTHDQVVMFIK 580
Cdd:cd23063     4 IEKTEKKSFGICIVRGeVKVSPNTKTTgifikGIIPDSPAHKC-GRLKVGDRILSVNGNDVRNSTEQAAIDLIK 76
PDZ_tamalin_CYTIP-like cd06713
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ ...
 508-582 2.82e-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: 43.38  E-value: 2.82e-05
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gi 1958779398 508 LVLIRITpdkEGRFGFNL-------KGGVDQKMPLVVSRINPESPADTCmpKLNEGDQIVLINGRDISEHTHDQVVMFIK 580
Cdd:cd06713     6 IILEKQD---NETFGFEIqtyglhhKNSNEVEMCTYVCRVHEDSPAYLA--GLTAGDVILSVNGVSVEGASHQEIVELIR 80


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gi 1958779398 581 AS 582
Cdd:cd06713    81 SS 82
FERM_C_PTPH13 cd13187
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many ...
 228-307 3.47e-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: 3.47e-05
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gi 1958779398 228 HNLDLMIGIASAGIAVYRKY----ICTSFYPWVNILKISFKRKKFFIHQRQKQAEsrEHIvaFNMLNYRSCKNLWKSCVE 303
Cdd:cd13187    14 STLSLWLGICSRGIIIYEEKngarTPVLRFPWRETQKISFDKKKFTIESRGGSGI--KHT--FYTDSYKKSQYLLQLCSA 89


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gi 1958779398 304 HHSF 307
Cdd:cd13187    90 QHKF 93
PDZ2-PTPN13_FRMPD2-like cd06792
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ...
 517-596 3.78e-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: 42.97  E-value: 3.78e-05
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gi 1958779398 517 KEGRFGFNLKGGVDQKMPL---VVSRINPESPADtCMPKLNEGDQIVLINGRDISEHTHDQVVMFIKASREshsrELALV 593
Cdd:cd06792    10 KDGSLGISVTGGINTSVRHggiYVKSLVPGGAAE-QDGRIQKGDRLLEVNGVSLEGVTHKQAVECLKNAGQ----VVTLV 84


                  ...
gi 1958779398 594 IRR 596
Cdd:cd06792    85 LER 87
FERM_F1_PTPN14 cd17191
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 33-112 3.85e-05

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


Pssm-ID: 340711  Cd Length: 87  Bit Score: 43.11  E-value: 3.85e-05
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gi 1958779398  33 IRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHgDDPVDSPRWLEASKPLRKQL-KGGLPCILHFRVRYFI 111
Cdd:cd17191     8 IRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWF-LSKSQQARWVELEKPLKKQLdKFANEPLLFFGVMFYV 86


                  .
gi 1958779398 112 P 112
Cdd:cd17191    87 P 87
FERM_C_MYLIP_IDOL cd13195
FERM domain C-lobe of E3 ubiquitin ligase myosin regulatory light chain-interacting protein ...
 217-333 4.10e-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: 4.10e-05
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gi 1958779398 217 YGVELHGGRDLHNLDLMIGIASAGIAVYRK-YICTSFYPWVNILKISFKRKKFFIHQRQKQAESRehIVAFNMLNYRSCK 295
Cdd:cd13195     1 YGVEFFEVRNIEGQKLLIGVGPHGITICNDdFEVIERIPYTAIQMATSSGRVFTLTYLSDDGSVK--VLEFKLPSTRAAS 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958779398 296 NLWKSCVEHHSFFQAKKLlpqEKNVLSQYwtlgSRNPK 333
Cdd:cd13195    79 GLYRAITEKHAFYRCETV---RSAVTDQF----SRDLK 109
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 801-881 4.37e-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: 44.52  E-value: 4.37e-05
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gi 1958779398 801 VTHLQYvawPDHGVPDDS--SDFLEFVKYV-RSLRVGGEPALVHCSAGIGRTGVLVtmetAMCLIERNLPvyPLDIVRKM 877
Cdd:cd14500    61 VHDWPF---DDGSPPPDDvvDDWLDLLKTRfKEEGKPGACIAVHCVAGLGRAPVLV----AIALIELGMK--PEDAVEFI 131


                  ....
gi 1958779398 878 RDQR 881
Cdd:cd14500   132 RKKR 135
PDZ_GOPC-like cd06800
PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and ...
 516-576 6.77e-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: 42.36  E-value: 6.77e-05
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gi 1958779398 516 DKEGrFGFNLKGGVDQKMPLVVSRINPESPADTCmPKLNEGDQIVLINGRDISEHTHDQVV 576
Cdd:cd06800     9 PHEG-LGISITGGKEHGVPILISEIHEGQPADRC-GGLYVGDAILSVNGIDLRDAKHKEAV 67
PDZ_SNX27-like cd23070
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density ...
 510-582 6.79e-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: 42.40  E-value: 6.79e-05
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gi 1958779398 510 LIRITPDKEGrFGFNLKGGVDQKMPL------------VVSRINPESPADtcMPKLNEGDQIVLINGRDISEHTHDQVVM 577
Cdd:cd23070     2 VVTIVKSETG-FGFNVRGQVSEGGQLrsingelyaplqHVSAVLEGGAAD--KAGVRKGDRILEVNGVNVEGATHKQVVD 78


                  ....*
gi 1958779398 578 FIKAS 582
Cdd:cd23070    79 LIKSG 83
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 515-596 8.09e-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: 8.09e-05
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gi 1958779398 515 PDKEGRFGFNLKGGVD-------QKMPLV-VSRINPESPADTCMpkLNEGDQIVLINGRDISEHTHDQVVMFIKASresh 586
Cdd:cd06702     6 VKAGGPLGLSIVGGSDhsshpfgVDEPGIfISKVIPDGAAAKSG--LRIGDRILSVNGKDLRHATHQEAVSALLSP---- 79

                          90
                  ....*....|
gi 1958779398 587 SRELALVIRR 596
Cdd:cd06702    80 GQEIKLLVRH 89
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
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gi 1958779398 217 YGVELHGGRDLHNLDLMIGIASAGIAVYR---KYICTSFYPWVNILKISFKRKKFFIhqrqKQAESREHIVAFNMLNYRS 293
Cdd:cd13194     2 YGVNYFEIKNKKGTDLWLGVDALGLNIYEpdnKLTPKIGFPWSEIRNISFNDKKFVI----KPIDKKAPDFVFYSPRLRI 77

                          90
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gi 1958779398 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
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gi 1958779398 521 FGFNLKGG--VDQKMPLVVS----------RINPESPADtcMPKLNEGDQIVLINGRDISEHTHDQVVMFIKAS 582
Cdd:cd06746    18 FGFVLRGAkaVGPILEFTPTpafpalqyleSVDPGGVAD--KAGLKKGDFLLEINGEDVVKASHEQVVNLIRQS 89
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
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gi 1958779398 540 INPESPADTCmPKLNEGDQIVLINGRDISEHTHDQVVMFIKAS 582
Cdd:cd06671    43 VLEDSPAGRN-GTLKTGDRILEVNGVDLRNATHEEAVEAIRNA 84
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 535-600 1.94e-04

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


Pssm-ID: 440556 [Multi-domain]  Cd Length: 341  Bit Score: 44.48  E-value: 1.94e-04
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gi 1958779398 535 LVVSRINPESPADTcmPKLNEGDQIVLINGRDISEHTHDQVVMFIKA----------SRESHSRELALVIRRKAVR 600
Cdd:COG0793    73 VVVVSVIPGSPAEK--AGIKPGDIILAIDGKSVAGLTLDDAVKLLRGkagtkvtltiKRPGEGEPITVTLTRAEIK 146
PRK15375 PRK15375
type III secretion system effector GTPase-activating protein SptP;
797-891 2.63e-04

type III secretion system effector GTPase-activating protein SptP;


Pssm-ID: 185273 [Multi-domain]  Cd Length: 535  Bit Score: 44.79  E-value: 2.63e-04
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gi 1958779398 797 EEHTVTHLQYVAWPDHGvPDDSSDFLEFV-KYVRSLRVGGEPA---------LVHCSAGIGRTGvlvTMETAMCLieRNL 866
Cdd:PRK15375  419 KRYTIPVLHVKNWPDHQ-PLPSTDQLEYLaDRVKNSNQNGAPGrsssdkhlpMIHCLGGVGRTG---TMAAALVL--KDN 492

                          90       100
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gi 1958779398 867 PVYPLDIVR-KMRDQR-AMMVQTSSQY 891
Cdd:PRK15375  493 PHSNLEQVRaDFRNSRnNRMLEDASQF 519
PDZ4_PTPN13-like cd06696
PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 513-596 3.10e-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: 40.37  E-value: 3.10e-04
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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 513 ITPDKeGRFGFNLKGGVDQKMPLVVSRINPESPADTcmpKLNEGDQIVLINGRDISEHTHDQVVMFIKASreshSRELAL 592
Cdd:cd06696     9 TKSEK-GSLGFTVTKGKDDNGCYIHDIVQDPAKSDG---RLRPGDRLIMVNGVDVTNMSHTEAVSLLRAA----PKEVTL 80


                  ....
gi 1958779398 593 VIRR 596
Cdd:cd06696    81 VLGR 84
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 ...
 522-596 3.48e-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: 40.32  E-value: 3.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958779398 522 GFNLKGGVDQKM-PLVVSRINPESPADTcMPKLNEGDQIVLINGRDISEHTHDQVVMFIKASReshSRELALVIRR 596
Cdd:cd06762    15 GFSLAGGSDLENkSITVHRVFPSGLAAQ-EGTIQKGDRILSINGKSLKGVTHGDALSVLKQAR---LPKVAVVVIR 86
PDZ_RapGEF2_RapGEF6-like cd06755
PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange ...
 515-582 3.70e-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: 39.94  E-value: 3.70e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958779398 515 PDKEGRFGFNLKGGVDQKMPLVVSRINPESPADTCmpKLNEGDQIVLINGRDISEHTHDQVVMFIKAS 582
Cdd:cd06755     8 PSRESPLHFSLLGGSEKGFGIFVSKVEKGSKAAEA--GLKRGDQILEVNGQNFENITLKKALEILRNN 73
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 1958779398 522 GFNLKGGVDQKMPLVVSRINPESPADTCmpKLNEGDQIVLINGRDISEHTHDQVVMFIKAsreshSRELALVIR 595
Cdd:cd06738    16 GCSISSGPTQKPGIFISNVKPGSLAEEV--GLEVGDQIVEVNGTSFTNVDHKEAVMALKS-----SRHLTITVR 82
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 1958779398 536 VVSRINPESPADTCmpKLNEGDQIVLINGRDIseHTHDQVVMFIkasRESHSRELALVIRR 596
Cdd:pfam17820   1 VVTAVVPGSPAERA--GLRVGDVILAVNGKPV--RSLEDVARLL---QGSAGESVTLTVRR 54
Y_phosphatase3 pfam13350
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
 806-853 8.31e-04

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


Pssm-ID: 463853 [Multi-domain]  Cd Length: 243  Bit Score: 42.23  E-value: 8.31e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958779398 806 YVAWPDHGVPddssdflEFVKYVRSLRVGGEPALVHCSAGIGRTGVLV 853
Cdd:pfam13350 107 YRDMVTSARA-------AYRALFEALADNDGPVLFHCTAGKDRTGVAA 147
FERM_F1_FRMD4A cd17199
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 31-111 8.92e-04

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: 39.18  E-value: 8.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  31 CSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDpVDSPRWLEASKPLRKQ--LKGGLPCILHFRVR 108
Cdd:cd17199     5 CQVHLLDDRKLELLVQPKLLAKELLDLVASHFNLKEKEYFGIAFTDE-TGHLNWLQLDRRVLEHdfPKKSGPVVLYFCVR 83


                  ...
gi 1958779398 109 YFI 111
Cdd:cd17199    84 FYI 86
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 1958779398 218 GVELHGGRDLHNLDLMIGIASAGIAVYR---KYICTSFYPWVNILKISFKRKKFFIH---QRQKQAESREHIVAFNML-- 289
Cdd:cd13191     1 GVHYYEVKDKNGIPWWLGVSYKGIGQYDlqdKVKPRKFFQWKQLENLYFRDRKFSIEvrdPRRNSHRSRRTFQSSSVSvh 80

                          90       100
                  ....*....|....*....|....*...
gi 1958779398 290 -----NYRSCKNLWKSCVEHHSFFQAKK 312
Cdd:cd13191    81 vwygqTPALCKTIWSMAIAQHQFYLDRK 108
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
 779-862 1.23e-03

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


Pssm-ID: 464208 [Multi-domain]  Cd Length: 157  Bit Score: 40.37  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 779 CTIAYVSREMLVTNTETGEEHTVTH--LQY--VAWPDHGVPDDSsDFLEFVKYVRSLrvGGEPALV-HCSAGIGRTgvlv 853
Cdd:pfam14566  74 LTVVDVWESDVQTPEEVYERLKAEGpgVDYrrIPITDEKAPLEE-DFDALISIVKDA--PEDTALVfNCQMGRGRT---- 146

                          90
                  ....*....|..
gi 1958779398 854 TmeTAM---CLI 862
Cdd:pfam14566 147 T--TAMviaDLV 156
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 802-863 1.31e-03

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: 40.44  E-value: 1.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958779398 802 THLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVGGePALVHCSAGIGRTGVLVtmetAMCLIE 863
Cdd:cd14529    57 DGVKYVNLPLSATRPTESDVQSFLLIMDLKLAPG-PVLIHCKHGKDRTGLVS----ALYRIV 113
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 1958779398 528 GVDQKMPLVVSRINPESPADTCmpKLNEGDQIVLINGRDIseHTHDQVVMFIKASREshsRELALVIRR 596
Cdd:COG0750   123 GVPVLTPPVVGEVVPGSPAAKA--GLQPGDRIVAINGQPV--TSWDDLVDIIRASPG---KPLTLTVER 184
PDZ3_ZO1-like_domain cd06729
PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 517-578 2.14e-03

PDZ domain 3 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 3 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 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: 467211 [Multi-domain]  Cd Length: 82  Bit Score: 37.93  E-value: 2.14e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958779398 517 KEGRFGFNLKGGVDqkMPLVVSRINPESPADtcMPKLNEGDQIVLINGRDISEHTHDQVVMF 578
Cdd:cd06729     9 KGGSVGLRLAGGND--VGIFVAGVQEGSPAE--KQGLQEGDQILKVNGVDFRNLTREEAVLF 66
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 1958779398 785 SREMLVTNTETgEEHTVTH--LQYV--AWPDHGVPDDSS-DflEFVKYVRSLrvggePA----LVHCSAGIGRTgvlvTM 855
Cdd:cd14495   135 PKTVKVESVRT-EEELVKKkgAHYVriAATDHVWPDDEEiD--AFVAFYRSL-----PAdawlHFHCRAGKGRT----TT 202

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958779398 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 1958779398 521 FGFNLKGGVDQKMP------LVVSRINPESPADTcmpKLNEGDQIVLINGRDISEHTHDQVVMFIKASREshsrELALVI 594
Cdd:cd06727    13 FGIAVSGGRDNPHFqsgdtsIVISDVLKGGPAEG---KLQENDRVVSVNGVSMENVEHSFAVQILRKCGK----TANITV 85


                  ..
gi 1958779398 595 RR 596
Cdd:cd06727    86 KR 87
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 809-881 2.82e-03

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 39.62  E-value: 2.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958779398 809 WP--DHGVPDDS--SDFLEFVKYVRSLRVGGEPAL-VHCSAGIGRTGVLVtmetAMCLIERNlPVYPLDIVRKMRDQR 881
Cdd:PTZ00242   67 WPfdDGAPPPKAviDNWLRLLDQEFAKQSTPPETIaVHCVAGLGRAPILV----ALALVEYG-GMEPLDAVGFVREKR 139
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 1958779398 519 GRFGFNLKGGVDQ---KMPLVVSRINPESPADTcMPKLNEGDQIVLINGRDISEHTHDQVVMFIKASR 583
Cdd:cd06680    11 GSLGFSIVGGYEEshgNQPFFVKSIVPGTPAYN-DGRLKCGDIILAVNGVSTVGMSHAALVPLLKEQR 77
PDZ_CNK1_2_3-like cd06748
PDZ domain of connector enhancer of kinase suppressor of ras 1 (CNK1), CNK2, CNK3, and related ...
 536-595 3.46e-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: 37.20  E-value: 3.46e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 536 VVSRINPESPADTCMpKLNEGDQIVLINGRDISEHTHDQVVmfiKASREShSRELALVIR 595
Cdd:cd06748    27 VITGTKENSPADRCG-KIHAGDEVIQVNYQTVVGWQLKNLV---RALRED-PHGVTLTLK 81
PDZ2-PDZRN4-like cd06716
PDZ domain 2 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 537-596 4.47e-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: 4.47e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 537 VSRINPESPADTcMPKLNEGDQIVLINGRDIseHTHDQVVMFIKASREShsreLALVIRR 596
Cdd:cd06716    35 VSEVDPNSIAAK-DGRIREGDQILQINGVDV--QNREEAIALLSEEEKS----ITLLVAR 87
PDZ12_MUPP1-like cd06675
PDZ domain 12 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 10 of protein-associated tight ...
 513-580 4.55e-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: 36.96  E-value: 4.55e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958779398 513 ITPDKEGRFGFNLKGGVDQKM---PLVVSRINPESPADTCMpKLNEGDQIVLINGRDISEHTHDQVVMFIK 580
Cdd:cd06675     5 IKRGPQDSLGISIAGGVGSPLgdvPVFIAMIQPNGVAAQTG-KLKVGDRIVSINGQSTDGLTHSEAVNLLK 74
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
760-885 4.56e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 38.42  E-value: 4.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398  760 DPPDIMDHGIFH-IQCQAEDCTIAYVSREMLVTnteTGEEHTVTHLqyvawpdhgvpddSSDFLEFVKYVRSLRVGGEPA 838
Cdd:smart00195  18 NLALLKKLGITHvINVTNEVPNYNGSDFTYLGV---PIDDNTETKI-------------SPYFPEAVEFIEDAESKGGKV 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1958779398  839 LVHCSAGIGRTGVLVtmeTAMCLIERNLPVYplDIVRKMRDQRAMMV 885
Cdd:smart00195  82 LVHCQAGVSRSATLI---IAYLMKTRNMSLN--DAYDFVKDRRPIIS 123
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 766-848 4.95e-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: 4.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 766 DHGIFHI-QCQAEDCTIAYvsremlvtntetgeEHTVTHLQyVAWPDHGVPDDSSDFLEFVKYVRSLRVGGEPALVHCSA 844
Cdd:cd14498    24 KLGITHIlNVAGEPPPNKF--------------PDGIKYLR-IPIEDSPDEDILSHFEEAIEFIEEALKKGGKVLVHCQA 88


                  ....
gi 1958779398 845 GIGR 848
Cdd:cd14498    89 GVSR 92
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 5.10e-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: 36.84  E-value: 5.10e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958779398 512 RITPDKEgrFGFNLKGGVDqkMPL---VVSRINPESPADTcMPKLNEGDQIVLINGRDISEHTHDQVVMFIK 580
Cdd:cd06677    10 RSDPYEE--LGISIVGGND--TPLiniVIQEVYRDGVIAR-DGRLLPGDQILEVNGVDISNVTHSQARSVLR 76
Oca4 COG2365
Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];
729-911 5.32e-03

Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];


Pssm-ID: 441932 [Multi-domain]  Cd Length: 248  Bit Score: 39.56  E-value: 5.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 729 WQVVWDQKLSLVVMLTTLTERGRTkchqywpdpPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVA 808
Cdd:COG2365    41 LARLADLGIRTVIDLRSPAEVARA---------PDRLPPGVRYVHLPVLPDDAEALLEELRDGDLTPGDAEEFMLELYRA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958779398 809 WPDHGVPDdssdflEFVKYVRSLRVGGE-PALVHCSAGIGRTGVL---------VTMETAM---CLIERNLPVYPLDIVR 875
Cdd:COG2365   112 FVDPDAAD------AYRAAFRALADAENgPVLFHCTAGKDRTGVAaallllalgVPRETIMadyLLTNEYLAPLRARLLA 185

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958779398 876 KMRDQRAMMVQTssqykfVCEAILRVYEEGLVQTLD 911
Cdd:COG2365   186 ALRAALGDEDPE------LLAPLLGVRPEYLEAALD 215
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 1958779398 522 GFNLKGGVDQKM---PLVVSRINPESPADTCMPkLNEGDQIVLINGRDISEHTHDQVVMFIKA 581
Cdd:cd06763    14 GFSLEGGKGSPLgdrPLTIKRIFKGGAAEQSGV-LQVGDEILQINGTSLQGLTRFEAWNIIKS 75
PDZ5_DrPTPN13-like cd23060
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ...
 515-583 6.20e-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: 36.56  E-value: 6.20e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958779398 515 PDKEGrFGFNLKGGvDQKMPLVVSRINPESPADTcMPKLNEGDQIVLINGRDISEHTHDQVVMFIKASR 583
Cdd:cd23060     7 PANGG-LGFSLVGG-EGGSGIFVKSISPGGVADR-DGRLQVGDRLLQVNGESVIGLSHSKAVNILRKAK 72
DSP_MKP_classI cd14565
dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; ...
 798-849 7.65e-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: 37.75  E-value: 7.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958779398 798 EHTVTHLQYVAWP--DHGVPDDSSDFLEFVKYVRSLRVGGEPALVHCSAGIGRT 849
Cdd:cd14565    39 NHFEDHFQYKSIPveDSHNADISSWFEEAIGFIDKVKASGGRVLVHCQAGISRS 92
DSP_DUSP4 cd14640
dual specificity phosphatase domain of dual specificity protein phosphatase 4; Dual ...
 799-852 9.02e-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: 9.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958779398 799 HTVTHLQYVAWP--DHGVPDDSSDFLEFVKYVRSLRVGGEPALVHCSAGIGRTGVL 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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