NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1928577684|ref|NP_001375384|]
View 

FERM and PDZ domain-containing protein 3 isoform 2 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
FERM_F1_FRMPD3 cd17169
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ ...
 10-102 1.73e-58

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ domain-containing protein 3 (FRMPD3); FRMPD3 is an uncharacterized FERM and PDZ domain-containing protein. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


:

Pssm-ID: 340689  Cd Length: 93  Bit Score: 196.20  E-value: 1.73e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684   10 IPNVLKVFLENGQIKSFTFDGRTTVKDVMATLQDRLSLRSIEHFALVLEYTGPEQNHKFLILQDKQPLAYVVQRTHYHGM 89
Cdd:cd17169      1 IPNVLKVFLENGQIKSFTFDGRTTVKDVMLTLQDRLSLRHIEHFALVLEYGGPEQNHKFLLLQDKQPLAHVVQRTHYQGM 80

                           90
                   ....*....|...
gi 1928577684   90 KCLFRISFFPKDP 102
Cdd:cd17169     81 KCLFRICFFPKDP 93
FERM_C_FRMPD1_FRMPD3_FRMPD4 cd13183
FERM domain C-lobe of FERM and PDZ domain containing proteins 1, 3, and 4 (FRMPD1, 3, 4); The ...
 228-331 7.51e-52

FERM domain C-lobe of FERM and PDZ domain containing proteins 1, 3, and 4 (FRMPD1, 3, 4); The function of FRMPD1, FRMPD3, and FRMPD4 is unknown at present. These proteins contain an N-terminal PDZ (post synaptic density protein (PSD95), Drosophila disc large tumor suppressor (Dlg1), and zonula occludens-1 protein (zo-1) domain and a C-terminal FERM domain. PDZ (also known as DHR (Dlg homologous region) or GLGF (glycine-leucine-glycine-phenylalanine) domains) help anchor transmembrane proteins to the cytoskeleton and hold together signaling complexes. PDZ domains bind to a short region of the C-terminus of other specific proteins. The FERM domain is composed of three subdomains: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3), which form a clover leaf fold. 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: 270004  Cd Length: 105  Bit Score: 177.59  E-value: 7.51e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  228 TGVLFNTVGL-DEKHSATTLLVGPRHGISHVIDLKTNLTTVLSEFSKISKIQLFRENQGVARVETSIMDAKPLVLLMEWP 306
Cdd:cd13183      1 GGRSFQATLMlQDRESEVTLLVGPRYGISHVINHKLNLLALLAEFSHISRIELLRESDKVSRVELHIHDVKPITLLMESP 80

                           90       100
                   ....*....|....*....|....*
gi 1928577684  307 EATNFACLIAGYCRLLLDSRKMVFS 331
Cdd:cd13183     81 DAKDLACLIAGYYRLLVDPRRSIFS 105
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 13-232 6.47e-36

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: 135.50  E-value: 6.47e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684    13 VLKVFLENGQIKSFTFDGRTTVKDVMATLQDRLSLRSIEHFALVLEYTGPEQNHkFLilqdkQPLAYV-VQRTHYHGMKC 91
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRH-WL-----DPAKTLlDQDVKSEPLTL 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684    92 LFRISFFPKDPvELLRRDPAAFEYLYIQSRNDVIRERFGMEpkPEMLLGLAALHIYITVsatrPSQKITLKNVEKEWGLE 171
Cdd:smart00295   75 YFRVKFYPPDP-NQLKEDPTRLNLLYLQVRNDILEGRLPCP--EEEALLLAALALQAEF----GDYDEELHDLRGELSLK 147

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1928577684   172 PFLPPSLLQGIKEKNLRKSLSQQLKAHqmhpssstKG-SAIQAKLQYLRILNELPTFtGVLF 232
Cdd:smart00295  148 RFLPKQLLDSRKLKEWRERIVELHKEL--------IGlSPEEAKLKYLELARKLPTY-GVEL 200
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 712-1089 1.26e-03

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  712 TGQSPAPTGARRKIPQSEVQVQGDRPYSLAVHPALSPQLSEQKNLSLLPPVPEDRGPGHSRAGLEMSLRSATPSLSEEQV 791
Cdd:PHA03307    72 PPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAAS 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  792 SELRENLPKEVrlspklildPKGNVTPAIISAALQQVVHSKslATPGTALATPSNRGERRLEASMGRPEVTMSRPEVSVM 871
Cdd:PHA03307   152 PPAAGASPAAV---------ASDAASSRQAALPLSSPEETA--RAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSP 220

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  872 SSSVSKNLKFkmspGAPETTRNSQQQLGPEVSASPRASTGSRADNLHLSPPEDRFPVQSFPPKSYLSRVSRDSMGKQATG 951
Cdd:PHA03307   221 APAPGRSAAD----DAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSP 296

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  952 EVAGKGGPEGAKPPPNKQSVVSGQGDKGQLESLSKSSKLEETSLVPRAgypmalQSPSCQPRSHSPSCQPRGPSPSSQSR 1031
Cdd:PHA03307   297 SPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPG------PSPSRSPSPSRPPPPADPSSPRKRPR 370

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684 1032 GqSPSCQPRSQSPLRPL--ATSRQVSTMPSRKLETTLDGAHSASEGPTKPKSSRGPFRLR 1089
Cdd:PHA03307   371 P-SRAPSSPAASAGRPTrrRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYAR 429
 
Name Accession Description Interval E-value
FERM_F1_FRMPD3 cd17169
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ ...
 10-102 1.73e-58

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ domain-containing protein 3 (FRMPD3); FRMPD3 is an uncharacterized FERM and PDZ domain-containing protein. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340689  Cd Length: 93  Bit Score: 196.20  E-value: 1.73e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684   10 IPNVLKVFLENGQIKSFTFDGRTTVKDVMATLQDRLSLRSIEHFALVLEYTGPEQNHKFLILQDKQPLAYVVQRTHYHGM 89
Cdd:cd17169      1 IPNVLKVFLENGQIKSFTFDGRTTVKDVMLTLQDRLSLRHIEHFALVLEYGGPEQNHKFLLLQDKQPLAHVVQRTHYQGM 80

                           90
                   ....*....|...
gi 1928577684   90 KCLFRISFFPKDP 102
Cdd:cd17169     81 KCLFRICFFPKDP 93
FERM_C_FRMPD1_FRMPD3_FRMPD4 cd13183
FERM domain C-lobe of FERM and PDZ domain containing proteins 1, 3, and 4 (FRMPD1, 3, 4); The ...
 228-331 7.51e-52

FERM domain C-lobe of FERM and PDZ domain containing proteins 1, 3, and 4 (FRMPD1, 3, 4); The function of FRMPD1, FRMPD3, and FRMPD4 is unknown at present. These proteins contain an N-terminal PDZ (post synaptic density protein (PSD95), Drosophila disc large tumor suppressor (Dlg1), and zonula occludens-1 protein (zo-1) domain and a C-terminal FERM domain. PDZ (also known as DHR (Dlg homologous region) or GLGF (glycine-leucine-glycine-phenylalanine) domains) help anchor transmembrane proteins to the cytoskeleton and hold together signaling complexes. PDZ domains bind to a short region of the C-terminus of other specific proteins. The FERM domain is composed of three subdomains: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3), which form a clover leaf fold. 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: 270004  Cd Length: 105  Bit Score: 177.59  E-value: 7.51e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  228 TGVLFNTVGL-DEKHSATTLLVGPRHGISHVIDLKTNLTTVLSEFSKISKIQLFRENQGVARVETSIMDAKPLVLLMEWP 306
Cdd:cd13183      1 GGRSFQATLMlQDRESEVTLLVGPRYGISHVINHKLNLLALLAEFSHISRIELLRESDKVSRVELHIHDVKPITLLMESP 80

                           90       100
                   ....*....|....*....|....*
gi 1928577684  307 EATNFACLIAGYCRLLLDSRKMVFS 331
Cdd:cd13183     81 DAKDLACLIAGYYRLLVDPRRSIFS 105
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 13-232 6.47e-36

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: 135.50  E-value: 6.47e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684    13 VLKVFLENGQIKSFTFDGRTTVKDVMATLQDRLSLRSIEHFALVLEYTGPEQNHkFLilqdkQPLAYV-VQRTHYHGMKC 91
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRH-WL-----DPAKTLlDQDVKSEPLTL 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684    92 LFRISFFPKDPvELLRRDPAAFEYLYIQSRNDVIRERFGMEpkPEMLLGLAALHIYITVsatrPSQKITLKNVEKEWGLE 171
Cdd:smart00295   75 YFRVKFYPPDP-NQLKEDPTRLNLLYLQVRNDILEGRLPCP--EEEALLLAALALQAEF----GDYDEELHDLRGELSLK 147

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1928577684   172 PFLPPSLLQGIKEKNLRKSLSQQLKAHqmhpssstKG-SAIQAKLQYLRILNELPTFtGVLF 232
Cdd:smart00295  148 RFLPKQLLDSRKLKEWRERIVELHKEL--------IGlSPEEAKLKYLELARKLPTY-GVEL 200
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 102-232 6.75e-25

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 101.19  E-value: 6.75e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  102 PVELLRRDPAAFEYLYIQSRNDVIRERFgmEPKPEMLLGLAALHIYITVSATRPSQKItlknvEKEWGLEPFLPPSLLQG 181
Cdd:pfam00373    1 DLELLLQDEVTRHLLYLQAKDDILEGRL--PCSEEEALLLAALQLQAEFGDYQPSSHT-----SEYLSLESFLPKQLLRK 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1928577684  182 IKEKNLRKSLSQQLKAHQ-MhpssstkgSAIQAKLQYLRILNELPTFTGVLF 232
Cdd:pfam00373   74 MKSKELEKRVLEAHKNLRgL--------SAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 112-224 1.15e-13

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: 68.43  E-value: 1.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  112 AFEYLYIQSRNDVIRERFgmEPKPEMLLGLAALHIYITVSATRPSQKitlknVEKEWGLEPFLPPSLLQGIKEKNLRKSL 191
Cdd:cd14473      1 TRYLLYLQVKRDILEGRL--PCSEETAALLAALALQAEYGDYDPSEH-----KPKYLSLKRFLPKQLLKQRKPEEWEKRI 73

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1928577684  192 SQQLKAHqmhpssstKG-SAIQAKLQYLRILNEL 224
Cdd:cd14473     74 VELHKKL--------RGlSPAEAKLKYLKIARKL 99
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 712-1089 1.26e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  712 TGQSPAPTGARRKIPQSEVQVQGDRPYSLAVHPALSPQLSEQKNLSLLPPVPEDRGPGHSRAGLEMSLRSATPSLSEEQV 791
Cdd:PHA03307    72 PPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAAS 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  792 SELRENLPKEVrlspklildPKGNVTPAIISAALQQVVHSKslATPGTALATPSNRGERRLEASMGRPEVTMSRPEVSVM 871
Cdd:PHA03307   152 PPAAGASPAAV---------ASDAASSRQAALPLSSPEETA--RAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSP 220

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  872 SSSVSKNLKFkmspGAPETTRNSQQQLGPEVSASPRASTGSRADNLHLSPPEDRFPVQSFPPKSYLSRVSRDSMGKQATG 951
Cdd:PHA03307   221 APAPGRSAAD----DAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSP 296

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  952 EVAGKGGPEGAKPPPNKQSVVSGQGDKGQLESLSKSSKLEETSLVPRAgypmalQSPSCQPRSHSPSCQPRGPSPSSQSR 1031
Cdd:PHA03307   297 SPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPG------PSPSRSPSPSRPPPPADPSSPRKRPR 370

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684 1032 GqSPSCQPRSQSPLRPL--ATSRQVSTMPSRKLETTLDGAHSASEGPTKPKSSRGPFRLR 1089
Cdd:PHA03307   371 P-SRAPSSPAASAGRPTrrRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYAR 429
CytochromB561_N pfam09786
Cytochrome B561, N terminal; Members of this family are found in the N terminal region of ...
 965-1167 4.33e-03

Cytochrome B561, N terminal; Members of this family are found in the N terminal region of cytochrome B561, as well as in various other putative uncharacterized proteins.


Pssm-ID: 462899  Cd Length: 579  Bit Score: 41.73  E-value: 4.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  965 PPNKQSVVSGQGDKGQLESLSKSSKLEETSLVPRAGYPMALQSPSCQPRSHSPSCQPRGPSpSSQSRGQSPSCQPRSQSP 1044
Cdd:pfam09786   93 SPSKGTKTPSRLTNQQLGLLGLKPNDSSFVTTHRKKPPKSKSSPQSPSPVLVPLHQSVSPS-SSESRKGGDKSPAGSGKK 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684 1045 LRPLATSRQVSTMPSRKLETTL-DGAHSAS----EGPTKPKSSRGPFRLR-NLFSATFPTRQKKETDERQAQ--LQKVKQ 1116
Cdd:pfam09786  172 LRSFSTSSKSPASPSVYLRGSPvPLNSSPLpsdrNYENSVQSSPEIDSAVsTPWSRKRATIGKEIRTEKMLErfLAEVDE 251

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1928577684 1117 YELEFLEELLKP---PSQGELPGTEYLQPPAPGRCS--CQLRSSPVQQGPG-----MSREQ 1167
Cdd:pfam09786  252 KITESAFGKASPsnvSGSANRSGSTRSTPLRSVRMSpgSQKFTTPPKKGEGdlpspMSMEE 312
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 687-1049 5.75e-03

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 41.20  E-value: 5.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  687 AAQAVLTAPYALGPPDPNPSPQPAVTGQSPAPTGARRKIPQSEVQVQGD-RPYSLAVHPALSPQLSEQKNLSL------- 758
Cdd:COG5180    121 GALPAPAAAAALPKAKVTREATSASAGVALAAALLQRSDPILAKDPDGDsASTLPPPAEKLDKVLTEPRDALKdspekld 200

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  759 LPPVPED-----------RGPGHSRAGLEMSLRSATPSLSEEQVSELRENLPKEVRlspklildPKGNVTpaiisAALQQ 827
Cdd:COG5180    201 RPKVEVKdeaqeeppdltGGADHPRPEAASSPKVDPPSTSEARSRPATVDAQPEMR--------PPADAK-----ERRRA 267

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  828 VVHSKSLATPGTALATpsnrgERRLEASMGRPEVTMSRPEVSVMSSSVSKNLK-FKMSPGAPETTRNSQQQLGPEVSASP 906
Cdd:COG5180    268 AIGDTPAAEPPGLPVL-----EAGSEPQSDAPEAETARPIDVKGVASAPPATRpVRPPGGARDPGTPRPGQPTERPAGVP 342

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  907 RASTGSRADNLHLSPPEDRFPVQ---SFPPKSYLSRVSRDSMGKQATGEVAGKGGPEGAKPPPNKQSVVSGQGDKGQLES 983
Cdd:COG5180    343 EAASDAGQPPSAYPPAEEAVPGKpleQGAPRPGSSGGDGAPFQPPNGAPQPGLGRRGAPGPPMGAGDLVQAALDGGGRET 422

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1928577684  984 LSKSS-KLEETSLVPRAGYPMALQSPSCQPRSHSPSCQPRGPS--PSSQSRGQSPSCQPRSQSPLRPLA 1049
Cdd:COG5180    423 ASLGGaAGGAGQGPKADFVPGDAESVSGPAGLADQAGAAASTAmaDFVAPVTDATPVDVADVLGVRPDA 491
 
Name Accession Description Interval E-value
FERM_F1_FRMPD3 cd17169
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ ...
 10-102 1.73e-58

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ domain-containing protein 3 (FRMPD3); FRMPD3 is an uncharacterized FERM and PDZ domain-containing protein. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340689  Cd Length: 93  Bit Score: 196.20  E-value: 1.73e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684   10 IPNVLKVFLENGQIKSFTFDGRTTVKDVMATLQDRLSLRSIEHFALVLEYTGPEQNHKFLILQDKQPLAYVVQRTHYHGM 89
Cdd:cd17169      1 IPNVLKVFLENGQIKSFTFDGRTTVKDVMLTLQDRLSLRHIEHFALVLEYGGPEQNHKFLLLQDKQPLAHVVQRTHYQGM 80

                           90
                   ....*....|...
gi 1928577684   90 KCLFRISFFPKDP 102
Cdd:cd17169     81 KCLFRICFFPKDP 93
FERM_C_FRMPD1_FRMPD3_FRMPD4 cd13183
FERM domain C-lobe of FERM and PDZ domain containing proteins 1, 3, and 4 (FRMPD1, 3, 4); The ...
 228-331 7.51e-52

FERM domain C-lobe of FERM and PDZ domain containing proteins 1, 3, and 4 (FRMPD1, 3, 4); The function of FRMPD1, FRMPD3, and FRMPD4 is unknown at present. These proteins contain an N-terminal PDZ (post synaptic density protein (PSD95), Drosophila disc large tumor suppressor (Dlg1), and zonula occludens-1 protein (zo-1) domain and a C-terminal FERM domain. PDZ (also known as DHR (Dlg homologous region) or GLGF (glycine-leucine-glycine-phenylalanine) domains) help anchor transmembrane proteins to the cytoskeleton and hold together signaling complexes. PDZ domains bind to a short region of the C-terminus of other specific proteins. The FERM domain is composed of three subdomains: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3), which form a clover leaf fold. 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: 270004  Cd Length: 105  Bit Score: 177.59  E-value: 7.51e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  228 TGVLFNTVGL-DEKHSATTLLVGPRHGISHVIDLKTNLTTVLSEFSKISKIQLFRENQGVARVETSIMDAKPLVLLMEWP 306
Cdd:cd13183      1 GGRSFQATLMlQDRESEVTLLVGPRYGISHVINHKLNLLALLAEFSHISRIELLRESDKVSRVELHIHDVKPITLLMESP 80

                           90       100
                   ....*....|....*....|....*
gi 1928577684  307 EATNFACLIAGYCRLLLDSRKMVFS 331
Cdd:cd13183     81 DAKDLACLIAGYYRLLVDPRRSIFS 105
FERM_F1_FRMPD1_like cd17088
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ ...
 10-99 6.32e-45

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ domain-containing proteins FRMPD1, FRMPD3, FRMPD4, and similar proteins; This family includes FERM and PDZ domain-containing proteins FRMPD1, FRMPD3, and FRMPD4, which all contain a PDZ domain and a FERM domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain of the FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). FRMPD1, also termed FERM domain-containing protein 2, is an activator of G-protein signaling 3 (AGS3)-binding protein that regulates the subcellular location of AGS3 and its interaction with G-proteins. FRMPD4, also termed PDZ domain-containing protein 10, or PSD-95-interacting regulator of spine morphogenesis (Preso), is a multiscaffolding protein that modulates both Homer1 and post-synaptic density protein 95 activity. Both FRMPD1 and FRMPD4 can associate with the tetratricopeptide repeat (TPR) motif-containing adaptor protein LGN. The biological role of FRMPD3 remains unclear.


Pssm-ID: 340608  Cd Length: 90  Bit Score: 157.05  E-value: 6.32e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684   10 IPNVLKVFLENGQIKSFTFDGRTTVKDVMATLQDRLSLRSIEHFALVLEYTGPEQNHKFLILQDKQPLAYVVQRTHYHGM 89
Cdd:cd17088      1 MPNVLKVYLENGQTKSFKYDQSTTVKDVLLSLQEKLGIKSMEHFSLVLEYVKSPRTNKLSLLQPDESLAQVAARPGSHHL 80

                           90
                   ....*....|
gi 1928577684   90 KCLFRISFFP 99
Cdd:cd17088     81 RCLFRISFVP 90
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 13-232 6.47e-36

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: 135.50  E-value: 6.47e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684    13 VLKVFLENGQIKSFTFDGRTTVKDVMATLQDRLSLRSIEHFALVLEYTGPEQNHkFLilqdkQPLAYV-VQRTHYHGMKC 91
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRH-WL-----DPAKTLlDQDVKSEPLTL 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684    92 LFRISFFPKDPvELLRRDPAAFEYLYIQSRNDVIRERFGMEpkPEMLLGLAALHIYITVsatrPSQKITLKNVEKEWGLE 171
Cdd:smart00295   75 YFRVKFYPPDP-NQLKEDPTRLNLLYLQVRNDILEGRLPCP--EEEALLLAALALQAEF----GDYDEELHDLRGELSLK 147

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1928577684   172 PFLPPSLLQGIKEKNLRKSLSQQLKAHqmhpssstKG-SAIQAKLQYLRILNELPTFtGVLF 232
Cdd:smart00295  148 RFLPKQLLDSRKLKEWRERIVELHKEL--------IGlSPEEAKLKYLELARKLPTY-GVEL 200
FERM_F1_FRMPD4 cd17170
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ ...
 9-102 4.35e-33

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ domain-containing protein 4 (FRMPD4); FRMPD4, also termed PDZ domain-containing protein 10, or PSD-95-interacting regulator of spine morphogenesis (Preso), is a multiscaffolding protein that modulates both Homer1 and postsynaptic density protein 95 activity. It can associate with the tetratricopeptide repeat (TPR) motif-containing adaptor protein LGN. Moreover, FRMPD4 is asymmetrically distributed in the cytosol and nuclei of neural stem/progenitor cells in the adult brain, suggesting a significant role in cell differentiation via association with cell polarity machinery. FRMPD4 contains a WW domain, a PDZ domain, and a FERM domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain of the FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340690  Cd Length: 94  Bit Score: 123.63  E-value: 4.35e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684    9 LIPNVLKVFLENGQIKSFTFDGRTTVKDVMATLQDRLSLRSIEHFALVLEYTGPEQNHKFLILQDKQPLAYVVQRTHYHG 88
Cdd:cd17170      1 FMPNVLKVYLENGQTKSFRFDCSTSIKDVILTLQEKLSIKCIEHFSLMLEQRTEGSGTKLLLLHEQETLTQVTQRPGSHK 80

                           90
                   ....*....|....
gi 1928577684   89 MKCLFRISFFPKDP 102
Cdd:cd17170     81 MRCLFRISFVPKDP 94
FERM_F1_FRMPD1 cd17168
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ ...
 10-101 2.07e-27

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ domain-containing protein 1 (FRMPD1); FRMPD1, also termed FERM domain-containing protein 2, is an activator of G-protein signaling 3 (AGS3)-binding protein that regulates the subcellular location of AGS3 and its interaction with G-proteins. It also binds to the tetratricopeptide repeat (TPR) motif-containing adaptor protein LGN. FRMPD1 contains a PDZ domain and a FERM domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340688  Cd Length: 90  Bit Score: 107.26  E-value: 2.07e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684   10 IPNVLKVFLENGQIKSFTFDGRTTVKDVMATLQDRLSLRSIEHFALVLEytgpEQNH--KFLILQDKQPLAYVVQRTHYH 87
Cdd:cd17168      1 MPNVLKVYLENGQTKAFKFESNTTVKDIILTLKEKLSIRSIEHFALVLE----EQYSisKLYLLHEEELIEQVVEKRESH 76

                           90
                   ....*....|....
gi 1928577684   88 GMKCLFRISFFPKD 101
Cdd:cd17168     77 DYRCLFRVCFVPKD 90
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 102-232 6.75e-25

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 101.19  E-value: 6.75e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  102 PVELLRRDPAAFEYLYIQSRNDVIRERFgmEPKPEMLLGLAALHIYITVSATRPSQKItlknvEKEWGLEPFLPPSLLQG 181
Cdd:pfam00373    1 DLELLLQDEVTRHLLYLQAKDDILEGRL--PCSEEEALLLAALQLQAEFGDYQPSSHT-----SEYLSLESFLPKQLLRK 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1928577684  182 IKEKNLRKSLSQQLKAHQ-MhpssstkgSAIQAKLQYLRILNELPTFTGVLF 232
Cdd:pfam00373   74 MKSKELEKRVLEAHKNLRgL--------SAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 112-224 1.15e-13

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: 68.43  E-value: 1.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  112 AFEYLYIQSRNDVIRERFgmEPKPEMLLGLAALHIYITVSATRPSQKitlknVEKEWGLEPFLPPSLLQGIKEKNLRKSL 191
Cdd:cd14473      1 TRYLLYLQVKRDILEGRL--PCSEETAALLAALALQAEYGDYDPSEH-----KPKYLSLKRFLPKQLLKQRKPEEWEKRI 73

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1928577684  192 SQQLKAHqmhpssstKG-SAIQAKLQYLRILNEL 224
Cdd:cd14473     74 VELHKKL--------RGlSPAEAKLKYLKIARKL 99
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 230-323 1.92e-08

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: 53.15  E-value: 1.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  230 VLFNTVGLDEKHSATTLLVGPrHGIsHVIDLKTNLTTVLSEFSKISKIQLFRENqgvaRVETSIMD-AKPLVLLMEWP-- 306
Cdd:cd00836      3 EFFPVKDKSKKGSPIILGVNP-EGI-SVYDELTGQPLVLFPWPNIKKISFSGAK----KFTIVVADeDKQSKLLFQTPsr 76

                           90
                   ....*....|....*..
gi 1928577684  307 EATNFACLIAGYCRLLL 323
Cdd:cd00836     77 QAKEIWKLIVGYHRFLL 93
FERM_C_FAK1 cd13190
FERM domain C-lobe of Focal Adhesion Kinase 1 and 2; FAK1 (also called FRNK/Focal adhesion ...
 243-333 3.41e-08

FERM domain C-lobe of Focal Adhesion Kinase 1 and 2; FAK1 (also called FRNK/Focal adhesion kinase-related nonkinase; p125FAK/pp125FAK;PTK2/Protein-tyrosine kinase 2 protein tyrosine kinase 2 (PTK2) is a non-receptor tyrosine kinase that localizes to focal adhesions in adherent cells. It has been implicated in diverse cellular roles including cell locomotion, mitogen response and cell survival. The N-terminal region of FAK1 contains a FERM domain, a linker, a kinase domain, and a C-terminal FRNK (FAK-related-non-kinase) domain. Three subdomains of FERM: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3), form a cloverleaf fold, similar to those of known FERM structures despite the low sequence conservation. The C-lobe/F3 within the FERM domain is part of the PH domain family. The phosphoinositide-binding site found in ERM family proteins is not present in the FERM domain of FAK1. The adjacent Src SH3 and SH2 binding sites in the linker of FAK1 associates with the F3 and F1 lobes and are thought to be involved in regulation. The FERM domain of FAK1 can inhibit enzymatic activity and repress FAK signaling. In an inactive state of FAK1, the FERM domain is thought to interact with the catalytic domain of FAK1 to repress its activity. Upon activation this interaction is disrupted and its kinase activity restored. The FRNK domain is thought to function as a negative regulator of kinase activity. The C-lobe/F3 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: 270011  Cd Length: 111  Bit Score: 53.02  E-value: 3.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  243 ATTLLVGPRHGISHVIDLKTNLTTvLSEFSKISKIQLFRENQGVAR------VETSimdAKPLVL-LMEWPEATNFACLI 315
Cdd:cd13190     16 PVDLVIGPEVGISYLTDKGSAPTH-LADFEQIQSIQTSKSEDKDGKallqlkIAGA---SEPLSItCSSLATAESLADLI 91

                           90
                   ....*....|....*...
gi 1928577684  316 AGYCRLLLDSRKMVFSRP 333
Cdd:cd13190     92 DGYCRLVNQTDSSLIIRP 109
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
 13-97 2.36e-07

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: 49.89  E-value: 2.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684   13 VLKVFLENGQIKSFTFDGRTTVKDVMATLQDRLSLRSIEHFALVleYTGPEQNHKFLILqDKQPLAYVVQRTHYHgmkCL 92
Cdd:cd01765      2 SCRVRLLDGTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLF--YEDNDGQKHWLDL-DKKISKQLKRSGPYQ---FY 75


                   ....*
gi 1928577684   93 FRISF 97
Cdd:cd01765     76 FRVKF 80
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 712-1089 1.26e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  712 TGQSPAPTGARRKIPQSEVQVQGDRPYSLAVHPALSPQLSEQKNLSLLPPVPEDRGPGHSRAGLEMSLRSATPSLSEEQV 791
Cdd:PHA03307    72 PPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAAS 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  792 SELRENLPKEVrlspklildPKGNVTPAIISAALQQVVHSKslATPGTALATPSNRGERRLEASMGRPEVTMSRPEVSVM 871
Cdd:PHA03307   152 PPAAGASPAAV---------ASDAASSRQAALPLSSPEETA--RAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSP 220

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  872 SSSVSKNLKFkmspGAPETTRNSQQQLGPEVSASPRASTGSRADNLHLSPPEDRFPVQSFPPKSYLSRVSRDSMGKQATG 951
Cdd:PHA03307   221 APAPGRSAAD----DAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSP 296

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  952 EVAGKGGPEGAKPPPNKQSVVSGQGDKGQLESLSKSSKLEETSLVPRAgypmalQSPSCQPRSHSPSCQPRGPSPSSQSR 1031
Cdd:PHA03307   297 SPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPG------PSPSRSPSPSRPPPPADPSSPRKRPR 370

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684 1032 GqSPSCQPRSQSPLRPL--ATSRQVSTMPSRKLETTLDGAHSASEGPTKPKSSRGPFRLR 1089
Cdd:PHA03307   371 P-SRAPSSPAASAGRPTrrRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYAR 429
PHA03247 PHA03247
large tegument protein UL36; Provisional
 918-1207 2.85e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 2.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  918 HLSPPEDRFPVQSFPPKSYLSRVSRDSMGKQATGEVAGK---GGPEGAKPPPNKQSVVSGqgdkgqLESLSKSSKLEETS 994
Cdd:PHA03247  2480 YRRPAEARFPFAAGAAPDPGGGGPPDPDAPPAPSRLAPAilpDEPVGEPVHPRMLTWIRG------LEELASDDAGDPPP 2553

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  995 LVPRAGYPMALQSPSCQPRshspsCQPRGPSPSSQSRGQSPSCQPRSQSPLRPLATSRQvstmPSRKLETTLDGAHSASE 1074
Cdd:PHA03247  2554 PLPPAAPPAAPDRSVPPPR-----PAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGD----PRGPAPPSPLPPDTHAP 2624

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684 1075 GPTKPKSSRGPFRLRNLFSATFPTRQKKETDERQAQLQKVKQYELEFLEELLKPPSQGELPG---------TEYLQPPAP 1145
Cdd:PHA03247  2625 DPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRaarptvgslTSLADPPPP 2704

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1928577684 1146 GRC--SCQLRSSPVQQGPGMSREQRRSCDCKRICRGGRPQAAQTPAPGLRERERVPPTQRQPEA 1207
Cdd:PHA03247  2705 PPTpePAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPA 2768
CytochromB561_N pfam09786
Cytochrome B561, N terminal; Members of this family are found in the N terminal region of ...
 965-1167 4.33e-03

Cytochrome B561, N terminal; Members of this family are found in the N terminal region of cytochrome B561, as well as in various other putative uncharacterized proteins.


Pssm-ID: 462899  Cd Length: 579  Bit Score: 41.73  E-value: 4.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  965 PPNKQSVVSGQGDKGQLESLSKSSKLEETSLVPRAGYPMALQSPSCQPRSHSPSCQPRGPSpSSQSRGQSPSCQPRSQSP 1044
Cdd:pfam09786   93 SPSKGTKTPSRLTNQQLGLLGLKPNDSSFVTTHRKKPPKSKSSPQSPSPVLVPLHQSVSPS-SSESRKGGDKSPAGSGKK 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684 1045 LRPLATSRQVSTMPSRKLETTL-DGAHSAS----EGPTKPKSSRGPFRLR-NLFSATFPTRQKKETDERQAQ--LQKVKQ 1116
Cdd:pfam09786  172 LRSFSTSSKSPASPSVYLRGSPvPLNSSPLpsdrNYENSVQSSPEIDSAVsTPWSRKRATIGKEIRTEKMLErfLAEVDE 251

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1928577684 1117 YELEFLEELLKP---PSQGELPGTEYLQPPAPGRCS--CQLRSSPVQQGPG-----MSREQ 1167
Cdd:pfam09786  252 KITESAFGKASPsnvSGSANRSGSTRSTPLRSVRMSpgSQKFTTPPKKGEGdlpspMSMEE 312
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 935-1217 5.05e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 41.68  E-value: 5.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  935 SYLSRVSRDSMGKQATGEVAGKGGPEGAKPPPNKQSVVSGQGDKGQLESLSKSSKLEetslvpragypmALQSPSCQPRS 1014
Cdd:pfam03154    4 SMRTRRSRGSMSTLRSGRKKQTASPDGRASPTNEDLRSSGRNSPSAASTSSNDSKAE------------SMKKSSKKIKE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684 1015 HSPScqPRGPSPSSQSRGQSPSCQPRSQSPLRPLATSRQVSTMPSRKLETTLDGAHSASEGPTKPKSSRGPFRLRnlfSA 1094
Cdd:pfam03154   72 EAPS--PLKSAKRQREKGASDTEEPERATAKKSKTQEISRPNSPSEGEGESSDGRSVNDEGSSDPKDIDQDNRST---SP 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684 1095 TFPTRQKKETDERQAQLQKVKQYELEFLEELLKPPSQGELPGTEYLQ----PPAPGRCSCQLRSSP-VQQGPGMSREQRR 1169
Cdd:pfam03154  147 SIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQaataGPTPSAPSVPPQGSPaTSQPPNQTQSTAA 226

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1928577684 1170 SCDCKRICRGGRPQAAQTPAPGLRER-ERVPPTQRQPEAGPGLSLNSPI 1217
Cdd:pfam03154  227 PHTLIQQTPTLHPQRLPSPHPPLQPMtQPPPPSQVSPQPLPQPSLHGQM 275
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 687-1049 5.75e-03

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 41.20  E-value: 5.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  687 AAQAVLTAPYALGPPDPNPSPQPAVTGQSPAPTGARRKIPQSEVQVQGD-RPYSLAVHPALSPQLSEQKNLSL------- 758
Cdd:COG5180    121 GALPAPAAAAALPKAKVTREATSASAGVALAAALLQRSDPILAKDPDGDsASTLPPPAEKLDKVLTEPRDALKdspekld 200

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  759 LPPVPED-----------RGPGHSRAGLEMSLRSATPSLSEEQVSELRENLPKEVRlspklildPKGNVTpaiisAALQQ 827
Cdd:COG5180    201 RPKVEVKdeaqeeppdltGGADHPRPEAASSPKVDPPSTSEARSRPATVDAQPEMR--------PPADAK-----ERRRA 267

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  828 VVHSKSLATPGTALATpsnrgERRLEASMGRPEVTMSRPEVSVMSSSVSKNLK-FKMSPGAPETTRNSQQQLGPEVSASP 906
Cdd:COG5180    268 AIGDTPAAEPPGLPVL-----EAGSEPQSDAPEAETARPIDVKGVASAPPATRpVRPPGGARDPGTPRPGQPTERPAGVP 342

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928577684  907 RASTGSRADNLHLSPPEDRFPVQ---SFPPKSYLSRVSRDSMGKQATGEVAGKGGPEGAKPPPNKQSVVSGQGDKGQLES 983
Cdd:COG5180    343 EAASDAGQPPSAYPPAEEAVPGKpleQGAPRPGSSGGDGAPFQPPNGAPQPGLGRRGAPGPPMGAGDLVQAALDGGGRET 422

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1928577684  984 LSKSS-KLEETSLVPRAGYPMALQSPSCQPRSHSPSCQPRGPS--PSSQSRGQSPSCQPRSQSPLRPLA 1049
Cdd:COG5180    423 ASLGGaAGGAGQGPKADFVPGDAESVSGPAGLADQAGAAASTAmaDFVAPVTDATPVDVADVLGVRPDA 491
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH