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Conserved domains on  [gi|225543226|ref|NP_001139358|]
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rho guanine nucleotide exchange factor TIAM1 isoform 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PH2_Tiam1_2 cd01255
T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, C-terminal domain; ...
1235-1406 3.16e-107

T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, C-terminal domain; Tiam1 activates Rac GTPases to induce membrane ruffling and cell motility while Tiam2 (also called STEF (SIF (still life) and Tiam1 like-exchange factor) contributes to neurite growth. Tiam1/2 are Dbl-family of GEFs that possess a Dbl(DH) domain with a PH domain in tandem. DH-PH domain catalyzes the GDP/GTP exchange reaction in the GTPase cycle and facillitating the switch between inactive GDP-bound and active GTP-bound states. The DH domain of Tiam1 interacts with Switch regions 1 and 2 of Rac1 which blocks magnesium binding and GDP is released. Tiam1/2 possess two PH domains, which are often referred to as PHn and PHc domains. The DH-PH tandem domain is made up of the PHc domain while the PHn is part of a novel N-terminal PHCCEx domain which is made up of the PHn domain, a coiled coil region(CC), and an extra region (Ex). PHCCEx mediates binding to plasma membranes and signalling proteins in the activation of Rac GTPases. The PH domain resembles the beta-spectrin PH domain, suggesting non-canonical phosphatidylinositol binding. CC and Ex form a positively charged surface for protein binding. There are 2 motifs in Tiam1/2-interacting proteins that bind to the PHCCEx domain: Motif-I in CD44, ephrinBs, and the NMDA receptor and Motif-II in Par3 and JIP2. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 269957  Cd Length: 172  Bit Score: 337.82  E-value: 3.16e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226 1235 QKIHEEFGAVFDQLIAEQTGEKKEVADLSMGDLLLHTSVIWLNPPASLGKWKKEPELAAFVFKTAVVLVYKDGSKQKKKL 1314
Cdd:cd01255     1 QKIHEEYGAVFDQLIREQSGTKKEVADLSMGDLLLYGTVEWLNPPSSLGKVKKEPELAVFVFKTAVVLVCKERSKQKKKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226 1315 VGSHRLSIYEEWDPFRFRHMIPTEALQVRALPSADAEANAVCEIVHVKSESEGRPERVFHLCCSSPESRKDFLKSVHSIL 1394
Cdd:cd01255    81 MGSHRKSSYEERDPFRFRHLIPVSALQVRNSNTADTESRCLWELIHTKSELEGRPEKVFQLCCSTPEFKNAFLKVIRSIL 160
                         170
                  ....*....|..
gi 225543226 1395 RDKHRRQLLKTE 1406
Cdd:cd01255   161 REKVRRQSSKTE 172
PH1_Tiam1_2 cd01230
T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, N-terminal domain; ...
432-558 9.60e-83

T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, N-terminal domain; Tiam1 activates Rac GTPases to induce membrane ruffling and cell motility while Tiam2 (also called STEF (SIF (still life) and Tiam1 like-exchange factor) contributes to neurite growth. Tiam1/2 are Dbl-family of GEFs that possess a Dbl(DH) domain with a PH domain in tandem. DH-PH domain catalyzes the GDP/GTP exchange reaction in the GTPase cycle and facillitating the switch between inactive GDP-bound and active GTP-bound states. Tiam1/2 possess two PH domains, which are often referred to as PHn and PHc domains. The DH-PH tandem domain is made up of the PHc domain while the PHn is part of a novel N-terminal PHCCEx domain which is made up of the PHn domain, a coiled coil region(CC), and an extra region (Ex). PHCCEx mediates binding to plasma membranes and signalling proteins in the activation of Rac GTPases. The PH domain resembles the beta-spectrin PH domain, suggesting non-canonical phosphatidylinositol binding. CC and Ex form a positively charged surface for protein binding. There are 2 motifs in Tiam1/2-interacting proteins that bind to the PHCCEx domain: Motif-I in CD44, ephrinBs, and the NMDA receptor and Motif-II in Par3 and JIP2.Neither of these fall in the PHn domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 269937  Cd Length: 127  Bit Score: 266.63  E-value: 9.60e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226  432 GTVRKAGALAVKNFLVHKKNKKVESATRRKWKHYWVSLKGCTLFFYETDGRSGIDHNSVPKHAVWVENSIVQAVPEHPKK 511
Cdd:cd01230     1 GAVRKAGWLSVKNFLVHKKNKKVELATRRKWKKYWVCLKGCTLLFYECDERSGIDENSEPKHALFVEGSIVQAVPEHPKK 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 225543226  512 DFVFCLSNSLGDAFLFQTTSQTELENWITAIHSACAAAVARHHHKED 558
Cdd:cd01230    81 DFVFCLSNSFGDAYLFQATSQTELENWVTAIHSACASAFARQHGKED 127
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
1044-1233 3.86e-51

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


:

Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 178.26  E-value: 3.86e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226   1044 VICELLETERTYVKDLNCLMERYLKPLQKE-TFLTQDELDVLFGNLTEMVEFQVEFLKTLEdgvrlvpdleklEKVDQFK 1122
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKElKLLSPNELETLFGNIEEIYEFHRDFLDELE------------ERIEEWD 68
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226   1123 KVLFSLGGSFLYYADRFKLYSAFCASHTKVPKVLVKAKTDTAFKAFLDAQNPRQQHSS-TLESYLIKPIQRVLKYPLLLR 1201
Cdd:smart00325   69 DSVERIGDVFLKLEEFFKIYSEYCSNHPDALELLKKLKKNPRFQKFLKEIESSPQCRRlTLESLLLKPVQRLTKYPLLLK 148
                           170       180       190
                    ....*....|....*....|....*....|..
gi 225543226   1202 ELFALTDAESEEHYHLDVAIKTMNKVASHINE 1233
Cdd:smart00325  149 ELLKHTPEDHEDREDLKKALKAIKELANQVNE 180
Tiam_CC_Ex super family cl39723
T-lymphoma invasion and metastasis CC-Ex domain; This is the CC and Ex subdomains found in ...
572-669 1.02e-34

T-lymphoma invasion and metastasis CC-Ex domain; This is the CC and Ex subdomains found in PH-CC-Ex globular domain from Tiam1 and Tiam2 proteins (T-lymphoma invasion and metastasis). The CC subdomain forms an antiparallel coiled coil with two long alpha-helices, together with the C-terminal Ex subdomain they form a small globular domain comprising three alpha-helices. The CC subdomain of the Tiam2 PHCCEx domain follows the C-terminal alpha1 helix of the PH pfam00169 subdomain through a four-residue linker.


The actual alignment was detected with superfamily member pfam18385:

Pssm-ID: 408184  Cd Length: 98  Bit Score: 128.33  E-value: 1.02e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226   572 QKIDMDEKMKKMGEMQLSSVTDSKKKKTILDQIFVWEQNLEQFQMDLFRFRCYLASLQGGELPNPKRLLAFASRPTKVAM 651
Cdd:pfam18385    1 QKIDMDEKMKKMGEMQLSSVTDAKKKKTILDQVFLWGENTEQERLSLFLFAQYLAECQGAELPCPTYMLIYASETDKLAS 80
                           90
                   ....*....|....*...
gi 225543226   652 GRLGIFSVSSFHALVAAR 669
Cdd:pfam18385   81 GTLGVARVGTYQSQVAAR 98
RBD pfam02196
Raf-like Ras-binding domain;
766-839 1.60e-18

Raf-like Ras-binding domain;


:

Pssm-ID: 426652  Cd Length: 69  Bit Score: 81.03  E-value: 1.60e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225543226   766 PSWFCLPNNQPALTVVRPGDTARDTLELICKTHQLDHSAHYLRLKFLmenrvQFYIPQPEEDIYELLYKEIEIC 839
Cdd:pfam02196    1 LCRVYLPNGQRTVVQVRPGETVRDALSKLCKKRGLNPEACDVYLVGG-----QKYPLDWDTDSSTLEGEEIRVE 69
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
846-925 2.17e-07

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


:

Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 49.87  E-value: 2.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226  846 IHIEKSDAaaDNYGFLLSSvDEDGIRRLYVNSVKETGLASKKGLKAGDEILEINNRAAGTLNSSMLKDFL--SQPSLGLL 923
Cdd:cd00992     4 VTLRKDPG--GGLGFSLRG-GKDSGGGIFVSRVEPGGPAERGGLRVGDRILEVNGVSVEGLTHEEAVELLknSGDEVTLT 80

                  ..
gi 225543226  924 VR 925
Cdd:cd00992    81 VR 82
 
Name Accession Description Interval E-value
PH2_Tiam1_2 cd01255
T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, C-terminal domain; ...
1235-1406 3.16e-107

T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, C-terminal domain; Tiam1 activates Rac GTPases to induce membrane ruffling and cell motility while Tiam2 (also called STEF (SIF (still life) and Tiam1 like-exchange factor) contributes to neurite growth. Tiam1/2 are Dbl-family of GEFs that possess a Dbl(DH) domain with a PH domain in tandem. DH-PH domain catalyzes the GDP/GTP exchange reaction in the GTPase cycle and facillitating the switch between inactive GDP-bound and active GTP-bound states. The DH domain of Tiam1 interacts with Switch regions 1 and 2 of Rac1 which blocks magnesium binding and GDP is released. Tiam1/2 possess two PH domains, which are often referred to as PHn and PHc domains. The DH-PH tandem domain is made up of the PHc domain while the PHn is part of a novel N-terminal PHCCEx domain which is made up of the PHn domain, a coiled coil region(CC), and an extra region (Ex). PHCCEx mediates binding to plasma membranes and signalling proteins in the activation of Rac GTPases. The PH domain resembles the beta-spectrin PH domain, suggesting non-canonical phosphatidylinositol binding. CC and Ex form a positively charged surface for protein binding. There are 2 motifs in Tiam1/2-interacting proteins that bind to the PHCCEx domain: Motif-I in CD44, ephrinBs, and the NMDA receptor and Motif-II in Par3 and JIP2. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269957  Cd Length: 172  Bit Score: 337.82  E-value: 3.16e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226 1235 QKIHEEFGAVFDQLIAEQTGEKKEVADLSMGDLLLHTSVIWLNPPASLGKWKKEPELAAFVFKTAVVLVYKDGSKQKKKL 1314
Cdd:cd01255     1 QKIHEEYGAVFDQLIREQSGTKKEVADLSMGDLLLYGTVEWLNPPSSLGKVKKEPELAVFVFKTAVVLVCKERSKQKKKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226 1315 VGSHRLSIYEEWDPFRFRHMIPTEALQVRALPSADAEANAVCEIVHVKSESEGRPERVFHLCCSSPESRKDFLKSVHSIL 1394
Cdd:cd01255    81 MGSHRKSSYEERDPFRFRHLIPVSALQVRNSNTADTESRCLWELIHTKSELEGRPEKVFQLCCSTPEFKNAFLKVIRSIL 160
                         170
                  ....*....|..
gi 225543226 1395 RDKHRRQLLKTE 1406
Cdd:cd01255   161 REKVRRQSSKTE 172
PH1_Tiam1_2 cd01230
T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, N-terminal domain; ...
432-558 9.60e-83

T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, N-terminal domain; Tiam1 activates Rac GTPases to induce membrane ruffling and cell motility while Tiam2 (also called STEF (SIF (still life) and Tiam1 like-exchange factor) contributes to neurite growth. Tiam1/2 are Dbl-family of GEFs that possess a Dbl(DH) domain with a PH domain in tandem. DH-PH domain catalyzes the GDP/GTP exchange reaction in the GTPase cycle and facillitating the switch between inactive GDP-bound and active GTP-bound states. Tiam1/2 possess two PH domains, which are often referred to as PHn and PHc domains. The DH-PH tandem domain is made up of the PHc domain while the PHn is part of a novel N-terminal PHCCEx domain which is made up of the PHn domain, a coiled coil region(CC), and an extra region (Ex). PHCCEx mediates binding to plasma membranes and signalling proteins in the activation of Rac GTPases. The PH domain resembles the beta-spectrin PH domain, suggesting non-canonical phosphatidylinositol binding. CC and Ex form a positively charged surface for protein binding. There are 2 motifs in Tiam1/2-interacting proteins that bind to the PHCCEx domain: Motif-I in CD44, ephrinBs, and the NMDA receptor and Motif-II in Par3 and JIP2.Neither of these fall in the PHn domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269937  Cd Length: 127  Bit Score: 266.63  E-value: 9.60e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226  432 GTVRKAGALAVKNFLVHKKNKKVESATRRKWKHYWVSLKGCTLFFYETDGRSGIDHNSVPKHAVWVENSIVQAVPEHPKK 511
Cdd:cd01230     1 GAVRKAGWLSVKNFLVHKKNKKVELATRRKWKKYWVCLKGCTLLFYECDERSGIDENSEPKHALFVEGSIVQAVPEHPKK 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 225543226  512 DFVFCLSNSLGDAFLFQTTSQTELENWITAIHSACAAAVARHHHKED 558
Cdd:cd01230    81 DFVFCLSNSFGDAYLFQATSQTELENWVTAIHSACASAFARQHGKED 127
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
1044-1233 3.86e-51

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 178.26  E-value: 3.86e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226   1044 VICELLETERTYVKDLNCLMERYLKPLQKE-TFLTQDELDVLFGNLTEMVEFQVEFLKTLEdgvrlvpdleklEKVDQFK 1122
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKElKLLSPNELETLFGNIEEIYEFHRDFLDELE------------ERIEEWD 68
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226   1123 KVLFSLGGSFLYYADRFKLYSAFCASHTKVPKVLVKAKTDTAFKAFLDAQNPRQQHSS-TLESYLIKPIQRVLKYPLLLR 1201
Cdd:smart00325   69 DSVERIGDVFLKLEEFFKIYSEYCSNHPDALELLKKLKKNPRFQKFLKEIESSPQCRRlTLESLLLKPVQRLTKYPLLLK 148
                           170       180       190
                    ....*....|....*....|....*....|..
gi 225543226   1202 ELFALTDAESEEHYHLDVAIKTMNKVASHINE 1233
Cdd:smart00325  149 ELLKHTPEDHEDREDLKKALKAIKELANQVNE 180
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
1041-1232 3.36e-50

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 175.95  E-value: 3.36e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226 1041 LRKVICELLETERTYVKDLNCLMERYLKPLQKE-TFLTQDELDVLFGNLTEMVEFQVEFLKTLEdgvrlvpdlEKLEKVD 1119
Cdd:cd00160     1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKElLPLSPEEVELLFGNIEEIYEFHRIFLKSLE---------ERVEEWD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226 1120 QFKkvlFSLGGSFLYYADRFKLYSAFCASHTKVPKVLVK-AKTDTAFKAFLDAQNpRQQHSSTLESYLIKPIQRVLKYPL 1198
Cdd:cd00160    72 KSG---PRIGDVFLKLAPFFKIYSEYCSNHPDALELLKKlKKFNKFFQEFLEKAE-SECGRLKLESLLLKPVQRLTKYPL 147
                         170       180       190
                  ....*....|....*....|....*....|....
gi 225543226 1199 LLRELFALTDAESEEHYHLDVAIKTMNKVASHIN 1232
Cdd:cd00160   148 LLKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
1044-1232 1.80e-41

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 425783 [Multi-domain]  Cd Length: 176  Bit Score: 150.52  E-value: 1.80e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226  1044 VICELLETERTYVKDLNCLMERYLKPLQKETFLTQDELDVLFGNLTEMVEFQVEFLktledgvrlvpdlekLEKVDQFKK 1123
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEIKTIFSNIEEIYELHRQLL---------------LEELLKEWI 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226  1124 VLFSLGGSFLYYADRFKLYSAFCASHTKVPKVLVKA-KTDTAFKAFLDAQNPRQQHSS-TLESYLIKPIQRVLKYPLLLR 1201
Cdd:pfam00621   66 SIQRIGDIFLKFAPGFKVYSTYCSNYPKALELLKKLlKKNPKFRAFLEELEANPECRGlDLNSFLIKPVQRIPRYPLLLK 145
                          170       180       190
                   ....*....|....*....|....*....|.
gi 225543226  1202 ELFALTDAESEEHYHLDVAIKTMNKVASHIN 1232
Cdd:pfam00621  146 ELLKHTPPDHPDYEDLKKALEAIKEVAKQIN 176
Tiam_CC_Ex pfam18385
T-lymphoma invasion and metastasis CC-Ex domain; This is the CC and Ex subdomains found in ...
572-669 1.02e-34

T-lymphoma invasion and metastasis CC-Ex domain; This is the CC and Ex subdomains found in PH-CC-Ex globular domain from Tiam1 and Tiam2 proteins (T-lymphoma invasion and metastasis). The CC subdomain forms an antiparallel coiled coil with two long alpha-helices, together with the C-terminal Ex subdomain they form a small globular domain comprising three alpha-helices. The CC subdomain of the Tiam2 PHCCEx domain follows the C-terminal alpha1 helix of the PH pfam00169 subdomain through a four-residue linker.


Pssm-ID: 408184  Cd Length: 98  Bit Score: 128.33  E-value: 1.02e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226   572 QKIDMDEKMKKMGEMQLSSVTDSKKKKTILDQIFVWEQNLEQFQMDLFRFRCYLASLQGGELPNPKRLLAFASRPTKVAM 651
Cdd:pfam18385    1 QKIDMDEKMKKMGEMQLSSVTDAKKKKTILDQVFLWGENTEQERLSLFLFAQYLAECQGAELPCPTYMLIYASETDKLAS 80
                           90
                   ....*....|....*...
gi 225543226   652 GRLGIFSVSSFHALVAAR 669
Cdd:pfam18385   81 GTLGVARVGTYQSQVAAR 98
RBD pfam02196
Raf-like Ras-binding domain;
766-839 1.60e-18

Raf-like Ras-binding domain;


Pssm-ID: 426652  Cd Length: 69  Bit Score: 81.03  E-value: 1.60e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225543226   766 PSWFCLPNNQPALTVVRPGDTARDTLELICKTHQLDHSAHYLRLKFLmenrvQFYIPQPEEDIYELLYKEIEIC 839
Cdd:pfam02196    1 LCRVYLPNGQRTVVQVRPGETVRDALSKLCKKRGLNPEACDVYLVGG-----QKYPLDWDTDSSTLEGEEIRVE 69
RBD smart00455
Raf-like Ras-binding domain;
766-832 4.51e-18

Raf-like Ras-binding domain;


Pssm-ID: 128731  Cd Length: 70  Bit Score: 79.64  E-value: 4.51e-18
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 225543226    766 PSWFCLPNNQPALTVVRPGDTARDTLELICKTHQLDHSAHYLRL----KFLMENRVQFYIPQpEEDIYELL 832
Cdd:smart00455    1 TCKVHLPDNQRTVVKVRPGKTVRDALAKALKKRGLNPECCVVRLrgekKPLDLNQPISSLDG-QELVVEEL 70
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
452-547 6.71e-14

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574  Cd Length: 102  Bit Score: 69.11  E-value: 6.71e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226    452 KKVESATRRKWKHYWVSLKGCTLFFYETDGRSGIdhnSVPKHAVWVENSIVQAVPE--HPKKDFVFCLSNSLGDAFLFQT 529
Cdd:smart00233    8 YKKSGGGKKSWKKRYFVLFNSTLLYYKSKKDKKS---YKPKGSIDLSGCTVREAPDpdSSKKPHCFEIKTSDRKTLLLQA 84
                            90
                    ....*....|....*...
gi 225543226    530 TSQTELENWITAIHSACA 547
Cdd:smart00233   85 ESEEEREKWVEALRKAIA 102
PH pfam00169
PH domain; PH stands for pleckstrin homology.
452-547 6.20e-13

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 395117 [Multi-domain]  Cd Length: 105  Bit Score: 66.43  E-value: 6.20e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226   452 KKVESATRRKWKHYWVSLKGCTLFFYETDGRsgiDHNSVPKHAVWVENSIVQAV--PEHPKKDFVFCLSNSL---GDAFL 526
Cdd:pfam00169    8 LKKGGGKKKSWKKRYFVLFDGSLLYYKDDKS---KKSKEPKGSISLSGCEVVEVvaSDSPKRKFCFELRTGErtgKRTYL 84
                           90       100
                   ....*....|....*....|.
gi 225543226   527 FQTTSQTELENWITAIHSACA 547
Cdd:pfam00169   85 LQAESEEERKDWIKAIQSAIR 105
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
846-925 2.17e-07

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 49.87  E-value: 2.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226  846 IHIEKSDAaaDNYGFLLSSvDEDGIRRLYVNSVKETGLASKKGLKAGDEILEINNRAAGTLNSSMLKDFL--SQPSLGLL 923
Cdd:cd00992     4 VTLRKDPG--GGLGFSLRG-GKDSGGGIFVSRVEPGGPAERGGLRVGDRILEVNGVSVEGLTHEEAVELLknSGDEVTLT 80

                  ..
gi 225543226  924 VR 925
Cdd:cd00992    81 VR 82
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
842-901 8.70e-07

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: 48.14  E-value: 8.70e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226    842 VTQNIHIEKSDAaadNYGFLLSSVDEDGiRRLYVNSVKETGLASKKGLKAGDEILEINNR 901
Cdd:smart00228    1 EPRLVELEKGGG---GLGFSLVGGKDEG-GGVVVSSVVPGSPAAKAGLRVGDVILEVNGT 56
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
859-901 6.11e-06

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 45.73  E-value: 6.11e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 225543226   859 GFLLSSVDEDGIRRLYVNSVKETGLASKKGLKAGDEILEINNR 901
Cdd:pfam00595   13 GFSLKGGSDQGDPGIFVSEVLPGGAAEAGGLKVGDRILSINGQ 55
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
1033-1266 3.41e-05

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 48.73  E-value: 3.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226 1033 RQLSDADKLRK-VICELLETERTYVKDLNCLMERYLKPLQKETFLTQDE----LDVLFGNLTEMVEFQVEFLKTLEDGVR 1107
Cdd:COG5422   476 ESLPKQEIKRQeAIYEVIYTERDFVKDLEYLRDTWIKPLEESNIIPENArrnfIKHVFANINEIYAVNSKLLKALTNRQC 555
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226 1108 LVPdleklekvdqfkkVLFSLGGSFLYYADRFKLYSAFCASHTKVPKVLVKAKTDTAFKAFLDAQNPRQQHSSTLE--SY 1185
Cdd:COG5422   556 LSP-------------IVNGIADIFLDYVPKFEPFIKYGASQPYAKYEFEREKSVNPNFARFDHEVERLDESRKLEldGY 622
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226 1186 LIKPIQRVLKYPLLLRELFALTDAESEEHYHLDVAIKTMNKVASHINEMQKIHEEFGAVFdqLIAEQTGEKKEVADLSMG 1265
Cdd:COG5422   623 LTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVIDMLREFLSRLNFESGKAENRGDLF--HLNQQLLFKPEYVNLGLN 700

                  .
gi 225543226 1266 D 1266
Cdd:COG5422   701 D 701
PH pfam00169
PH domain; PH stands for pleckstrin homology.
1283-1395 9.11e-03

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 395117 [Multi-domain]  Cd Length: 105  Bit Score: 37.54  E-value: 9.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226  1283 GKWKKepelAAFVFKTAVVLVYKDGSKQKKKlvgshrlsiyeewdpfRFRHMIPTEALQVRALPSADAEANAVC-EIVHv 1361
Cdd:pfam00169   16 KSWKK----RYFVLFDGSLLYYKDDKSKKSK----------------EPKGSISLSGCEVVEVVASDSPKRKFCfELRT- 74
                           90       100       110
                   ....*....|....*....|....*....|....
gi 225543226  1362 kseSEGRPERVFHLCCSSPESRKDFLKSVHSILR 1395
Cdd:pfam00169   75 ---GERTGKRTYLLQAESEEERKDWIKAIQSAIR 105
 
Name Accession Description Interval E-value
PH2_Tiam1_2 cd01255
T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, C-terminal domain; ...
1235-1406 3.16e-107

T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, C-terminal domain; Tiam1 activates Rac GTPases to induce membrane ruffling and cell motility while Tiam2 (also called STEF (SIF (still life) and Tiam1 like-exchange factor) contributes to neurite growth. Tiam1/2 are Dbl-family of GEFs that possess a Dbl(DH) domain with a PH domain in tandem. DH-PH domain catalyzes the GDP/GTP exchange reaction in the GTPase cycle and facillitating the switch between inactive GDP-bound and active GTP-bound states. The DH domain of Tiam1 interacts with Switch regions 1 and 2 of Rac1 which blocks magnesium binding and GDP is released. Tiam1/2 possess two PH domains, which are often referred to as PHn and PHc domains. The DH-PH tandem domain is made up of the PHc domain while the PHn is part of a novel N-terminal PHCCEx domain which is made up of the PHn domain, a coiled coil region(CC), and an extra region (Ex). PHCCEx mediates binding to plasma membranes and signalling proteins in the activation of Rac GTPases. The PH domain resembles the beta-spectrin PH domain, suggesting non-canonical phosphatidylinositol binding. CC and Ex form a positively charged surface for protein binding. There are 2 motifs in Tiam1/2-interacting proteins that bind to the PHCCEx domain: Motif-I in CD44, ephrinBs, and the NMDA receptor and Motif-II in Par3 and JIP2. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269957  Cd Length: 172  Bit Score: 337.82  E-value: 3.16e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226 1235 QKIHEEFGAVFDQLIAEQTGEKKEVADLSMGDLLLHTSVIWLNPPASLGKWKKEPELAAFVFKTAVVLVYKDGSKQKKKL 1314
Cdd:cd01255     1 QKIHEEYGAVFDQLIREQSGTKKEVADLSMGDLLLYGTVEWLNPPSSLGKVKKEPELAVFVFKTAVVLVCKERSKQKKKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226 1315 VGSHRLSIYEEWDPFRFRHMIPTEALQVRALPSADAEANAVCEIVHVKSESEGRPERVFHLCCSSPESRKDFLKSVHSIL 1394
Cdd:cd01255    81 MGSHRKSSYEERDPFRFRHLIPVSALQVRNSNTADTESRCLWELIHTKSELEGRPEKVFQLCCSTPEFKNAFLKVIRSIL 160
                         170
                  ....*....|..
gi 225543226 1395 RDKHRRQLLKTE 1406
Cdd:cd01255   161 REKVRRQSSKTE 172
PH1_Tiam1_2 cd01230
T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, N-terminal domain; ...
432-558 9.60e-83

T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, N-terminal domain; Tiam1 activates Rac GTPases to induce membrane ruffling and cell motility while Tiam2 (also called STEF (SIF (still life) and Tiam1 like-exchange factor) contributes to neurite growth. Tiam1/2 are Dbl-family of GEFs that possess a Dbl(DH) domain with a PH domain in tandem. DH-PH domain catalyzes the GDP/GTP exchange reaction in the GTPase cycle and facillitating the switch between inactive GDP-bound and active GTP-bound states. Tiam1/2 possess two PH domains, which are often referred to as PHn and PHc domains. The DH-PH tandem domain is made up of the PHc domain while the PHn is part of a novel N-terminal PHCCEx domain which is made up of the PHn domain, a coiled coil region(CC), and an extra region (Ex). PHCCEx mediates binding to plasma membranes and signalling proteins in the activation of Rac GTPases. The PH domain resembles the beta-spectrin PH domain, suggesting non-canonical phosphatidylinositol binding. CC and Ex form a positively charged surface for protein binding. There are 2 motifs in Tiam1/2-interacting proteins that bind to the PHCCEx domain: Motif-I in CD44, ephrinBs, and the NMDA receptor and Motif-II in Par3 and JIP2.Neither of these fall in the PHn domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269937  Cd Length: 127  Bit Score: 266.63  E-value: 9.60e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226  432 GTVRKAGALAVKNFLVHKKNKKVESATRRKWKHYWVSLKGCTLFFYETDGRSGIDHNSVPKHAVWVENSIVQAVPEHPKK 511
Cdd:cd01230     1 GAVRKAGWLSVKNFLVHKKNKKVELATRRKWKKYWVCLKGCTLLFYECDERSGIDENSEPKHALFVEGSIVQAVPEHPKK 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 225543226  512 DFVFCLSNSLGDAFLFQTTSQTELENWITAIHSACAAAVARHHHKED 558
Cdd:cd01230    81 DFVFCLSNSFGDAYLFQATSQTELENWVTAIHSACASAFARQHGKED 127
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
1044-1233 3.86e-51

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 178.26  E-value: 3.86e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226   1044 VICELLETERTYVKDLNCLMERYLKPLQKE-TFLTQDELDVLFGNLTEMVEFQVEFLKTLEdgvrlvpdleklEKVDQFK 1122
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKElKLLSPNELETLFGNIEEIYEFHRDFLDELE------------ERIEEWD 68
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226   1123 KVLFSLGGSFLYYADRFKLYSAFCASHTKVPKVLVKAKTDTAFKAFLDAQNPRQQHSS-TLESYLIKPIQRVLKYPLLLR 1201
Cdd:smart00325   69 DSVERIGDVFLKLEEFFKIYSEYCSNHPDALELLKKLKKNPRFQKFLKEIESSPQCRRlTLESLLLKPVQRLTKYPLLLK 148
                           170       180       190
                    ....*....|....*....|....*....|..
gi 225543226   1202 ELFALTDAESEEHYHLDVAIKTMNKVASHINE 1233
Cdd:smart00325  149 ELLKHTPEDHEDREDLKKALKAIKELANQVNE 180
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
1041-1232 3.36e-50

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 175.95  E-value: 3.36e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226 1041 LRKVICELLETERTYVKDLNCLMERYLKPLQKE-TFLTQDELDVLFGNLTEMVEFQVEFLKTLEdgvrlvpdlEKLEKVD 1119
Cdd:cd00160     1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKElLPLSPEEVELLFGNIEEIYEFHRIFLKSLE---------ERVEEWD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226 1120 QFKkvlFSLGGSFLYYADRFKLYSAFCASHTKVPKVLVK-AKTDTAFKAFLDAQNpRQQHSSTLESYLIKPIQRVLKYPL 1198
Cdd:cd00160    72 KSG---PRIGDVFLKLAPFFKIYSEYCSNHPDALELLKKlKKFNKFFQEFLEKAE-SECGRLKLESLLLKPVQRLTKYPL 147
                         170       180       190
                  ....*....|....*....|....*....|....
gi 225543226 1199 LLRELFALTDAESEEHYHLDVAIKTMNKVASHIN 1232
Cdd:cd00160   148 LLKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
1044-1232 1.80e-41

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 425783 [Multi-domain]  Cd Length: 176  Bit Score: 150.52  E-value: 1.80e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226  1044 VICELLETERTYVKDLNCLMERYLKPLQKETFLTQDELDVLFGNLTEMVEFQVEFLktledgvrlvpdlekLEKVDQFKK 1123
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEIKTIFSNIEEIYELHRQLL---------------LEELLKEWI 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226  1124 VLFSLGGSFLYYADRFKLYSAFCASHTKVPKVLVKA-KTDTAFKAFLDAQNPRQQHSS-TLESYLIKPIQRVLKYPLLLR 1201
Cdd:pfam00621   66 SIQRIGDIFLKFAPGFKVYSTYCSNYPKALELLKKLlKKNPKFRAFLEELEANPECRGlDLNSFLIKPVQRIPRYPLLLK 145
                          170       180       190
                   ....*....|....*....|....*....|.
gi 225543226  1202 ELFALTDAESEEHYHLDVAIKTMNKVASHIN 1232
Cdd:pfam00621  146 ELLKHTPPDHPDYEDLKKALEAIKEVAKQIN 176
Tiam_CC_Ex pfam18385
T-lymphoma invasion and metastasis CC-Ex domain; This is the CC and Ex subdomains found in ...
572-669 1.02e-34

T-lymphoma invasion and metastasis CC-Ex domain; This is the CC and Ex subdomains found in PH-CC-Ex globular domain from Tiam1 and Tiam2 proteins (T-lymphoma invasion and metastasis). The CC subdomain forms an antiparallel coiled coil with two long alpha-helices, together with the C-terminal Ex subdomain they form a small globular domain comprising three alpha-helices. The CC subdomain of the Tiam2 PHCCEx domain follows the C-terminal alpha1 helix of the PH pfam00169 subdomain through a four-residue linker.


Pssm-ID: 408184  Cd Length: 98  Bit Score: 128.33  E-value: 1.02e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226   572 QKIDMDEKMKKMGEMQLSSVTDSKKKKTILDQIFVWEQNLEQFQMDLFRFRCYLASLQGGELPNPKRLLAFASRPTKVAM 651
Cdd:pfam18385    1 QKIDMDEKMKKMGEMQLSSVTDAKKKKTILDQVFLWGENTEQERLSLFLFAQYLAECQGAELPCPTYMLIYASETDKLAS 80
                           90
                   ....*....|....*...
gi 225543226   652 GRLGIFSVSSFHALVAAR 669
Cdd:pfam18385   81 GTLGVARVGTYQSQVAAR 98
RBD pfam02196
Raf-like Ras-binding domain;
766-839 1.60e-18

Raf-like Ras-binding domain;


Pssm-ID: 426652  Cd Length: 69  Bit Score: 81.03  E-value: 1.60e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225543226   766 PSWFCLPNNQPALTVVRPGDTARDTLELICKTHQLDHSAHYLRLKFLmenrvQFYIPQPEEDIYELLYKEIEIC 839
Cdd:pfam02196    1 LCRVYLPNGQRTVVQVRPGETVRDALSKLCKKRGLNPEACDVYLVGG-----QKYPLDWDTDSSTLEGEEIRVE 69
RBD smart00455
Raf-like Ras-binding domain;
766-832 4.51e-18

Raf-like Ras-binding domain;


Pssm-ID: 128731  Cd Length: 70  Bit Score: 79.64  E-value: 4.51e-18
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 225543226    766 PSWFCLPNNQPALTVVRPGDTARDTLELICKTHQLDHSAHYLRL----KFLMENRVQFYIPQpEEDIYELL 832
Cdd:smart00455    1 TCKVHLPDNQRTVVKVRPGKTVRDALAKALKKRGLNPECCVVRLrgekKPLDLNQPISSLDG-QELVVEEL 70
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
452-547 6.71e-14

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574  Cd Length: 102  Bit Score: 69.11  E-value: 6.71e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226    452 KKVESATRRKWKHYWVSLKGCTLFFYETDGRSGIdhnSVPKHAVWVENSIVQAVPE--HPKKDFVFCLSNSLGDAFLFQT 529
Cdd:smart00233    8 YKKSGGGKKSWKKRYFVLFNSTLLYYKSKKDKKS---YKPKGSIDLSGCTVREAPDpdSSKKPHCFEIKTSDRKTLLLQA 84
                            90
                    ....*....|....*...
gi 225543226    530 TSQTELENWITAIHSACA 547
Cdd:smart00233   85 ESEEEREKWVEALRKAIA 102
PH pfam00169
PH domain; PH stands for pleckstrin homology.
452-547 6.20e-13

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 395117 [Multi-domain]  Cd Length: 105  Bit Score: 66.43  E-value: 6.20e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226   452 KKVESATRRKWKHYWVSLKGCTLFFYETDGRsgiDHNSVPKHAVWVENSIVQAV--PEHPKKDFVFCLSNSL---GDAFL 526
Cdd:pfam00169    8 LKKGGGKKKSWKKRYFVLFDGSLLYYKDDKS---KKSKEPKGSISLSGCEVVEVvaSDSPKRKFCFELRTGErtgKRTYL 84
                           90       100
                   ....*....|....*....|.
gi 225543226   527 FQTTSQTELENWITAIHSACA 547
Cdd:pfam00169   85 LQAESEEERKDWIKAIQSAIR 105
PH_EFA6 cd13295
Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and ...
443-548 9.93e-11

Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and Sec7 domain containing) is an guanine nucleotide exchange factor for ADP ribosylation factor 6 (ARF6), which is involved in membrane recycling. EFA6 has four structurally related polypeptides: EFA6A, EFA6B, EFA6C and EFA6D. It consists of a N-terminal proline rich region (PR), a SEC7 domain, a PH domain, a PR, a coiled-coil region, and a C-terminal PR. The EFA6 PH domain regulates its association with the plasma membrane. EFA6 activates Arf6 through its Sec7 catalytic domain and modulates this activity through its C-terminal domain, which rearranges the actin cytoskeleton in fibroblastic cell lines. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270107  Cd Length: 126  Bit Score: 60.81  E-value: 9.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226  443 KNFLVHK----KNKKVESATRRKWKHYWVSLKGCTLFFYETDGrsGIDHNSV---PKHAVWVENSIVQAVPEHPKKDFVF 515
Cdd:cd13295     9 KGYLMRKccadPDGKKTPFGKRGWKMFYATLKGLVLYLHKDEY--GCKKALRyesLRNAISVHHSLATKATDYTKKPHVF 86
                          90       100       110
                  ....*....|....*....|....*....|...
gi 225543226  516 CLSNSLGDAFLFQTTSQTELENWITAIHSACAA 548
Cdd:cd13295    87 RLRTADWREYLFQASDTKEMQSWIEAINLVAAA 119
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
452-542 1.58e-10

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 59.09  E-value: 1.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226  452 KKVESATRRKWKHYWVSLKGCTLFFYETDGrsgiDHNSVPKHAVWVENSIVQAVPEHPKKDFVFCLSNSLGDAFLFQTTS 531
Cdd:cd00821     6 LKRGGGGLKSWKKRWFVLFEGVLLYYKSKK----DSSYKPKGSIPLSGILEVEEVSPKERPHCFELVTPDGRTYYLQADS 81
                          90
                  ....*....|.
gi 225543226  532 QTELENWITAI 542
Cdd:cd00821    82 EEERQEWLKAL 92
PH_beta_spectrin cd10571
Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a ...
450-545 1.25e-08

Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a major component of the cytoskeleton underlying cellular membranes. Beta spectrin consists of multiple spectrin repeats followed by a PH domain, which binds to inositol-1,4,5-trisphosphate. The PH domain of beta-spectrin is thought to play a role in the association of spectrin with the plasma membrane of cells. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269975  Cd Length: 106  Bit Score: 54.16  E-value: 1.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226  450 KNKKvesATRRKWKHYWVSLKGCTLFFYEtDGRsgiDHNSVPKHAVWVENSIVQAVPE----HPKKDFVFCLSNSLGDAF 525
Cdd:cd10571    14 GGKK---ASNRSWKNVYTVLRGQELSFYK-DQK---AAKSGITYAAEPPLNLYNAVCEvasdYTKKKHVFRLKLSDGAEF 86
                          90       100
                  ....*....|....*....|
gi 225543226  526 LFQTTSQTELENWITAIHSA 545
Cdd:cd10571    87 LFQAKDEEEMNQWVKKISFA 106
PH_ARHGAP21-like cd01253
ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho ...
435-544 3.23e-08

ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with a RhoGAP domain. These proteins functions as a GTPase-activating protein (GAP) for RHOA and CDC42. ARHGAP21 controls the Arp2/3 complex and F-actin dynamics at the Golgi complex by regulating the activity of the small GTPase Cdc42. It is recruited to the Golgi by to GTPase, ARF1, through its PH domain and its helical motif. It is also required for CTNNA1 recruitment to adherens junctions. ARHGAP21 and it related proteins all contains a PH domain and a RhoGAP domain. Some of the members have additional N-terminal domains including PDZ, SH3, and SPEC. The ARHGAP21 PH domain interacts with the GTPbound forms of both ARF1 and ARF6 ARF-binding domain/ArfBD. The members here include: ARHGAP15, ARHGAP21, and ARHGAP23. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269955  Cd Length: 113  Bit Score: 53.14  E-value: 3.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226  435 RKAGALAVKNFLVHKKNKkvesATRRKWKHYWVSLKGCTLFFYEtDGRSGIDHNSVPKHA---VWVENSIVQAVPEHPKK 511
Cdd:cd01253     1 AREGWLHYKQIVTDKGKR----VSDRSWKQAWAVLRGHSLYLYK-DKREQTPALSIELGSeqrISIRGCIVDIAYSYTKR 75
                          90       100       110
                  ....*....|....*....|....*....|...
gi 225543226  512 DFVFCLSNSLGDAFLFQTTSQTELENWITAIHS 544
Cdd:cd01253    76 KHVFRLTTSDFSEYLFQAEDRDDMLGWIKAIQE 108
PH_9 pfam15410
Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.
459-547 1.48e-07

Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.


Pssm-ID: 434701  Cd Length: 118  Bit Score: 51.66  E-value: 1.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226   459 RRKWKHYWVSLKGCTLFFYETDGRS--------GIDHNSvPKHAVWVENSIVQAVPEHPKKDFVFCLSNSLGDAFLFQTT 530
Cdd:pfam15410   23 KRSWKMVYAVLKDLVLYLYKDEHPPessqfedkKSLKNA-PVGKIRLHHALATPAPDYTKKSHVFRLQTADGAEYLFQTG 101
                           90
                   ....*....|....*..
gi 225543226   531 SQTELENWITAIHSACA 547
Cdd:pfam15410  102 SPKELQEWVDTLNYWAA 118
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
846-925 2.17e-07

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 49.87  E-value: 2.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226  846 IHIEKSDAaaDNYGFLLSSvDEDGIRRLYVNSVKETGLASKKGLKAGDEILEINNRAAGTLNSSMLKDFL--SQPSLGLL 923
Cdd:cd00992     4 VTLRKDPG--GGLGFSLRG-GKDSGGGIFVSRVEPGGPAERGGLRVGDRILEVNGVSVEGLTHEEAVELLknSGDEVTLT 80

                  ..
gi 225543226  924 VR 925
Cdd:cd00992    81 VR 82
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
842-901 8.70e-07

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: 48.14  E-value: 8.70e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226    842 VTQNIHIEKSDAaadNYGFLLSSVDEDGiRRLYVNSVKETGLASKKGLKAGDEILEINNR 901
Cdd:smart00228    1 EPRLVELEKGGG---GLGFSLVGGKDEG-GGVVVSSVVPGSPAAKAGLRVGDVILEVNGT 56
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
859-901 6.11e-06

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 45.73  E-value: 6.11e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 225543226   859 GFLLSSVDEDGIRRLYVNSVKETGLASKKGLKAGDEILEINNR 901
Cdd:pfam00595   13 GFSLKGGSDQGDPGIFVSEVLPGGAAEAGGLKVGDRILSINGQ 55
PH1_PH_fungal cd13298
Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal ...
447-544 6.30e-06

Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal proteins are unknown, but they all contain 2 PH domains. This cd represents the first PH repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270110  Cd Length: 106  Bit Score: 46.46  E-value: 6.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226  447 VHKKNKKvesatRRKWKHYWVSLKGCTLFFY----ETDGRSGIDHNSVpkHAVwvensivqAVPEHPKKDFVFCL-SNSl 521
Cdd:cd13298    12 LLKRSRK-----TKNWKKRWVVLRPCQLSYYkdekEYKLRRVINLSEL--LAV--------APLKDKKRKNVFGIyTPS- 75
                          90       100
                  ....*....|....*....|...
gi 225543226  522 gDAFLFQTTSQTELENWITAIHS 544
Cdd:cd13298    76 -KNLHFRATSEKDANEWVEALRE 97
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
858-909 1.64e-05

PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. Heterodimerization through PDZ-PDZ domain interactions adds to the domain's versatility, and PDZ domain-mediated interactions may be modulated dynamically through target phosphorylation. Some PDZ domains play a role in scaffolding supramolecular complexes. PDZ domains are found in diverse signaling proteins in bacteria, archebacteria, and eurkayotes. This CD contains two distinct structural subgroups with either a N- or C-terminal beta-strand forming the peptide-binding groove base. The circular permutation placing the strand on the N-terminus appears to be found in Eumetazoa only, while the C-terminal variant is found in all three kingdoms of life, and seems to co-occur with protease domains. PDZ domains have been named after PSD95(post synaptic density protein), DlgA (Drosophila disc large tumor suppressor), and ZO1, a mammalian tight junction protein.


Pssm-ID: 238080 [Multi-domain]  Cd Length: 70  Bit Score: 44.22  E-value: 1.64e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 225543226  858 YGFLLSSVDEDGIrrlYVNSVKETGLASKKGLKAGDEILEINNRAAGTLNSS 909
Cdd:cd00136     3 LGFSIRGGTEGGV---VVLSVEPGSPAERAGLQAGDVILAVNGTDVKNLTLE 51
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
1033-1266 3.41e-05

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 48.73  E-value: 3.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226 1033 RQLSDADKLRK-VICELLETERTYVKDLNCLMERYLKPLQKETFLTQDE----LDVLFGNLTEMVEFQVEFLKTLEDGVR 1107
Cdd:COG5422   476 ESLPKQEIKRQeAIYEVIYTERDFVKDLEYLRDTWIKPLEESNIIPENArrnfIKHVFANINEIYAVNSKLLKALTNRQC 555
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226 1108 LVPdleklekvdqfkkVLFSLGGSFLYYADRFKLYSAFCASHTKVPKVLVKAKTDTAFKAFLDAQNPRQQHSSTLE--SY 1185
Cdd:COG5422   556 LSP-------------IVNGIADIFLDYVPKFEPFIKYGASQPYAKYEFEREKSVNPNFARFDHEVERLDESRKLEldGY 622
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226 1186 LIKPIQRVLKYPLLLRELFALTDAESEEHYHLDVAIKTMNKVASHINEMQKIHEEFGAVFdqLIAEQTGEKKEVADLSMG 1265
Cdd:COG5422   623 LTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVIDMLREFLSRLNFESGKAENRGDLF--HLNQQLLFKPEYVNLGLN 700

                  .
gi 225543226 1266 D 1266
Cdd:COG5422   701 D 701
PH1_Pleckstrin_2 cd13301
Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 1; Pleckstrin is a protein found in ...
445-556 8.39e-05

Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 1; Pleckstrin is a protein found in platelets. This name is derived from platelet and leukocyte C kinase substrate and the KSTR string of amino acids. Pleckstrin 2 contains two PH domains and a DEP (dishvelled, egl-10, and pleckstrin) domain. Unlike pleckstrin 1, pleckstrin 2 does not contain obvious sites of PKC phosphorylation. Pleckstrin 2 plays a role in actin rearrangement, large lamellipodia and peripheral ruffle formation, and may help orchestrate cytoskeletal arrangement. The PH domains of pleckstrin 2 are thought to contribute to lamellipodia formation. This cd contains the first PH domain repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270113  Cd Length: 108  Bit Score: 43.13  E-value: 8.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226  445 FLVHKKNKkvesatRRKWKHYWVSLKGCTLFFYEtdGRSgidhNSVPKHAVWVENS-IVQAVPEHPKKDFVFCLSNSLGD 523
Cdd:cd13301     8 YLVKKGHV------VNNWKARWFVLKEDGLEYYK--KKT----DSSPKGMIPLKGCtITSPCLEYGKRPLVFKLTTAKGQ 75
                          90       100       110
                  ....*....|....*....|....*....|...
gi 225543226  524 AFLFQTTSQTELENWITAIHSACAAAVARHHHK 556
Cdd:cd13301    76 EHFFQACSREERDAWAKDITKAITCLEGGKRFA 108
PDZ_2 pfam13180
PDZ domain;
872-906 2.82e-04

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 40.72  E-value: 2.82e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 225543226   872 RLYVNSVKETGLASKKGLKAGDEILEINNRAAGTL 906
Cdd:pfam13180    7 GVVVVSVKSSGPAAKAGLKAGDVILSIDGRKINDL 41
PH_PLEKHJ1 cd13258
Pleckstrin homology domain containing, family J member 1 Pleckstrin homology (PH) domain; ...
452-545 3.16e-04

Pleckstrin homology domain containing, family J member 1 Pleckstrin homology (PH) domain; PLEKHJ1 (also called GNRPX2/Guanine nucleotide-releasing protein x ). It contains a single PH domain. Very little information is known about PLEKHJ1. PLEKHJ1 has been shown to interact with IKBKG (inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase gamma) and KRT33B (keratin 33B). PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270078  Cd Length: 123  Bit Score: 41.93  E-value: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226  452 KKVESATRRkwkhyWVSLKGCTLFFYETDGRSgidHNSVPKHAVWVENSIVQAVPEHPKKdFVFCLSNS--LGDAFLFQT 529
Cdd:cd13258    31 KKSEVFKER-----WFKLKGNLLFYFRTNEFG---DCSEPIGAIVLENCRVQMEEITEKP-FAFSIVFNdePEKKYIFSC 101
                          90
                  ....*....|....*.
gi 225543226  530 TSQTELENWITAIHSA 545
Cdd:cd13258   102 RSEEQCEQWIEALRQA 117
PH_CNK_mammalian-like cd01260
Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; ...
450-545 5.41e-04

Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; CNK family members function as protein scaffolds, regulating the activity and the subcellular localization of RAS activated RAF. There is a single CNK protein present in Drosophila and Caenorhabditis elegans in contrast to mammals which have 3 CNK proteins (CNK1, CNK2, and CNK3). All of the CNK members contain a sterile a motif (SAM), a conserved region in CNK (CRIC) domain, and a PSD-95/DLG-1/ZO-1 (PDZ) domain, and, with the exception of CNK3, a PH domain. A CNK2 splice variant CNK2A also has a PDZ domain-binding motif at its C terminus and Drosophila CNK (D-CNK) also has a domain known as the Raf-interacting region (RIR) that mediates binding of the Drosophila Raf kinase. This cd contains CNKs from mammals, chickens, amphibians, fish, and crustacea. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269962  Cd Length: 114  Bit Score: 41.24  E-value: 5.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226  450 KNKKVESATRRKWKHYWVSLKGCTLFFYETDGRSGID-HNSVPkhavwvENSIVQAvpEHPKKDFVFCLSNSLGDAFLFQ 528
Cdd:cd01260    21 KKKEAKSFFGQKWKKYWFVLKGSSLYWYSNQQDEKAEgFINLP------DFKIERA--SECKKKYAFKACHPKIKTFYFA 92
                          90
                  ....*....|....*..
gi 225543226  529 TTSQTELENWITAIHSA 545
Cdd:cd01260    93 AENLDDMNKWLSKLNMA 109
PH_RhoGAP2 cd13378
Rho GTPase activating protein 2 Pleckstrin homology (PH) domain; RhoGAP2 (also called RhoGap22 ...
453-542 6.75e-04

Rho GTPase activating protein 2 Pleckstrin homology (PH) domain; RhoGAP2 (also called RhoGap22 or ArhGap22) are involved in cell polarity, cell morphology and cytoskeletal organization. They activate a GTPase belonging to the RAS superfamily of small GTP-binding proteins. The encoded protein is insulin-responsive, is dependent on the kinase Akt, and requires the Akt-dependent 14-3-3 binding protein which binds sequentially to two serine residues resulting in regulation of cell motility. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 241529  Cd Length: 116  Bit Score: 41.09  E-value: 6.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226  453 KVESATRRKWKHYWVSLKGCTLFFYETDgrsgidHNSVPKHAVWVENSIVQAV---PEHPKKDFVFCLSNSLGD------ 523
Cdd:cd13378    10 KKQRSIMKNWQQRWFVLRGDQLFYYKDE------EETKPQGCISLQGSQVNELppnPEEPGKHLFEILPGGAGDrekvpm 83
                          90       100
                  ....*....|....*....|..
gi 225543226  524 ---AFLFQTTSQTELENWITAI 542
Cdd:cd13378    84 nheAFLLMANSQSDMEDWVKAI 105
PH_ARHGAP9-like cd13233
Beta-spectrin pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like ...
451-545 9.32e-04

Beta-spectrin pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with RhoGAP domain. The ARHGAP members here all have a PH domain upstream of their C-terminal RhoGAP domain. Some have additional N-terminal SH3 and WW domains. The members here include: ARHGAP9, ARHGAP12, ARHGAP15, and ARHGAP27. ARHGAP27 and ARHGAP12 shared the common-domain structure, consisting of SH3, WW, PH, and RhoGAP domains. The PH domain of ArhGAP9 employs a non-canonical phosphoinositide binding mechanism, a variation of the spectrin- Ins(4,5)P2-binding mode, that gives rise to a unique PI binding profile, namely a preference for both PI(4,5)P2 and the PI 3-kinase products PI(3,4,5)P3 and PI(3,4)P2. This lipid binding mechanism is also employed by the PH domain of Tiam1 and Slm1. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270053  Cd Length: 110  Bit Score: 40.34  E-value: 9.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226  451 NKKVesatRRKWKHYWVSLKGCTLFFYEtDGRSGIDHN---SVPKHAVWVENSIVQAVPEHPKKDFVFCLSNSLGDAFLF 527
Cdd:cd13233    15 GKKL----RKNWSTSWVVLTSSHLLFYK-DAKSAAKSGnpySKPESSVDLRGASIEWAKEKSSRKNVFQISTVTGTEFLL 89
                          90
                  ....*....|....*...
gi 225543226  528 QTTSQTELENWITAIHSA 545
Cdd:cd13233    90 QSDNDTEIREWFDAIKAV 107
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
874-907 3.32e-03

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


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 37.12  E-value: 3.32e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 225543226   874 YVNSVKETGLASKKGLKAGDEILEINNRAAGTLN 907
Cdd:pfam17820    1 VVTAVVPGSPAERAGLRVGDVILAVNGKPVRSLE 34
PH_RalGPS1_2 cd13310
Ral GEF with PH domain and SH3 binding motif 1 and 2 Pleckstrin homology (PH) domain; RalGPS1 ...
462-547 3.57e-03

Ral GEF with PH domain and SH3 binding motif 1 and 2 Pleckstrin homology (PH) domain; RalGPS1 (also called Ral GEF with PH domain and SH3 binding motif 1;RALGEF2/ Ral guanine nucleotide exchange factor 2; RalA exchange factor RalGPS1; Ral guanine nucleotide exchange factor RalGPS1A2; ras-specific guanine nucleotide-releasing factor RalGPS1) and RalGPS2 (also called Ral GEF with PH domain and SH3 binding motif 2; Ral-A exchange factor RalGPS2; ras-specific guanine nucleotide-releasing factor RalGPS22). They activate small GTPase Ral proteins such as RalA and RalB by stimulating the exchange of Ral bound GDP to GTP, thereby regulating various downstream cellular processes. Structurally they contain an N-terminal Cdc25-like catalytic domain, followed by a PXXP motif and a C-terminal PH domain. The Cdc25-like catalytic domain interacts with Ral and its PH domain ensures the correct membrane localization. Its PXXP motif is thought to interact with the SH3 domain of Grb2. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270120  Cd Length: 116  Bit Score: 38.78  E-value: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226  462 WKHYWVSLKGCTLFFYETDGRSGIDHN---SVPKHAVWVENSIVqAVPEHPKKDFVFCLSNS-LGDAFLFQTTSQTELEN 537
Cdd:cd13310    23 WQRYWVQLWGTSLVYYAPKSLKGTERSdfkSEPCKIVSISGWMV-VLGDDPEHPDSFQLTDPeKGNVYKFRAGSRSNALL 101
                          90
                  ....*....|
gi 225543226  538 WITAIHSACA 547
Cdd:cd13310   102 WLKHLKDACK 111
PDZ_serine_protease cd00987
PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins ...
873-902 4.81e-03

PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins involved in heat-shock response, chaperone function, and apoptosis. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238487 [Multi-domain]  Cd Length: 90  Bit Score: 37.62  E-value: 4.81e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 225543226  873 LYVNSVKETGLASKKGLKAGDEILEINNRA 902
Cdd:cd00987    26 VLVASVDPGSPAAKAGLKPGDVILAVNGKP 55
PH-GRAM1_AGT26 cd13215
Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, ...
431-542 6.05e-03

Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, repeat 1; ATG26 (also called UGT51/UDP-glycosyltransferase 51), a member of the glycosyltransferase 28 family, resulting in the biosynthesis of sterol glucoside. ATG26 in decane metabolism and autophagy. There are 32 known autophagy-related (ATG) proteins, 17 are components of the core autophagic machinery essential for all autophagy-related pathways and 15 are the additional components required only for certain pathways or species. The core autophagic machinery includes 1) the ATG9 cycling system (ATG1, ATG2, ATG9, ATG13, ATG18, and ATG27), 2) the phosphatidylinositol 3-kinase complex (ATG6/VPS30, ATG14, VPS15, and ATG34), and 3) the ubiquitin-like protein system (ATG3, ATG4, ATG5, ATG7, ATG8, ATG10, ATG12, and ATG16). Less is known about how the core machinery is adapted or modulated with additional components to accommodate the nonselective sequestration of bulk cytosol (autophagosome formation) or selective sequestration of specific cargos (Cvt vesicle, pexophagosome, or bacteria-containing autophagosome formation). The pexophagosome-specific additions include the ATG30-ATG11-ATG17 receptor-adaptors complex, the coiled-coil protein ATG25, and the sterol glucosyltransferase ATG26. ATG26 is necessary for the degradation of medium peroxisomes. It contains 2 GRAM domains and a single PH domain. PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. PH domains also have diverse functions. They are often involved in targeting proteins to the plasma membrane, but few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275402  Cd Length: 116  Bit Score: 38.37  E-value: 6.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226  431 QGTVRKAGALavknflvHKKNKKvesatRRKWKHYWVSLKGCTLFFYETDG-----RSGIDHNSVPKhavwvensiVQAV 505
Cdd:cd13215    18 SGAVIKSGYL-------SKRSKR-----TLRYTRYWFVLKGDTLSWYNSSTdlyfpAGTIDLRYATS---------IELS 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 225543226  506 PEHPKKDFVFCLSNSlGDAFLFQTTSQTELENWITAI 542
Cdd:cd13215    77 KSNGEATTSFKIVTN-SRTYKFKADSETSADEWVKAL 112
PH pfam00169
PH domain; PH stands for pleckstrin homology.
1283-1395 9.11e-03

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 395117 [Multi-domain]  Cd Length: 105  Bit Score: 37.54  E-value: 9.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543226  1283 GKWKKepelAAFVFKTAVVLVYKDGSKQKKKlvgshrlsiyeewdpfRFRHMIPTEALQVRALPSADAEANAVC-EIVHv 1361
Cdd:pfam00169   16 KSWKK----RYFVLFDGSLLYYKDDKSKKSK----------------EPKGSISLSGCEVVEVVASDSPKRKFCfELRT- 74
                           90       100       110
                   ....*....|....*....|....*....|....
gi 225543226  1362 kseSEGRPERVFHLCCSSPESRKDFLKSVHSILR 1395
Cdd:pfam00169   75 ---GERTGKRTYLLQAESEEERKDWIKAIQSAIR 105
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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