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Conserved domains on  [gi|196001959|ref|XP_002110847|]
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uncharacterized protein TRIADDRAFT_22773 [Trichoplax adhaerens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 893-1071 5.28e-73

RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.


:

Pssm-ID: 459872  Cd Length: 179  Bit Score: 239.80  E-value: 5.28e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959   893 EMAEQMCLLHYYIYAAIGSGELLQKSWMKGDRDTKAPNVLRAIHYFNHTSRLVATEILNRSQPAARAAVIEKWAQIANNC 972
Cdd:pfam00617    1 ELARQLTLIEFELFRKIKPRELLGSAWSKKDKKENSPNIEAMIARFNKLSNWVASEILSEEDLKKRAKVIKKFIKIAEHC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959   973 RCMNNFNTVMAIVAALTNSSIHRLKKTWEKVSKQEKLIIKRLEELASADRRFKNVKEALRCCQPPCVPYLGLYLSDLTFM 1052
Cdd:pfam00617   81 RELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASPPCIPFLGLYLTDLTFI 160

                          170
                   ....*....|....*....
gi 196001959  1053 EEANPSETDDQLINFSKLR 1071
Cdd:pfam00617  161 EEGNPDFLEGGLINFEKRR 179
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 136-317 1.04e-29

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: 116.63  E-value: 1.04e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959    136 IFFQLYESERNYVQQMSILVSCYLRPLKMAASSkkpsVTHDEVNSIFLNCETILFLHQIILKILHSRIENWPTLQ--IGN 213
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKL----LSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSVerIGD 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959    214 LLDVFLPTLAIYQEYVRNHHYSLQVLAECKIRPTFNKLLCQLEQKPACLGAKLENYLTYPMHEVPNIIVTLHKLLAFTPP 293
Cdd:smart00325   77 VFLKLEEFFKIYSEYCSNHPDALELLKKLKKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLLLKELLKHTPE 156

                           170       180
                    ....*....|....*....|....
gi 196001959    294 GHVDRKSLENAQGVLNEIARVMQD 317
Cdd:smart00325  157 DHEDREDLKKALKAIKELANQVNE 180
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 526-575 6.97e-07

RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small GTPases appear to possess this motif/domain N-terminal to the RasGef (Cdc25-like) domain.


:

Pssm-ID: 459873  Cd Length: 104  Bit Score: 48.84  E-value: 6.97e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 196001959   526 QIRHASTTKLIQRLLDLRF-LSVDYLNVFLLTHHVFTTSEHVIDELLQFYN 575
Cdd:pfam00618    1 QVKAGTLEKLVEYLTSTRImLDDSFLSTFLLTYRSFTTPAELLELLIERYN 51
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 388-481 3.82e-03

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 [Multi-domain]  Cd Length: 102  Bit Score: 37.91  E-value: 3.82e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959    388 RLCFLFTKHLIITSHLQSGRLHIVKecGKIQLSEAILEEELDDDGKilyvfnRSKFLqFKLTinpsNSTPYSVVFAAATE 467
Cdd:smart00233   21 RYFVLFNSTLLYYKSKKDKKSYKPK--GSIDLSGCTVREAPDPDSS------KKPHC-FEIK----TSDRKTLLLQAESE 87

                            90
                    ....*....|....
gi 196001959    468 REKAAWTTDIGQCI 481
Cdd:smart00233   88 EEREKWVEALRKAI 101
 
Name Accession Description Interval E-value
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 893-1071 5.28e-73

RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.


Pssm-ID: 459872  Cd Length: 179  Bit Score: 239.80  E-value: 5.28e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959   893 EMAEQMCLLHYYIYAAIGSGELLQKSWMKGDRDTKAPNVLRAIHYFNHTSRLVATEILNRSQPAARAAVIEKWAQIANNC 972
Cdd:pfam00617    1 ELARQLTLIEFELFRKIKPRELLGSAWSKKDKKENSPNIEAMIARFNKLSNWVASEILSEEDLKKRAKVIKKFIKIAEHC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959   973 RCMNNFNTVMAIVAALTNSSIHRLKKTWEKVSKQEKLIIKRLEELASADRRFKNVKEALRCCQPPCVPYLGLYLSDLTFM 1052
Cdd:pfam00617   81 RELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASPPCIPFLGLYLTDLTFI 160

                          170
                   ....*....|....*....
gi 196001959  1053 EEANPSETDDQLINFSKLR 1071
Cdd:pfam00617  161 EEGNPDFLEGGLINFEKRR 179
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
893-1122 2.63e-71

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 237.53  E-value: 2.63e-71
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959    893 EMAEQMCLLHYYIYAAIGSGELLQKSWMKGDRDTKAP-NVLRAIHYFNHTSRLVATEILNRSQPAARAAVIEKWAQIANN 971
Cdd:smart00147    8 ELAEQLTLLDFELFRKIDPSELLGSVWGKRSKKSPSPlNLEAFIRRFNEVSNWVATEILKQTTPKDRAELLSKFIQVAKH 87

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959    972 CRCMNNFNTVMAIVAALTNSSIHRLKKTWEKVSKQEKLIIKRLEELASADRRFKNVKEALRCC-QPPCVPYLGLYLSDLT 1050
Cdd:smart00147   88 CRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCnLPPCIPFLGVLLKDLT 167

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 196001959   1051 FMEEANPSETDDQLINFSKLRMIAHLIEEIRIYQGTPYRMRCLPKVMKYILNAKPINCDKQ--LFELSLQLEPR 1122
Cdd:smart00147  168 FIDEGNPDFLENGLVNFEKRRQIAEILREIRQLQSQPYNLRPNRSDIQSLLQQLLDHLDEEeeLYQLSLKIEPR 241
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 886-1118 3.05e-67

Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of the Ras superfamily function as molecular switches in fundamental events such as signal transduction, cytoskeleton dynamics and intracellular trafficking. Guanine-nucleotide-exchange factors (GEFs) positively regulate these GTP-binding proteins in response to a variety of signals. GEFs catalyze the dissociation of GDP from the inactive GTP-binding proteins. GTP can then bind and induce structural changes that allow interaction with effectors.


Pssm-ID: 238087 [Multi-domain]  Cd Length: 237  Bit Score: 225.98  E-value: 3.05e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959  886 LDEIPVLEMAEQMCLLHYYIYAAIGSGELLQKSWMKGDR-DTKAPNVLRAIHYFNHTSRLVATEILNRSQPAARAAVIEK 964
Cdd:cd00155     1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKnIHLSPNLERFIERFNNLSNWVASEILLCTNPKKRARLLSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959  965 WAQIANNCRCMNNFNTVMAIVAALTNSSIHRLKKTWEKVSKQEKLIIKRLEELASADRRFKNVKEALRCC--QPPCVPYL 1042
Cdd:cd00155    81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVgpNPPCVPFL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 196001959 1043 GLYLSDLTFMEEANPSETDDQLINFSKLRMIAHLIEEIRIYQGTPYRMRCLPKVMKYILNAKPINCDKQ-LFELSLQ 1118
Cdd:cd00155   161 GVYLKDLTFLHEGNPDFLEGNLVNFEKRRKIAEILREIRQLQSNSYELNRDEDILAFLWKLLELILNEDeLYELSLE 237
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 136-317 1.04e-29

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: 116.63  E-value: 1.04e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959    136 IFFQLYESERNYVQQMSILVSCYLRPLKMAASSkkpsVTHDEVNSIFLNCETILFLHQIILKILHSRIENWPTLQ--IGN 213
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKL----LSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSVerIGD 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959    214 LLDVFLPTLAIYQEYVRNHHYSLQVLAECKIRPTFNKLLCQLEQKPACLGAKLENYLTYPMHEVPNIIVTLHKLLAFTPP 293
Cdd:smart00325   77 VFLKLEEFFKIYSEYCSNHPDALELLKKLKKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLLLKELLKHTPE 156

                           170       180
                    ....*....|....*....|....
gi 196001959    294 GHVDRKSLENAQGVLNEIARVMQD 317
Cdd:smart00325  157 DHEDREDLKKALKAIKELANQVNE 180
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 133-313 8.03e-28

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: 111.24  E-value: 8.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959  133 RNGIFFQLYESERNYVQQMSILVSCYLRPLKMAASSkkpsVTHDEVNSIFLNCETILFLHQIILKILHSRIENW--PTLQ 210
Cdd:cd00160     1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLP----LSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWdkSGPR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959  211 IGNLLDVFLPTLAIYQEYVRNHHYSLQVLAECKirpTFNKLL--CQLEQKPACLGAKLENYLTYPMHEVPNIIVTLHKLL 288
Cdd:cd00160    77 IGDVFLKLAPFFKIYSEYCSNHPDALELLKKLK---KFNKFFqeFLEKAESECGRLKLESLLLKPVQRLTKYPLLLKELL 153

                         170       180
                  ....*....|....*....|....*
gi 196001959  289 AFTPPGHVDRKSLENAQGVLNEIAR 313
Cdd:cd00160   154 KHTPDGHEDREDLKKALEAIKEVAS 178
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 136-313 3.43e-27

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: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 109.31  E-value: 3.43e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959   136 IFFQLYESERNYVQQMSILVSCYLRPLkmaasSKKPSVTHDEVNSIFLNCETILFLHQIILkiLHSRIENWPTLQ-IGNL 214
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPN-----SKPLSESEEEIKTIFSNIEEIYELHRQLL--LEELLKEWISIQrIGDI 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959   215 LDVFLPTLAIYQEYVRNHHYSLQVLAECKIR-PTFNKLLCQLEQKPACLGAKLENYLTYPMHEVPNIIVTLHKLLAFTPP 293
Cdd:pfam00621   74 FLKFAPGFKVYSTYCSNYPKALKLLKKLLKKnPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPP 153

                          170       180
                   ....*....|....*....|
gi 196001959   294 GHVDRKSLENAQGVLNEIAR 313
Cdd:pfam00621  154 DHPDYEDLKKALEAIKEVAK 173
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 526-575 6.97e-07

RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small GTPases appear to possess this motif/domain N-terminal to the RasGef (Cdc25-like) domain.


Pssm-ID: 459873  Cd Length: 104  Bit Score: 48.84  E-value: 6.97e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 196001959   526 QIRHASTTKLIQRLLDLRF-LSVDYLNVFLLTHHVFTTSEHVIDELLQFYN 575
Cdd:pfam00618    1 QVKAGTLEKLVEYLTSTRImLDDSFLSTFLLTYRSFTTPAELLELLIERYN 51
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 523-594 1.06e-04

Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small GTPases appear to possess this domain N-terminal to the RasGef (Cdc25-like) domain. The recent crystal structureof Sos shows that this domain is alpha-helical and plays a "purely structural role" (Nature 394, 337-343).


Pssm-ID: 214571  Cd Length: 127  Bit Score: 43.09  E-value: 1.06e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 196001959    523 KVPQIRHASTTKLIQRLLD-LRFLSVDYLNVFLLTHHVFTTSEHVIDELLQFYNSWKGNSNGIDKHNFEYISD 594
Cdd:smart00229    1 DGGLIKGGTLEALIEHLTEaFDKADPSFVETFLLTYRSFITTQELLQLLLYRYNAIPPESWVEEKVNPRRVKN 73
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 534-575 3.23e-04

Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also called REM domain (Ras exchanger motif). This domain is common in nucleotide exchange factors for Ras-like small GTPases and is typically found immediately N-terminal to the RasGef (Cdc25-like) domain. REM contacts the GTPase and is assumed to participate in the catalytic activity of the exchange factor. Proteins with the REM domain include Sos1 and Sos2, which relay signals from tyrosine-kinase mediated signalling to Ras, RasGRP1-4, RasGRF1,2, CNrasGEF, and RAP-specific nucleotide exchange factors, to name a few.


Pssm-ID: 100121  Cd Length: 122  Bit Score: 41.63  E-value: 3.23e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 196001959  534 KLIQRLLD-LRFLSVDYLNVFLLTHHVFTTSEHVIDELLQFYN 575
Cdd:cd06224     4 ALIEHLTStFDMPDPSFVSTFLLTYRSFTTPTELLEKLIERYE 46
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 388-481 3.82e-03

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 [Multi-domain]  Cd Length: 102  Bit Score: 37.91  E-value: 3.82e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959    388 RLCFLFTKHLIITSHLQSGRLHIVKecGKIQLSEAILEEELDDDGKilyvfnRSKFLqFKLTinpsNSTPYSVVFAAATE 467
Cdd:smart00233   21 RYFVLFNSTLLYYKSKKDKKSYKPK--GSIDLSGCTVREAPDPDSS------KKPHC-FEIK----TSDRKTLLLQAESE 87

                            90
                    ....*....|....
gi 196001959    468 REKAAWTTDIGQCI 481
Cdd:smart00233   88 EEREKWVEALRKAI 101
PH1_FARP1-like cd01220
FERM, RhoGEF and pleckstrin domain-containing protein 1 and related proteins Pleckstrin ...
 388-482 3.93e-03

FERM, RhoGEF and pleckstrin domain-containing protein 1 and related proteins Pleckstrin Homology (PH) domain, repeat 1; Members here include FARP1 (also called Chondrocyte-derived ezrin-like protein; PH domain-containing family C member 2), FARP2 (also called FIR/FERM domain including RhoGEF; FGD1-related Cdc42-GEF/FRG), and FARP6 (also called Zinc finger FYVE domain-containing protein 24). They are members of the Dbl family guanine nucleotide exchange factors (GEFs) which are upstream positive regulators of Rho GTPases. Little is known about FARP1 and FARP6, though FARP1 has increased expression in differentiated chondrocytes. FARP2 is thought to regulate neurite remodeling by mediating the signaling pathways from membrane proteins to Rac. It is found in brain, lung, and testis, as well as embryonic hippocampal and cortical neurons. FARP1 and FARP2 are composed of a N-terminal FERM domain, a proline-rich (PR) domain, Dbl-homology (DH), and two C-terminal PH domains. FARP6 is composed of Dbl-homology (DH), and two C-terminal PH domains separated by a FYVE domain. This hierarchy contains 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: 269928  Cd Length: 109  Bit Score: 38.07  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959  388 RLCFLFTKHLIITSHLQSGRLHIvKECGKIQLsEAILEEELDDDGKILYVFnrskflqfklTINPSNStpySVVFAAATE 467
Cdd:cd01220    25 RMFFLFSDVLLYTSRSPTPSLQF-KVHGQLPL-RGLMVEESEPEWGVAHCF----------TIYGGNR---ALTVAASSE 89

                          90
                  ....*....|....*
gi 196001959  468 REKAAWTTDIGQCIE 482
Cdd:cd01220    90 EEKERWLEDLQRAID 104
 
Name Accession Description Interval E-value
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 893-1071 5.28e-73

RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.


Pssm-ID: 459872  Cd Length: 179  Bit Score: 239.80  E-value: 5.28e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959   893 EMAEQMCLLHYYIYAAIGSGELLQKSWMKGDRDTKAPNVLRAIHYFNHTSRLVATEILNRSQPAARAAVIEKWAQIANNC 972
Cdd:pfam00617    1 ELARQLTLIEFELFRKIKPRELLGSAWSKKDKKENSPNIEAMIARFNKLSNWVASEILSEEDLKKRAKVIKKFIKIAEHC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959   973 RCMNNFNTVMAIVAALTNSSIHRLKKTWEKVSKQEKLIIKRLEELASADRRFKNVKEALRCCQPPCVPYLGLYLSDLTFM 1052
Cdd:pfam00617   81 RELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASPPCIPFLGLYLTDLTFI 160

                          170
                   ....*....|....*....
gi 196001959  1053 EEANPSETDDQLINFSKLR 1071
Cdd:pfam00617  161 EEGNPDFLEGGLINFEKRR 179
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
893-1122 2.63e-71

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 237.53  E-value: 2.63e-71
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959    893 EMAEQMCLLHYYIYAAIGSGELLQKSWMKGDRDTKAP-NVLRAIHYFNHTSRLVATEILNRSQPAARAAVIEKWAQIANN 971
Cdd:smart00147    8 ELAEQLTLLDFELFRKIDPSELLGSVWGKRSKKSPSPlNLEAFIRRFNEVSNWVATEILKQTTPKDRAELLSKFIQVAKH 87

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959    972 CRCMNNFNTVMAIVAALTNSSIHRLKKTWEKVSKQEKLIIKRLEELASADRRFKNVKEALRCC-QPPCVPYLGLYLSDLT 1050
Cdd:smart00147   88 CRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCnLPPCIPFLGVLLKDLT 167

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 196001959   1051 FMEEANPSETDDQLINFSKLRMIAHLIEEIRIYQGTPYRMRCLPKVMKYILNAKPINCDKQ--LFELSLQLEPR 1122
Cdd:smart00147  168 FIDEGNPDFLENGLVNFEKRRQIAEILREIRQLQSQPYNLRPNRSDIQSLLQQLLDHLDEEeeLYQLSLKIEPR 241
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 886-1118 3.05e-67

Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of the Ras superfamily function as molecular switches in fundamental events such as signal transduction, cytoskeleton dynamics and intracellular trafficking. Guanine-nucleotide-exchange factors (GEFs) positively regulate these GTP-binding proteins in response to a variety of signals. GEFs catalyze the dissociation of GDP from the inactive GTP-binding proteins. GTP can then bind and induce structural changes that allow interaction with effectors.


Pssm-ID: 238087 [Multi-domain]  Cd Length: 237  Bit Score: 225.98  E-value: 3.05e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959  886 LDEIPVLEMAEQMCLLHYYIYAAIGSGELLQKSWMKGDR-DTKAPNVLRAIHYFNHTSRLVATEILNRSQPAARAAVIEK 964
Cdd:cd00155     1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKnIHLSPNLERFIERFNNLSNWVASEILLCTNPKKRARLLSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959  965 WAQIANNCRCMNNFNTVMAIVAALTNSSIHRLKKTWEKVSKQEKLIIKRLEELASADRRFKNVKEALRCC--QPPCVPYL 1042
Cdd:cd00155    81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVgpNPPCVPFL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 196001959 1043 GLYLSDLTFMEEANPSETDDQLINFSKLRMIAHLIEEIRIYQGTPYRMRCLPKVMKYILNAKPINCDKQ-LFELSLQ 1118
Cdd:cd00155   161 GVYLKDLTFLHEGNPDFLEGNLVNFEKRRKIAEILREIRQLQSNSYELNRDEDILAFLWKLLELILNEDeLYELSLE 237
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 136-317 1.04e-29

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: 116.63  E-value: 1.04e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959    136 IFFQLYESERNYVQQMSILVSCYLRPLKMAASSkkpsVTHDEVNSIFLNCETILFLHQIILKILHSRIENWPTLQ--IGN 213
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKL----LSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSVerIGD 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959    214 LLDVFLPTLAIYQEYVRNHHYSLQVLAECKIRPTFNKLLCQLEQKPACLGAKLENYLTYPMHEVPNIIVTLHKLLAFTPP 293
Cdd:smart00325   77 VFLKLEEFFKIYSEYCSNHPDALELLKKLKKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLLLKELLKHTPE 156

                           170       180
                    ....*....|....*....|....
gi 196001959    294 GHVDRKSLENAQGVLNEIARVMQD 317
Cdd:smart00325  157 DHEDREDLKKALKAIKELANQVNE 180
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 133-313 8.03e-28

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: 111.24  E-value: 8.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959  133 RNGIFFQLYESERNYVQQMSILVSCYLRPLKMAASSkkpsVTHDEVNSIFLNCETILFLHQIILKILHSRIENW--PTLQ 210
Cdd:cd00160     1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLP----LSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWdkSGPR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959  211 IGNLLDVFLPTLAIYQEYVRNHHYSLQVLAECKirpTFNKLL--CQLEQKPACLGAKLENYLTYPMHEVPNIIVTLHKLL 288
Cdd:cd00160    77 IGDVFLKLAPFFKIYSEYCSNHPDALELLKKLK---KFNKFFqeFLEKAESECGRLKLESLLLKPVQRLTKYPLLLKELL 153

                         170       180
                  ....*....|....*....|....*
gi 196001959  289 AFTPPGHVDRKSLENAQGVLNEIAR 313
Cdd:cd00160   154 KHTPDGHEDREDLKKALEAIKEVAS 178
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 136-313 3.43e-27

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: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 109.31  E-value: 3.43e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959   136 IFFQLYESERNYVQQMSILVSCYLRPLkmaasSKKPSVTHDEVNSIFLNCETILFLHQIILkiLHSRIENWPTLQ-IGNL 214
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPN-----SKPLSESEEEIKTIFSNIEEIYELHRQLL--LEELLKEWISIQrIGDI 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959   215 LDVFLPTLAIYQEYVRNHHYSLQVLAECKIR-PTFNKLLCQLEQKPACLGAKLENYLTYPMHEVPNIIVTLHKLLAFTPP 293
Cdd:pfam00621   74 FLKFAPGFKVYSTYCSNYPKALKLLKKLLKKnPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPP 153

                          170       180
                   ....*....|....*....|
gi 196001959   294 GHVDRKSLENAQGVLNEIAR 313
Cdd:pfam00621  154 DHPDYEDLKKALEAIKEVAK 173
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 526-575 6.97e-07

RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small GTPases appear to possess this motif/domain N-terminal to the RasGef (Cdc25-like) domain.


Pssm-ID: 459873  Cd Length: 104  Bit Score: 48.84  E-value: 6.97e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 196001959   526 QIRHASTTKLIQRLLDLRF-LSVDYLNVFLLTHHVFTTSEHVIDELLQFYN 575
Cdd:pfam00618    1 QVKAGTLEKLVEYLTSTRImLDDSFLSTFLLTYRSFTTPAELLELLIERYN 51
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 523-594 1.06e-04

Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small GTPases appear to possess this domain N-terminal to the RasGef (Cdc25-like) domain. The recent crystal structureof Sos shows that this domain is alpha-helical and plays a "purely structural role" (Nature 394, 337-343).


Pssm-ID: 214571  Cd Length: 127  Bit Score: 43.09  E-value: 1.06e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 196001959    523 KVPQIRHASTTKLIQRLLD-LRFLSVDYLNVFLLTHHVFTTSEHVIDELLQFYNSWKGNSNGIDKHNFEYISD 594
Cdd:smart00229    1 DGGLIKGGTLEALIEHLTEaFDKADPSFVETFLLTYRSFITTQELLQLLLYRYNAIPPESWVEEKVNPRRVKN 73
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 534-575 3.23e-04

Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also called REM domain (Ras exchanger motif). This domain is common in nucleotide exchange factors for Ras-like small GTPases and is typically found immediately N-terminal to the RasGef (Cdc25-like) domain. REM contacts the GTPase and is assumed to participate in the catalytic activity of the exchange factor. Proteins with the REM domain include Sos1 and Sos2, which relay signals from tyrosine-kinase mediated signalling to Ras, RasGRP1-4, RasGRF1,2, CNrasGEF, and RAP-specific nucleotide exchange factors, to name a few.


Pssm-ID: 100121  Cd Length: 122  Bit Score: 41.63  E-value: 3.23e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 196001959  534 KLIQRLLD-LRFLSVDYLNVFLLTHHVFTTSEHVIDELLQFYN 575
Cdd:cd06224     4 ALIEHLTStFDMPDPSFVSTFLLTYRSFTTPTELLEKLIERYE 46
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 388-481 3.82e-03

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 [Multi-domain]  Cd Length: 102  Bit Score: 37.91  E-value: 3.82e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959    388 RLCFLFTKHLIITSHLQSGRLHIVKecGKIQLSEAILEEELDDDGKilyvfnRSKFLqFKLTinpsNSTPYSVVFAAATE 467
Cdd:smart00233   21 RYFVLFNSTLLYYKSKKDKKSYKPK--GSIDLSGCTVREAPDPDSS------KKPHC-FEIK----TSDRKTLLLQAESE 87

                            90
                    ....*....|....
gi 196001959    468 REKAAWTTDIGQCI 481
Cdd:smart00233   88 EEREKWVEALRKAI 101
PH1_FARP1-like cd01220
FERM, RhoGEF and pleckstrin domain-containing protein 1 and related proteins Pleckstrin ...
 388-482 3.93e-03

FERM, RhoGEF and pleckstrin domain-containing protein 1 and related proteins Pleckstrin Homology (PH) domain, repeat 1; Members here include FARP1 (also called Chondrocyte-derived ezrin-like protein; PH domain-containing family C member 2), FARP2 (also called FIR/FERM domain including RhoGEF; FGD1-related Cdc42-GEF/FRG), and FARP6 (also called Zinc finger FYVE domain-containing protein 24). They are members of the Dbl family guanine nucleotide exchange factors (GEFs) which are upstream positive regulators of Rho GTPases. Little is known about FARP1 and FARP6, though FARP1 has increased expression in differentiated chondrocytes. FARP2 is thought to regulate neurite remodeling by mediating the signaling pathways from membrane proteins to Rac. It is found in brain, lung, and testis, as well as embryonic hippocampal and cortical neurons. FARP1 and FARP2 are composed of a N-terminal FERM domain, a proline-rich (PR) domain, Dbl-homology (DH), and two C-terminal PH domains. FARP6 is composed of Dbl-homology (DH), and two C-terminal PH domains separated by a FYVE domain. This hierarchy contains 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: 269928  Cd Length: 109  Bit Score: 38.07  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196001959  388 RLCFLFTKHLIITSHLQSGRLHIvKECGKIQLsEAILEEELDDDGKILYVFnrskflqfklTINPSNStpySVVFAAATE 467
Cdd:cd01220    25 RMFFLFSDVLLYTSRSPTPSLQF-KVHGQLPL-RGLMVEESEPEWGVAHCF----------TIYGGNR---ALTVAASSE 89

                          90
                  ....*....|....*
gi 196001959  468 REKAAWTTDIGQCIE 482
Cdd:cd01220    90 EEKERWLEDLQRAID 104
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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