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Conserved domains on  [gi|755562360|ref|XP_011246915|]
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RAS guanyl-releasing protein 2 isoform X4 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
150-387 6.23e-86

Guanine nucleotide exchange factor for Ras-like small GTPases;


:

Pssm-ID: 214539  Cd Length: 242  Bit Score: 264.11  E-value: 6.23e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755562360   150 FDHLEPMELAEHLTYLEYRSFCKILFQDYHSFVTHGCTVDNP---VLERFISLFNSVSQWVQLMILSKPTATQRALVITH 226
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKKSPsplNLEAFIRRFNEVSNWVATEILKQTTPKDRAELLSK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755562360   227 FVHVAERLLQLQNFNTLMAVVGGLSHSSISRLKETHSHVSPDTIKLWEGLTELVTATGNYSNYRRRLAACV-GFRFPILG 305
Cdd:smart00147  81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCNlPPCIPFLG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755562360   306 VHLKDLVALQLALPDWLDpgRTRLNGAKMRQLFCILEELAMVTSLRPPVQAN-PDLLSLLTVSLDQYQTEDELYQLSLQR 384
Cdd:smart00147 161 VLLKDLTFIDEGNPDFLE--NGLVNFEKRRQIAEILREIRQLQSQPYNLRPNrSDIQSLLQQLLDHLDEEEELYQLSLKI 238

                   ...
gi 755562360   385 EPR 387
Cdd:smart00147 239 EPR 241
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
7-121 4.71e-23

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: 94.32  E-value: 4.71e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755562360     7 LDKGCTVEELLRGCIEAFDDsgkvRDPQLVRMFLMMHPWYIPSSQLASKLLHFYQ-------QSRKDNSNSLQMKTCHLV 79
Cdd:smart00229   4 LIKGGTLEALIEHLTEAFDK----ADPSFVETFLLTYRSFITTQELLQLLLYRYNaippeswVEEKVNPRRVKNRVLNIL 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 755562360    80 RYWISAFPAEFDLNPELAEQIKELKALLDQE-GNRRHSSLIDI 121
Cdd:smart00229  80 RTWVENYWEDFEDDPKLISFLLEFLELVDDEkYPGLVTSLLNL 122
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
407-452 4.80e-05

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG5126:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 43.24  E-value: 4.80e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 755562360 407 LEEWTSVAKpkldqALVAEHIEKMVESVFRNFDVDGDGHISQEEFQ 452
Cdd:COG5126   52 REEFVAGME-----SLFEATVEPFARAAFDLLDTDGDGKISADEFR 92
 
Name Accession Description Interval E-value
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
150-387 6.23e-86

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 264.11  E-value: 6.23e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755562360   150 FDHLEPMELAEHLTYLEYRSFCKILFQDYHSFVTHGCTVDNP---VLERFISLFNSVSQWVQLMILSKPTATQRALVITH 226
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKKSPsplNLEAFIRRFNEVSNWVATEILKQTTPKDRAELLSK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755562360   227 FVHVAERLLQLQNFNTLMAVVGGLSHSSISRLKETHSHVSPDTIKLWEGLTELVTATGNYSNYRRRLAACV-GFRFPILG 305
Cdd:smart00147  81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCNlPPCIPFLG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755562360   306 VHLKDLVALQLALPDWLDpgRTRLNGAKMRQLFCILEELAMVTSLRPPVQAN-PDLLSLLTVSLDQYQTEDELYQLSLQR 384
Cdd:smart00147 161 VLLKDLTFIDEGNPDFLE--NGLVNFEKRRQIAEILREIRQLQSQPYNLRPNrSDIQSLLQQLLDHLDEEEELYQLSLKI 238

                   ...
gi 755562360   385 EPR 387
Cdd:smart00147 239 EPR 241
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
150-383 5.31e-84

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: 259.11  E-value: 5.31e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755562360 150 FDHLEPMELAEHLTYLEYRSFCKILFQDYHSFVTHGCTVD---NPVLERFISLFNSVSQWVQLMILSKPTATQRALVITH 226
Cdd:cd00155    1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKNihlSPNLERFIERFNNLSNWVASEILLCTNPKKRARLLSK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755562360 227 FVHVAERLLQLQNFNTLMAVVGGLSHSSISRLKETHSHVSPDTIKLWEGLTELVTATGNYSNYRRRLAAC--VGFRFPIL 304
Cdd:cd00155   81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVgpNPPCVPFL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755562360 305 GVHLKDLVALQLALPDWLDPGrtRLNGAKMRQLFCILEELAMVTSLRPPVQANPDLLSLLTVSLDQYQTEDELYQLSLQ 383
Cdd:cd00155  161 GVYLKDLTFLHEGNPDFLEGN--LVNFEKRRKIAEILREIRQLQSNSYELNRDEDILAFLWKLLELILNEDELYELSLE 237
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
157-335 2.06e-61

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


Pssm-ID: 459872  Cd Length: 179  Bit Score: 198.59  E-value: 2.06e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755562360  157 ELAEHLTYLEYRSFCKILFQDY--HSFVTHGCTVDNPVLERFISLFNSVSQWVQLMILSKPTATQRALVITHFVHVAERL 234
Cdd:pfam00617   1 ELARQLTLIEFELFRKIKPRELlgSAWSKKDKKENSPNIEAMIARFNKLSNWVASEILSEEDLKKRAKVIKKFIKIAEHC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755562360  235 LQLQNFNTLMAVVGGLSHSSISRLKETHSHVSPDTIKLWEGLTELVTATGNYSNYRRRLAACVGFRFPILGVHLKDLVAL 314
Cdd:pfam00617  81 RELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASPPCIPFLGLYLTDLTFI 160
                         170       180
                  ....*....|....*....|.
gi 755562360  315 QLALPDWLDPGrtRLNGAKMR 335
Cdd:pfam00617 161 EEGNPDFLEGG--LINFEKRR 179
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
7-121 4.71e-23

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: 94.32  E-value: 4.71e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755562360     7 LDKGCTVEELLRGCIEAFDDsgkvRDPQLVRMFLMMHPWYIPSSQLASKLLHFYQ-------QSRKDNSNSLQMKTCHLV 79
Cdd:smart00229   4 LIKGGTLEALIEHLTEAFDK----ADPSFVETFLLTYRSFITTQELLQLLLYRYNaippeswVEEKVNPRRVKNRVLNIL 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 755562360    80 RYWISAFPAEFDLNPELAEQIKELKALLDQE-GNRRHSSLIDI 121
Cdd:smart00229  80 RTWVENYWEDFEDDPKLISFLLEFLELVDDEkYPGLVTSLLNL 122
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
12-123 2.01e-17

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: 78.22  E-value: 2.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755562360  12 TVEELLRGCIEAFDDSgkvrDPQLVRMFLMMHPWYIPSSQLASKLLHFYQ----------QSRKDNSNSLQMKTCHLVRY 81
Cdd:cd06224    1 TLEALIEHLTSTFDMP----DPSFVSTFLLTYRSFTTPTELLEKLIERYEiappenleynDWDKKKSKPIRLRVLNVLRT 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 755562360  82 WISAFPAEFDLNPELAEQIKELKALLDQEGNRRHSSLIDIES 123
Cdd:cd06224   77 WVENYPYDFFDDEELLELLEEFLNRLVQEGALLQELKKLLRK 118
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
407-452 4.80e-05

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 43.24  E-value: 4.80e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 755562360 407 LEEWTSVAKpkldqALVAEHIEKMVESVFRNFDVDGDGHISQEEFQ 452
Cdd:COG5126   52 REEFVAGME-----SLFEATVEPFARAAFDLLDTDGDGKISADEFR 92
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
431-452 4.47e-04

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 37.38  E-value: 4.47e-04
                          10        20
                  ....*....|....*....|..
gi 755562360  431 VESVFRNFDVDGDGHISQEEFQ 452
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFK 23
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
430-454 9.22e-04

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 37.53  E-value: 9.22e-04
                         10        20
                 ....*....|....*....|....*
gi 755562360 430 MVESVFRNFDVDGDGHISQEEFQII 454
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAA 25
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
431-454 2.27e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 35.43  E-value: 2.27e-03
                           10        20
                   ....*....|....*....|....
gi 755562360   431 VESVFRNFDVDGDGHISQEEFQII 454
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDL 25
 
Name Accession Description Interval E-value
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
150-387 6.23e-86

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 264.11  E-value: 6.23e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755562360   150 FDHLEPMELAEHLTYLEYRSFCKILFQDYHSFVTHGCTVDNP---VLERFISLFNSVSQWVQLMILSKPTATQRALVITH 226
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKKSPsplNLEAFIRRFNEVSNWVATEILKQTTPKDRAELLSK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755562360   227 FVHVAERLLQLQNFNTLMAVVGGLSHSSISRLKETHSHVSPDTIKLWEGLTELVTATGNYSNYRRRLAACV-GFRFPILG 305
Cdd:smart00147  81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCNlPPCIPFLG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755562360   306 VHLKDLVALQLALPDWLDpgRTRLNGAKMRQLFCILEELAMVTSLRPPVQAN-PDLLSLLTVSLDQYQTEDELYQLSLQR 384
Cdd:smart00147 161 VLLKDLTFIDEGNPDFLE--NGLVNFEKRRQIAEILREIRQLQSQPYNLRPNrSDIQSLLQQLLDHLDEEEELYQLSLKI 238

                   ...
gi 755562360   385 EPR 387
Cdd:smart00147 239 EPR 241
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
150-383 5.31e-84

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: 259.11  E-value: 5.31e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755562360 150 FDHLEPMELAEHLTYLEYRSFCKILFQDYHSFVTHGCTVD---NPVLERFISLFNSVSQWVQLMILSKPTATQRALVITH 226
Cdd:cd00155    1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKNihlSPNLERFIERFNNLSNWVASEILLCTNPKKRARLLSK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755562360 227 FVHVAERLLQLQNFNTLMAVVGGLSHSSISRLKETHSHVSPDTIKLWEGLTELVTATGNYSNYRRRLAAC--VGFRFPIL 304
Cdd:cd00155   81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVgpNPPCVPFL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755562360 305 GVHLKDLVALQLALPDWLDPGrtRLNGAKMRQLFCILEELAMVTSLRPPVQANPDLLSLLTVSLDQYQTEDELYQLSLQ 383
Cdd:cd00155  161 GVYLKDLTFLHEGNPDFLEGN--LVNFEKRRKIAEILREIRQLQSNSYELNRDEDILAFLWKLLELILNEDELYELSLE 237
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
157-335 2.06e-61

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


Pssm-ID: 459872  Cd Length: 179  Bit Score: 198.59  E-value: 2.06e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755562360  157 ELAEHLTYLEYRSFCKILFQDY--HSFVTHGCTVDNPVLERFISLFNSVSQWVQLMILSKPTATQRALVITHFVHVAERL 234
Cdd:pfam00617   1 ELARQLTLIEFELFRKIKPRELlgSAWSKKDKKENSPNIEAMIARFNKLSNWVASEILSEEDLKKRAKVIKKFIKIAEHC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755562360  235 LQLQNFNTLMAVVGGLSHSSISRLKETHSHVSPDTIKLWEGLTELVTATGNYSNYRRRLAACVGFRFPILGVHLKDLVAL 314
Cdd:pfam00617  81 RELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASPPCIPFLGLYLTDLTFI 160
                         170       180
                  ....*....|....*....|.
gi 755562360  315 QLALPDWLDPGrtRLNGAKMR 335
Cdd:pfam00617 161 EEGNPDFLEGG--LINFEKRR 179
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
7-121 4.71e-23

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: 94.32  E-value: 4.71e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755562360     7 LDKGCTVEELLRGCIEAFDDsgkvRDPQLVRMFLMMHPWYIPSSQLASKLLHFYQ-------QSRKDNSNSLQMKTCHLV 79
Cdd:smart00229   4 LIKGGTLEALIEHLTEAFDK----ADPSFVETFLLTYRSFITTQELLQLLLYRYNaippeswVEEKVNPRRVKNRVLNIL 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 755562360    80 RYWISAFPAEFDLNPELAEQIKELKALLDQE-GNRRHSSLIDI 121
Cdd:smart00229  80 RTWVENYWEDFEDDPKLISFLLEFLELVDDEkYPGLVTSLLNL 122
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
12-123 2.01e-17

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: 78.22  E-value: 2.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755562360  12 TVEELLRGCIEAFDDSgkvrDPQLVRMFLMMHPWYIPSSQLASKLLHFYQ----------QSRKDNSNSLQMKTCHLVRY 81
Cdd:cd06224    1 TLEALIEHLTSTFDMP----DPSFVSTFLLTYRSFTTPTELLEKLIERYEiappenleynDWDKKKSKPIRLRVLNVLRT 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 755562360  82 WISAFPAEFDLNPELAEQIKELKALLDQEGNRRHSSLIDIES 123
Cdd:cd06224   77 WVENYPYDFFDDEELLELLEEFLNRLVQEGALLQELKKLLRK 118
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
407-452 4.80e-05

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 43.24  E-value: 4.80e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 755562360 407 LEEWTSVAKpkldqALVAEHIEKMVESVFRNFDVDGDGHISQEEFQ 452
Cdd:COG5126   52 REEFVAGME-----SLFEATVEPFARAAFDLLDTDGDGKISADEFR 92
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
431-452 4.47e-04

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 37.38  E-value: 4.47e-04
                          10        20
                  ....*....|....*....|..
gi 755562360  431 VESVFRNFDVDGDGHISQEEFQ 452
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFK 23
EF-hand_5 pfam13202
EF hand;
431-452 5.09e-04

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 37.30  E-value: 5.09e-04
                          10        20
                  ....*....|....*....|..
gi 755562360  431 VESVFRNFDVDGDGHISQEEFQ 452
Cdd:pfam13202   1 LKDTFRQIDLNGDGKISKEELR 22
EF-hand_7 pfam13499
EF-hand domain pair;
428-454 6.77e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.00  E-value: 6.77e-04
                          10        20
                  ....*....|....*....|....*..
gi 755562360  428 EKMVESVFRNFDVDGDGHISQEEFQII 454
Cdd:pfam13499  39 DEEVEELFKEFDLDKDGRISFEEFLEL 65
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
430-454 9.22e-04

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 37.53  E-value: 9.22e-04
                         10        20
                 ....*....|....*....|....*
gi 755562360 430 MVESVFRNFDVDGDGHISQEEFQII 454
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAA 25
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
424-477 2.03e-03

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 38.62  E-value: 2.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755562360 424 AEHIEKMvESVFRNFDVDGDGHISQEEFQII-RGNFPYLSAFGDLDQNQAHSCQE 477
Cdd:COG5126    1 DLQRRKL-DRRFDLLDADGDGVLERDDFEALfRRLWATLFSEADTDGDGRISREE 54
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
431-454 2.27e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 35.43  E-value: 2.27e-03
                           10        20
                   ....*....|....*....|....
gi 755562360   431 VESVFRNFDVDGDGHISQEEFQII 454
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDL 25
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
428-452 2.30e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 36.37  E-value: 2.30e-03
                         10        20
                 ....*....|....*....|....*
gi 755562360 428 EKMVESVFRNFDVDGDGHISQEEFQ 452
Cdd:cd00051   35 EEEIDEMIREVDKDGDGKIDFEEFL 59
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
401-451 3.38e-03

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 39.20  E-value: 3.38e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755562360 401 PPRPPVL--EEWTSVAKPkldqalvaEH----IEKMVESVFRNFDVDGDGHISQEEF 451
Cdd:cd16225  142 EPEDGLLdvEEFLSFRHP--------EHsrgmLKNMVKEILHDLDQDGDEKLTLDEF 190
EF-hand_6 pfam13405
EF-hand domain;
431-454 4.25e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 34.84  E-value: 4.25e-03
                          10        20
                  ....*....|....*....|....
gi 755562360  431 VESVFRNFDVDGDGHISQEEFQII 454
Cdd:pfam13405   2 LREAFKLFDKDGDGKISLEELRKA 25
 
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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