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Conserved domains on  [gi|50285195|ref|XP_445026|]
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BUD5 [Nakaseomyces glabratus]

Protein Classification

guanine nucleotide exchange factor( domain architecture ID 10345996)

guanine nucleotide exchange factor activates Ras-like small GTPases

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.
 968-1163 2.74e-50

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


:

Pssm-ID: 459872  Cd Length: 179  Bit Score: 175.86  E-value: 2.74e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285195    968 EVAKQLTILESLLFMRLTPFDIVNY---KANSTITSSNVAAITSFTNQLSQYVMNGILTPRiNDATRTTILKAWLRIALS 1044
Cdd:pfam00617    1 ELARQLTLIEFELFRKIKPRELLGSawsKKDKKENSPNIEAMIARFNKLSNWVASEILSEE-DLKKRAKVIKKFIKIAEH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285195   1045 ALYLRNFNSVASIMTAIQNHSITRLTGVWQQLSRKDTLLYEYLSRIIHPNHNFKVYRQKLKKIiddssqgsiipvksHVP 1124
Cdd:pfam00617   80 CRELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSA--------------SPP 145

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 50285195   1125 VVPFFNLFLQDITFIHEGNSTfrnpdsFRPNKPINVDKF 1163
Cdd:pfam00617  146 CIPFLGLYLTDLTFIEEGNPD------FLEGGLINFEKR 178
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 688-821 1.13e-21

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: 91.71  E-value: 1.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285195  688 TCRGLVFKLTDELDHPSSFFVSTFLLNFRSFMKSYELVTELINRFDLADMENklrdnkpKGKYSTTASKLKNRRRLICSV 767
Cdd:cd06224    1 TLEALIEHLTSTFDMPDPSFVSTFLLTYRSFTTPTELLEKLIERYEIAPPEN-------LEYNDWDKKKSKPIRLRVLNV 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 50285195  768 FNEWMESYW-DYNTDFECISTMINFFNEGMADylpresKMLIQTAAKLILKFNEL 821
Cdd:cd06224   74 LRTWVENYPyDFFDDEELLELLEEFLNRLVQE------GALLQELKKLLRKLLKL 122
SH3 super family cl17036
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 152-210 3.37e-08

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.


The actual alignment was detected with superfamily member cd11883:

Pssm-ID: 473055  Cd Length: 55  Bit Score: 51.13  E-value: 3.37e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50285195  152 FIIANHEFDPSSLQnkedasiCLPFKKNDVAFVHVVDESGWGEVTLIKNN---ERGWVPFNY 210
Cdd:cd11883    1 VVVALYDFTPKSKN-------QLSFKAGDIIYVLNKDPSGWWDGVIISSSgkvKRGWFPSNY 55
 
Name Accession Description Interval E-value
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 968-1163 2.74e-50

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


Pssm-ID: 459872  Cd Length: 179  Bit Score: 175.86  E-value: 2.74e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285195    968 EVAKQLTILESLLFMRLTPFDIVNY---KANSTITSSNVAAITSFTNQLSQYVMNGILTPRiNDATRTTILKAWLRIALS 1044
Cdd:pfam00617    1 ELARQLTLIEFELFRKIKPRELLGSawsKKDKKENSPNIEAMIARFNKLSNWVASEILSEE-DLKKRAKVIKKFIKIAEH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285195   1045 ALYLRNFNSVASIMTAIQNHSITRLTGVWQQLSRKDTLLYEYLSRIIHPNHNFKVYRQKLKKIiddssqgsiipvksHVP 1124
Cdd:pfam00617   80 CRELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSA--------------SPP 145

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 50285195   1125 VVPFFNLFLQDITFIHEGNSTfrnpdsFRPNKPINVDKF 1163
Cdd:pfam00617  146 CIPFLGLYLTDLTFIEEGNPD------FLEGGLINFEKR 178
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
964-1247 7.53e-43

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 156.64  E-value: 7.53e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285195     964 LNPLEVAKQLTILESLLFMRLTPFDIVNYKANST----ITSSNVAAITSFTNQLSQYVMNGIL---TPRIndatRTTILK 1036
Cdd:smart00147    4 LDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRskksPSPLNLEAFIRRFNEVSNWVATEILkqtTPKD----RAELLS 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285195    1037 AWLRIALSALYLRNFNSVASIMTAIQNHSITRLTGVWQQLSRKDTLLYEYLSRIIHPNHNFKVYRQKLKKIIddssqgsi 1116
Cdd:smart00147   80 KFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCN-------- 151

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285195    1117 ipvksHVPVVPFFNLFLQDITFIHEGNstfrnpDSFRPNKPINVDKFYRITKIVTTMQFFQ-VGYNTNSSEDAPK---RE 1192
Cdd:smart00147  152 -----LPPCIPFLGVLLKDLTFIDEGN------PDFLENGLVNFEKRRQIAEILREIRQLQsQPYNLRPNRSDIQsllQQ 220

                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 50285195    1193 SFFRLTEEMGLdtkniasvpllqelivyelwkvnnvfsidsdraYQLSLQIQPRN 1247
Cdd:smart00147  221 LLDHLDEEEEL---------------------------------YQLSLKIEPRV 242
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 964-1187 1.04e-41

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: 153.18  E-value: 1.04e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285195  964 LNPLEVAKQLTILESLLFMRLTPFDIVNYKANST----ITSSNVAAITSFTNQLSQYVMNGILTPRiNDATRTTILKAWL 1039
Cdd:cd00155    4 LDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKdkniHLSPNLERFIERFNNLSNWVASEILLCT-NPKKRARLLSKFI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285195 1040 RIALSALYLRNFNSVASIMTAIQNHSITRLTGVWQQLSRKDTLLYEYLSRIIHPNHNFKVYRQKLKKIIDDssqgsiipv 1119
Cdd:cd00155   83 QVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVGPN--------- 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50285195 1120 kshVPVVPFFNLFLQDITFIHEGNstfrnpDSFRPNKPINVDKFYRITKIVTTMQFFQ-VGYNTNSSED 1187
Cdd:cd00155  154 ---PPCVPFLGVYLKDLTFLHEGN------PDFLEGNLVNFEKRRKIAEILREIRQLQsNSYELNRDED 213
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 688-821 1.13e-21

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: 91.71  E-value: 1.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285195  688 TCRGLVFKLTDELDHPSSFFVSTFLLNFRSFMKSYELVTELINRFDLADMENklrdnkpKGKYSTTASKLKNRRRLICSV 767
Cdd:cd06224    1 TLEALIEHLTSTFDMPDPSFVSTFLLTYRSFTTPTELLEKLIERYEIAPPEN-------LEYNDWDKKKSKPIRLRVLNV 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 50285195  768 FNEWMESYW-DYNTDFECISTMINFFNEGMADylpresKMLIQTAAKLILKFNEL 821
Cdd:cd06224   74 LRTWVENYPyDFFDDEELLELLEEFLNRLVQE------GALLQELKKLLRKLLKL 122
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 683-791 2.86e-20

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: 86.97  E-value: 2.86e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285195    683 ELITATCRGLVFKLTDELDHPSSFFVSTFLLNFRSFMKSYELVTELINRFDLADmenklrDNKPKGKYSTTASKLKNRRR 762
Cdd:pfam00618    1 QVKAGTLEKLVEYLTSTRIMLDDSFLSTFLLTYRSFTTPAELLELLIERYNIPP------PLDLSSDSYWISKKTLPIRI 74

                           90       100       110
                   ....*....|....*....|....*....|
gi 50285195    763 LICSVFNEWMESYW-DYNTDFECISTMINF 791
Cdd:pfam00618   75 RVLSVLRHWVENYFsDFNDDPVLLSRLEKF 104
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 692-814 8.33e-12

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: 63.51  E-value: 8.33e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285195     692 LVFKLTDELDHPSSFFVSTFLLNFRSFMKSYELVTELINRFDLADMENKLRDNKPKGKysttasklknRRRLICSVFNEW 771
Cdd:smart00229   13 LIEHLTEAFDKADPSFVETFLLTYRSFITTQELLQLLLYRYNAIPPESWVEEKVNPRR----------VKNRVLNILRTW 82

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 50285195     772 MESYW-DYNTDFECISTMINFFNEGMADYLPRESKMLIQTAAKL 814
Cdd:smart00229   83 VENYWeDFEDDPKLISFLLEFLELVDDEKYPGLVTSLLNLLRRL 126
SH3_Sdc25 cd11883
Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is ...
 152-210 3.37e-08

Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is composed of the Saccharomyces cerevisiae guanine nucleotide exchange factors (GEFs) Sdc25 and Cdc25, and similar proteins. These GEFs regulate Ras by stimulating the GDP/GTP exchange on Ras. Cdc25 is involved in the Ras/PKA pathway that plays an important role in the regulation of metabolism, stress responses, and proliferation, depending on available nutrients and conditions. Proteins in this subfamily contain an N-terminal SH3 domain as well as REM (Ras exchanger motif) and RasGEF domains at the C-terminus. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212816  Cd Length: 55  Bit Score: 51.13  E-value: 3.37e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50285195  152 FIIANHEFDPSSLQnkedasiCLPFKKNDVAFVHVVDESGWGEVTLIKNN---ERGWVPFNY 210
Cdd:cd11883    1 VVVALYDFTPKSKN-------QLSFKAGDIIYVLNKDPSGWWDGVIISSSgkvKRGWFPSNY 55
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 152-212 6.22e-05

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 41.75  E-value: 6.22e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50285195     152 FIIANHEFDPsslQNKEDasicLPFKKNDVAFVHVVDESGWGEVTLiKNNERGWVPFNYFQ 212
Cdd:smart00326    4 QVRALYDYTA---QDPDE----LSFKKGDIITVLEKSDDGWWKGRL-GRGKEGLFPSNYVE 56
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 174-207 6.84e-03

SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 35.64  E-value: 6.84e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 50285195    174 LPFKKNDVAFVHVVDESGWGEVTLiKNNERGWVP 207
Cdd:pfam00018   14 LSFKKGDIIIVLEKSEDGWWKGRN-KGGKEGLIP 46
 
Name Accession Description Interval E-value
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 968-1163 2.74e-50

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


Pssm-ID: 459872  Cd Length: 179  Bit Score: 175.86  E-value: 2.74e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285195    968 EVAKQLTILESLLFMRLTPFDIVNY---KANSTITSSNVAAITSFTNQLSQYVMNGILTPRiNDATRTTILKAWLRIALS 1044
Cdd:pfam00617    1 ELARQLTLIEFELFRKIKPRELLGSawsKKDKKENSPNIEAMIARFNKLSNWVASEILSEE-DLKKRAKVIKKFIKIAEH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285195   1045 ALYLRNFNSVASIMTAIQNHSITRLTGVWQQLSRKDTLLYEYLSRIIHPNHNFKVYRQKLKKIiddssqgsiipvksHVP 1124
Cdd:pfam00617   80 CRELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSA--------------SPP 145

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 50285195   1125 VVPFFNLFLQDITFIHEGNSTfrnpdsFRPNKPINVDKF 1163
Cdd:pfam00617  146 CIPFLGLYLTDLTFIEEGNPD------FLEGGLINFEKR 178
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
964-1247 7.53e-43

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 156.64  E-value: 7.53e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285195     964 LNPLEVAKQLTILESLLFMRLTPFDIVNYKANST----ITSSNVAAITSFTNQLSQYVMNGIL---TPRIndatRTTILK 1036
Cdd:smart00147    4 LDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRskksPSPLNLEAFIRRFNEVSNWVATEILkqtTPKD----RAELLS 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285195    1037 AWLRIALSALYLRNFNSVASIMTAIQNHSITRLTGVWQQLSRKDTLLYEYLSRIIHPNHNFKVYRQKLKKIIddssqgsi 1116
Cdd:smart00147   80 KFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSCN-------- 151

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285195    1117 ipvksHVPVVPFFNLFLQDITFIHEGNstfrnpDSFRPNKPINVDKFYRITKIVTTMQFFQ-VGYNTNSSEDAPK---RE 1192
Cdd:smart00147  152 -----LPPCIPFLGVLLKDLTFIDEGN------PDFLENGLVNFEKRRQIAEILREIRQLQsQPYNLRPNRSDIQsllQQ 220

                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 50285195    1193 SFFRLTEEMGLdtkniasvpllqelivyelwkvnnvfsidsdraYQLSLQIQPRN 1247
Cdd:smart00147  221 LLDHLDEEEEL---------------------------------YQLSLKIEPRV 242
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 964-1187 1.04e-41

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: 153.18  E-value: 1.04e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285195  964 LNPLEVAKQLTILESLLFMRLTPFDIVNYKANST----ITSSNVAAITSFTNQLSQYVMNGILTPRiNDATRTTILKAWL 1039
Cdd:cd00155    4 LDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKdkniHLSPNLERFIERFNNLSNWVASEILLCT-NPKKRARLLSKFI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285195 1040 RIALSALYLRNFNSVASIMTAIQNHSITRLTGVWQQLSRKDTLLYEYLSRIIHPNHNFKVYRQKLKKIIDDssqgsiipv 1119
Cdd:cd00155   83 QVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVGPN--------- 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50285195 1120 kshVPVVPFFNLFLQDITFIHEGNstfrnpDSFRPNKPINVDKFYRITKIVTTMQFFQ-VGYNTNSSED 1187
Cdd:cd00155  154 ---PPCVPFLGVYLKDLTFLHEGN------PDFLEGNLVNFEKRRKIAEILREIRQLQsNSYELNRDED 213
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 688-821 1.13e-21

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: 91.71  E-value: 1.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285195  688 TCRGLVFKLTDELDHPSSFFVSTFLLNFRSFMKSYELVTELINRFDLADMENklrdnkpKGKYSTTASKLKNRRRLICSV 767
Cdd:cd06224    1 TLEALIEHLTSTFDMPDPSFVSTFLLTYRSFTTPTELLEKLIERYEIAPPEN-------LEYNDWDKKKSKPIRLRVLNV 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 50285195  768 FNEWMESYW-DYNTDFECISTMINFFNEGMADylpresKMLIQTAAKLILKFNEL 821
Cdd:cd06224   74 LRTWVENYPyDFFDDEELLELLEEFLNRLVQE------GALLQELKKLLRKLLKL 122
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 683-791 2.86e-20

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: 86.97  E-value: 2.86e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285195    683 ELITATCRGLVFKLTDELDHPSSFFVSTFLLNFRSFMKSYELVTELINRFDLADmenklrDNKPKGKYSTTASKLKNRRR 762
Cdd:pfam00618    1 QVKAGTLEKLVEYLTSTRIMLDDSFLSTFLLTYRSFTTPAELLELLIERYNIPP------PLDLSSDSYWISKKTLPIRI 74

                           90       100       110
                   ....*....|....*....|....*....|
gi 50285195    763 LICSVFNEWMESYW-DYNTDFECISTMINF 791
Cdd:pfam00618   75 RVLSVLRHWVENYFsDFNDDPVLLSRLEKF 104
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 692-814 8.33e-12

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: 63.51  E-value: 8.33e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285195     692 LVFKLTDELDHPSSFFVSTFLLNFRSFMKSYELVTELINRFDLADMENKLRDNKPKGKysttasklknRRRLICSVFNEW 771
Cdd:smart00229   13 LIEHLTEAFDKADPSFVETFLLTYRSFITTQELLQLLLYRYNAIPPESWVEEKVNPRR----------VKNRVLNILRTW 82

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 50285195     772 MESYW-DYNTDFECISTMINFFNEGMADYLPRESKMLIQTAAKL 814
Cdd:smart00229   83 VENYWeDFEDDPKLISFLLEFLELVDDEKYPGLVTSLLNLLRRL 126
SH3_Sdc25 cd11883
Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is ...
 152-210 3.37e-08

Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is composed of the Saccharomyces cerevisiae guanine nucleotide exchange factors (GEFs) Sdc25 and Cdc25, and similar proteins. These GEFs regulate Ras by stimulating the GDP/GTP exchange on Ras. Cdc25 is involved in the Ras/PKA pathway that plays an important role in the regulation of metabolism, stress responses, and proliferation, depending on available nutrients and conditions. Proteins in this subfamily contain an N-terminal SH3 domain as well as REM (Ras exchanger motif) and RasGEF domains at the C-terminus. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212816  Cd Length: 55  Bit Score: 51.13  E-value: 3.37e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50285195  152 FIIANHEFDPSSLQnkedasiCLPFKKNDVAFVHVVDESGWGEVTLIKNN---ERGWVPFNY 210
Cdd:cd11883    1 VVVALYDFTPKSKN-------QLSFKAGDIIYVLNKDPSGWWDGVIISSSgkvKRGWFPSNY 55
SH3_Myosin-I_fungi cd11858
Src homology 3 domain of Type I fungal Myosins; Type I myosins (myosin-I) are actin-dependent ...
 174-212 1.56e-05

Src homology 3 domain of Type I fungal Myosins; Type I myosins (myosin-I) are actin-dependent motors in endocytic actin structures and actin patches. They play roles in membrane traffic in endocytic and secretory pathways, cell motility, and mechanosensing. Saccharomyces cerevisiae has two myosins-I, Myo3 and Myo5, which are involved in endocytosis and the polarization of the actin cytoskeleton. Myosin-I contains an N-terminal actin-activated ATPase, a phospholipid-binding TH1 (tail homology 1) domain, and a C-terminal extension which includes an F-actin-binding TH2 domain, an SH3 domain, and an acidic peptide that participates in activating the Arp2/3complex. The SH3 domain of myosin-I is required for myosin-I-induced actin polymerization. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212792 [Multi-domain]  Cd Length: 55  Bit Score: 43.53  E-value: 1.56e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 50285195  174 LPFKKNDVAFVHVVDESGWGEVTLIKNNERGWVPFNYFQ 212
Cdd:cd11858   16 LSLKKDDIVYIVQKEDNGWWLAKKLDESKEGWVPAAYLE 54
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 152-212 6.22e-05

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 41.75  E-value: 6.22e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50285195     152 FIIANHEFDPsslQNKEDasicLPFKKNDVAFVHVVDESGWGEVTLiKNNERGWVPFNYFQ 212
Cdd:smart00326    4 QVRALYDYTA---QDPDE----LSFKKGDIITVLEKSDDGWWKGRL-GRGKEGLFPSNYVE 56
SH3_alphaPIX cd12060
Src Homology 3 domain of alpha-Pak Interactive eXchange factor; Alpha-PIX, also called Rho ...
 165-213 9.59e-05

Src Homology 3 domain of alpha-Pak Interactive eXchange factor; Alpha-PIX, also called Rho guanine nucleotide exchange factor 6 (ARHGEF6) or Cool (Cloned out of Library)-2, activates small GTPases by exchanging bound GDP for free GTP. It acts as a GEF for both Cdc42 and Rac 1, and is localized in dendritic spines where it regulates spine morphogenesis. It controls dendritic length and spine density in the hippocampus. Mutations in the ARHGEF6 gene cause X-linked intellectual disability in humans. PIX proteins contain an N-terminal SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains, and a C-terminal leucine-zipper domain for dimerization. The SH3 domain of PIX binds to an atypical PxxxPR motif in p21-activated kinases (PAKs) with high affinity. The binding of PAKs to PIX facilitate the localization of PAKs to focal complexes and also localizes PAKs to PIX targets Cdc43 and Rac, leading to the activation of PAKs. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212993  Cd Length: 58  Bit Score: 41.53  E-value: 9.59e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 50285195  165 QNKEDASIClpfkKNDVAFVHVVDESGWGEVTLikNNERGWVPFNYFQD 213
Cdd:cd12060   13 TNEDELSVC----KGDIIYVTRVEEGGWWEGTL--NGKTGWFPSNYVRE 55
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 154-210 2.20e-04

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.


Pssm-ID: 212690 [Multi-domain]  Cd Length: 51  Bit Score: 40.14  E-value: 2.20e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 50285195  154 IANHEFDPsslQNKEDasicLPFKKNDVAFVHVVDESGWGEVTLiKNNERGWVPFNY 210
Cdd:cd00174    3 RALYDYEA---QDDDE----LSFKKGDIITVLEKDDDGWWEGEL-NGGREGLFPANY 51
SH3_RIM-BP_3 cd12013
Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 153-213 8.35e-04

Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212946  Cd Length: 61  Bit Score: 38.90  E-value: 8.35e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50285195  153 IIANHEFDPSSLQNKEDASICLPFKKNDVAFVH-VVDESGW--GEVtlikNNERGWVPFNYFQD 213
Cdd:cd12013    2 MVALFDYDPRESSPNVDAEVELSFRAGDIITVFgEMDEDGFyyGEL----NGQRGLVPSNFLEE 61
SH3_ARHGEF5_19 cd11940
Src homology 3 domain of the Rho guanine nucleotide exchange factors ARHGEF5 and ARHGEF19; ...
 174-212 1.80e-03

Src homology 3 domain of the Rho guanine nucleotide exchange factors ARHGEF5 and ARHGEF19; ARHGEF5, also called ephexin-3 or TIM (Transforming immortalized mammary oncogene), is a potent activator of RhoA and it plays roles in regulating cell shape, adhesion, and migration. It binds to the SH3 domain of Src and is involved in regulating Src-induced podosome formation. ARHGEF19, also called ephexin-2 or WGEF (weak-similarity GEF), is highly expressed in the intestine, liver, heart and kidney. It activates RhoA, Cdc42, and Rac 1, and has been shown to activate RhoA in the Wnt-PCP (planar cell polarity) pathway. It is involved in the regulation of cell polarity and cytoskeletal reorganization. ARHGEF5 and ARHGEF19 contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), and SH3 domains. The SH3 domains of ARHGEFs play an autoinhibitory role through intramolecular interactions with a proline-rich region N-terminal to the DH domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212873  Cd Length: 55  Bit Score: 37.85  E-value: 1.80e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 50285195  174 LPFKKNDVAFVHVVDESGWGEVTLIKNNERGWVPFNYFQ 212
Cdd:cd11940   16 LTLEKADIIMVRQQSSDGWLEGVRLSDGERGWFPQSHVE 54
SH3_RIM-BP cd11851
Src homology 3 domains of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding ...
 154-212 2.78e-03

Src homology 3 domains of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212785  Cd Length: 62  Bit Score: 37.30  E-value: 2.78e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50285195  154 IANHEFDPSSLQNKEDASICLPFKKNDVAFVHV-VDESGW--GEvtlIKNNERGWVPFNYFQ 212
Cdd:cd11851    3 VALYDYNPETMSPNDDPEEELSFHAGDVVRVYGpMDEDGFyyGE---LEGGRKGLVPSNFVQ 61
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 174-207 6.84e-03

SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 35.64  E-value: 6.84e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 50285195    174 LPFKKNDVAFVHVVDESGWGEVTLiKNNERGWVP 207
Cdd:pfam00018   14 LSFKKGDIIIVLEKSEDGWWKGRN-KGGKEGLIP 46
 
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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