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Conserved domains on  [gi|18110536|ref|NP_476597|]
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Son of sevenless [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 825-1062 1.07e-81

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: 268.35  E-value: 1.07e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  825 LLTLHPLELARQLTLLEFEMYKNVKPSELVGSPWTKKDKEV-KSPNLLKIMKHTTNVTRWIEKSITEAENYEERLAIMQR 903
Cdd:cd00155    1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKNIhLSPNLERFIERFNNLSNWVASEILLCTNPKKRARLLSK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  904 AIEVMMVMLELNNFNGILSIVAAMGTASVYRLRWTFQGLPERYRKFLEECRELSD--DHLKKYQERLRSI--NPPCVPFF 979
Cdd:cd00155   81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDpsRNFKNYRKLLKSVgpNPPCVPFL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  980 GRYLTNILHLEEGNPDLLAnTELINFSKRRKVAEIIGEIQQYQNQPYCLNEESTIRQFFEQLDPfnglsDKQMSDYLYNE 1059
Cdd:cd00155  161 GVYLKDLTFLHEGNPDFLE-GNLVNFEKRRKIAEILREIRQLQSNSYELNRDEDILAFLWKLLE-----LILNEDELYEL 234


                 ...
gi 18110536 1060 SLR 1062
Cdd:cd00155  235 SLE 237
PH_SOS cd01261
Son of Sevenless (SOS) Pleckstrin homology (PH) domain; SOS is a Ras guanine nucleotide ...
 476-586 6.40e-46

Son of Sevenless (SOS) Pleckstrin homology (PH) domain; SOS is a Ras guanine nucleotide exchange factor. SOS is thought to transmit signals from activated receptor tyrosine kinases to the Ras signaling pathway. SOS contains a histone domain, Dbl-homology (DH), a PH domain, Rem domain, Cdc25 domain, and a Grb2 binding domain. The SOS PH domain binds to phosphatidylinositol-4,5-bisphosphate (PIP2) and phosphatidic acid (PA). SOS is dependent on Ras binding to the allosteric site via its histone domain for both a lower level of activity (Ras GDP) and maximal activity (Ras GTP). The DH domain blocks the allosteric Ras binding site in SOS. The PH domain is closely associated with the DH domain and the action of the DH-PH unit gates a reciprocal interaction between Ras and SOS. The C-terminal proline-rich domain of SOS binds to the adapter protein Grb2 which localizes the Sos protein to the plasma membrane and diminishes the negative effect of the C-terminal domain on the guanine nucleotide exchange activity of the CDC25-homology domain of SOS. 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: 269963  Cd Length: 109  Bit Score: 160.60  E-value: 6.40e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  476 QNCNEFIREDSLSKLGSGKRIwSERKVFLFDGLMVLCKANtKKQTPSAGATAyDYRLKEKYFMRRVDINDRPDSDDLKNS 555
Cdd:cd01261    1 QCCNEFIMEGTLGKVGSGKRK-TERHAFLFDGLLLLCKSN-RRRTSTGGPKP-EYRLKEKFFIRKVEINDLEDTEELKNA 77

                         90       100       110
                 ....*....|....*....|....*....|.
gi 18110536  556 FELAPRMQPPIVLTAKNAQHKHDWMADLLMV 586
Cdd:cd01261   78 FEIVPRDQPSVILFAKSAEEKNNWMAALVML 108
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 637-791 8.53e-41

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: 146.71  E-value: 8.53e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536     637 GVPMIKGATLCKLIERLTYHIY-ADPTFVRTFLTTYRYFCSPQQLLQLLVERFNIPDPslvyqdtgtagaggmggvggdk 715
Cdd:smart00229    1 DGGLIKGGTLEALIEHLTEAFDkADPSFVETFLLTYRSFITTQELLQLLLYRYNAIPP---------------------- 58

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18110536     716 ehkNSHREdwkryRKEYVQPVQFRVLNVLRHWVDHHFYDFEKDPMLLEKLLNFLEHVNGKSMRKWVDSVLKIVQRK 791
Cdd:smart00229   59 ---ESWVE-----EKVNPRRVKNRVLNILRTWVENYWEDFEDDPKLISFLLEFLELVDDEKYPGLVTSLLNLLRRL 126
HFD_SOS1_rpt1 cd22914
first histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ...
 68-145 2.07e-39

first histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; SOS-1 is a guanine nucleotide exchange factor for Ras that binds to GRB2. It promotes the exchange of Ras-bound GDP by GTP. It is a catalytic component of a trimeric complex that participates in transduction of signals from Ras to Rac, by promoting the Rac-specific guanine nucleotide exchange factor (GEF) activity. SOS-1 contains tandem histone folds at the N-terminal region. The model corresponds to the first repeat.


:

Pssm-ID: 467039  Cd Length: 78  Bit Score: 140.85  E-value: 2.07e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18110536   68 RWRGLFTPSLKKVLEQVHPRVTAKEDALLYVEKLCLRLLAMLCAKPlPHSVQDVEEKVNKSFPAPIDQWALNEAKEVI 145
Cdd:cd22914    1 KWRGLLVPALKKVQKQVHPTLVAKEDALEYIEELILQLLNMLCAAQ-PHSVQDVEERVQKTFPHPIDKWAIADAQAAL 77
HFD_SOS1_rpt2 cd22915
second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ...
 153-227 5.23e-34

second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; SOS-1 is a guanine nucleotide exchange factor for Ras that binds to GRB2. It promotes the exchange of Ras-bound GDP by GTP. It is a catalytic component of a trimeric complex that participates in transduction of signals from Ras to Rac, by promoting the Rac-specific guanine nucleotide exchange factor (GEF) activity. SOS-1 contains tandem histone folds at the N-terminal region. The model corresponds to the second repeat.


:

Pssm-ID: 467040  Cd Length: 75  Bit Score: 125.43  E-value: 5.23e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18110536  153 VLPTEKVHTLLQKDVLQYKIDSSVSAFLVAVLEYISADILKMAGDYVIKIAHCEITKEDIEVVMNADRVLMDMLN 227
Cdd:cd22915    1 LFPVDKIHPLLKKDLLVYKVDPQVSLYLVAVLEYIAADILKLAGNYVRNIRHYEITSQDIKVAMCADKVLMDLFG 75
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 249-432 3.25e-24

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: 101.22  E-value: 3.25e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  249 YEETVKELIHDEKQYQRDLHMIIRVFREELVKIVS--DPRELEPIFSNIMDIYEVTVTLLGSLEDVIEMSQeQSAPCVGS 326
Cdd:cd00160    1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLplSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWD-KSGPRIGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  327 CfeELAEAEEFDVYKKYAYDVTSQASRdaLNNLLSKpgASSLTTAGHGFRDAVKYY-LPKLLLVPICHAFVYFDYIKHL- 404
Cdd:cd00160   80 V--FLKLAPFFKIYSEYCSNHPDALEL--LKKLKKF--NKFFQEFLEKAESECGRLkLESLLLKPVQRLTKYPLLLKELl 153

                        170       180
                 ....*....|....*....|....*...
gi 18110536  405 KDLSSSQDDIESFEQVQGLLHPLHCDLE 432
Cdd:cd00160  154 KHTPDGHEDREDLKKALEAIKEVASQVN 181
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 1197-1502 6.85e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 6.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  1197 SVPAPHL--------PKKPGAHVWANNNSTLASASAMDVvfSPALPEHLPP----QSLPDSNPFASDTE----------- 1253
Cdd:PHA03247 2513 SRLAPAIlpdepvgePVHPRMLTWIRGLEELASDDAGDP--PPPLPPAAPPaapdRSVPPPRPAPRPSEpavtsrarrpd 2590

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  1254 APPSPlpklvVSPRHETGNRSPFHGRMQNSPTHSTASTVTLTGMSTSGGEEFCAGGFYFNSAHQGQPGAVPISPHVNVPM 1333
Cdd:PHA03247 2591 APPQS-----ARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPR 2665

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  1334 ATNMEYRAVPPPLPPRRKERTESCADMAQKRQAPDAPTlPPRDGELSPPPIPPRLNHSTGISYLRQSHGKSKEF----VG 1409
Cdd:PHA03247 2666 RARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPP-PPPTPEPAPHALVSATPLPPGPAAARQASPALPAApappAV 2744

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  1410 NSSLLLPNTSSIMIRR------NSAIEKRAAATSQPNQAAAGPISTTLVTVSQAVATDEPLPLPISPAASSSTTTSPLTP 1483
Cdd:PHA03247 2745 PAGPATPGGPARPARPpttagpPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824

                         330       340
                  ....*....|....*....|....*..
gi 18110536  1484 A--------MSPMSPNIPSHPVESTSS 1502
Cdd:PHA03247 2825 AgplppptsAQPTAPPPPPGPPPPSLP 2851
 
Name Accession Description Interval E-value
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 825-1062 1.07e-81

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: 268.35  E-value: 1.07e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  825 LLTLHPLELARQLTLLEFEMYKNVKPSELVGSPWTKKDKEV-KSPNLLKIMKHTTNVTRWIEKSITEAENYEERLAIMQR 903
Cdd:cd00155    1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKNIhLSPNLERFIERFNNLSNWVASEILLCTNPKKRARLLSK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  904 AIEVMMVMLELNNFNGILSIVAAMGTASVYRLRWTFQGLPERYRKFLEECRELSD--DHLKKYQERLRSI--NPPCVPFF 979
Cdd:cd00155   81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDpsRNFKNYRKLLKSVgpNPPCVPFL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  980 GRYLTNILHLEEGNPDLLAnTELINFSKRRKVAEIIGEIQQYQNQPYCLNEESTIRQFFEQLDPfnglsDKQMSDYLYNE 1059
Cdd:cd00155  161 GVYLKDLTFLHEGNPDFLE-GNLVNFEKRRKIAEILREIRQLQSNSYELNRDEDILAFLWKLLE-----LILNEDELYEL 234


                 ...
gi 18110536 1060 SLR 1062
Cdd:cd00155  235 SLE 237
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
825-1066 4.99e-80

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 263.72  E-value: 4.99e-80
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536     825 LLTLHPLELARQLTLLEFEMYKNVKPSELVGSPWTKKDKEVKSP-NLLKIMKHTTNVTRWIEKSITEAENYEERLAIMQR 903
Cdd:smart00147    1 LLLLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKKSPSPlNLEAFIRRFNEVSNWVATEILKQTTPKDRAELLSK 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536     904 AIEVMMVMLELNNFNGILSIVAAMGTASVYRLRWTFQGLPERYRKFLEECREL--SDDHLKKYQERLRSIN-PPCVPFFG 980
Cdd:smart00147   81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELlsPERNYKNYREALSSCNlPPCIPFLG 160

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536     981 RYLTNILHLEEGNPDLLANTeLINFSKRRKVAEIIGEIQQYQNQPYCLN-EESTIRQFFEQLdpFNGLSDKqmsDYLYNE 1059
Cdd:smart00147  161 VLLKDLTFIDEGNPDFLENG-LVNFEKRRQIAEILREIRQLQSQPYNLRpNRSDIQSLLQQL--LDHLDEE---EELYQL 234


                    ....*..
gi 18110536    1060 SLRIEPR 1066
Cdd:smart00147  235 SLKIEPR 241
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 832-1009 1.99e-64

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


Pssm-ID: 459872  Cd Length: 179  Bit Score: 216.69  E-value: 1.99e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536    832 ELARQLTLLEFEMYKNVKPSELVGSPWTKKDKEVKSPNLLKIMKHTTNVTRWIEKSITEAENYEERLAIMQRAIEVMMVM 911
Cdd:pfam00617    1 ELARQLTLIEFELFRKIKPRELLGSAWSKKDKKENSPNIEAMIARFNKLSNWVASEILSEEDLKKRAKVIKKFIKIAEHC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536    912 LELNNFNGILSIVAAMGTASVYRLRWTFQGLPERYRKFLEECREL--SDDHLKKYQERLRSINPPCVPFFGRYLTNILHL 989
Cdd:pfam00617   81 RELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLmsPSRNFKNYREALSSASPPCIPFLGLYLTDLTFI 160

                          170       180
                   ....*....|....*....|
gi 18110536    990 EEGNPDLLaNTELINFSKRR 1009
Cdd:pfam00617  161 EEGNPDFL-EGGLINFEKRR 179
PH_SOS cd01261
Son of Sevenless (SOS) Pleckstrin homology (PH) domain; SOS is a Ras guanine nucleotide ...
 476-586 6.40e-46

Son of Sevenless (SOS) Pleckstrin homology (PH) domain; SOS is a Ras guanine nucleotide exchange factor. SOS is thought to transmit signals from activated receptor tyrosine kinases to the Ras signaling pathway. SOS contains a histone domain, Dbl-homology (DH), a PH domain, Rem domain, Cdc25 domain, and a Grb2 binding domain. The SOS PH domain binds to phosphatidylinositol-4,5-bisphosphate (PIP2) and phosphatidic acid (PA). SOS is dependent on Ras binding to the allosteric site via its histone domain for both a lower level of activity (Ras GDP) and maximal activity (Ras GTP). The DH domain blocks the allosteric Ras binding site in SOS. The PH domain is closely associated with the DH domain and the action of the DH-PH unit gates a reciprocal interaction between Ras and SOS. The C-terminal proline-rich domain of SOS binds to the adapter protein Grb2 which localizes the Sos protein to the plasma membrane and diminishes the negative effect of the C-terminal domain on the guanine nucleotide exchange activity of the CDC25-homology domain of SOS. 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: 269963  Cd Length: 109  Bit Score: 160.60  E-value: 6.40e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  476 QNCNEFIREDSLSKLGSGKRIwSERKVFLFDGLMVLCKANtKKQTPSAGATAyDYRLKEKYFMRRVDINDRPDSDDLKNS 555
Cdd:cd01261    1 QCCNEFIMEGTLGKVGSGKRK-TERHAFLFDGLLLLCKSN-RRRTSTGGPKP-EYRLKEKFFIRKVEINDLEDTEELKNA 77

                         90       100       110
                 ....*....|....*....|....*....|.
gi 18110536  556 FELAPRMQPPIVLTAKNAQHKHDWMADLLMV 586
Cdd:cd01261   78 FEIVPRDQPSVILFAKSAEEKNNWMAALVML 108
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 637-791 8.53e-41

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: 146.71  E-value: 8.53e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536     637 GVPMIKGATLCKLIERLTYHIY-ADPTFVRTFLTTYRYFCSPQQLLQLLVERFNIPDPslvyqdtgtagaggmggvggdk 715
Cdd:smart00229    1 DGGLIKGGTLEALIEHLTEAFDkADPSFVETFLLTYRSFITTQELLQLLLYRYNAIPP---------------------- 58

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18110536     716 ehkNSHREdwkryRKEYVQPVQFRVLNVLRHWVDHHFYDFEKDPMLLEKLLNFLEHVNGKSMRKWVDSVLKIVQRK 791
Cdd:smart00229   59 ---ESWVE-----EKVNPRRVKNRVLNILRTWVENYWEDFEDDPKLISFLLEFLELVDDEKYPGLVTSLLNLLRRL 126
HFD_SOS1_rpt1 cd22914
first histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ...
 68-145 2.07e-39

first histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; SOS-1 is a guanine nucleotide exchange factor for Ras that binds to GRB2. It promotes the exchange of Ras-bound GDP by GTP. It is a catalytic component of a trimeric complex that participates in transduction of signals from Ras to Rac, by promoting the Rac-specific guanine nucleotide exchange factor (GEF) activity. SOS-1 contains tandem histone folds at the N-terminal region. The model corresponds to the first repeat.


Pssm-ID: 467039  Cd Length: 78  Bit Score: 140.85  E-value: 2.07e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18110536   68 RWRGLFTPSLKKVLEQVHPRVTAKEDALLYVEKLCLRLLAMLCAKPlPHSVQDVEEKVNKSFPAPIDQWALNEAKEVI 145
Cdd:cd22914    1 KWRGLLVPALKKVQKQVHPTLVAKEDALEYIEELILQLLNMLCAAQ-PHSVQDVEERVQKTFPHPIDKWAIADAQAAL 77
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 645-790 1.23e-34

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: 129.07  E-value: 1.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  645 TLCKLIERLTYH-IYADPTFVRTFLTTYRYFCSPQQLLQLLVERFNIPDPSLVyqdtgtagaggmggvggdkehknshre 723
Cdd:cd06224    1 TLEALIEHLTSTfDMPDPSFVSTFLLTYRSFTTPTELLEKLIERYEIAPPENL--------------------------- 53

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18110536  724 DWKRYRKEYVQPVQFRVLNVLRHWVDHHFYDFEKDPMLLEKLLNFLEHVN--GKSMRKWVDSVLKIVQR 790
Cdd:cd06224   54 EYNDWDKKKSKPIRLRVLNVLRTWVENYPYDFFDDEELLELLEEFLNRLVqeGALLQELKKLLRKLLKL 122
HFD_SOS1_rpt2 cd22915
second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ...
 153-227 5.23e-34

second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; SOS-1 is a guanine nucleotide exchange factor for Ras that binds to GRB2. It promotes the exchange of Ras-bound GDP by GTP. It is a catalytic component of a trimeric complex that participates in transduction of signals from Ras to Rac, by promoting the Rac-specific guanine nucleotide exchange factor (GEF) activity. SOS-1 contains tandem histone folds at the N-terminal region. The model corresponds to the second repeat.


Pssm-ID: 467040  Cd Length: 75  Bit Score: 125.43  E-value: 5.23e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18110536  153 VLPTEKVHTLLQKDVLQYKIDSSVSAFLVAVLEYISADILKMAGDYVIKIAHCEITKEDIEVVMNADRVLMDMLN 227
Cdd:cd22915    1 LFPVDKIHPLLKKDLLVYKVDPQVSLYLVAVLEYIAADILKLAGNYVRNIRHYEITSQDIKVAMCADKVLMDLFG 75
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 641-768 2.37e-33

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: 124.72  E-value: 2.37e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536    641 IKGATLCKLIERLTYHIYA-DPTFVRTFLTTYRYFCSPQQLLQLLVERFNIPDPSLVYQDtgtagaggmggvggdkEHKN 719
Cdd:pfam00618    2 VKAGTLEKLVEYLTSTRIMlDDSFLSTFLLTYRSFTTPAELLELLIERYNIPPPLDLSSD----------------SYWI 65

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 18110536    720 SHREDwkryrkeyvqPVQFRVLNVLRHWVDHHFYDFEKDPMLLEKLLNF 768
Cdd:pfam00618   66 SKKTL----------PIRIRVLSVLRHWVENYFSDFNDDPVLLSRLEKF 104
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 249-432 3.25e-24

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: 101.22  E-value: 3.25e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  249 YEETVKELIHDEKQYQRDLHMIIRVFREELVKIVS--DPRELEPIFSNIMDIYEVTVTLLGSLEDVIEMSQeQSAPCVGS 326
Cdd:cd00160    1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLplSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWD-KSGPRIGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  327 CfeELAEAEEFDVYKKYAYDVTSQASRdaLNNLLSKpgASSLTTAGHGFRDAVKYY-LPKLLLVPICHAFVYFDYIKHL- 404
Cdd:cd00160   80 V--FLKLAPFFKIYSEYCSNHPDALEL--LKKLKKF--NKFFQEFLEKAESECGRLkLESLLLKPVQRLTKYPLLLKELl 153

                        170       180
                 ....*....|....*....|....*...
gi 18110536  405 KDLSSSQDDIESFEQVQGLLHPLHCDLE 432
Cdd:cd00160  154 KHTPDGHEDREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 253-433 3.65e-22

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: 95.45  E-value: 3.65e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536     253 VKELIHDEKQYQRDLHMIIRVFREELVKIVS--DPRELEPIFSNIMDIYEVTVTLLGSLEDVIEMSqEQSAPCVGSCfeE 330
Cdd:smart00325    2 LKELLQTERNYVRDLKLLVEVFLKPLKKELKllSPNELETLFGNIEEIYEFHRDFLDELEERIEEW-DDSVERIGDV--F 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536     331 LAEAEEFDVYKKYAYDVTSQASRdaLNNLLSKPGASSLTTAGHGFRDAVKYYLPKLLLVPICHAFVYFDYIKHLKDLSS- 409
Cdd:smart00325   79 LKLEEFFKIYSEYCSNHPDALEL--LKKLKKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLLLKELLKHTPe 156

                           170       180
                    ....*....|....*....|....
gi 18110536     410 SQDDIESFEQVQGLLHPLHCDLEK 433
Cdd:smart00325  157 DHEDREDLKKALKAIKELANQVNE 180
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 481-587 2.40e-12

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: 64.88  E-value: 2.40e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536     481 FIREDSLSKLGS-GKRIWSERKVFLFDGLMVLCKANTKKQtpsagatayDYRLKEKYFMR--RVDINDRPDSDDLKNSFE 557
Cdd:smart00233    1 VIKEGWLYKKSGgGKKSWKKRYFVLFNSTLLYYKSKKDKK---------SYKPKGSIDLSgcTVREAPDPDSSKKPHCFE 71

                            90       100       110
                    ....*....|....*....|....*....|
gi 18110536     558 LAPRMQPPIVLTAKNAQHKHDWMADLLMVI 587
Cdd:smart00233   72 IKTSDRKTLLLQAESEEEREKWVEALRKAI 101
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 482-587 5.41e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 55.26  E-value: 5.41e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536    482 IREDSLSKLGSGKRI-WSERKVFLFDGLMVLCKANTKKQtpsagatayDYRLKEKYFMR--RVDINDRPDSDDLKNSFEL 558
Cdd:pfam00169    2 VKEGWLLKKGGGKKKsWKKRYFVLFDGSLLYYKDDKSGK---------SKEPKGSISLSgcEVVEVVASDSPKRKFCFEL 72

                           90       100       110
                   ....*....|....*....|....*....|..
gi 18110536    559 APRMQPP---IVLTAKNAQHKHDWMADLLMVI 587
Cdd:pfam00169   73 RTGERTGkrtYLLQAESEEERKDWIKAIQSAI 104
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 253-327 3.82e-08

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: 54.61  E-value: 3.82e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18110536    253 VKELIHDEKQYQRDLHMIIRVFREELVKIVSD-PRELEPIFSNIMDIYEVTVTLLgsLEDVIEmsQEQSAPCVGSC 327
Cdd:pfam00621    2 IKELLQTERSYVRDLEILVEVFLPPNSKPLSEsEEEIKTIFSNIEEIYELHRQLL--LEELLK--EWISIQRIGDI 73
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1197-1502 6.85e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 6.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  1197 SVPAPHL--------PKKPGAHVWANNNSTLASASAMDVvfSPALPEHLPP----QSLPDSNPFASDTE----------- 1253
Cdd:PHA03247 2513 SRLAPAIlpdepvgePVHPRMLTWIRGLEELASDDAGDP--PPPLPPAAPPaapdRSVPPPRPAPRPSEpavtsrarrpd 2590

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  1254 APPSPlpklvVSPRHETGNRSPFHGRMQNSPTHSTASTVTLTGMSTSGGEEFCAGGFYFNSAHQGQPGAVPISPHVNVPM 1333
Cdd:PHA03247 2591 APPQS-----ARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPR 2665

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  1334 ATNMEYRAVPPPLPPRRKERTESCADMAQKRQAPDAPTlPPRDGELSPPPIPPRLNHSTGISYLRQSHGKSKEF----VG 1409
Cdd:PHA03247 2666 RARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPP-PPPTPEPAPHALVSATPLPPGPAAARQASPALPAApappAV 2744

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  1410 NSSLLLPNTSSIMIRR------NSAIEKRAAATSQPNQAAAGPISTTLVTVSQAVATDEPLPLPISPAASSSTTTSPLTP 1483
Cdd:PHA03247 2745 PAGPATPGGPARPARPpttagpPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824

                         330       340
                  ....*....|....*....|....*..
gi 18110536  1484 A--------MSPMSPNIPSHPVESTSS 1502
Cdd:PHA03247 2825 AgplppptsAQPTAPPPPPGPPPPSLP 2851
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
147-197 7.86e-04

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 41.39  E-value: 7.86e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18110536  147 SKKRKSVLPTEKVHTLLQKDVLQYKIDSSVSAFLVAVLEYISADILKMAGD 197
Cdd:COG5262   20 SAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEILELAGN 70
SOBP pfam15279
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
 1217-1386 3.34e-03

Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual disability. It carries a zinc-finger of the zf-C2H2 type at the N-terminus, and a highly characteriztic C-terminal PhPhPhPhPhPh motif. The deduced 873-amino acid protein contains an N-terminal nuclear localization signal (NLS), followed by 2 FCS-type zinc finger motifs, a proline-rich region (PR1), a putative RNA-binding motif region, and a C-terminal NLS embedded in a second proline-rich motif. SOBP is expressed in various human tissues, including developing mouse brain at embryonic day 14. In postnatal and adult mouse brain SOBP is expressed in all neurons, with intense staining in the limbic system. Highest expression is in layer V cortical neurons, hippocampus, pyriform cortex, dorsomedial nucleus of thalamus, amygdala, and hypothalamus. Postnatal expression of SOBP in the limbic system corresponds to a time of active synaptogenesis. the family is also referred to as Jackson circler, JXC1. In seven affected siblings from a consanguineous Israeli Arab family with mental retardation, anterior maxillary protrusion, and strabismus mutations were found in this protein.


Pssm-ID: 464609 [Multi-domain]  Cd Length: 325  Bit Score: 41.34  E-value: 3.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536   1217 STLASASAMDVVFSPALPEHL--PPQSLPDSNPFASDTEAPPSPLPKLVvsPRHETGNRSPFHgrmqnSPTHSTASTVTL 1294
Cdd:pfam15279   98 SSSASPSSSPTSSNSSKPLISvaSSSKLLAPKPHEPPSLPPPPLPPKKG--RRHRPGLHPPLG-----RPPGSPPMSMTP 170

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536   1295 TGMSTSGGEEFCAGGFYFNSAHQG-QPGAVPISPHV---NVPMATNMEYRAVPPPLPPRRKERTESCAD--MAQKRQAPD 1368
Cdd:pfam15279  171 RGLLGKPQQHPPPSPLPAFMEPSSmPPPFLRPPPSIpqpNSPLSNPMLPGIGPPPKPPRNLGPPSNPMHrpPFSPHHPPP 250

                          170
                   ....*....|....*...
gi 18110536   1369 APTLPPrdgelSPPPIPP 1386
Cdd:pfam15279  251 PPTPPG-----PPPGLPP 263
H2A smart00414
Histone 2A;
155-227 6.95e-03

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 37.70  E-value: 6.95e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18110536     155 PTEKVHTLLQKDVLQYKIDSSVSAFLVAVLEYISADILKMAGDYVIKIAHCEITKEDIEVVMNADRVLMDMLN 227
Cdd:smart00414   11 PVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNKLLK 83
 
Name Accession Description Interval E-value
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 825-1062 1.07e-81

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: 268.35  E-value: 1.07e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  825 LLTLHPLELARQLTLLEFEMYKNVKPSELVGSPWTKKDKEV-KSPNLLKIMKHTTNVTRWIEKSITEAENYEERLAIMQR 903
Cdd:cd00155    1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKNIhLSPNLERFIERFNNLSNWVASEILLCTNPKKRARLLSK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  904 AIEVMMVMLELNNFNGILSIVAAMGTASVYRLRWTFQGLPERYRKFLEECRELSD--DHLKKYQERLRSI--NPPCVPFF 979
Cdd:cd00155   81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDpsRNFKNYRKLLKSVgpNPPCVPFL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  980 GRYLTNILHLEEGNPDLLAnTELINFSKRRKVAEIIGEIQQYQNQPYCLNEESTIRQFFEQLDPfnglsDKQMSDYLYNE 1059
Cdd:cd00155  161 GVYLKDLTFLHEGNPDFLE-GNLVNFEKRRKIAEILREIRQLQSNSYELNRDEDILAFLWKLLE-----LILNEDELYEL 234


                 ...
gi 18110536 1060 SLR 1062
Cdd:cd00155  235 SLE 237
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
825-1066 4.99e-80

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 263.72  E-value: 4.99e-80
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536     825 LLTLHPLELARQLTLLEFEMYKNVKPSELVGSPWTKKDKEVKSP-NLLKIMKHTTNVTRWIEKSITEAENYEERLAIMQR 903
Cdd:smart00147    1 LLLLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKKSPSPlNLEAFIRRFNEVSNWVATEILKQTTPKDRAELLSK 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536     904 AIEVMMVMLELNNFNGILSIVAAMGTASVYRLRWTFQGLPERYRKFLEECREL--SDDHLKKYQERLRSIN-PPCVPFFG 980
Cdd:smart00147   81 FIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELlsPERNYKNYREALSSCNlPPCIPFLG 160

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536     981 RYLTNILHLEEGNPDLLANTeLINFSKRRKVAEIIGEIQQYQNQPYCLN-EESTIRQFFEQLdpFNGLSDKqmsDYLYNE 1059
Cdd:smart00147  161 VLLKDLTFIDEGNPDFLENG-LVNFEKRRQIAEILREIRQLQSQPYNLRpNRSDIQSLLQQL--LDHLDEE---EELYQL 234


                    ....*..
gi 18110536    1060 SLRIEPR 1066
Cdd:smart00147  235 SLKIEPR 241
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 832-1009 1.99e-64

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


Pssm-ID: 459872  Cd Length: 179  Bit Score: 216.69  E-value: 1.99e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536    832 ELARQLTLLEFEMYKNVKPSELVGSPWTKKDKEVKSPNLLKIMKHTTNVTRWIEKSITEAENYEERLAIMQRAIEVMMVM 911
Cdd:pfam00617    1 ELARQLTLIEFELFRKIKPRELLGSAWSKKDKKENSPNIEAMIARFNKLSNWVASEILSEEDLKKRAKVIKKFIKIAEHC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536    912 LELNNFNGILSIVAAMGTASVYRLRWTFQGLPERYRKFLEECREL--SDDHLKKYQERLRSINPPCVPFFGRYLTNILHL 989
Cdd:pfam00617   81 RELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLmsPSRNFKNYREALSSASPPCIPFLGLYLTDLTFI 160

                          170       180
                   ....*....|....*....|
gi 18110536    990 EEGNPDLLaNTELINFSKRR 1009
Cdd:pfam00617  161 EEGNPDFL-EGGLINFEKRR 179
PH_SOS cd01261
Son of Sevenless (SOS) Pleckstrin homology (PH) domain; SOS is a Ras guanine nucleotide ...
 476-586 6.40e-46

Son of Sevenless (SOS) Pleckstrin homology (PH) domain; SOS is a Ras guanine nucleotide exchange factor. SOS is thought to transmit signals from activated receptor tyrosine kinases to the Ras signaling pathway. SOS contains a histone domain, Dbl-homology (DH), a PH domain, Rem domain, Cdc25 domain, and a Grb2 binding domain. The SOS PH domain binds to phosphatidylinositol-4,5-bisphosphate (PIP2) and phosphatidic acid (PA). SOS is dependent on Ras binding to the allosteric site via its histone domain for both a lower level of activity (Ras GDP) and maximal activity (Ras GTP). The DH domain blocks the allosteric Ras binding site in SOS. The PH domain is closely associated with the DH domain and the action of the DH-PH unit gates a reciprocal interaction between Ras and SOS. The C-terminal proline-rich domain of SOS binds to the adapter protein Grb2 which localizes the Sos protein to the plasma membrane and diminishes the negative effect of the C-terminal domain on the guanine nucleotide exchange activity of the CDC25-homology domain of SOS. 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: 269963  Cd Length: 109  Bit Score: 160.60  E-value: 6.40e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  476 QNCNEFIREDSLSKLGSGKRIwSERKVFLFDGLMVLCKANtKKQTPSAGATAyDYRLKEKYFMRRVDINDRPDSDDLKNS 555
Cdd:cd01261    1 QCCNEFIMEGTLGKVGSGKRK-TERHAFLFDGLLLLCKSN-RRRTSTGGPKP-EYRLKEKFFIRKVEINDLEDTEELKNA 77

                         90       100       110
                 ....*....|....*....|....*....|.
gi 18110536  556 FELAPRMQPPIVLTAKNAQHKHDWMADLLMV 586
Cdd:cd01261   78 FEIVPRDQPSVILFAKSAEEKNNWMAALVML 108
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 637-791 8.53e-41

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: 146.71  E-value: 8.53e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536     637 GVPMIKGATLCKLIERLTYHIY-ADPTFVRTFLTTYRYFCSPQQLLQLLVERFNIPDPslvyqdtgtagaggmggvggdk 715
Cdd:smart00229    1 DGGLIKGGTLEALIEHLTEAFDkADPSFVETFLLTYRSFITTQELLQLLLYRYNAIPP---------------------- 58

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18110536     716 ehkNSHREdwkryRKEYVQPVQFRVLNVLRHWVDHHFYDFEKDPMLLEKLLNFLEHVNGKSMRKWVDSVLKIVQRK 791
Cdd:smart00229   59 ---ESWVE-----EKVNPRRVKNRVLNILRTWVENYWEDFEDDPKLISFLLEFLELVDDEKYPGLVTSLLNLLRRL 126
HFD_SOS1_rpt1 cd22914
first histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ...
 68-145 2.07e-39

first histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; SOS-1 is a guanine nucleotide exchange factor for Ras that binds to GRB2. It promotes the exchange of Ras-bound GDP by GTP. It is a catalytic component of a trimeric complex that participates in transduction of signals from Ras to Rac, by promoting the Rac-specific guanine nucleotide exchange factor (GEF) activity. SOS-1 contains tandem histone folds at the N-terminal region. The model corresponds to the first repeat.


Pssm-ID: 467039  Cd Length: 78  Bit Score: 140.85  E-value: 2.07e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18110536   68 RWRGLFTPSLKKVLEQVHPRVTAKEDALLYVEKLCLRLLAMLCAKPlPHSVQDVEEKVNKSFPAPIDQWALNEAKEVI 145
Cdd:cd22914    1 KWRGLLVPALKKVQKQVHPTLVAKEDALEYIEELILQLLNMLCAAQ-PHSVQDVEERVQKTFPHPIDKWAIADAQAAL 77
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 645-790 1.23e-34

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: 129.07  E-value: 1.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  645 TLCKLIERLTYH-IYADPTFVRTFLTTYRYFCSPQQLLQLLVERFNIPDPSLVyqdtgtagaggmggvggdkehknshre 723
Cdd:cd06224    1 TLEALIEHLTSTfDMPDPSFVSTFLLTYRSFTTPTELLEKLIERYEIAPPENL--------------------------- 53

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18110536  724 DWKRYRKEYVQPVQFRVLNVLRHWVDHHFYDFEKDPMLLEKLLNFLEHVN--GKSMRKWVDSVLKIVQR 790
Cdd:cd06224   54 EYNDWDKKKSKPIRLRVLNVLRTWVENYPYDFFDDEELLELLEEFLNRLVqeGALLQELKKLLRKLLKL 122
HFD_SOS1_rpt2 cd22915
second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ...
 153-227 5.23e-34

second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; SOS-1 is a guanine nucleotide exchange factor for Ras that binds to GRB2. It promotes the exchange of Ras-bound GDP by GTP. It is a catalytic component of a trimeric complex that participates in transduction of signals from Ras to Rac, by promoting the Rac-specific guanine nucleotide exchange factor (GEF) activity. SOS-1 contains tandem histone folds at the N-terminal region. The model corresponds to the second repeat.


Pssm-ID: 467040  Cd Length: 75  Bit Score: 125.43  E-value: 5.23e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18110536  153 VLPTEKVHTLLQKDVLQYKIDSSVSAFLVAVLEYISADILKMAGDYVIKIAHCEITKEDIEVVMNADRVLMDMLN 227
Cdd:cd22915    1 LFPVDKIHPLLKKDLLVYKVDPQVSLYLVAVLEYIAADILKLAGNYVRNIRHYEITSQDIKVAMCADKVLMDLFG 75
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 641-768 2.37e-33

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: 124.72  E-value: 2.37e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536    641 IKGATLCKLIERLTYHIYA-DPTFVRTFLTTYRYFCSPQQLLQLLVERFNIPDPSLVYQDtgtagaggmggvggdkEHKN 719
Cdd:pfam00618    2 VKAGTLEKLVEYLTSTRIMlDDSFLSTFLLTYRSFTTPAELLELLIERYNIPPPLDLSSD----------------SYWI 65

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 18110536    720 SHREDwkryrkeyvqPVQFRVLNVLRHWVDHHFYDFEKDPMLLEKLLNF 768
Cdd:pfam00618   66 SKKTL----------PIRIRVLSVLRHWVENYFSDFNDDPVLLSRLEKF 104
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 249-432 3.25e-24

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: 101.22  E-value: 3.25e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  249 YEETVKELIHDEKQYQRDLHMIIRVFREELVKIVS--DPRELEPIFSNIMDIYEVTVTLLGSLEDVIEMSQeQSAPCVGS 326
Cdd:cd00160    1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLplSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWD-KSGPRIGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  327 CfeELAEAEEFDVYKKYAYDVTSQASRdaLNNLLSKpgASSLTTAGHGFRDAVKYY-LPKLLLVPICHAFVYFDYIKHL- 404
Cdd:cd00160   80 V--FLKLAPFFKIYSEYCSNHPDALEL--LKKLKKF--NKFFQEFLEKAESECGRLkLESLLLKPVQRLTKYPLLLKELl 153

                        170       180
                 ....*....|....*....|....*...
gi 18110536  405 KDLSSSQDDIESFEQVQGLLHPLHCDLE 432
Cdd:cd00160  154 KHTPDGHEDREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 253-433 3.65e-22

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: 95.45  E-value: 3.65e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536     253 VKELIHDEKQYQRDLHMIIRVFREELVKIVS--DPRELEPIFSNIMDIYEVTVTLLGSLEDVIEMSqEQSAPCVGSCfeE 330
Cdd:smart00325    2 LKELLQTERNYVRDLKLLVEVFLKPLKKELKllSPNELETLFGNIEEIYEFHRDFLDELEERIEEW-DDSVERIGDV--F 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536     331 LAEAEEFDVYKKYAYDVTSQASRdaLNNLLSKPGASSLTTAGHGFRDAVKYYLPKLLLVPICHAFVYFDYIKHLKDLSS- 409
Cdd:smart00325   79 LKLEEFFKIYSEYCSNHPDALEL--LKKLKKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLLLKELLKHTPe 156

                           170       180
                    ....*....|....*....|....
gi 18110536     410 SQDDIESFEQVQGLLHPLHCDLEK 433
Cdd:smart00325  157 DHEDREDLKKALKAIKELANQVNE 180
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 481-587 2.40e-12

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: 64.88  E-value: 2.40e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536     481 FIREDSLSKLGS-GKRIWSERKVFLFDGLMVLCKANTKKQtpsagatayDYRLKEKYFMR--RVDINDRPDSDDLKNSFE 557
Cdd:smart00233    1 VIKEGWLYKKSGgGKKSWKKRYFVLFNSTLLYYKSKKDKK---------SYKPKGSIDLSgcTVREAPDPDSSKKPHCFE 71

                            90       100       110
                    ....*....|....*....|....*....|
gi 18110536     558 LAPRMQPPIVLTAKNAQHKHDWMADLLMVI 587
Cdd:smart00233   72 IKTSDRKTLLLQAESEEEREKWVEALRKAI 101
PH_Collybistin_ASEF cd01224
Collybistin/APC-stimulated guanine nucleotide exchange factor pleckstrin homology (PH) domain; ...
 456-580 2.65e-09

Collybistin/APC-stimulated guanine nucleotide exchange factor pleckstrin homology (PH) domain; Collybistin (also called PEM2) is homologous to the Dbl proteins ASEF (also called ARHGEF4/RhoGEF4) and SPATA13 (Spermatogenesis-associated protein 13; also called ASEF2). It activates CDC42 specifically and not any other Rho-family GTPases. Collybistin consists of an SH3 domain, followed by a RhoGEF/DH and PH domain. In Dbl proteins, the DH and PH domains catalyze the exchange of GDP for GTP in Rho GTPases, allowing them to signal to downstream effectors. It induces submembrane clustering of the receptor-associated peripheral membrane protein gephyrin, which is thought to form a scaffold underneath the postsynaptic membrane linking receptors to the cytoskeleton. It also acts as a tumor suppressor that links adenomatous polyposis coli (APC) protein, a negative regulator of the Wnt signaling pathway and promotes the phosphorylation and degradation of beta-catenin, to Cdc42. Autoinhibition of collybistin is accomplished by the binding of its SH3 domain with both the RhoGEF and PH domains to block access of Cdc42 to the GTPase-binding site. Inactivation promotes cancer progression. 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: 269931  Cd Length: 138  Bit Score: 57.27  E-value: 2.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  456 IERTRELQMKVEHWEDKDVGQNCNEFIREDSLSKLGSGKRiwSERKVFLFDGLMVLCKANTKKqtpsagATAYDYrlKEK 535
Cdd:cd01224    4 LEKLAAWQSTVEGWEGEDLSDRSSELIHSGELTKISAGRA--QERTFFLFDHQLVYCKKDLLR------RKNYIY--KGR 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18110536  536 YFMRRVDINDRPDSDD------LKNSFELAPRMQPP-IVLTAKNAQHKHDWM 580
Cdd:cd01224   74 IDTDNMEIEDLPDGKDdesgvtVKNAWKIYNASKNKwYVLCAKSAEEKQRWL 125
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 482-587 5.41e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 55.26  E-value: 5.41e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536    482 IREDSLSKLGSGKRI-WSERKVFLFDGLMVLCKANTKKQtpsagatayDYRLKEKYFMR--RVDINDRPDSDDLKNSFEL 558
Cdd:pfam00169    2 VKEGWLLKKGGGKKKsWKKRYFVLFDGSLLYYKDDKSGK---------SKEPKGSISLSgcEVVEVVASDSPKRKFCFEL 72

                           90       100       110
                   ....*....|....*....|....*....|..
gi 18110536    559 APRMQPP---IVLTAKNAQHKHDWMADLLMVI 587
Cdd:pfam00169   73 RTGERTGkrtYLLQAESEEERKDWIKAIQSAI 104
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 253-327 3.82e-08

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: 54.61  E-value: 3.82e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18110536    253 VKELIHDEKQYQRDLHMIIRVFREELVKIVSD-PRELEPIFSNIMDIYEVTVTLLgsLEDVIEmsQEQSAPCVGSC 327
Cdd:pfam00621    2 IKELLQTERSYVRDLEILVEVFLPPNSKPLSEsEEEIKTIFSNIEEIYELHRQLL--LEELLK--EWISIQRIGDI 73
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1197-1502 6.85e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 6.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  1197 SVPAPHL--------PKKPGAHVWANNNSTLASASAMDVvfSPALPEHLPP----QSLPDSNPFASDTE----------- 1253
Cdd:PHA03247 2513 SRLAPAIlpdepvgePVHPRMLTWIRGLEELASDDAGDP--PPPLPPAAPPaapdRSVPPPRPAPRPSEpavtsrarrpd 2590

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  1254 APPSPlpklvVSPRHETGNRSPFHGRMQNSPTHSTASTVTLTGMSTSGGEEFCAGGFYFNSAHQGQPGAVPISPHVNVPM 1333
Cdd:PHA03247 2591 APPQS-----ARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPR 2665

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  1334 ATNMEYRAVPPPLPPRRKERTESCADMAQKRQAPDAPTlPPRDGELSPPPIPPRLNHSTGISYLRQSHGKSKEF----VG 1409
Cdd:PHA03247 2666 RARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPP-PPPTPEPAPHALVSATPLPPGPAAARQASPALPAApappAV 2744

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  1410 NSSLLLPNTSSIMIRR------NSAIEKRAAATSQPNQAAAGPISTTLVTVSQAVATDEPLPLPISPAASSSTTTSPLTP 1483
Cdd:PHA03247 2745 PAGPATPGGPARPARPpttagpPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824

                         330       340
                  ....*....|....*....|....*..
gi 18110536  1484 A--------MSPMSPNIPSHPVESTSS 1502
Cdd:PHA03247 2825 AgplppptsAQPTAPPPPPGPPPPSLP 2851
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 483-583 1.04e-05

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


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 45.61  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  483 REDSLSKLGSG-KRIWSERKVFLFDGLMVLCKANTKKqtpsagatayDYRLKEKYFMRRVDINDRPDSDDLKNSFELAPR 561
Cdd:cd00821    1 KEGYLLKRGGGgLKSWKKRWFVLFEGVLLYYKSKKDS----------SYKPKGSIPLSGILEVEEVSPKERPHCFELVTP 70

                         90       100
                 ....*....|....*....|..
gi 18110536  562 MQPPIVLTAKNAQHKHDWMADL 583
Cdd:cd00821   71 DGRTYYLQADSEEERQEWLKAL 92
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1154-1386 3.74e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 3.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  1154 EQSPQHNPHAFSVFAPviIPERNTSSWSGTPQHTRTdqnngEVSVPAPHLPKKPGAhvwANNNSTLASASAMDVVFSPAL 1233
Cdd:PHA03247 2705 PPTPEPAPHALVSATP--LPPGPAAARQASPALPAA-----PAPPAVPAGPATPGG---PARPARPPTTAGPPAPAPPAA 2774

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  1234 PEHLPPQSL--PDSNPFASDTEAPPSPL----PKLVVSPRHETGNRSPFHGRMQNSPTHSTASTVTLTG----MSTSGGE 1303
Cdd:PHA03247 2775 PAAGPPRRLtrPAVASLSESRESLPSPWdpadPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPgpppPSLPLGG 2854

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  1304 EFCAGGFYFNSAHQGQPGAVPISPhvNVPMATNMEYRAVPP-----PLPPRRKERTESCADMAQKR-----QAPDAPTLP 1373
Cdd:PHA03247 2855 SVAPGGDVRRRPPSRSPAAKPAAP--ARPPVRRLARPAVSRstesfALPPDQPERPPQPQAPPPPQpqpqpPPPPQPQPP 2932

                         250
                  ....*....|...
gi 18110536  1374 PRDGELSPPPIPP 1386
Cdd:PHA03247 2933 PPPPPRPQPPLAP 2945
PH_PLEKHG1_G2_G3 cd13243
Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) ...
 451-587 9.55e-05

Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) domain; PLEKHG1 (also called ARHGEF41), PLEKHG2 (also called ARHGEF42 or CLG/common-site lymphoma/leukemia guanine nucleotide exchange factor2), and PLEKHG3 (also called ARHGEF43) have RhoGEF DH/double-homology domains in tandem with a PH domain which is involved in phospholipid binding. They function as a guanine nucleotide exchange factor (GEF) and are involved in the regulation of Rho protein signal transduction. Mutations in PLEKHG1 have been associated panic disorder (PD), an anxiety disorder characterized by panic attacks and anticipatory anxiety. 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: 270063 [Multi-domain]  Cd Length: 147  Bit Score: 44.26  E-value: 9.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  451 RRQLAIERTRELQMKVEHWEDKDVgQNCNEFIREDSLSKLGSGkriwSERKVFLFDGLMVLCKantKKQTpsagaTAYDY 530
Cdd:cd13243   23 RKHEHAVRVQEIQSLLDGWEGPEL-TTYGDLVLEGTFRMAGAK----NERLLFLFDKMLLITK---KRED-----GILQY 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18110536  531 RLkekYFM-RRVDINDRPDSDDLknSFEL----APRMQppIVLTAKNAQHKHDWMADLLMVI 587
Cdd:cd13243   90 KT---HIMcSNLMLSESIPKEPL--SFQVlpfdNPKLQ--YTLQAKNQEQKRLWTQEIKRLI 144
PHA03378 PHA03378
EBNA-3B; Provisional
 1199-1468 2.09e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 46.21  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  1199 PAPHLPKK----PGAHVWA-----NNNSTLASASAMdvvfspalpehLPPQSLPDS--NPFASDTEA-PPSPLPKLVVSP 1266
Cdd:PHA03378  649 PTPHQPPQveitPYKPTWTqighiPYQPSPTGANTM-----------LPIQWAPGTmqPPPRAPTPMrPPAAPPGRAQRP 717

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  1267 RHETGNRSPFHGRMQNSPTHSTASTVTLTGMSTSGGEEFCAGGFYFNSAHQGQPGAVPISPHVNVPMATNMEYRAVPPPL 1346
Cdd:PHA03378  718 AAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQ 797

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  1347 PPrrkertescadmaqkrqapdaPTLPPRDGELSPPPIPPRLNHSTGISYLRQSHGKSKefvGNSSLLLPntssimirrn 1426
Cdd:PHA03378  798 PP---------------------PQAGPTSMQLMPRAAPGQQGPTKQILRQLLTGGVKR---GRPSLKKP---------- 843

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 18110536  1427 SAIEKRAAATSQPNqaaagPISTTLVTVSQAVATDEPLPLPI 1468
Cdd:PHA03378  844 AALERQAAAGPTPS-----PGSGTSDKIVQAPVFYPPVLQPI 880
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
147-197 7.86e-04

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 41.39  E-value: 7.86e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18110536  147 SKKRKSVLPTEKVHTLLQKDVLQYKIDSSVSAFLVAVLEYISADILKMAGD 197
Cdd:COG5262   20 SAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEILELAGN 70
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 147-196 9.57e-04

histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core component of the nucleosome, which wraps and compacts DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.


Pssm-ID: 467020  Cd Length: 89  Bit Score: 39.82  E-value: 9.57e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 18110536  147 SKKRKSVLPTEKVHTLLQKDVLQYKIDSSVSAFLVAVLEYISADILKMAG 196
Cdd:cd00074    4 SKRAGLQFPVGRIHRLLKKGTYAKRVGAGAPVYLAAVLEYLTAEILELAG 53
PH_puratrophin-1 cd13242
Puratrophin-1 pleckstrin homology (PH) domain; Puratrophin-1 (also called Purkinje cell ...
 478-583 1.34e-03

Puratrophin-1 pleckstrin homology (PH) domain; Puratrophin-1 (also called Purkinje cell atrophy-associated protein 1 or PLEKHG4/Pleckstrin homology domain-containing family G member 4) contains a spectrin repeat, a RhoGEF (DH) domain, and a PH domain. It is thought to function in intracellular signaling and cytoskeleton dynamics at the Golgi. Puratrophin-1 is expressed in kidney, Leydig cells in the testis, epithelial cells in the prostate gland and Langerhans islet in the pancreas. A single nucleotide substitution in the puratrophin-1 gene were once thought to result in autosomal dominant cerebellar ataxia (ADCA), but now it has been demonstrated that this ataxia is a result of defects in the BEAN gene. Puratrophin contains a domain architecture similar to that of Dbl family members Dbs and Trio. Dbs is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a RhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Trio is a multidomain signaling protein that contains two RhoGEF(DH)-PH domains in tandem. 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: 270062  Cd Length: 136  Bit Score: 40.74  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  478 CNEFIREDSLSKLGSGKRiwSERKVFLFDGLMVLCKanTKKqtPSAGATAYDYrlkeKYFMRRVDINDRPDSDDLKNSFE 557
Cdd:cd13242   26 QGQLLRQDEFLVWQGRKK--CLRHVFLFEDLILFSK--PKK--TPGGKDVYIY----KHSIKTSDIGLTENVGDSGLKFE 95

                         90       100
                 ....*....|....*....|....*....
gi 18110536  558 LAPRMQPP---IVLTAKNAQHKHDWMADL 583
Cdd:cd13242   96 IWFRRRKArdtYILQATSPEIKQAWTSDI 124
SOBP pfam15279
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
 1217-1386 3.34e-03

Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual disability. It carries a zinc-finger of the zf-C2H2 type at the N-terminus, and a highly characteriztic C-terminal PhPhPhPhPhPh motif. The deduced 873-amino acid protein contains an N-terminal nuclear localization signal (NLS), followed by 2 FCS-type zinc finger motifs, a proline-rich region (PR1), a putative RNA-binding motif region, and a C-terminal NLS embedded in a second proline-rich motif. SOBP is expressed in various human tissues, including developing mouse brain at embryonic day 14. In postnatal and adult mouse brain SOBP is expressed in all neurons, with intense staining in the limbic system. Highest expression is in layer V cortical neurons, hippocampus, pyriform cortex, dorsomedial nucleus of thalamus, amygdala, and hypothalamus. Postnatal expression of SOBP in the limbic system corresponds to a time of active synaptogenesis. the family is also referred to as Jackson circler, JXC1. In seven affected siblings from a consanguineous Israeli Arab family with mental retardation, anterior maxillary protrusion, and strabismus mutations were found in this protein.


Pssm-ID: 464609 [Multi-domain]  Cd Length: 325  Bit Score: 41.34  E-value: 3.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536   1217 STLASASAMDVVFSPALPEHL--PPQSLPDSNPFASDTEAPPSPLPKLVvsPRHETGNRSPFHgrmqnSPTHSTASTVTL 1294
Cdd:pfam15279   98 SSSASPSSSPTSSNSSKPLISvaSSSKLLAPKPHEPPSLPPPPLPPKKG--RRHRPGLHPPLG-----RPPGSPPMSMTP 170

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536   1295 TGMSTSGGEEFCAGGFYFNSAHQG-QPGAVPISPHV---NVPMATNMEYRAVPPPLPPRRKERTESCAD--MAQKRQAPD 1368
Cdd:pfam15279  171 RGLLGKPQQHPPPSPLPAFMEPSSmPPPFLRPPPSIpqpNSPLSNPMLPGIGPPPKPPRNLGPPSNPMHrpPFSPHHPPP 250

                          170
                   ....*....|....*...
gi 18110536   1369 APTLPPrdgelSPPPIPP 1386
Cdd:pfam15279  251 PPTPPG-----PPPGLPP 263
PH1_Kalirin_Trio_like cd13240
Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; ...
 499-591 3.57e-03

Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; RhoGEFs, Kalirin and Trio, the mammalian homologs of Drosophila Trio and Caenorhabditis elegans UNC-73 regulate a novel step in secretory granule maturation. Their signaling modulates the extent to which regulated cargo enter and remain in the regulated secretory pathway. This allows for fine tuning of peptides released by a single secretory cell type with impaired signaling leading to pathological states. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Kalirin and Trio are encoded by separate genes in mammals and by a single one in invertebrates. Kalirin and Trio share the same complex multidomain structure and display several splice variants. The longest Kalirin and Trio proteins have a Sec14 domain, a stretch of spectrin repeats, a RhoGEF(DH)/PH cassette (also called GEF1), an SH3 domain, a second RhoGEF(DH)/PH cassette (also called GEF2), a second SH3 domain, Ig/FNIII domains, and a kinase domain. The first RhoGEF(DH)/PH cassette catalyzes exchange on Rac1 and RhoG while the second RhoGEF(DH)/PH cassette is specific for RhoA. Kalirin and Trio are closely related to p63RhoGEF and have PH domains of similar function. 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.


Pssm-ID: 270060  Cd Length: 123  Bit Score: 38.90  E-value: 3.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110536  499 ERKVFLFDGLMVLckanTKKQTPSAGATAYDYrlKEKYFMRRVDINDRPDSDDLKnsFELAPRMQPP----IVLTAKNAQ 574
Cdd:cd13240   35 ERHVFLFELCLVF----SKEVKDSNGKSKYIY--KSRLMTSEIGVTEHIEGDPCK--FALWTGRVPTsdnkIVLKASSLE 106

                         90
                 ....*....|....*..
gi 18110536  575 HKHDWMADLLMVITKSM 591
Cdd:cd13240  107 VKQTWVKKLREVIQERI 123
H2A smart00414
Histone 2A;
155-227 6.95e-03

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 37.70  E-value: 6.95e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18110536     155 PTEKVHTLLQKDVLQYKIDSSVSAFLVAVLEYISADILKMAGDYVIKIAHCEITKEDIEVVMNADRVLMDMLN 227
Cdd:smart00414   11 PVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNKLLK 83
 
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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