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Conserved domains on  [gi|2217360702|ref|XP_047274490|]
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disheveled-associated activator of morphogenesis 2 isoform X6 [Homo sapiens]

Protein Classification

formin homology family protein( domain architecture ID 10273102)

formin homology family protein is a cytoskeletal remodeling protein that may be involved a diverse array of cellular functions including the regulation of actin dynamics as well as the stability and organization of microtubules

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
646-1020 1.10e-138

Formin Homology 2 Domain;


:

Pssm-ID: 396655  Cd Length: 372  Bit Score: 423.22  E-value: 1.10e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702  646 KKRVPQPSHPLKSFNWVKLNEERVPGTVWNEIDDMQVFRILDLEDFEKMFSAYQRHQKELGStEDIYLASRKVKELSVID 725
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKS-EDKSSSKKKPKEVSLLD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702  726 GRRAQNCIILLSKLKLSNEEIRQAILKMDEqEDLAKDMLEQLLKFIPEKSDIDLLEEHKHEIERMARADRFLYEMSRIDH 805
Cdd:pfam02181   80 PKRAQNIAILLRKLKLPPEEIIQAILEGDE-DALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKIPR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702  806 YQQRLQALFFKKKFQERLAEAKPKVEAILLASRELVRSKRLRQMLEVILAIGNFMNKGQ-RGGAYGFRVASLNKIADTKS 884
Cdd:pfam02181  159 LEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTrRGQAKGFKLSSLLKLSDTKS 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702  885 SiDRNISLLHYLIMILEKHFPDILNMPSELQHLPEAAKVNLAELEKEVGNLRRGLRAVEVELEYQrRQVREPSDKFVPVM 964
Cdd:pfam02181  239 T-DNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELS-ALDEHPDDKFREVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217360702  965 SDFITVSSFSFSELEDQLNEARDKFAKALMHFGEHDSKMQPDEFFGIFDTFLQAFS 1020
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEFK 372
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
282-486 3.08e-62

Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.


:

Pssm-ID: 461885 [Multi-domain]  Cd Length: 195  Bit Score: 210.21  E-value: 3.08e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702  282 GGHKKVLQAMLHYQVYAAERTRFQTLLNELDRSlgrYRDEVNLKTAIMSFINAVLNAGageDNLEFRLHLRYEFLMLGIQ 361
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSS---ENDNVEYKVATMQFINALVNSP---EDLQFRLHLRSEFTALGLD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702  362 PVIDKLRQHENAILDKHLDFFEMVRNEDDLELARRFDMVHIDTKSASQMFELIHKKLKYTEAYPCLLSVLHHCLQMpYKR 441
Cdd:pfam06367   75 RILDKLRELENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLI-RDD 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2217360702  442 NGGYFQQWQLLDRILQQIVLQDErgvDPDLAPLENFNVKNIVNML 486
Cdd:pfam06367  154 EEELPSYWKLLEELVSQIVLHRT---KPDPKFDERKNLEIDINRL 195
Drf_GBD super family cl05720
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
92-279 3.33e-49

Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, leading to activation of the Drf protein.


The actual alignment was detected with superfamily member pfam06371:

Pssm-ID: 461886  Cd Length: 188  Bit Score: 172.89  E-value: 3.33e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702   92 PIPNAEELNIRFAELVDELDLTDKNREAMFALPPEKKWQIYCSKK----KEQEDPNKL-----ATSWPDYYIDRINSmaa 162
Cdd:pfam06371    2 PKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKstnfQKEGGGSKSdsesnETGSPEYYVKKLKD--- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702  163 mqslyafdeeeTEMRNQVVEDLKTALRTQPMRFVTRFIELEGLTCLLNFLRSMDHATCESR----IHTSLIGCIKALMNN 238
Cdd:pfam06371   79 -----------DSISSKQLESLRVALRTQPLSWVRRFIEAQGLGALLNVLSKINRKKSQEEedldREYEILKCLKALMNN 147
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2217360702  239 SQGRAHVLAQPEAISTIAQSLRTENSKTKVAVLEILGAVCL 279
Cdd:pfam06371  148 KFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
646-1020 1.10e-138

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 423.22  E-value: 1.10e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702  646 KKRVPQPSHPLKSFNWVKLNEERVPGTVWNEIDDMQVFRILDLEDFEKMFSAYQRHQKELGStEDIYLASRKVKELSVID 725
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKS-EDKSSSKKKPKEVSLLD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702  726 GRRAQNCIILLSKLKLSNEEIRQAILKMDEqEDLAKDMLEQLLKFIPEKSDIDLLEEHKHEIERMARADRFLYEMSRIDH 805
Cdd:pfam02181   80 PKRAQNIAILLRKLKLPPEEIIQAILEGDE-DALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKIPR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702  806 YQQRLQALFFKKKFQERLAEAKPKVEAILLASRELVRSKRLRQMLEVILAIGNFMNKGQ-RGGAYGFRVASLNKIADTKS 884
Cdd:pfam02181  159 LEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTrRGQAKGFKLSSLLKLSDTKS 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702  885 SiDRNISLLHYLIMILEKHFPDILNMPSELQHLPEAAKVNLAELEKEVGNLRRGLRAVEVELEYQrRQVREPSDKFVPVM 964
Cdd:pfam02181  239 T-DNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELS-ALDEHPDDKFREVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217360702  965 SDFITVSSFSFSELEDQLNEARDKFAKALMHFGEHDSKMQPDEFFGIFDTFLQAFS 1020
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEFK 372
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
647-1025 2.72e-77

Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, especially in the context of cytokinesis and cell polarisation. Members of this family have been found to interact with Rho-GTPases, profilin and other actin-assoziated proteins. These interactions are mediated by the proline-rich FH1 domain, usually located in front of FH2 (but not listed in SMART). Despite this cytosolic function, vertebrate formins have been assigned functions within the nucleus. A set of Formin-Binding Proteins (FBPs) has been shown to bind FH1 with their WW domain.


Pssm-ID: 214697 [Multi-domain]  Cd Length: 392  Bit Score: 259.97  E-value: 2.72e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702   647 KRVPQPSHPLKSFNWVKLNEERVPGTVWNEIDDMQvfrILDLEDFEKMFSAYQRHQKELGSTED--IYLASRKVKELSVI 724
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFSAKEKTKSASKDVSEkkSILKKKASQEFKIL 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702   725 DGRRAQNCIILLSKLKLSNEEIRQAILKMDEqEDLAKDMLEQLLKFIPEKSDIDLLEEHKHE-IERMARADRFLYEMSRI 803
Cdd:smart00498   78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDE-DVLSVDLLEQLLKYAPTKEELKKLREYKEEdPEELARAEQFLLLISNI 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702   804 DHYQQRLQALFFKKKFQERLAEAKPKVEAILLASRELVRSKRLRQMLEVILAIGNFMNKG-QRGGAYGFRVASLNKIADT 882
Cdd:smart00498  157 PYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGsRRGQAYGFKLSSLLKLSDV 236
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702   883 KSSiDRNISLLHYLIMILEKHFpdILNMPSELQHlpeaakvnlaelekevgnlrrglraveveleyqrrqvrepSDKFVP 962
Cdd:smart00498  237 KSA-DNKTTLLHFLVKIIRKKY--LGGLSDPENL----------------------------------------DDKFIE 273
                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217360702   963 VMSDFITVSSFSFSELEDQLNEARDKFAKALMHFGEHDSKMQPDEFFGIFDTFLQAFSEARQD 1025
Cdd:smart00498  274 VMKPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEE 336
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
282-486 3.08e-62

Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.


Pssm-ID: 461885 [Multi-domain]  Cd Length: 195  Bit Score: 210.21  E-value: 3.08e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702  282 GGHKKVLQAMLHYQVYAAERTRFQTLLNELDRSlgrYRDEVNLKTAIMSFINAVLNAGageDNLEFRLHLRYEFLMLGIQ 361
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSS---ENDNVEYKVATMQFINALVNSP---EDLQFRLHLRSEFTALGLD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702  362 PVIDKLRQHENAILDKHLDFFEMVRNEDDLELARRFDMVHIDTKSASQMFELIHKKLKYTEAYPCLLSVLHHCLQMpYKR 441
Cdd:pfam06367   75 RILDKLRELENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLI-RDD 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2217360702  442 NGGYFQQWQLLDRILQQIVLQDErgvDPDLAPLENFNVKNIVNML 486
Cdd:pfam06367  154 EEELPSYWKLLEELVSQIVLHRT---KPDPKFDERKNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
92-279 3.33e-49

Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, leading to activation of the Drf protein.


Pssm-ID: 461886  Cd Length: 188  Bit Score: 172.89  E-value: 3.33e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702   92 PIPNAEELNIRFAELVDELDLTDKNREAMFALPPEKKWQIYCSKK----KEQEDPNKL-----ATSWPDYYIDRINSmaa 162
Cdd:pfam06371    2 PKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKstnfQKEGGGSKSdsesnETGSPEYYVKKLKD--- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702  163 mqslyafdeeeTEMRNQVVEDLKTALRTQPMRFVTRFIELEGLTCLLNFLRSMDHATCESR----IHTSLIGCIKALMNN 238
Cdd:pfam06371   79 -----------DSISSKQLESLRVALRTQPLSWVRRFIEAQGLGALLNVLSKINRKKSQEEedldREYEILKCLKALMNN 147
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2217360702  239 SQGRAHVLAQPEAISTIAQSLRTENSKTKVAVLEILGAVCL 279
Cdd:pfam06371  148 KFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
646-1020 1.10e-138

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 423.22  E-value: 1.10e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702  646 KKRVPQPSHPLKSFNWVKLNEERVPGTVWNEIDDMQVFRILDLEDFEKMFSAYQRHQKELGStEDIYLASRKVKELSVID 725
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKS-EDKSSSKKKPKEVSLLD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702  726 GRRAQNCIILLSKLKLSNEEIRQAILKMDEqEDLAKDMLEQLLKFIPEKSDIDLLEEHKHEIERMARADRFLYEMSRIDH 805
Cdd:pfam02181   80 PKRAQNIAILLRKLKLPPEEIIQAILEGDE-DALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKIPR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702  806 YQQRLQALFFKKKFQERLAEAKPKVEAILLASRELVRSKRLRQMLEVILAIGNFMNKGQ-RGGAYGFRVASLNKIADTKS 884
Cdd:pfam02181  159 LEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTrRGQAKGFKLSSLLKLSDTKS 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702  885 SiDRNISLLHYLIMILEKHFPDILNMPSELQHLPEAAKVNLAELEKEVGNLRRGLRAVEVELEYQrRQVREPSDKFVPVM 964
Cdd:pfam02181  239 T-DNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELS-ALDEHPDDKFREVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217360702  965 SDFITVSSFSFSELEDQLNEARDKFAKALMHFGEHDSKMQPDEFFGIFDTFLQAFS 1020
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEFK 372
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
647-1025 2.72e-77

Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, especially in the context of cytokinesis and cell polarisation. Members of this family have been found to interact with Rho-GTPases, profilin and other actin-assoziated proteins. These interactions are mediated by the proline-rich FH1 domain, usually located in front of FH2 (but not listed in SMART). Despite this cytosolic function, vertebrate formins have been assigned functions within the nucleus. A set of Formin-Binding Proteins (FBPs) has been shown to bind FH1 with their WW domain.


Pssm-ID: 214697 [Multi-domain]  Cd Length: 392  Bit Score: 259.97  E-value: 2.72e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702   647 KRVPQPSHPLKSFNWVKLNEERVPGTVWNEIDDMQvfrILDLEDFEKMFSAYQRHQKELGSTED--IYLASRKVKELSVI 724
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFSAKEKTKSASKDVSEkkSILKKKASQEFKIL 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702   725 DGRRAQNCIILLSKLKLSNEEIRQAILKMDEqEDLAKDMLEQLLKFIPEKSDIDLLEEHKHE-IERMARADRFLYEMSRI 803
Cdd:smart00498   78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDE-DVLSVDLLEQLLKYAPTKEELKKLREYKEEdPEELARAEQFLLLISNI 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702   804 DHYQQRLQALFFKKKFQERLAEAKPKVEAILLASRELVRSKRLRQMLEVILAIGNFMNKG-QRGGAYGFRVASLNKIADT 882
Cdd:smart00498  157 PYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGsRRGQAYGFKLSSLLKLSDV 236
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702   883 KSSiDRNISLLHYLIMILEKHFpdILNMPSELQHlpeaakvnlaelekevgnlrrglraveveleyqrrqvrepSDKFVP 962
Cdd:smart00498  237 KSA-DNKTTLLHFLVKIIRKKY--LGGLSDPENL----------------------------------------DDKFIE 273
                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217360702   963 VMSDFITVSSFSFSELEDQLNEARDKFAKALMHFGEHDSKMQPDEFFGIFDTFLQAFSEARQD 1025
Cdd:smart00498  274 VMKPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEE 336
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
282-486 3.08e-62

Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.


Pssm-ID: 461885 [Multi-domain]  Cd Length: 195  Bit Score: 210.21  E-value: 3.08e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702  282 GGHKKVLQAMLHYQVYAAERTRFQTLLNELDRSlgrYRDEVNLKTAIMSFINAVLNAGageDNLEFRLHLRYEFLMLGIQ 361
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSS---ENDNVEYKVATMQFINALVNSP---EDLQFRLHLRSEFTALGLD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702  362 PVIDKLRQHENAILDKHLDFFEMVRNEDDLELARRFDMVHIDTKSASQMFELIHKKLKYTEAYPCLLSVLHHCLQMpYKR 441
Cdd:pfam06367   75 RILDKLRELENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLI-RDD 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2217360702  442 NGGYFQQWQLLDRILQQIVLQDErgvDPDLAPLENFNVKNIVNML 486
Cdd:pfam06367  154 EEELPSYWKLLEELVSQIVLHRT---KPDPKFDERKNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
92-279 3.33e-49

Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, leading to activation of the Drf protein.


Pssm-ID: 461886  Cd Length: 188  Bit Score: 172.89  E-value: 3.33e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702   92 PIPNAEELNIRFAELVDELDLTDKNREAMFALPPEKKWQIYCSKK----KEQEDPNKL-----ATSWPDYYIDRINSmaa 162
Cdd:pfam06371    2 PKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKstnfQKEGGGSKSdsesnETGSPEYYVKKLKD--- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702  163 mqslyafdeeeTEMRNQVVEDLKTALRTQPMRFVTRFIELEGLTCLLNFLRSMDHATCESR----IHTSLIGCIKALMNN 238
Cdd:pfam06371   79 -----------DSISSKQLESLRVALRTQPLSWVRRFIEAQGLGALLNVLSKINRKKSQEEedldREYEILKCLKALMNN 147
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2217360702  239 SQGRAHVLAQPEAISTIAQSLRTENSKTKVAVLEILGAVCL 279
Cdd:pfam06371  148 KFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
DUF4795 pfam16043
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. ...
737-824 8.72e-03

Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 285 and 978 amino acids in length.


Pssm-ID: 464990 [Multi-domain]  Cd Length: 181  Bit Score: 38.44  E-value: 8.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360702  737 SKLKLSNEEIRQAILKMDEQEDLAKDMLEQLLKFIPEKSDIDLLEEHKHEIE-RMARADRFLYEMSRIDhyqQRLQALFF 815
Cdd:pfam16043   88 ETLEELNQMLQELLDKLEGQEDAWKKALETLSEELDTKLDRLELDPLKELLErRIKALQKLLQEGSEEL---DEAEAAGF 164

                   ....*....
gi 2217360702  816 KKKFQERLA 824
Cdd:pfam16043  165 RKKLLERFH 173
 
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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