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Conserved domains on  [gi|220902586|gb|AAF49761|]
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Formin-like, isoform A [Drosophila melanogaster]

Protein Classification

Drf_FH3 and FH2 domain-containing protein (domain architecture ID 10273102)

protein containing domains Drf_GBD, Drf_FH3, and FH2

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
687-1063 6.74e-123

Formin Homology 2 Domain;


:

Pssm-ID: 280362  Cd Length: 372  Bit Score: 383.15  E-value: 6.74e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   687 IKRKVPTKYKLPTLNWIALKPNQVRGTIFNELDDEKIFKQIDFNEFEERFKIGiggalrngSNGTEVDGSLQSSKRFKRP 766
Cdd:pfam02181    1 IKKPIKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAK--------AKTKKNKKSEKSKSSKKKP 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   767 DNVSLLEHTRLRNIAISRRKLGMPIDDVIAAIHSLDLKKLSLENVELLQKMVPTDAEVKSYKEYiieRKDQQLLTEEDKF 846
Cdd:pfam02181   73 KKVTLLDPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEY---KGDPSELGRAEQF 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   847 MLQLSRVERISSKLAIMNYMGNFVDSVHLISPQVQSIAGASTSLKQSRKFKAVLEIVLAFGNYLNS-NKRGPAYGFKLQS 925
Cdd:pfam02181  150 LLELSKIPRLEARLRALLFKSTFEEEVEELKPSLEALIAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSS 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   926 LDTLIDTKSTDKRSSLLHYIVATIRAKFPELLNFESELYGTDKAASVALENVVADVQELEKGMDLVRKEAELRVKGAQ-- 1003
Cdd:pfam02181  230 LLKLSDTKSTDNKTTLLHYLVKIIREKFPELLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDEHpd 309
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 220902586  1004 ---THILRDFLNNSEDKLKKIKSDLRHAQEAFKECVEYFGDSSRNADAAAFFALIVRFTRAFK 1063
Cdd:pfam02181  310 dkfREVLKEFLKEAEEKLDKLESLLREALELFKELVEYFGEDPKETSPNEFFKILRDFLKEFK 372
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
374-567 1.70e-54

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


:

Pssm-ID: 336384  Cd Length: 195  Bit Score: 188.25  E-value: 1.70e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   374 GGHEIILGSFDNFKDVCQEKRRFQTLMEYFMNFEAFNIDFMVACMQFMNIVVHSVEDMNYRVHLQYEFTALGLDKYLERI 453
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFRSLVGALDSSENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTRLGLDRILDKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   454 RLTESEELKVQISAYLDNVF-DVAALMEDSETKTSALERVQELEDQLEREIDRNSEFLYKYAELESEsLTLKTEREQLAM 532
Cdd:pfam06367   81 RELENEELDDQLQIFEENREeDVEELLERFDDVNVDLDDPSELFELLKNKLKDTEAEPHLLSILQHL-LLIRDDEEELPQ 159
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 220902586   533 IRQKLEEELTVMQRMLQHNEQELKKRDTLLHTKNM 567
Cdd:pfam06367  160 YWKLLEELVSQIVLHRTKPDPAFDERKNLEIDINR 194
Drf_GBD super family cl05720
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
77-371 1.42e-17

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: 310750  Cd Length: 190  Bit Score: 81.98  E-value: 1.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586    77 PMPTTDELDRRFAKVLASMDLPPDKAKLLRNYDDEKKWDMICDQEMVQAKDPpshYLSKLRTYLDPKASRShrlylfyFL 156
Cdd:pfam06371    2 QKPDEDEILKLFEELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYLKTNFQGE---GGSKSDSKSNETGSPE-------YY 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   157 CQKRKMVGESTST-QVLRDLEISLRTNHIEWVKEFLDdtNQGLDALVDYLsfrlqmmrheqrlqgvlcaseerlnltngg 235
Cdd:pfam06371   72 VKKLKDDSIDSSLsKCLESLRVALRSQPLSWVRRFIG--AQGLSALLNIL------------------------------ 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   236 dggeivmgnsssvspgggggllshgnstghglangtldsrqqhtmsygflrptiadaldspslkrrSRHIAKLNMGAATD 315
Cdd:pfam06371  120 ------------------------------------------------------------------SKINRKKAQSEEDL 133
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 220902586   316 DIHVSIM-CLRAIMNNKYGFNMVIQHREAINCIALSLIHKSLRTKALVLELLAAICL 371
Cdd:pfam06371  134 KIEYEILkCLKALMNNKFGLDHVLGHPSSILLLAQSLDSERLKTRKLALELLTALCL 190
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
687-1063 6.74e-123

Formin Homology 2 Domain;


Pssm-ID: 280362  Cd Length: 372  Bit Score: 383.15  E-value: 6.74e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   687 IKRKVPTKYKLPTLNWIALKPNQVRGTIFNELDDEKIFKQIDFNEFEERFKIGiggalrngSNGTEVDGSLQSSKRFKRP 766
Cdd:pfam02181    1 IKKPIKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAK--------AKTKKNKKSEKSKSSKKKP 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   767 DNVSLLEHTRLRNIAISRRKLGMPIDDVIAAIHSLDLKKLSLENVELLQKMVPTDAEVKSYKEYiieRKDQQLLTEEDKF 846
Cdd:pfam02181   73 KKVTLLDPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEY---KGDPSELGRAEQF 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   847 MLQLSRVERISSKLAIMNYMGNFVDSVHLISPQVQSIAGASTSLKQSRKFKAVLEIVLAFGNYLNS-NKRGPAYGFKLQS 925
Cdd:pfam02181  150 LLELSKIPRLEARLRALLFKSTFEEEVEELKPSLEALIAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSS 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   926 LDTLIDTKSTDKRSSLLHYIVATIRAKFPELLNFESELYGTDKAASVALENVVADVQELEKGMDLVRKEAELRVKGAQ-- 1003
Cdd:pfam02181  230 LLKLSDTKSTDNKTTLLHYLVKIIREKFPELLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDEHpd 309
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 220902586  1004 ---THILRDFLNNSEDKLKKIKSDLRHAQEAFKECVEYFGDSSRNADAAAFFALIVRFTRAFK 1063
Cdd:pfam02181  310 dkfREVLKEFLKEAEEKLDKLESLLREALELFKELVEYFGEDPKETSPNEFFKILRDFLKEFK 372
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
688-1073 3.03e-61

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  Cd Length: 392  Bit Score: 214.91  E-value: 3.03e-61
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586    688 KRKVPTKYKLPTLNWIALKPNQVRGTIFNELDDEKIFkqiDFNEFEERFkigiggALRNGSNGTEVDGSLQSSKRFKRPD 767
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEESEG---DLDELEELF------SAKEKTKSASKDVSEKKSILKKKAS 71
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586    768 -NVSLLEHTRLRNIAISRRKLGMPIDDVIAAIHSLDLKKLSLENVELLQKMVPTDAEVKSYKEYiiERKDQQLLTEEDKF 846
Cdd:smart00498   72 qEFKILDPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREY--KEEDPEELARAEQF 149
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586    847 MLQLSRVERISSKLAIMNYMGNFVDSVHLISPQVQSIAGASTSLKQSRKFKAVLEIVLAFGNYLNS-NKRGPAYGFKLQS 925
Cdd:smart00498  150 LLLISNIPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGgSRRGQAYGFKLSS 229
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586    926 LDTLIDTKSTDKRSSLLHYIVATIRAKFpeLLNFESELYGTDKAASVALEnvvadvqelekgmdlvrkeaelrvkgaqth 1005
Cdd:smart00498  230 LLKLSDVKSADNKTTLLHFLVKIIRKKY--LGGLSDPENLDDKFIEVMKP------------------------------ 277
                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 220902586   1006 ilrdFLNNSEDKLKKIKSDLRHAQEAFKECVEYFGDSSRNADAAAFFALIVRFTRAFKQHDQENEQRL 1073
Cdd:smart00498  278 ----FLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKE 341
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
374-567 1.70e-54

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


Pssm-ID: 336384  Cd Length: 195  Bit Score: 188.25  E-value: 1.70e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   374 GGHEIILGSFDNFKDVCQEKRRFQTLMEYFMNFEAFNIDFMVACMQFMNIVVHSVEDMNYRVHLQYEFTALGLDKYLERI 453
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFRSLVGALDSSENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTRLGLDRILDKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   454 RLTESEELKVQISAYLDNVF-DVAALMEDSETKTSALERVQELEDQLEREIDRNSEFLYKYAELESEsLTLKTEREQLAM 532
Cdd:pfam06367   81 RELENEELDDQLQIFEENREeDVEELLERFDDVNVDLDDPSELFELLKNKLKDTEAEPHLLSILQHL-LLIRDDEEELPQ 159
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 220902586   533 IRQKLEEELTVMQRMLQHNEQELKKRDTLLHTKNM 567
Cdd:pfam06367  160 YWKLLEELVSQIVLHRTKPDPAFDERKNLEIDINR 194
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
77-371 1.42e-17

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


Pssm-ID: 310750  Cd Length: 190  Bit Score: 81.98  E-value: 1.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586    77 PMPTTDELDRRFAKVLASMDLPPDKAKLLRNYDDEKKWDMICDQEMVQAKDPpshYLSKLRTYLDPKASRShrlylfyFL 156
Cdd:pfam06371    2 QKPDEDEILKLFEELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYLKTNFQGE---GGSKSDSKSNETGSPE-------YY 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   157 CQKRKMVGESTST-QVLRDLEISLRTNHIEWVKEFLDdtNQGLDALVDYLsfrlqmmrheqrlqgvlcaseerlnltngg 235
Cdd:pfam06371   72 VKKLKDDSIDSSLsKCLESLRVALRSQPLSWVRRFIG--AQGLSALLNIL------------------------------ 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   236 dggeivmgnsssvspgggggllshgnstghglangtldsrqqhtmsygflrptiadaldspslkrrSRHIAKLNMGAATD 315
Cdd:pfam06371  120 ------------------------------------------------------------------SKINRKKAQSEEDL 133
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 220902586   316 DIHVSIM-CLRAIMNNKYGFNMVIQHREAINCIALSLIHKSLRTKALVLELLAAICL 371
Cdd:pfam06371  134 KIEYEILkCLKALMNNKFGLDHVLGHPSSILLLAQSLDSERLKTRKLALELLTALCL 190
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
450-593 2.97e-05

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 48.17  E-value: 2.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586  450 LERIRLTESEELKVQISAYLDNVFDVAALMEDSETKTSALER-VQELEDQLEREIDRNSEFLYKYAELESESLTLKTERE 528
Cdd:COG1196   363 LEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKReIESLEERLERLSERLEDLKEELKELEAELEELQTELE 442
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 220902586  529 QLAMIRQKLEEELTVMQRMLQHNEQELKKRDTLLHTKNMELQTLSRSLPRSASSGDGSLANGGLM 593
Cdd:COG1196   443 ELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVL 507
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
484-576 1.27e-04

SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.


Pssm-ID: 275056 [Multi-domain]  Cd Length: 198  Bit Score: 44.23  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   484 TKTSALERVQELEDQLEREIDRNSEFLYKYAELESESLTLKTEREQLAMIRQKLEEELTVMQRmLQHNEQELKKRDTLLH 563
Cdd:TIGR04211   60 DTPSARERLPELQQELAELQEELAELQEQLAELRQENQELKQQLSTLEAELEELQKELERIKQ-ISANAIELDEENRELR 138
                           90
                   ....*....|...
gi 220902586   564 TKNMELQTLSRSL 576
Cdd:TIGR04211  139 EELAELKQENEAL 151
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
687-1063 6.74e-123

Formin Homology 2 Domain;


Pssm-ID: 280362  Cd Length: 372  Bit Score: 383.15  E-value: 6.74e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   687 IKRKVPTKYKLPTLNWIALKPNQVRGTIFNELDDEKIFKQIDFNEFEERFKIGiggalrngSNGTEVDGSLQSSKRFKRP 766
Cdd:pfam02181    1 IKKPIKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAK--------AKTKKNKKSEKSKSSKKKP 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   767 DNVSLLEHTRLRNIAISRRKLGMPIDDVIAAIHSLDLKKLSLENVELLQKMVPTDAEVKSYKEYiieRKDQQLLTEEDKF 846
Cdd:pfam02181   73 KKVTLLDPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEY---KGDPSELGRAEQF 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   847 MLQLSRVERISSKLAIMNYMGNFVDSVHLISPQVQSIAGASTSLKQSRKFKAVLEIVLAFGNYLNS-NKRGPAYGFKLQS 925
Cdd:pfam02181  150 LLELSKIPRLEARLRALLFKSTFEEEVEELKPSLEALIAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSS 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   926 LDTLIDTKSTDKRSSLLHYIVATIRAKFPELLNFESELYGTDKAASVALENVVADVQELEKGMDLVRKEAELRVKGAQ-- 1003
Cdd:pfam02181  230 LLKLSDTKSTDNKTTLLHYLVKIIREKFPELLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDEHpd 309
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 220902586  1004 ---THILRDFLNNSEDKLKKIKSDLRHAQEAFKECVEYFGDSSRNADAAAFFALIVRFTRAFK 1063
Cdd:pfam02181  310 dkfREVLKEFLKEAEEKLDKLESLLREALELFKELVEYFGEDPKETSPNEFFKILRDFLKEFK 372
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
688-1073 3.03e-61

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  Cd Length: 392  Bit Score: 214.91  E-value: 3.03e-61
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586    688 KRKVPTKYKLPTLNWIALKPNQVRGTIFNELDDEKIFkqiDFNEFEERFkigiggALRNGSNGTEVDGSLQSSKRFKRPD 767
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEESEG---DLDELEELF------SAKEKTKSASKDVSEKKSILKKKAS 71
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586    768 -NVSLLEHTRLRNIAISRRKLGMPIDDVIAAIHSLDLKKLSLENVELLQKMVPTDAEVKSYKEYiiERKDQQLLTEEDKF 846
Cdd:smart00498   72 qEFKILDPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREY--KEEDPEELARAEQF 149
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586    847 MLQLSRVERISSKLAIMNYMGNFVDSVHLISPQVQSIAGASTSLKQSRKFKAVLEIVLAFGNYLNS-NKRGPAYGFKLQS 925
Cdd:smart00498  150 LLLISNIPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGgSRRGQAYGFKLSS 229
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586    926 LDTLIDTKSTDKRSSLLHYIVATIRAKFpeLLNFESELYGTDKAASVALEnvvadvqelekgmdlvrkeaelrvkgaqth 1005
Cdd:smart00498  230 LLKLSDVKSADNKTTLLHFLVKIIRKKY--LGGLSDPENLDDKFIEVMKP------------------------------ 277
                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 220902586   1006 ilrdFLNNSEDKLKKIKSDLRHAQEAFKECVEYFGDSSRNADAAAFFALIVRFTRAFKQHDQENEQRL 1073
Cdd:smart00498  278 ----FLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKE 341
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
374-567 1.70e-54

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


Pssm-ID: 336384  Cd Length: 195  Bit Score: 188.25  E-value: 1.70e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   374 GGHEIILGSFDNFKDVCQEKRRFQTLMEYFMNFEAFNIDFMVACMQFMNIVVHSVEDMNYRVHLQYEFTALGLDKYLERI 453
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFRSLVGALDSSENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTRLGLDRILDKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   454 RLTESEELKVQISAYLDNVF-DVAALMEDSETKTSALERVQELEDQLEREIDRNSEFLYKYAELESEsLTLKTEREQLAM 532
Cdd:pfam06367   81 RELENEELDDQLQIFEENREeDVEELLERFDDVNVDLDDPSELFELLKNKLKDTEAEPHLLSILQHL-LLIRDDEEELPQ 159
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 220902586   533 IRQKLEEELTVMQRMLQHNEQELKKRDTLLHTKNM 567
Cdd:pfam06367  160 YWKLLEELVSQIVLHRTKPDPAFDERKNLEIDINR 194
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
77-371 1.42e-17

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


Pssm-ID: 310750  Cd Length: 190  Bit Score: 81.98  E-value: 1.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586    77 PMPTTDELDRRFAKVLASMDLPPDKAKLLRNYDDEKKWDMICDQEMVQAKDPpshYLSKLRTYLDPKASRShrlylfyFL 156
Cdd:pfam06371    2 QKPDEDEILKLFEELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYLKTNFQGE---GGSKSDSKSNETGSPE-------YY 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   157 CQKRKMVGESTST-QVLRDLEISLRTNHIEWVKEFLDdtNQGLDALVDYLsfrlqmmrheqrlqgvlcaseerlnltngg 235
Cdd:pfam06371   72 VKKLKDDSIDSSLsKCLESLRVALRSQPLSWVRRFIG--AQGLSALLNIL------------------------------ 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   236 dggeivmgnsssvspgggggllshgnstghglangtldsrqqhtmsygflrptiadaldspslkrrSRHIAKLNMGAATD 315
Cdd:pfam06371  120 ------------------------------------------------------------------SKINRKKAQSEEDL 133
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 220902586   316 DIHVSIM-CLRAIMNNKYGFNMVIQHREAINCIALSLIHKSLRTKALVLELLAAICL 371
Cdd:pfam06371  134 KIEYEILkCLKALMNNKFGLDHVLGHPSSILLLAQSLDSERLKTRKLALELLTALCL 190
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
450-593 2.97e-05

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 48.17  E-value: 2.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586  450 LERIRLTESEELKVQISAYLDNVFDVAALMEDSETKTSALER-VQELEDQLEREIDRNSEFLYKYAELESESLTLKTERE 528
Cdd:COG1196   363 LEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKReIESLEERLERLSERLEDLKEELKELEAELEELQTELE 442
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 220902586  529 QLAMIRQKLEEELTVMQRMLQHNEQELKKRDTLLHTKNMELQTLSRSLPRSASSGDGSLANGGLM 593
Cdd:COG1196   443 ELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVL 507
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
484-576 1.27e-04

SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.


Pssm-ID: 275056 [Multi-domain]  Cd Length: 198  Bit Score: 44.23  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   484 TKTSALERVQELEDQLEREIDRNSEFLYKYAELESESLTLKTEREQLAMIRQKLEEELTVMQRmLQHNEQELKKRDTLLH 563
Cdd:TIGR04211   60 DTPSARERLPELQQELAELQEELAELQEQLAELRQENQELKQQLSTLEAELEELQKELERIKQ-ISANAIELDEENRELR 138
                           90
                   ....*....|...
gi 220902586   564 TKNMELQTLSRSL 576
Cdd:TIGR04211  139 EELAELKQENEAL 151
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
472-558 1.19e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 335541 [Multi-domain]  Cd Length: 154  Bit Score: 40.65  E-value: 1.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   472 VFDVAALMEDSETKTSALERVQELEDQLEREIDR-NSEFLYKYAELESESLTLKTEREQlaMIRQKLEEeltvMQRMLQH 550
Cdd:pfam03938   20 VVDVQKILQESPEGKAAQAQLEKEFKKRQAELEAkEKELQKLYEELQKDGALMREEKEQ--ELQKKEQE----LQQLQQK 93

                   ....*...
gi 220902586   551 NEQELKKR 558
Cdd:pfam03938   94 AQQELQKK 101
APG6 pfam04111
Autophagy protein Apg6; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
446-576 1.84e-03

Autophagy protein Apg6; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.


Pssm-ID: 335623 [Multi-domain]  Cd Length: 307  Bit Score: 41.39  E-value: 1.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586   446 LDKYLERIRLTESEelKVQISAYLDNVfdvaalmEDSETKTSALERVQELEDQLEREIdrnseflykyAELESESLTLKT 525
Cdd:pfam04111   11 LEELDKELEQLEKE--RDAYQEFLKKL-------EKEDESDEEIEALEKELEKLEKEE----------EELLQELEELEK 71
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 220902586   526 EREQLAMIRQKLEEELtvmqRMLQHNEQELKKRDTLLHTKNMELQTLSRSL 576
Cdd:pfam04111   72 EREELDAELEKLEEEL----EELDQEEEEYWREYNALQLELLEFQDERDSL 118
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
446-576 8.61e-03

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 40.08  E-value: 8.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220902586  446 LDKYLERIRLTES--EELKVQISAYLDNVFDVAALMEDSETKTSALErvQELEDQLEREIDRNSEFLYKYAELESESLTL 523
Cdd:COG1196   325 LEELKEKIEALKEelEERETLLEELEQLLAELEEAKEELEEKLSALL--EELEELFEALREELAELEAELAEIRNELEEL 402
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 220902586  524 KTEREQLAMIRQKLEEELTVMQRMLQHNEQELKKRDTLLHTKNMELQTLSRSL 576
Cdd:COG1196   403 KREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQL 455
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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