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Conserved domains on  [gi|6708478|gb|AAF25953|]
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formin-like protein, partial [Mus musculus]

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;
628-993 1.54e-128

Formin Homology 2 Domain;


:

Pssm-ID: 280362  Cd Length: 372  Bit Score: 395.87  E-value: 1.54e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478     628 KKPIQTKFRMPLLNWVALKPSQITGTVFTELNDEKVLQELDMNDFEEHFKTKSQGPcLDISALKGKASQKAPTKTILIEA 707
Cdd:pfam02181    2 KKPIKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTK-KNKKSEKSKSSKKKPKKVTLLDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478     708 NRAKNLAITLRKGNLGADRICQAIETYDLQTLSLDFLELLTRFLPTDYERSLIARFEkeqRPMEELSEEDRFMLRFSRIQ 787
Cdd:pfam02181   81 KRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYK---GDPSELGRAEQFLLELSKIP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478     788 RLPERMNTLTFLGNFPDTAQLLMPQLNAIIAASMSIKSSDKLRQILEIVLAFGNYMNS-SKRGAAYGFRLQSLDALLEMK 866
Cdd:pfam02181  158 RLEARLRALLFKSTFEEEVEELKPSLEALIAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDTK 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478     867 STDRKQTLLHYLVKVIAEKYPQLTGFHSDLHFLDKAGSVSLDSVLGDVRSLQRGLELTQREFVRQDD--------CLVLK 938
Cdd:pfam02181  238 STDNKTTLLHYLVKIIREKFPELLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALdehpddkfREVLK 317
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 6708478     939 EFLRANSPTMDKLLADSKTAQEAYESVVEYFGENPKTTSPSMFFSLFSRFTKAYK 993
Cdd:pfam02181  318 EFLKEAEEKLDKLESLLREALELFKELVEYFGEDPKETSPNEFFKILRDFLKEFK 372
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
283-432 1.14e-43

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


:

Pssm-ID: 336384  Cd Length: 195  Bit Score: 157.05  E-value: 1.14e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478     283 GGHDIILAAFDNFKEVCGEQHRFEKLMEYFRH-EDSNIDFMVACMQFINIVVHSVENMNFRVFLQYEFTHLGLDLYLERL 361
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFRSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTRLGLDRILDKL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6708478     362 RLTESDKLQVQIQAYLDNVF-DVGTLLEETETKNAVLEHMEELQEQvatLTERLRDTENDSMaKIAELEKQL 432
Cdd:pfam06367   81 RELENEELDDQLQIFEENREeDVEELLERFDDVNVDLDDPSELFEL---LKNKLKDTEAEPH-LLSILQHLL 148
Drf_GBD super family cl05720
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
28-280 1.38e-20

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: 90.46  E-value: 1.38e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478      28 PMPAAGELEERFTRVLNCMNLPPDKVQLLSQYDNEKKWELIC------DQERFQVKNP--------PAAYIQKLKSyldt 93
Cdd:pfam06371    2 QKPDEDEILKLFEELMEEMNLPEEKRRPMLAKPIEKKWQLIVqylktnFQGEGGSKSDsksnetgsPEYYVKKLKD---- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478      94 ggvsrkvasDWMSNLGFKrrvqestqVLRELETSLRTNHIGWVQEFLNEEnrGLDVLLEYLafaQCSVAydmestdsvas 173
Cdd:pfam06371   78 ---------DSIDSSLSK--------CLESLRVALRSQPLSWVRRFIGAQ--GLSALLNIL---SKINR----------- 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478     174 gaEKSkpldQSVEDLskappssvpksrltikltpahsrkalrnsrivsqkDDVHVCIMCLRAIMNYQSGFSLVMNHPACV 253
Cdd:pfam06371  125 --KKA----QSEEDL-----------------------------------KIEYEILKCLKALMNNKFGLDHVLGHPSSI 163
                          250       260
                   ....*....|....*....|....*..
gi 6708478     254 NEIALSLNNKSPRTKALVLELLAAVCL 280
Cdd:pfam06371  164 LLLAQSLDSERLKTRKLALELLTALCL 190
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
628-993 1.54e-128

Formin Homology 2 Domain;


Pssm-ID: 280362  Cd Length: 372  Bit Score: 395.87  E-value: 1.54e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478     628 KKPIQTKFRMPLLNWVALKPSQITGTVFTELNDEKVLQELDMNDFEEHFKTKSQGPcLDISALKGKASQKAPTKTILIEA 707
Cdd:pfam02181    2 KKPIKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTK-KNKKSEKSKSSKKKPKKVTLLDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478     708 NRAKNLAITLRKGNLGADRICQAIETYDLQTLSLDFLELLTRFLPTDYERSLIARFEkeqRPMEELSEEDRFMLRFSRIQ 787
Cdd:pfam02181   81 KRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYK---GDPSELGRAEQFLLELSKIP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478     788 RLPERMNTLTFLGNFPDTAQLLMPQLNAIIAASMSIKSSDKLRQILEIVLAFGNYMNS-SKRGAAYGFRLQSLDALLEMK 866
Cdd:pfam02181  158 RLEARLRALLFKSTFEEEVEELKPSLEALIAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDTK 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478     867 STDRKQTLLHYLVKVIAEKYPQLTGFHSDLHFLDKAGSVSLDSVLGDVRSLQRGLELTQREFVRQDD--------CLVLK 938
Cdd:pfam02181  238 STDNKTTLLHYLVKIIREKFPELLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALdehpddkfREVLK 317
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 6708478     939 EFLRANSPTMDKLLADSKTAQEAYESVVEYFGENPKTTSPSMFFSLFSRFTKAYK 993
Cdd:pfam02181  318 EFLKEAEEKLDKLESLLREALELFKELVEYFGEDPKETSPNEFFKILRDFLKEFK 372
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
628-1050 4.16e-104

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: 332.01  E-value: 4.16e-104
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478      628 KKPIQTKFRMPLLNWVALKPSQITGTVFTELNDEkvlQELDMNDFEEHF--KTKSQGPCLDISALKGKASQKAPTKTILI 705
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEE---SEGDLDELEELFsaKEKTKSASKDVSEKKSILKKKASQEFKIL 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478      706 EANRAKNLAITLRKGNLGADRICQAIETYDLQTLSLDFLELLTRFLPTDYERSLIARFEKEQrpMEELSEEDRFMLRFSR 785
Cdd:smart00498   78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEED--PEELARAEQFLLLISN 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478      786 IQRLPERMNTLTFLGNFPDTAQLLMPQLNAIIAASMSIKSSDKLRQILEIVLAFGNYMNS-SKRGAAYGFRLQSLDALLE 864
Cdd:smart00498  156 IPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGgSRRGQAYGFKLSSLLKLSD 235
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478      865 MKSTDRKQTLLHYLVKVIAEKYpqltgfhsdlhfldkagsvsldsvlgdVRSLQRGLELtqrefvrqDD--CLVLKEFLR 942
Cdd:smart00498  236 VKSADNKTTLLHFLVKIIRKKY---------------------------LGGLSDPENL--------DDkfIEVMKPFLK 280
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478      943 ANSPTMDKLLADSKTAQEAYESVVEYFGENPKTTSPSMFFSLFSRFTKAYKKAEQEvEQWKKEAAAD---TSGRE--EPP 1017
Cdd:smart00498  281 AAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEE-NIKKEEEEEErrkKLVKEttEYE 359
                           410       420       430
                    ....*....|....*....|....*....|...
gi 6708478     1018 TPKSPPKARRQQMDLISELKRKQQKEPLIYESD 1050
Cdd:smart00498  360 QSSSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
283-432 1.14e-43

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


Pssm-ID: 336384  Cd Length: 195  Bit Score: 157.05  E-value: 1.14e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478     283 GGHDIILAAFDNFKEVCGEQHRFEKLMEYFRH-EDSNIDFMVACMQFINIVVHSVENMNFRVFLQYEFTHLGLDLYLERL 361
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFRSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTRLGLDRILDKL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6708478     362 RLTESDKLQVQIQAYLDNVF-DVGTLLEETETKNAVLEHMEELQEQvatLTERLRDTENDSMaKIAELEKQL 432
Cdd:pfam06367   81 RELENEELDDQLQIFEENREeDVEELLERFDDVNVDLDDPSELFEL---LKNKLKDTEAEPH-LLSILQHLL 148
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
28-280 1.38e-20

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: 90.46  E-value: 1.38e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478      28 PMPAAGELEERFTRVLNCMNLPPDKVQLLSQYDNEKKWELIC------DQERFQVKNP--------PAAYIQKLKSyldt 93
Cdd:pfam06371    2 QKPDEDEILKLFEELMEEMNLPEEKRRPMLAKPIEKKWQLIVqylktnFQGEGGSKSDsksnetgsPEYYVKKLKD---- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478      94 ggvsrkvasDWMSNLGFKrrvqestqVLRELETSLRTNHIGWVQEFLNEEnrGLDVLLEYLafaQCSVAydmestdsvas 173
Cdd:pfam06371   78 ---------DSIDSSLSK--------CLESLRVALRSQPLSWVRRFIGAQ--GLSALLNIL---SKINR----------- 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478     174 gaEKSkpldQSVEDLskappssvpksrltikltpahsrkalrnsrivsqkDDVHVCIMCLRAIMNYQSGFSLVMNHPACV 253
Cdd:pfam06371  125 --KKA----QSEEDL-----------------------------------KIEYEILKCLKALMNNKFGLDHVLGHPSSI 163
                          250       260
                   ....*....|....*....|....*..
gi 6708478     254 NEIALSLNNKSPRTKALVLELLAAVCL 280
Cdd:pfam06371  164 LLLAQSLDSERLKTRKLALELLTALCL 190
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
358-448 5.49e-04

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 42.34  E-value: 5.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478   358 LERLRLTESDKLQVQIQAYLDNVFDVGTLLEEtetKNAVLEHMEELQEQVATLT---ERLRDTENDSMAKIAELEKQLSQ 434
Cdd:cd07596   80 SEAQANQELVKLLEPLKEYLRYCQAVKETLDD---RADALLTLQSLKKDLASKKaqlEKLKAAPGIKPAKVEELEEELEE 156
                         90
                 ....*....|....
gi 6708478   435 ARKELETLRERFSE 448
Cdd:cd07596  157 AESALEEARKRYEE 170
alaS PRK00252
alanyl-tRNA synthetase; Reviewed
392-445 1.32e-03

alanyl-tRNA synthetase; Reviewed


Pssm-ID: 234701 [Multi-domain]  Cd Length: 865  Bit Score: 42.77  E-value: 1.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 6708478    392 TKNAVLEHMEELQEQVATLTERLRDTENDSMAKIAELEKQLSQARKELETLRER 445
Cdd:PRK00252  688 TGEAALEYLNEQEALLKELAALLKAKPSELPERVEALLEELKELEKELEQLKAK 741
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
628-993 1.54e-128

Formin Homology 2 Domain;


Pssm-ID: 280362  Cd Length: 372  Bit Score: 395.87  E-value: 1.54e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478     628 KKPIQTKFRMPLLNWVALKPSQITGTVFTELNDEKVLQELDMNDFEEHFKTKSQGPcLDISALKGKASQKAPTKTILIEA 707
Cdd:pfam02181    2 KKPIKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTK-KNKKSEKSKSSKKKPKKVTLLDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478     708 NRAKNLAITLRKGNLGADRICQAIETYDLQTLSLDFLELLTRFLPTDYERSLIARFEkeqRPMEELSEEDRFMLRFSRIQ 787
Cdd:pfam02181   81 KRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYK---GDPSELGRAEQFLLELSKIP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478     788 RLPERMNTLTFLGNFPDTAQLLMPQLNAIIAASMSIKSSDKLRQILEIVLAFGNYMNS-SKRGAAYGFRLQSLDALLEMK 866
Cdd:pfam02181  158 RLEARLRALLFKSTFEEEVEELKPSLEALIAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDTK 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478     867 STDRKQTLLHYLVKVIAEKYPQLTGFHSDLHFLDKAGSVSLDSVLGDVRSLQRGLELTQREFVRQDD--------CLVLK 938
Cdd:pfam02181  238 STDNKTTLLHYLVKIIREKFPELLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALdehpddkfREVLK 317
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 6708478     939 EFLRANSPTMDKLLADSKTAQEAYESVVEYFGENPKTTSPSMFFSLFSRFTKAYK 993
Cdd:pfam02181  318 EFLKEAEEKLDKLESLLREALELFKELVEYFGEDPKETSPNEFFKILRDFLKEFK 372
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
628-1050 4.16e-104

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: 332.01  E-value: 4.16e-104
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478      628 KKPIQTKFRMPLLNWVALKPSQITGTVFTELNDEkvlQELDMNDFEEHF--KTKSQGPCLDISALKGKASQKAPTKTILI 705
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEE---SEGDLDELEELFsaKEKTKSASKDVSEKKSILKKKASQEFKIL 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478      706 EANRAKNLAITLRKGNLGADRICQAIETYDLQTLSLDFLELLTRFLPTDYERSLIARFEKEQrpMEELSEEDRFMLRFSR 785
Cdd:smart00498   78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEED--PEELARAEQFLLLISN 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478      786 IQRLPERMNTLTFLGNFPDTAQLLMPQLNAIIAASMSIKSSDKLRQILEIVLAFGNYMNS-SKRGAAYGFRLQSLDALLE 864
Cdd:smart00498  156 IPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGgSRRGQAYGFKLSSLLKLSD 235
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478      865 MKSTDRKQTLLHYLVKVIAEKYpqltgfhsdlhfldkagsvsldsvlgdVRSLQRGLELtqrefvrqDD--CLVLKEFLR 942
Cdd:smart00498  236 VKSADNKTTLLHFLVKIIRKKY---------------------------LGGLSDPENL--------DDkfIEVMKPFLK 280
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478      943 ANSPTMDKLLADSKTAQEAYESVVEYFGENPKTTSPSMFFSLFSRFTKAYKKAEQEvEQWKKEAAAD---TSGRE--EPP 1017
Cdd:smart00498  281 AAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEE-NIKKEEEEEErrkKLVKEttEYE 359
                           410       420       430
                    ....*....|....*....|....*....|...
gi 6708478     1018 TPKSPPKARRQQMDLISELKRKQQKEPLIYESD 1050
Cdd:smart00498  360 QSSSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
283-432 1.14e-43

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


Pssm-ID: 336384  Cd Length: 195  Bit Score: 157.05  E-value: 1.14e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478     283 GGHDIILAAFDNFKEVCGEQHRFEKLMEYFRH-EDSNIDFMVACMQFINIVVHSVENMNFRVFLQYEFTHLGLDLYLERL 361
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFRSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTRLGLDRILDKL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6708478     362 RLTESDKLQVQIQAYLDNVF-DVGTLLEETETKNAVLEHMEELQEQvatLTERLRDTENDSMaKIAELEKQL 432
Cdd:pfam06367   81 RELENEELDDQLQIFEENREeDVEELLERFDDVNVDLDDPSELFEL---LKNKLKDTEAEPH-LLSILQHLL 148
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
28-280 1.38e-20

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: 90.46  E-value: 1.38e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478      28 PMPAAGELEERFTRVLNCMNLPPDKVQLLSQYDNEKKWELIC------DQERFQVKNP--------PAAYIQKLKSyldt 93
Cdd:pfam06371    2 QKPDEDEILKLFEELMEEMNLPEEKRRPMLAKPIEKKWQLIVqylktnFQGEGGSKSDsksnetgsPEYYVKKLKD---- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478      94 ggvsrkvasDWMSNLGFKrrvqestqVLRELETSLRTNHIGWVQEFLNEEnrGLDVLLEYLafaQCSVAydmestdsvas 173
Cdd:pfam06371   78 ---------DSIDSSLSK--------CLESLRVALRSQPLSWVRRFIGAQ--GLSALLNIL---SKINR----------- 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478     174 gaEKSkpldQSVEDLskappssvpksrltikltpahsrkalrnsrivsqkDDVHVCIMCLRAIMNYQSGFSLVMNHPACV 253
Cdd:pfam06371  125 --KKA----QSEEDL-----------------------------------KIEYEILKCLKALMNNKFGLDHVLGHPSSI 163
                          250       260
                   ....*....|....*....|....*..
gi 6708478     254 NEIALSLNNKSPRTKALVLELLAAVCL 280
Cdd:pfam06371  164 LLLAQSLDSERLKTRKLALELLTALCL 190
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
358-448 5.49e-04

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 42.34  E-value: 5.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478   358 LERLRLTESDKLQVQIQAYLDNVFDVGTLLEEtetKNAVLEHMEELQEQVATLT---ERLRDTENDSMAKIAELEKQLSQ 434
Cdd:cd07596   80 SEAQANQELVKLLEPLKEYLRYCQAVKETLDD---RADALLTLQSLKKDLASKKaqlEKLKAAPGIKPAKVEELEEELEE 156
                         90
                 ....*....|....
gi 6708478   435 ARKELETLRERFSE 448
Cdd:cd07596  157 AESALEEARKRYEE 170
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
358-450 6.14e-04

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation.


Pssm-ID: 336322 [Multi-domain]  Cd Length: 556  Bit Score: 43.66  E-value: 6.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478     358 LERLRLTESDKLQVQIQAYLDNVFDvgTLLEETETKNAVLEHMEELQEQVATLTERLRDTE-------------NDSMAK 424
Cdd:pfam06160  267 LKVLELEDAEEELKTIEDYIDSLYD--DFEKEVEAKKYVEKNLKELKDKLEHAEKQNKELKeeidrlkqsydlnEDELER 344
                           90       100
                   ....*....|....*....|....*.
gi 6708478     425 IAELEKQLSQARKELETLRERFSEST 450
Cdd:pfam06160  345 LRELEKELKELEKDYDELVERLANKK 370
Herpes_UL6 pfam01763
Herpesvirus UL6 like; This family consists of various proteins from the herpesviridae that are ...
393-466 1.05e-03

Herpesvirus UL6 like; This family consists of various proteins from the herpesviridae that are similar to herpes simplex virus type I UL6 virion protein. UL6 is essential for cleavage and packaging of the viral genome.


Pssm-ID: 280017  Cd Length: 563  Bit Score: 42.74  E-value: 1.05e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6708478     393 KNAVLEHMEE-LQEQVATLtERLRDTENDSMAKIAELEKQLSQARKelETLRERFSESTPMGTSRRIPEPEKVPV 466
Cdd:pfam01763  363 SNSVNKCLEGqINEQFDTI-EGLKKENADLLRKLREIETELSRSRA--EALAEASQRSDDMLTSSTDASLENLPQ 434
alaS PRK00252
alanyl-tRNA synthetase; Reviewed
392-445 1.32e-03

alanyl-tRNA synthetase; Reviewed


Pssm-ID: 234701 [Multi-domain]  Cd Length: 865  Bit Score: 42.77  E-value: 1.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 6708478    392 TKNAVLEHMEELQEQVATLTERLRDTENDSMAKIAELEKQLSQARKELETLRER 445
Cdd:PRK00252  688 TGEAALEYLNEQEALLKELAALLKAKPSELPERVEALLEELKELEKELEQLKAK 741
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
386-448 1.40e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 316375 [Multi-domain]  Cd Length: 200  Bit Score: 41.05  E-value: 1.40e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478     386 LLEETETKNAVL-EHMEELQEQVATLTERLRDTENDSM------AKIAELEKQLSQARKELETLRERFSE 448
Cdd:pfam13851   48 LMSEIAQENKRLtEPLKKAQEEVEELRKQLKNYEKDKQslknlkARLKVLEKELKDLKWEHEVLEQRFEK 117
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
358-441 2.99e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 313078 [Multi-domain]  Cd Length: 306  Bit Score: 40.86  E-value: 2.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6708478     358 LERLRLTESDKLQVQIQAYLDNvfdvgtLLEETETKNAVLEHMEELQEQVATLTERLRDTENDSMAKIAELEKQLSQARK 437
Cdd:pfam09787   80 LEAQQQAEADSLREQVQDLEEQ------LHLERQAREETEAELSRLQEELRYAEEELHRSKATLQGRIKEREKEIERLRN 153

                   ....
gi 6708478     438 ELET 441
Cdd:pfam09787  154 QLTT 157
 
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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