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Conserved domains on  [gi|557128958|ref|NP_001273381|]
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disheveled-associated activator of morphogenesis 1 isoform b [Mus musculus]

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;
600-973 2.76e-132

Formin Homology 2 Domain;


:

Pssm-ID: 396655  Cd Length: 372  Bit Score: 405.50  E-value: 2.76e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958   600 KKNIPQPTNALKSFNWSKLPENKLDGTVWTEIDDTKVFKILDLEDLERTFSAYQRQQKEADaIDDTLSSKLKVKELSVID 679
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKK-SEDKSSSKKKPKEVSLLD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958   680 GRRAQNCNILLSRLKLSNDEIKRAILTMDEqEDLPKDMLEQLLKFVPEKSDIDLLEEHKHELDRMAKADRFLFEMSRINH 759
Cdd:pfam02181   80 PKRAQNIAILLRKLKLPPEEIIQAILEGDE-DALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKIPR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958   760 YQQRLQSLYFKKKFAERVAEVKPKVEAIRSGSEEVFRSRALKQLLEVVLAFGNYMNKGQ-RGNAYGFKISSLNKIADTKS 838
Cdd:pfam02181  159 LEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTrRGQAKGFKLSSLLKLSDTKS 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958   839 SiDKNITLLHYLITIVENKYPKVLNLSEELRDIPQAAKVNMTELDKEISTLRSGLKAVETELEYQKsQPPQPGDKFVSVV 918
Cdd:pfam02181  239 T-DNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSA-LDEHPDDKFREVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 557128958   919 SQFITLASFSFSDVEDLLAEAKELFTKAVKHFGEEAGKIQPDEFFGIFDQFLQAV 973
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
235-439 1.39e-63

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: 213.67  E-value: 1.39e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958   235 GGHKKVLQAMLHYQKYASERTRFQTLINDLDKStgrYRDEVSLKTAIMSFINAVLSQGagvESLDFRLHLRYEFLMLGIQ 314
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSS---ENDNVEYKVATMQFINALVNSP---EDLQFRLHLRSEFTALGLD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958   315 PVIDKLREHENSTLDRHLDFFEMLRNEDELEFAKRFELVHIDTKSATQMFELTRRRLTHSEAYPHFMSILHHCLQMpYKR 394
Cdd:pfam06367   75 RILDKLRELENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLI-RDD 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 557128958   395 SGNTVQYWLLLDRIIQQIVIQNDKGQDPDStplENFNIKNVVRML 439
Cdd:pfam06367  154 EEELPSYWKLLEELVSQIVLHRTKPDPKFD---ERKNLEIDINRL 195
Drf_GBD super family cl05720
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
45-232 3.16e-56

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: 192.92  E-value: 3.16e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958    45 LPMPPVEELDVMFSELVDELDLTDKHREAMFALPAEKKWQIYCS--KKKDQEENKG--------ATSWPEFYIDQLNSMA 114
Cdd:pfam06371    1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQykSTNFQKEGGGsksdsesnETGSPEYYVKKLKDDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958   115 ARksllalekeeeeerSKTIESLKTALRTKPMRFVTRFIDLDGLSCILNFLKTMDYETSESR----IHTSLIGCIKALMN 190
Cdd:pfam06371   81 IS--------------SKQLESLRVALRTQPLSWVRRFIEAQGLGALLNVLSKINRKKSQEEedldREYEILKCLKALMN 146
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 557128958   191 NSQGRAHVLAHSESINVIAQSLSTENIKTKVAVLEILGAVCL 232
Cdd:pfam06371  147 NKFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
PRK12704 super family cl36166
phosphodiesterase; Provisional
444-513 1.79e-04

phosphodiesterase; Provisional


The actual alignment was detected with superfamily member PRK12704:

Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.54  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958  444 EVKQWKEQAEKMRKE-HNELQQK-----------------LEKKERECDAKTQEKEEMMQTLNKMKEKLEKETTEHKQVK 505
Cdd:PRK12704   65 EIHKLRNEFEKELRErRNELQKLekrllqkeenldrklelLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL 144

                  ....*...
gi 557128958  506 QQVADLTA 513
Cdd:PRK12704  145 ERISGLTA 152
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
600-973 2.76e-132

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 405.50  E-value: 2.76e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958   600 KKNIPQPTNALKSFNWSKLPENKLDGTVWTEIDDTKVFKILDLEDLERTFSAYQRQQKEADaIDDTLSSKLKVKELSVID 679
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKK-SEDKSSSKKKPKEVSLLD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958   680 GRRAQNCNILLSRLKLSNDEIKRAILTMDEqEDLPKDMLEQLLKFVPEKSDIDLLEEHKHELDRMAKADRFLFEMSRINH 759
Cdd:pfam02181   80 PKRAQNIAILLRKLKLPPEEIIQAILEGDE-DALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKIPR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958   760 YQQRLQSLYFKKKFAERVAEVKPKVEAIRSGSEEVFRSRALKQLLEVVLAFGNYMNKGQ-RGNAYGFKISSLNKIADTKS 838
Cdd:pfam02181  159 LEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTrRGQAKGFKLSSLLKLSDTKS 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958   839 SiDKNITLLHYLITIVENKYPKVLNLSEELRDIPQAAKVNMTELDKEISTLRSGLKAVETELEYQKsQPPQPGDKFVSVV 918
Cdd:pfam02181  239 T-DNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSA-LDEHPDDKFREVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 557128958   919 SQFITLASFSFSDVEDLLAEAKELFTKAVKHFGEEAGKIQPDEFFGIFDQFLQAV 973
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
601-1031 1.09e-79

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: 265.75  E-value: 1.09e-79
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958    601 KNIPQPTNALKSFNWSKLPENKLDGTVWTEIDDTKvfkILDLEDLERTFSAYQRQQKEADAIDD--TLSSKLKVKELSVI 678
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFSAKEKTKSASKDVSEkkSILKKKASQEFKIL 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958    679 DGRRAQNCNILLSRLKLSNDEIKRAILTMDEqEDLPKDMLEQLLKFVPEKSDIDLLEEHKHE-LDRMAKADRFLFEMSRI 757
Cdd:smart00498   78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDE-DVLSVDLLEQLLKYAPTKEELKKLREYKEEdPEELARAEQFLLLISNI 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958    758 NHYQQRLQSLYFKKKFAERVAEVKPKVEAIRSGSEEVFRSRALKQLLEVVLAFGNYMNKG-QRGNAYGFKISSLNKIADT 836
Cdd:smart00498  157 PYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGsRRGQAYGFKLSSLLKLSDV 236
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958    837 KSSiDKNITLLHYLITIVENKYPKVLNLSEELRdipqaakvnmteldkeistlrsglkaveteleyqksqppqpgDKFVS 916
Cdd:smart00498  237 KSA-DNKTTLLHFLVKIIRKKYLGGLSDPENLD------------------------------------------DKFIE 273
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958    917 VVSQFITLASFSFSDVEDLLAEAKELFTKAVKHFGEEAGKIQPDEFFGIFDQFLQAVAEAKQENENMRKRKEEEERRArl 996
Cdd:smart00498  274 VMKPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEEEERRKKL-- 351
                           410       420       430       440
                    ....*....|....*....|....*....|....*....|....
gi 557128958    997 eaqLKEQRERERKVRKAKESS---------EESGEFDDLVSALR 1031
Cdd:smart00498  352 ---VKETTEYEQSSSRQKERNpsmdfeverDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
235-439 1.39e-63

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: 213.67  E-value: 1.39e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958   235 GGHKKVLQAMLHYQKYASERTRFQTLINDLDKStgrYRDEVSLKTAIMSFINAVLSQGagvESLDFRLHLRYEFLMLGIQ 314
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSS---ENDNVEYKVATMQFINALVNSP---EDLQFRLHLRSEFTALGLD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958   315 PVIDKLREHENSTLDRHLDFFEMLRNEDELEFAKRFELVHIDTKSATQMFELTRRRLTHSEAYPHFMSILHHCLQMpYKR 394
Cdd:pfam06367   75 RILDKLRELENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLI-RDD 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 557128958   395 SGNTVQYWLLLDRIIQQIVIQNDKGQDPDStplENFNIKNVVRML 439
Cdd:pfam06367  154 EEELPSYWKLLEELVSQIVLHRTKPDPKFD---ERKNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
45-232 3.16e-56

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: 192.92  E-value: 3.16e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958    45 LPMPPVEELDVMFSELVDELDLTDKHREAMFALPAEKKWQIYCS--KKKDQEENKG--------ATSWPEFYIDQLNSMA 114
Cdd:pfam06371    1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQykSTNFQKEGGGsksdsesnETGSPEYYVKKLKDDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958   115 ARksllalekeeeeerSKTIESLKTALRTKPMRFVTRFIDLDGLSCILNFLKTMDYETSESR----IHTSLIGCIKALMN 190
Cdd:pfam06371   81 IS--------------SKQLESLRVALRTQPLSWVRRFIEAQGLGALLNVLSKINRKKSQEEedldREYEILKCLKALMN 146
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 557128958   191 NSQGRAHVLAHSESINVIAQSLSTENIKTKVAVLEILGAVCL 232
Cdd:pfam06371  147 NKFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
PRK12704 PRK12704
phosphodiesterase; Provisional
444-513 1.79e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.54  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958  444 EVKQWKEQAEKMRKE-HNELQQK-----------------LEKKERECDAKTQEKEEMMQTLNKMKEKLEKETTEHKQVK 505
Cdd:PRK12704   65 EIHKLRNEFEKELRErRNELQKLekrllqkeenldrklelLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL 144

                  ....*...
gi 557128958  506 QQVADLTA 513
Cdd:PRK12704  145 ERISGLTA 152
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
442-519 3.18e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 3.18e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557128958   442 ENEVKQWKEQAEKMRKEHNELQQKLEKKERECDAKTQEKEEMMQTLNKMKEKLEKETTEHKQVKQQVADLTAQLHELN 519
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
Clusterin pfam01093
Clusterin;
443-497 2.61e-03

Clusterin;


Pssm-ID: 460061 [Multi-domain]  Cd Length: 418  Bit Score: 41.41  E-value: 2.61e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 557128958   443 NEVKQWKEQAEKMRKEHNELQQKLEKKErecdaktQEKEEMMQTLNKMKEKLEKE 497
Cdd:pfam01093   22 IGVKQMKTMMERREEEHKKLMKSLEKSK-------EKKEEALKLAKEVEEKLEEE 69
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
443-526 8.28e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 8.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958  443 NEVKQWKEQAEKMRKEHNELQQKLEKKERECDAKTQEKEEMMQTLNKMKEKLEKETtehKQVKQQVADLTAQLHELNRRA 522
Cdd:COG4942   160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL---AELQQEAEELEALIARLEAEA 236

                  ....
gi 557128958  523 VCAA 526
Cdd:COG4942   237 AAAA 240
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
600-973 2.76e-132

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 405.50  E-value: 2.76e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958   600 KKNIPQPTNALKSFNWSKLPENKLDGTVWTEIDDTKVFKILDLEDLERTFSAYQRQQKEADaIDDTLSSKLKVKELSVID 679
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKK-SEDKSSSKKKPKEVSLLD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958   680 GRRAQNCNILLSRLKLSNDEIKRAILTMDEqEDLPKDMLEQLLKFVPEKSDIDLLEEHKHELDRMAKADRFLFEMSRINH 759
Cdd:pfam02181   80 PKRAQNIAILLRKLKLPPEEIIQAILEGDE-DALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKIPR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958   760 YQQRLQSLYFKKKFAERVAEVKPKVEAIRSGSEEVFRSRALKQLLEVVLAFGNYMNKGQ-RGNAYGFKISSLNKIADTKS 838
Cdd:pfam02181  159 LEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTrRGQAKGFKLSSLLKLSDTKS 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958   839 SiDKNITLLHYLITIVENKYPKVLNLSEELRDIPQAAKVNMTELDKEISTLRSGLKAVETELEYQKsQPPQPGDKFVSVV 918
Cdd:pfam02181  239 T-DNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSA-LDEHPDDKFREVL 316
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 557128958   919 SQFITLASFSFSDVEDLLAEAKELFTKAVKHFGEEAGKIQPDEFFGIFDQFLQAV 973
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
601-1031 1.09e-79

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: 265.75  E-value: 1.09e-79
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958    601 KNIPQPTNALKSFNWSKLPENKLDGTVWTEIDDTKvfkILDLEDLERTFSAYQRQQKEADAIDD--TLSSKLKVKELSVI 678
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFSAKEKTKSASKDVSEkkSILKKKASQEFKIL 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958    679 DGRRAQNCNILLSRLKLSNDEIKRAILTMDEqEDLPKDMLEQLLKFVPEKSDIDLLEEHKHE-LDRMAKADRFLFEMSRI 757
Cdd:smart00498   78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDE-DVLSVDLLEQLLKYAPTKEELKKLREYKEEdPEELARAEQFLLLISNI 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958    758 NHYQQRLQSLYFKKKFAERVAEVKPKVEAIRSGSEEVFRSRALKQLLEVVLAFGNYMNKG-QRGNAYGFKISSLNKIADT 836
Cdd:smart00498  157 PYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGsRRGQAYGFKLSSLLKLSDV 236
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958    837 KSSiDKNITLLHYLITIVENKYPKVLNLSEELRdipqaakvnmteldkeistlrsglkaveteleyqksqppqpgDKFVS 916
Cdd:smart00498  237 KSA-DNKTTLLHFLVKIIRKKYLGGLSDPENLD------------------------------------------DKFIE 273
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958    917 VVSQFITLASFSFSDVEDLLAEAKELFTKAVKHFGEEAGKIQPDEFFGIFDQFLQAVAEAKQENENMRKRKEEEERRArl 996
Cdd:smart00498  274 VMKPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEEEERRKKL-- 351
                           410       420       430       440
                    ....*....|....*....|....*....|....*....|....
gi 557128958    997 eaqLKEQRERERKVRKAKESS---------EESGEFDDLVSALR 1031
Cdd:smart00498  352 ---VKETTEYEQSSSRQKERNpsmdfeverDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
235-439 1.39e-63

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: 213.67  E-value: 1.39e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958   235 GGHKKVLQAMLHYQKYASERTRFQTLINDLDKStgrYRDEVSLKTAIMSFINAVLSQGagvESLDFRLHLRYEFLMLGIQ 314
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSS---ENDNVEYKVATMQFINALVNSP---EDLQFRLHLRSEFTALGLD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958   315 PVIDKLREHENSTLDRHLDFFEMLRNEDELEFAKRFELVHIDTKSATQMFELTRRRLTHSEAYPHFMSILHHCLQMpYKR 394
Cdd:pfam06367   75 RILDKLRELENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLI-RDD 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 557128958   395 SGNTVQYWLLLDRIIQQIVIQNDKGQDPDStplENFNIKNVVRML 439
Cdd:pfam06367  154 EEELPSYWKLLEELVSQIVLHRTKPDPKFD---ERKNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
45-232 3.16e-56

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: 192.92  E-value: 3.16e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958    45 LPMPPVEELDVMFSELVDELDLTDKHREAMFALPAEKKWQIYCS--KKKDQEENKG--------ATSWPEFYIDQLNSMA 114
Cdd:pfam06371    1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQykSTNFQKEGGGsksdsesnETGSPEYYVKKLKDDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958   115 ARksllalekeeeeerSKTIESLKTALRTKPMRFVTRFIDLDGLSCILNFLKTMDYETSESR----IHTSLIGCIKALMN 190
Cdd:pfam06371   81 IS--------------SKQLESLRVALRTQPLSWVRRFIEAQGLGALLNVLSKINRKKSQEEedldREYEILKCLKALMN 146
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 557128958   191 NSQGRAHVLAHSESINVIAQSLSTENIKTKVAVLEILGAVCL 232
Cdd:pfam06371  147 NKFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
PRK12704 PRK12704
phosphodiesterase; Provisional
444-513 1.79e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.54  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958  444 EVKQWKEQAEKMRKE-HNELQQK-----------------LEKKERECDAKTQEKEEMMQTLNKMKEKLEKETTEHKQVK 505
Cdd:PRK12704   65 EIHKLRNEFEKELRErRNELQKLekrllqkeenldrklelLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL 144

                  ....*...
gi 557128958  506 QQVADLTA 513
Cdd:PRK12704  145 ERISGLTA 152
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
442-519 3.18e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 3.18e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557128958   442 ENEVKQWKEQAEKMRKEHNELQQKLEKKERECDAKTQEKEEMMQTLNKMKEKLEKETTEHKQVKQQVADLTAQLHELN 519
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
Clusterin pfam01093
Clusterin;
443-497 2.61e-03

Clusterin;


Pssm-ID: 460061 [Multi-domain]  Cd Length: 418  Bit Score: 41.41  E-value: 2.61e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 557128958   443 NEVKQWKEQAEKMRKEHNELQQKLEKKErecdaktQEKEEMMQTLNKMKEKLEKE 497
Cdd:pfam01093   22 IGVKQMKTMMERREEEHKKLMKSLEKSK-------EKKEEALKLAKEVEEKLEEE 69
PRK12704 PRK12704
phosphodiesterase; Provisional
442-518 7.66e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 7.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958  442 ENEVKQWKEQAEKMR----KEHNELQQKLEKKERecdaKTQEKEEM----MQTLNKMKEKLEKETTEHKQVKQQVADLTA 513
Cdd:PRK12704   56 KEALLEAKEEIHKLRnefeKELRERRNELQKLEK----RLLQKEENldrkLELLEKREEELEKKEKELEQKQQELEKKEE 131

                  ....*
gi 557128958  514 QLHEL 518
Cdd:PRK12704  132 ELEEL 136
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
443-526 8.28e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 8.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958  443 NEVKQWKEQAEKMRKEHNELQQKLEKKERECDAKTQEKEEMMQTLNKMKEKLEKETtehKQVKQQVADLTAQLHELNRRA 522
Cdd:COG4942   160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL---AELQQEAEELEALIARLEAEA 236

                  ....
gi 557128958  523 VCAA 526
Cdd:COG4942   237 AAAA 240
RNase_Y_N pfam12072
RNase Y N-terminal region;
444-513 8.65e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 38.71  E-value: 8.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557128958   444 EVKQWKEQAEK----MRKEH----NELQQK----------LEKKERECDAKTQEKEEMMQTLNKMKEKLEKETTEHKQVK 505
Cdd:pfam12072   61 EIHKLRAEAERelkeRRNELqrqeRRLLQKeetldrkdesLEKKEESLEKKEKELEAQQQQLEEKEEELEELIEEQRQEL 140

                   ....*...
gi 557128958   506 QQVADLTA 513
Cdd:pfam12072  141 ERISGLTS 148
 
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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