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Conserved domains on  [gi|1720371123|ref|XP_030102496|]
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disheveled-associated activator of morphogenesis 1 isoform X1 [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;
600-982 9.19e-131

Formin Homology 2 Domain;


:

Pssm-ID: 396655  Cd Length: 372  Bit Score: 401.65  E-value: 9.19e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  600 KKNIPQPTNALKSFNWSKLPENKLDGTVWTEIDDTKVFKILDLEDLERTFSAYqrqqeffvnnSKQKEADAIDDTLSSKL 679
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAK----------AKTKKNKKSEDKSSSKK 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  680 KVKELSVIDGRRAQNCNILLSRLKLSNDEIKRAILTMDEqEDLPKDMLEQLLKFVPEKSDIDLLEEHKHELDRMAKADRF 759
Cdd:pfam02181   71 KPKEVSLLDPKRAQNIAILLRKLKLPPEEIIQAILEGDE-DALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQF 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  760 LFEMSRINHYQQRLQSLYFKKKFAERVAEVKPKVEAIRSGSEEVFRSRALKQLLEVVLAFGNYMNKGQ-RGNAYGFKISS 838
Cdd:pfam02181  150 LLELSKIPRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTrRGQAKGFKLSS 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  839 LNKIADTKSSiDKNITLLHYLITIVENKYPKVLNLSEELRDIPQAAKVNMTELDKEISTLRSGLKAVETELEYQKsQPPQ 918
Cdd:pfam02181  230 LLKLSDTKST-DNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSA-LDEH 307
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720371123  919 PGDKFVSVVSQFITLASFSFSDVEDLLAEAKELFTKAVKHFGEEAGKIQPDEFFGIFDQFLQAV 982
Cdd:pfam02181  308 PDDKFREVLKEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
235-439 1.84e-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: 1.84e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  235 GGHKKVLQAMLHYQKYASERTRFQTLINDLDKStgrYRDEVSLKTAIMSFINAVLSQGagvESLDFRLHLRYEFLMLGIQ 314
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSS---ENDNVEYKVATMQFINALVNSP---EDLQFRLHLRSEFTALGLD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  315 PVIDKLREHENSTLDRHLDFFEMLRNEDELEFAKRFELVHIDTKSATQMFELTRRRLTHSEAYPHFMSILHHCLQMpYKR 394
Cdd:pfam06367   75 RILDKLRELENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLI-RDD 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1720371123  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 3.26e-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: 192.53  E-value: 3.26e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123   45 LPMPPVEELDVMFSELVDELDLTDKHREAMFALPAEKKWQIYCS--KKKDQEENKG--------ATSWPEFYIDQLNSMA 114
Cdd:pfam06371    1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQykSTNFQKEGGGsksdsesnETGSPEYYVKKLKDDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  115 ARksllalekeeeeerSKTIESLKTALRTKPMRFVTRFIDLDGLSCILNFLKTMDYETSESR----IHTSLIGCIKALMN 190
Cdd:pfam06371   81 IS--------------SKQLESLRVALRTQPLSWVRRFIEAQGLGALLNVLSKINRKKSQEEedldREYEILKCLKALMN 146
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1720371123  191 NSQGRAHVLAHSESINVIAQSLSTENIKTKVAVLEILGAVCL 232
Cdd:pfam06371  147 NKFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
PRK12704 super family cl36166
phosphodiesterase; Provisional
444-513 1.68e-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: 1.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  444 EVKQWKEQAEKMRKE-HNELQQK-----------------LEKKERECDAKTQEKEEMMQTLNKMKEKLEKETTEHKQVK 505
Cdd:PRK12704    65 EIHKLRNEFEKELRErRNELQKLekrllqkeenldrklelLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL 144

                   ....*...
gi 1720371123  506 QQVADLTA 513
Cdd:PRK12704   145 ERISGLTA 152
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
600-982 9.19e-131

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 401.65  E-value: 9.19e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  600 KKNIPQPTNALKSFNWSKLPENKLDGTVWTEIDDTKVFKILDLEDLERTFSAYqrqqeffvnnSKQKEADAIDDTLSSKL 679
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAK----------AKTKKNKKSEDKSSSKK 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  680 KVKELSVIDGRRAQNCNILLSRLKLSNDEIKRAILTMDEqEDLPKDMLEQLLKFVPEKSDIDLLEEHKHELDRMAKADRF 759
Cdd:pfam02181   71 KPKEVSLLDPKRAQNIAILLRKLKLPPEEIIQAILEGDE-DALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQF 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  760 LFEMSRINHYQQRLQSLYFKKKFAERVAEVKPKVEAIRSGSEEVFRSRALKQLLEVVLAFGNYMNKGQ-RGNAYGFKISS 838
Cdd:pfam02181  150 LLELSKIPRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTrRGQAKGFKLSS 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  839 LNKIADTKSSiDKNITLLHYLITIVENKYPKVLNLSEELRDIPQAAKVNMTELDKEISTLRSGLKAVETELEYQKsQPPQ 918
Cdd:pfam02181  230 LLKLSDTKST-DNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSA-LDEH 307
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720371123  919 PGDKFVSVVSQFITLASFSFSDVEDLLAEAKELFTKAVKHFGEEAGKIQPDEFFGIFDQFLQAV 982
Cdd:pfam02181  308 PDDKFREVLKEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
601-1040 1.53e-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: 1.53e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123   601 KNIPQPTNALKSFNWSKLPENKLDGTVWTEIDDTKvfkILDLEDLERTFSAyqrqqeffvNNSKQKEADAIDD--TLSSK 678
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFSA---------KEKTKSASKDVSEkkSILKK 68
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123   679 LKVKELSVIDGRRAQNCNILLSRLKLSNDEIKRAILTMDEqEDLPKDMLEQLLKFVPEKSDIDLLEEHKHE-LDRMAKAD 757
Cdd:smart00498   69 KASQEFKILDPKRSQNLAILLRKLHMSYEEIKEAILEGDE-DVLSVDLLEQLLKYAPTKEELKKLREYKEEdPEELARAE 147
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123   758 RFLFEMSRINHYQQRLQSLYFKKKFAERVAEVKPKVEAIRSGSEEVFRSRALKQLLEVVLAFGNYMNKG-QRGNAYGFKI 836
Cdd:smart00498  148 QFLLLISNIPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGsRRGQAYGFKL 227
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123   837 SSLNKIADTKSSiDKNITLLHYLITIVENKYPKVLNLSEELRdipqaakvnmteldkeistlrsglkaveteleyqksqp 916
Cdd:smart00498  228 SSLLKLSDVKSA-DNKTTLLHFLVKIIRKKYLGGLSDPENLD-------------------------------------- 268
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123   917 pqpgDKFVSVVSQFITLASFSFSDVEDLLAEAKELFTKAVKHFGEEAGKIQPDEFFGIFDQFLQAVAEAKQENENMRKRK 996
Cdd:smart00498  269 ----DKFIEVMKPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEE 344
                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1720371123   997 EEEERRArleaqLKEQRERERKVRKAKESS---------EESGEFDDLVSALR 1040
Cdd:smart00498  345 EERRKKL-----VKETTEYEQSSSRQKERNpsmdfeverDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
235-439 1.84e-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: 1.84e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  235 GGHKKVLQAMLHYQKYASERTRFQTLINDLDKStgrYRDEVSLKTAIMSFINAVLSQGagvESLDFRLHLRYEFLMLGIQ 314
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSS---ENDNVEYKVATMQFINALVNSP---EDLQFRLHLRSEFTALGLD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  315 PVIDKLREHENSTLDRHLDFFEMLRNEDELEFAKRFELVHIDTKSATQMFELTRRRLTHSEAYPHFMSILHHCLQMpYKR 394
Cdd:pfam06367   75 RILDKLRELENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLI-RDD 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1720371123  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 3.26e-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: 192.53  E-value: 3.26e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123   45 LPMPPVEELDVMFSELVDELDLTDKHREAMFALPAEKKWQIYCS--KKKDQEENKG--------ATSWPEFYIDQLNSMA 114
Cdd:pfam06371    1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQykSTNFQKEGGGsksdsesnETGSPEYYVKKLKDDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  115 ARksllalekeeeeerSKTIESLKTALRTKPMRFVTRFIDLDGLSCILNFLKTMDYETSESR----IHTSLIGCIKALMN 190
Cdd:pfam06371   81 IS--------------SKQLESLRVALRTQPLSWVRRFIEAQGLGALLNVLSKINRKKSQEEedldREYEILKCLKALMN 146
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1720371123  191 NSQGRAHVLAHSESINVIAQSLSTENIKTKVAVLEILGAVCL 232
Cdd:pfam06371  147 NKFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
PRK12704 PRK12704
phosphodiesterase; Provisional
444-513 1.68e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.54  E-value: 1.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  444 EVKQWKEQAEKMRKE-HNELQQK-----------------LEKKERECDAKTQEKEEMMQTLNKMKEKLEKETTEHKQVK 505
Cdd:PRK12704    65 EIHKLRNEFEKELRErRNELQKLekrllqkeenldrklelLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL 144

                   ....*...
gi 1720371123  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 3.19e-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: 3.19e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720371123  442 ENEVKQWKEQAEKMRKEHNELQQKLEKKERECDAKTQEKEEMMQTLNKMKEKLEKETTEHKQVKQQVADLTAQLHELN 519
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
Clusterin pfam01093
Clusterin;
443-497 2.82e-03

Clusterin;


Pssm-ID: 460061 [Multi-domain]  Cd Length: 418  Bit Score: 41.41  E-value: 2.82e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720371123  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 8.00e-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: 8.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  443 NEVKQWKEQAEKMRKEHNELQQKLEKKERECDAKTQEKEEMMQTLNKMKEKLEKETtehKQVKQQVADLTAQLHELNRRA 522
Cdd:COG4942    160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL---AELQQEAEELEALIARLEAEA 236

                   ....
gi 1720371123  523 VCAA 526
Cdd:COG4942    237 AAAA 240
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
600-982 9.19e-131

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 401.65  E-value: 9.19e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  600 KKNIPQPTNALKSFNWSKLPENKLDGTVWTEIDDTKVFKILDLEDLERTFSAYqrqqeffvnnSKQKEADAIDDTLSSKL 679
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAK----------AKTKKNKKSEDKSSSKK 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  680 KVKELSVIDGRRAQNCNILLSRLKLSNDEIKRAILTMDEqEDLPKDMLEQLLKFVPEKSDIDLLEEHKHELDRMAKADRF 759
Cdd:pfam02181   71 KPKEVSLLDPKRAQNIAILLRKLKLPPEEIIQAILEGDE-DALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQF 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  760 LFEMSRINHYQQRLQSLYFKKKFAERVAEVKPKVEAIRSGSEEVFRSRALKQLLEVVLAFGNYMNKGQ-RGNAYGFKISS 838
Cdd:pfam02181  150 LLELSKIPRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTrRGQAKGFKLSS 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  839 LNKIADTKSSiDKNITLLHYLITIVENKYPKVLNLSEELRDIPQAAKVNMTELDKEISTLRSGLKAVETELEYQKsQPPQ 918
Cdd:pfam02181  230 LLKLSDTKST-DNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSA-LDEH 307
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720371123  919 PGDKFVSVVSQFITLASFSFSDVEDLLAEAKELFTKAVKHFGEEAGKIQPDEFFGIFDQFLQAV 982
Cdd:pfam02181  308 PDDKFREVLKEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
601-1040 1.53e-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: 1.53e-77
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123   601 KNIPQPTNALKSFNWSKLPENKLDGTVWTEIDDTKvfkILDLEDLERTFSAyqrqqeffvNNSKQKEADAIDD--TLSSK 678
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFSA---------KEKTKSASKDVSEkkSILKK 68
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123   679 LKVKELSVIDGRRAQNCNILLSRLKLSNDEIKRAILTMDEqEDLPKDMLEQLLKFVPEKSDIDLLEEHKHE-LDRMAKAD 757
Cdd:smart00498   69 KASQEFKILDPKRSQNLAILLRKLHMSYEEIKEAILEGDE-DVLSVDLLEQLLKYAPTKEELKKLREYKEEdPEELARAE 147
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123   758 RFLFEMSRINHYQQRLQSLYFKKKFAERVAEVKPKVEAIRSGSEEVFRSRALKQLLEVVLAFGNYMNKG-QRGNAYGFKI 836
Cdd:smart00498  148 QFLLLISNIPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGsRRGQAYGFKL 227
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123   837 SSLNKIADTKSSiDKNITLLHYLITIVENKYPKVLNLSEELRdipqaakvnmteldkeistlrsglkaveteleyqksqp 916
Cdd:smart00498  228 SSLLKLSDVKSA-DNKTTLLHFLVKIIRKKYLGGLSDPENLD-------------------------------------- 268
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123   917 pqpgDKFVSVVSQFITLASFSFSDVEDLLAEAKELFTKAVKHFGEEAGKIQPDEFFGIFDQFLQAVAEAKQENENMRKRK 996
Cdd:smart00498  269 ----DKFIEVMKPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEE 344
                           410       420       430       440       450
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1720371123   997 EEEERRArleaqLKEQRERERKVRKAKESS---------EESGEFDDLVSALR 1040
Cdd:smart00498  345 EERRKKL-----VKETTEYEQSSSRQKERNpsmdfeverDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
235-439 1.84e-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: 1.84e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  235 GGHKKVLQAMLHYQKYASERTRFQTLINDLDKStgrYRDEVSLKTAIMSFINAVLSQGagvESLDFRLHLRYEFLMLGIQ 314
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSS---ENDNVEYKVATMQFINALVNSP---EDLQFRLHLRSEFTALGLD 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  315 PVIDKLREHENSTLDRHLDFFEMLRNEDELEFAKRFELVHIDTKSATQMFELTRRRLTHSEAYPHFMSILHHCLQMpYKR 394
Cdd:pfam06367   75 RILDKLRELENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLI-RDD 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1720371123  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 3.26e-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: 192.53  E-value: 3.26e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123   45 LPMPPVEELDVMFSELVDELDLTDKHREAMFALPAEKKWQIYCS--KKKDQEENKG--------ATSWPEFYIDQLNSMA 114
Cdd:pfam06371    1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQykSTNFQKEGGGsksdsesnETGSPEYYVKKLKDDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  115 ARksllalekeeeeerSKTIESLKTALRTKPMRFVTRFIDLDGLSCILNFLKTMDYETSESR----IHTSLIGCIKALMN 190
Cdd:pfam06371   81 IS--------------SKQLESLRVALRTQPLSWVRRFIEAQGLGALLNVLSKINRKKSQEEedldREYEILKCLKALMN 146
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1720371123  191 NSQGRAHVLAHSESINVIAQSLSTENIKTKVAVLEILGAVCL 232
Cdd:pfam06371  147 NKFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
PRK12704 PRK12704
phosphodiesterase; Provisional
444-513 1.68e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.54  E-value: 1.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  444 EVKQWKEQAEKMRKE-HNELQQK-----------------LEKKERECDAKTQEKEEMMQTLNKMKEKLEKETTEHKQVK 505
Cdd:PRK12704    65 EIHKLRNEFEKELRErRNELQKLekrllqkeenldrklelLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL 144

                   ....*...
gi 1720371123  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 3.19e-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: 3.19e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720371123  442 ENEVKQWKEQAEKMRKEHNELQQKLEKKERECDAKTQEKEEMMQTLNKMKEKLEKETTEHKQVKQQVADLTAQLHELN 519
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
Clusterin pfam01093
Clusterin;
443-497 2.82e-03

Clusterin;


Pssm-ID: 460061 [Multi-domain]  Cd Length: 418  Bit Score: 41.41  E-value: 2.82e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720371123  443 NEVKQWKEQAEKMRKEHNELQQKLEKKErecdaktQEKEEMMQTLNKMKEKLEKE 497
Cdd:pfam01093   22 IGVKQMKTMMERREEEHKKLMKSLEKSK-------EKKEEALKLAKEVEEKLEEE 69
PRK12704 PRK12704
phosphodiesterase; Provisional
442-518 7.60e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 7.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  442 ENEVKQWKEQAEKMR----KEHNELQQKLEKKERecdaKTQEKEEM----MQTLNKMKEKLEKETTEHKQVKQQVADLTA 513
Cdd:PRK12704    56 KEALLEAKEEIHKLRnefeKELRERRNELQKLEK----RLLQKEENldrkLELLEKREEELEKKEKELEQKQQELEKKEE 131

                   ....*
gi 1720371123  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 8.00e-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: 8.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  443 NEVKQWKEQAEKMRKEHNELQQKLEKKERECDAKTQEKEEMMQTLNKMKEKLEKETtehKQVKQQVADLTAQLHELNRRA 522
Cdd:COG4942    160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL---AELQQEAEELEALIARLEAEA 236

                   ....
gi 1720371123  523 VCAA 526
Cdd:COG4942    237 AAAA 240
RNase_Y_N pfam12072
RNase Y N-terminal region;
444-513 8.42e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 38.71  E-value: 8.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371123  444 EVKQWKEQAEK----MRKEH----NELQQK----------LEKKERECDAKTQEKEEMMQTLNKMKEKLEKETTEHKQVK 505
Cdd:pfam12072   61 EIHKLRAEAERelkeRRNELqrqeRRLLQKeetldrkdesLEKKEESLEKKEKELEAQQQQLEEKEEELEELIEEQRQEL 140

                   ....*...
gi 1720371123  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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