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Conserved domains on  [gi|1907089107|ref|XP_036013503|]
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inverted formin-2 isoform X6 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FH2 super family cl19758
Formin Homology 2 Domain;
1-263 4.89e-53

Formin Homology 2 Domain;


The actual alignment was detected with superfamily member pfam02181:

Pssm-ID: 418645  Cd Length: 372  Bit Score: 185.17  E-value: 4.89e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107   1 MIQAGDTSKFDVEVLKQLLKLLPEKHEIENLRAFTEERAKLSNADQFYVLLLDIPCYPLRVECMmlcegtAIVLD----- 75
Cdd:pfam02181 103 AILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKIPRLEARLRAL------LFKSTfeeei 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107  76 -MVRPKAQLVLTACESLLTSQRLPVFCQLILKIGNFLNYGSHTGDADGFKISTLLKLTETKSQQSRVTLLHHVLEEVEKS 154
Cdd:pfam02181 177 eELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLSDTKSTDNKTTLLHYLVKIIREK 256
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107 155 HPDLLQLSRDLEPPSQAAGINVEIIHSEASA------NLKKLLEAERKVSASIPEVQKQYAERLQASIEASQELDKVFDA 228
Cdd:pfam02181 257 FPEVLDFSSELSHVKKAAKVNLEQLEKDVKQlerglkKLERELELSALDEHPDDKFREVLKEFLKSAEEKLDKLESLLRE 336
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907089107 229 IEQKKLELADYLCEDPQQLSLEDTFSTMKTFRDLF 263
Cdd:pfam02181 337 ALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
WH2_INF2 cd22061
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Inverted formin-2 (INF2); This ...
309-338 1.17e-13

Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Inverted formin-2 (INF2); This family contains the first tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) found in inverted formin-2 (INF2, also known as HBEBP2-binding protein C). INF2 is a formin protein with the unique ability to accelerate both actin polymerization and depolymerization, the latter requiring severing of the filament. It interacts with actin at its formin homology 2 (FH2) domain, while the WH2 domain acts as the diaphanous autoregulatory domain (DAD) and binds to actin monomers. INF2 plays a role in mitochondrial fission and dorsal stress fiber formation. It accelerates actin nucleation and elongation by interacting with the fast-growing ends (barbed ends) of actin filaments, but also accelerates disassembly of actin through encircling and severing filaments. Mutations in INF2 lead to the kidney disease focal segmental glomerulosclerosis (FSGS) and the neurological disorder Charcot-Marie Tooth Disease (CMTD).


:

Pssm-ID: 409204  Cd Length: 30  Bit Score: 64.87  E-value: 1.17e-13
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907089107 309 KQEEVCVIDALLADIRKGFQLRKTARGRGD 338
Cdd:cd22061     1 KQEEVCVIDALLADIRKGFQLRKTARGRGD 30
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
346-574 3.24e-04

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 3.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107  346 APADPPKATEPATASNPTQGTNHPASEPLDTTAADEPQgwdlvDAVTPSPQPSKE-------EDGPPALERRSSWYVDAI 418
Cdd:PHA03307   143 SPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPE-----ETARAPSSPPAEpppstppAAASPRPPRRSSPISASA 217
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107  419 DFLDPEDTPDAQPSEGVWPVTLGDGQALNPLEFSSNKPPgvKSSHQDATDPEALWGVHRTEADSTSEGPEDEAQRGQSTH 498
Cdd:PHA03307   218 SSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECP--LPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERS 295
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907089107  499 lPRTGPGEDEDGEDTAPESAldtSLDRSFSEDAVTDSSGSGTLPRVQGRVSKGTSKRRKKRPSRNQEGLRSRPKAK 574
Cdd:PHA03307   296 -PSPSPSSPGSGPAPSSPRA---SSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRK 367
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
1-263 4.89e-53

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 185.17  E-value: 4.89e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107   1 MIQAGDTSKFDVEVLKQLLKLLPEKHEIENLRAFTEERAKLSNADQFYVLLLDIPCYPLRVECMmlcegtAIVLD----- 75
Cdd:pfam02181 103 AILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKIPRLEARLRAL------LFKSTfeeei 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107  76 -MVRPKAQLVLTACESLLTSQRLPVFCQLILKIGNFLNYGSHTGDADGFKISTLLKLTETKSQQSRVTLLHHVLEEVEKS 154
Cdd:pfam02181 177 eELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLSDTKSTDNKTTLLHYLVKIIREK 256
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107 155 HPDLLQLSRDLEPPSQAAGINVEIIHSEASA------NLKKLLEAERKVSASIPEVQKQYAERLQASIEASQELDKVFDA 228
Cdd:pfam02181 257 FPEVLDFSSELSHVKKAAKVNLEQLEKDVKQlerglkKLERELELSALDEHPDDKFREVLKEFLKSAEEKLDKLESLLRE 336
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907089107 229 IEQKKLELADYLCEDPQQLSLEDTFSTMKTFRDLF 263
Cdd:pfam02181 337 ALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
1-296 7.07e-40

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: 149.81  E-value: 7.07e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107    1 MIQAGDTSKFDVEVLKQLLKLLPEKHEIENLRAFTEERA-KLSNADQFYVLLLDIPCYPLRVECMMLcegTAIVLDMVR- 78
Cdd:smart00498 102 AILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEDPeELARAEQFLLLISNIPYLEERLNALLF---KANFEEEVEd 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107   79 --PKAQLVLTACESLLTSQRLPVFCQLILKIGNFLNYGSHTGDADGFKISTLLKLTETKSQQSRVTLLHHVLEEVEKSHp 156
Cdd:smart00498 179 lkPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGSRRGQAYGFKLSSLLKLSDVKSADNKTTLLHFLVKIIRKKY- 257
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107  157 dllqlSRDLEPPSQAaginveiiHSEASAnlkklleaerKVSASIPEVQKQYaerlqasieasQELDKVFDAIEQKKLEL 236
Cdd:smart00498 258 -----LGGLSDPENL--------DDKFIE----------VMKPFLKAAKEKY-----------DKLQKDLSDLKTRFEKL 303
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107  237 ADYLCEDPQQLSLEDTFSTMKTFRDLFTRALKENKDRKEQMakaERRKQQLAEEEARRPR 296
Cdd:smart00498 304 VEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEE---EERRKKLVKETTEYEQ 360
WH2_INF2 cd22061
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Inverted formin-2 (INF2); This ...
309-338 1.17e-13

Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Inverted formin-2 (INF2); This family contains the first tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) found in inverted formin-2 (INF2, also known as HBEBP2-binding protein C). INF2 is a formin protein with the unique ability to accelerate both actin polymerization and depolymerization, the latter requiring severing of the filament. It interacts with actin at its formin homology 2 (FH2) domain, while the WH2 domain acts as the diaphanous autoregulatory domain (DAD) and binds to actin monomers. INF2 plays a role in mitochondrial fission and dorsal stress fiber formation. It accelerates actin nucleation and elongation by interacting with the fast-growing ends (barbed ends) of actin filaments, but also accelerates disassembly of actin through encircling and severing filaments. Mutations in INF2 lead to the kidney disease focal segmental glomerulosclerosis (FSGS) and the neurological disorder Charcot-Marie Tooth Disease (CMTD).


Pssm-ID: 409204  Cd Length: 30  Bit Score: 64.87  E-value: 1.17e-13
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907089107 309 KQEEVCVIDALLADIRKGFQLRKTARGRGD 338
Cdd:cd22061     1 KQEEVCVIDALLADIRKGFQLRKTARGRGD 30
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
346-574 3.24e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 3.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107  346 APADPPKATEPATASNPTQGTNHPASEPLDTTAADEPQgwdlvDAVTPSPQPSKE-------EDGPPALERRSSWYVDAI 418
Cdd:PHA03307   143 SPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPE-----ETARAPSSPPAEpppstppAAASPRPPRRSSPISASA 217
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107  419 DFLDPEDTPDAQPSEGVWPVTLGDGQALNPLEFSSNKPPgvKSSHQDATDPEALWGVHRTEADSTSEGPEDEAQRGQSTH 498
Cdd:PHA03307   218 SSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECP--LPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERS 295
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907089107  499 lPRTGPGEDEDGEDTAPESAldtSLDRSFSEDAVTDSSGSGTLPRVQGRVSKGTSKRRKKRPSRNQEGLRSRPKAK 574
Cdd:PHA03307   296 -PSPSPSSPGSGPAPSSPRA---SSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRK 367
WH2 smart00246
Wiskott Aldrich syndrome homology region 2; Wiskott Aldrich syndrome homology region 2 / ...
317-332 6.78e-03

Wiskott Aldrich syndrome homology region 2; Wiskott Aldrich syndrome homology region 2 / actin-binding motif


Pssm-ID: 128542  Cd Length: 18  Bit Score: 34.10  E-value: 6.78e-03
                           10
                   ....*....|....*.
gi 1907089107  317 DALLADIRKGFQLRKT 332
Cdd:smart00246   3 SALLAQIRQGKKLKKV 18
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
1-263 4.89e-53

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 185.17  E-value: 4.89e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107   1 MIQAGDTSKFDVEVLKQLLKLLPEKHEIENLRAFTEERAKLSNADQFYVLLLDIPCYPLRVECMmlcegtAIVLD----- 75
Cdd:pfam02181 103 AILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELSKIPRLEARLRAL------LFKSTfeeei 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107  76 -MVRPKAQLVLTACESLLTSQRLPVFCQLILKIGNFLNYGSHTGDADGFKISTLLKLTETKSQQSRVTLLHHVLEEVEKS 154
Cdd:pfam02181 177 eELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLSDTKSTDNKTTLLHYLVKIIREK 256
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107 155 HPDLLQLSRDLEPPSQAAGINVEIIHSEASA------NLKKLLEAERKVSASIPEVQKQYAERLQASIEASQELDKVFDA 228
Cdd:pfam02181 257 FPEVLDFSSELSHVKKAAKVNLEQLEKDVKQlerglkKLERELELSALDEHPDDKFREVLKEFLKSAEEKLDKLESLLRE 336
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907089107 229 IEQKKLELADYLCEDPQQLSLEDTFSTMKTFRDLF 263
Cdd:pfam02181 337 ALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
1-296 7.07e-40

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: 149.81  E-value: 7.07e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107    1 MIQAGDTSKFDVEVLKQLLKLLPEKHEIENLRAFTEERA-KLSNADQFYVLLLDIPCYPLRVECMMLcegTAIVLDMVR- 78
Cdd:smart00498 102 AILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEDPeELARAEQFLLLISNIPYLEERLNALLF---KANFEEEVEd 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107   79 --PKAQLVLTACESLLTSQRLPVFCQLILKIGNFLNYGSHTGDADGFKISTLLKLTETKSQQSRVTLLHHVLEEVEKSHp 156
Cdd:smart00498 179 lkPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGSRRGQAYGFKLSSLLKLSDVKSADNKTTLLHFLVKIIRKKY- 257
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107  157 dllqlSRDLEPPSQAaginveiiHSEASAnlkklleaerKVSASIPEVQKQYaerlqasieasQELDKVFDAIEQKKLEL 236
Cdd:smart00498 258 -----LGGLSDPENL--------DDKFIE----------VMKPFLKAAKEKY-----------DKLQKDLSDLKTRFEKL 303
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107  237 ADYLCEDPQQLSLEDTFSTMKTFRDLFTRALKENKDRKEQMakaERRKQQLAEEEARRPR 296
Cdd:smart00498 304 VEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEE---EERRKKLVKETTEYEQ 360
WH2_INF2 cd22061
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Inverted formin-2 (INF2); This ...
309-338 1.17e-13

Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Inverted formin-2 (INF2); This family contains the first tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) found in inverted formin-2 (INF2, also known as HBEBP2-binding protein C). INF2 is a formin protein with the unique ability to accelerate both actin polymerization and depolymerization, the latter requiring severing of the filament. It interacts with actin at its formin homology 2 (FH2) domain, while the WH2 domain acts as the diaphanous autoregulatory domain (DAD) and binds to actin monomers. INF2 plays a role in mitochondrial fission and dorsal stress fiber formation. It accelerates actin nucleation and elongation by interacting with the fast-growing ends (barbed ends) of actin filaments, but also accelerates disassembly of actin through encircling and severing filaments. Mutations in INF2 lead to the kidney disease focal segmental glomerulosclerosis (FSGS) and the neurological disorder Charcot-Marie Tooth Disease (CMTD).


Pssm-ID: 409204  Cd Length: 30  Bit Score: 64.87  E-value: 1.17e-13
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907089107 309 KQEEVCVIDALLADIRKGFQLRKTARGRGD 338
Cdd:cd22061     1 KQEEVCVIDALLADIRKGFQLRKTARGRGD 30
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
346-574 3.24e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 3.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107  346 APADPPKATEPATASNPTQGTNHPASEPLDTTAADEPQgwdlvDAVTPSPQPSKE-------EDGPPALERRSSWYVDAI 418
Cdd:PHA03307   143 SPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPE-----ETARAPSSPPAEpppstppAAASPRPPRRSSPISASA 217
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107  419 DFLDPEDTPDAQPSEGVWPVTLGDGQALNPLEFSSNKPPgvKSSHQDATDPEALWGVHRTEADSTSEGPEDEAQRGQSTH 498
Cdd:PHA03307   218 SSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECP--LPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERS 295
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907089107  499 lPRTGPGEDEDGEDTAPESAldtSLDRSFSEDAVTDSSGSGTLPRVQGRVSKGTSKRRKKRPSRNQEGLRSRPKAK 574
Cdd:PHA03307   296 -PSPSPSSPGSGPAPSSPRA---SSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRK 367
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
188-312 2.53e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.88  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107 188 KKLLEAERKVSASIPEVQKQYAERLQASIEASQELDKVfdAIEQKKLELadylcEDPQQLSLEDTFSTMKTFRDLFTRAL 267
Cdd:pfam17380 316 RKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKREL-----ERIRQEEIAMEISRMRELERLQMERQ 388
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907089107 268 KENKDRKEQMAKAerRKQQLAEEEARRPRDEDGKPIRKGPGKQEE 312
Cdd:pfam17380 389 QKNERVRQELEAA--RKVKILEEERQRKIQQQKVEMEQIRAEQEE 431
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
338-569 3.04e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.54  E-value: 3.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107  338 DTEASGRVAPADPPKATEPATASNPTQGTNHPASEPL----------DTTAADEPQG-WDLVDAVTPSPQPSKE-EDGPP 405
Cdd:PHA03307   154 AAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPaepppstppaAASPRPPRRSsPISASASSPAPAPGRSaADDAG 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107  406 ALERRSSWYVDAIDFLDPED-TPDAQPSEGVWPVTLgdGQALNPLEFSSNKPPGVKSSHQDATDPEALWGVHRTEADSTS 484
Cdd:PHA03307   234 ASSSDSSSSESSGCGWGPENeCPLPRPAPITLPTRI--WEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSS 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089107  485 EGPEDEAQRGQSTHLPRTGPGEDEDGEDTAPESALDTSLDRSFSEDAVTDSSGSGTLPRVQ-----GRVSKGTSKRRKKR 559
Cdd:PHA03307   312 PRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSrapssPAASAGRPTRRRAR 391
                          250
                   ....*....|
gi 1907089107  560 PSRNQEGLRS 569
Cdd:PHA03307   392 AAVAGRARRR 401
WH2 smart00246
Wiskott Aldrich syndrome homology region 2; Wiskott Aldrich syndrome homology region 2 / ...
317-332 6.78e-03

Wiskott Aldrich syndrome homology region 2; Wiskott Aldrich syndrome homology region 2 / actin-binding motif


Pssm-ID: 128542  Cd Length: 18  Bit Score: 34.10  E-value: 6.78e-03
                           10
                   ....*....|....*.
gi 1907089107  317 DALLADIRKGFQLRKT 332
Cdd:smart00246   3 SALLAQIRQGKKLKKV 18
 
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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