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Conserved domains on  [gi|442622597|ref|NP_001260747|]
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missing-in-metastasis, isoform K [Drosophila melanogaster]

Protein Classification

BAR domain-containing protein( domain architecture ID 10166424)

BAR (Bin/Amphiphysin/Rvs) domain-containing protein may bind membranes and detect membrane curvature

CATH:  1.20.1270.60
Gene Ontology:  GO:0140090|GO:0097753
PubMed:  30456600|15649145|14993925|16524918|19379681
SCOP:  4001895

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
I-BAR_IMD_MIM cd07643
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Missing In Metastasis; ...
 7-238 6.88e-147

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Missing In Metastasis; The IMD domain, also called Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions. Members of this subfamily include missing in metastasis (MIM) or metastasis suppressor 1 (MTSS1), metastasis suppressor 1-like (MTSSL) or ABBA (Actin-Bundling protein with BAIAP2 homology), and similar proteins. They contain an N-terminal IMD and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. MIM was originally identified as a missing transcript from metastatic bladder and prostate cancer cells. It is a scaffold protein that functions in a signaling pathway between the PDGF receptor, Src kinases, and actin assembly. It may also function as a cofactor of the Sonic hedgehog (Shh) transcriptional pathway and may participate in tumor development and progression via this pathway. ABBA regulates actin and plasma membrane dynamics to promote the extension of radial glia, which is important in neuronal migration, axon guidance and neurogenesis. The IMD domain of MIM binds and bundles actin filaments, binds membranes, and interacts with the small GTPase Rac.


:

Pssm-ID: 153327  Cd Length: 231  Bit Score: 430.33  E-value: 6.88e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597   7 RDSSALGSLFQQIINDMKNTSPLWEDFVAKAGKLHTCLRAAIQAIAAYLDAFQKIADAATNSRGASKEIGTALTRVCLRH 86
Cdd:cd07643    1 KECSALGGLFQAIINDMKGSYPLWEDFVSKATKLHSQLRATIVATSAFLDAFQKIADAATNTRGATKEIGSALTRMCMRH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597  87 KAVETRLKTFTSTIMDCLVQPLQERIEDWKRTVATIDKDHAKEYKRCRSELKKRSSDTLRLQKKARKGQtDGLQSLMDSH 166
Cdd:cd07643   81 KSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTIRLQKKARKGK-GDLQPQLDSA 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622597 167 MQDVTLRRAELEEVEKKSLRAAMVEERLRYCSFVHMLQPVVHEECEVMSELGHLQEAMQSIALVTKEPSVLP 238
Cdd:cd07643  160 MQDVNDKYLLLEETEKKAVRNALIEERGRFCTFVSFLKPVLDEEISMLGEVTHLQTIMEDLASLTADPHKLP 231
Pneumo_att_G super family cl25814
Pneumovirinae attachment membrane glycoprotein G;
311-468 5.33e-04

Pneumovirinae attachment membrane glycoprotein G;


The actual alignment was detected with superfamily member pfam05539:

Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 43.11  E-value: 5.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597  311 PAIRLKPGESSDSGFCSSPALTTQTSNATNQTANVSTWPPhsqdgvdTLPPTADRPHTISTayekgHQRPPLTVYTFQNP 390
Cdd:pfam05539 232 PQTEPPPSQRGPSGSPQHPPSTTSQDQSTTGDGQEHTQRR-------KTPPATSNRRSPHS-----TATPPPTTKRQETG 299

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442622597  391 ETIHESGSCLNNGTAAPNGQPLSGQATPATQKSPAASLSRPPLPVRCSslerplsaqsnHRQGSGNNLLQRQCPSPIP 468
Cdd:pfam05539 300 RPTPRPTATTQSGSSPPHSSPPGVQANPTTQNLVDCKELDPPKPNSIC-----------YGVGIYNEALPRGCDIVVP 366
 
Name Accession Description Interval E-value
I-BAR_IMD_MIM cd07643
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Missing In Metastasis; ...
 7-238 6.88e-147

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Missing In Metastasis; The IMD domain, also called Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions. Members of this subfamily include missing in metastasis (MIM) or metastasis suppressor 1 (MTSS1), metastasis suppressor 1-like (MTSSL) or ABBA (Actin-Bundling protein with BAIAP2 homology), and similar proteins. They contain an N-terminal IMD and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. MIM was originally identified as a missing transcript from metastatic bladder and prostate cancer cells. It is a scaffold protein that functions in a signaling pathway between the PDGF receptor, Src kinases, and actin assembly. It may also function as a cofactor of the Sonic hedgehog (Shh) transcriptional pathway and may participate in tumor development and progression via this pathway. ABBA regulates actin and plasma membrane dynamics to promote the extension of radial glia, which is important in neuronal migration, axon guidance and neurogenesis. The IMD domain of MIM binds and bundles actin filaments, binds membranes, and interacts with the small GTPase Rac.


Pssm-ID: 153327  Cd Length: 231  Bit Score: 430.33  E-value: 6.88e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597   7 RDSSALGSLFQQIINDMKNTSPLWEDFVAKAGKLHTCLRAAIQAIAAYLDAFQKIADAATNSRGASKEIGTALTRVCLRH 86
Cdd:cd07643    1 KECSALGGLFQAIINDMKGSYPLWEDFVSKATKLHSQLRATIVATSAFLDAFQKIADAATNTRGATKEIGSALTRMCMRH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597  87 KAVETRLKTFTSTIMDCLVQPLQERIEDWKRTVATIDKDHAKEYKRCRSELKKRSSDTLRLQKKARKGQtDGLQSLMDSH 166
Cdd:cd07643   81 KSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTIRLQKKARKGK-GDLQPQLDSA 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622597 167 MQDVTLRRAELEEVEKKSLRAAMVEERLRYCSFVHMLQPVVHEECEVMSELGHLQEAMQSIALVTKEPSVLP 238
Cdd:cd07643  160 MQDVNDKYLLLEETEKKAVRNALIEERGRFCTFVSFLKPVLDEEISMLGEVTHLQTIMEDLASLTADPHKLP 231
IMD pfam08397
IRSp53/MIM homology domain; The N-terminal predicted helical stretch of the insulin receptor ...
 16-235 1.33e-67

IRSp53/MIM homology domain; The N-terminal predicted helical stretch of the insulin receptor tyrosine kinase substrate p53 (IRSp53) is an evolutionary conserved F-actin bundling domain involved in filopodium formation. The domain has been named IMD after the IRSp53 and missing in metastasis (MIM) proteins in which it occurs. Filopodium-inducing IMD activity is regulated by Cdc42 and Rac1 and is SH3-independent.


Pssm-ID: 429972  Cd Length: 218  Bit Score: 223.22  E-value: 1.33e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597   16 FQQIINDMKntsPLWEDFVAKAGKLHTCLRAAIQAIAAYLDAFQKIADAATNSRGaSKEIGTALTRVCLRHKAVETRLKT 95
Cdd:pfam08397   1 YKTIMEQFN---PALENFIYKGNNYLSALRTTVEAAEAYFDAFQKVGEMATNSRG-SRELGSALTQMCMRHRSIESKLEQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597   96 FTSTIMDCLVQPLQERIEDWKRTVATIDKDHAKEYKRCRSELKKRSSDTLRLQKKARKGQTDgLQSLMDSHMQDVTLRRA 175
Cdd:pfam08397  77 FVQAFHGGLLNPLEENTELDKKFANQLDKDYAKEYRHARAELKKCSSELLKLQKKADKGKGD-QQPQLDEALQDVNDKYL 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622597  176 ELEEVEKKSLRAAMVEERLRYCSFVHMLQPVVHEECEVMSE-LGHLQEAMQSIALVTKEPS 235
Cdd:pfam08397 156 LLEETVSQAVRAALIEERRRFCFLIEKLLPVSNTELQMLGEaITHLQNIVLLWKELTSEPH 216
Pneumo_att_G pfam05539
Pneumovirinae attachment membrane glycoprotein G;
311-468 5.33e-04

Pneumovirinae attachment membrane glycoprotein G;


Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 43.11  E-value: 5.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597  311 PAIRLKPGESSDSGFCSSPALTTQTSNATNQTANVSTWPPhsqdgvdTLPPTADRPHTISTayekgHQRPPLTVYTFQNP 390
Cdd:pfam05539 232 PQTEPPPSQRGPSGSPQHPPSTTSQDQSTTGDGQEHTQRR-------KTPPATSNRRSPHS-----TATPPPTTKRQETG 299

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442622597  391 ETIHESGSCLNNGTAAPNGQPLSGQATPATQKSPAASLSRPPLPVRCSslerplsaqsnHRQGSGNNLLQRQCPSPIP 468
Cdd:pfam05539 300 RPTPRPTATTQSGSSPPHSSPPGVQANPTTQNLVDCKELDPPKPNSIC-----------YGVGIYNEALPRGCDIVVP 366
PHA03378 PHA03378
EBNA-3B; Provisional
 359-543 2.16e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.59  E-value: 2.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597 359 LPPTADRPHTISTAYEKGHQRPPLTVYTFQNPETIHESGSCLNNGTAAPNGQpLSGQATPATQKSPAASLSRPPLPVRCS 438
Cdd:PHA03378 633 MRPLRMQPITFNVLVFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPTGANTM-LPIQWAPGTMQPPPRAPTPMRPPAAPP 711

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597 439 SLERPLSAQSNHRQGSGNNLLQRQCPSPIPAHITKGGAAGGGStrigRRSSINQSKPPPPVRRSSSVTPSPNASVG--LQ 516
Cdd:PHA03378 712 GRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRA----RPPAAAPGRARPPAAAPGAPTPQPPPQAPpaPQ 787

                        170       180
                 ....*....|....*....|....*..
gi 442622597 517 QQPQHATLSQQNHQLSSSSEHLPPPPP 543
Cdd:PHA03378 788 QRPRGAPTPQPPPQAGPTSMQLMPRAA 814
 
Name Accession Description Interval E-value
I-BAR_IMD_MIM cd07643
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Missing In Metastasis; ...
 7-238 6.88e-147

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Missing In Metastasis; The IMD domain, also called Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions. Members of this subfamily include missing in metastasis (MIM) or metastasis suppressor 1 (MTSS1), metastasis suppressor 1-like (MTSSL) or ABBA (Actin-Bundling protein with BAIAP2 homology), and similar proteins. They contain an N-terminal IMD and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. MIM was originally identified as a missing transcript from metastatic bladder and prostate cancer cells. It is a scaffold protein that functions in a signaling pathway between the PDGF receptor, Src kinases, and actin assembly. It may also function as a cofactor of the Sonic hedgehog (Shh) transcriptional pathway and may participate in tumor development and progression via this pathway. ABBA regulates actin and plasma membrane dynamics to promote the extension of radial glia, which is important in neuronal migration, axon guidance and neurogenesis. The IMD domain of MIM binds and bundles actin filaments, binds membranes, and interacts with the small GTPase Rac.


Pssm-ID: 153327  Cd Length: 231  Bit Score: 430.33  E-value: 6.88e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597   7 RDSSALGSLFQQIINDMKNTSPLWEDFVAKAGKLHTCLRAAIQAIAAYLDAFQKIADAATNSRGASKEIGTALTRVCLRH 86
Cdd:cd07643    1 KECSALGGLFQAIINDMKGSYPLWEDFVSKATKLHSQLRATIVATSAFLDAFQKIADAATNTRGATKEIGSALTRMCMRH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597  87 KAVETRLKTFTSTIMDCLVQPLQERIEDWKRTVATIDKDHAKEYKRCRSELKKRSSDTLRLQKKARKGQtDGLQSLMDSH 166
Cdd:cd07643   81 KSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTIRLQKKARKGK-GDLQPQLDSA 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622597 167 MQDVTLRRAELEEVEKKSLRAAMVEERLRYCSFVHMLQPVVHEECEVMSELGHLQEAMQSIALVTKEPSVLP 238
Cdd:cd07643  160 MQDVNDKYLLLEETEKKAVRNALIEERGRFCTFVSFLKPVLDEEISMLGEVTHLQTIMEDLASLTADPHKLP 231
IMD pfam08397
IRSp53/MIM homology domain; The N-terminal predicted helical stretch of the insulin receptor ...
 16-235 1.33e-67

IRSp53/MIM homology domain; The N-terminal predicted helical stretch of the insulin receptor tyrosine kinase substrate p53 (IRSp53) is an evolutionary conserved F-actin bundling domain involved in filopodium formation. The domain has been named IMD after the IRSp53 and missing in metastasis (MIM) proteins in which it occurs. Filopodium-inducing IMD activity is regulated by Cdc42 and Rac1 and is SH3-independent.


Pssm-ID: 429972  Cd Length: 218  Bit Score: 223.22  E-value: 1.33e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597   16 FQQIINDMKntsPLWEDFVAKAGKLHTCLRAAIQAIAAYLDAFQKIADAATNSRGaSKEIGTALTRVCLRHKAVETRLKT 95
Cdd:pfam08397   1 YKTIMEQFN---PALENFIYKGNNYLSALRTTVEAAEAYFDAFQKVGEMATNSRG-SRELGSALTQMCMRHRSIESKLEQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597   96 FTSTIMDCLVQPLQERIEDWKRTVATIDKDHAKEYKRCRSELKKRSSDTLRLQKKARKGQTDgLQSLMDSHMQDVTLRRA 175
Cdd:pfam08397  77 FVQAFHGGLLNPLEENTELDKKFANQLDKDYAKEYRHARAELKKCSSELLKLQKKADKGKGD-QQPQLDEALQDVNDKYL 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622597  176 ELEEVEKKSLRAAMVEERLRYCSFVHMLQPVVHEECEVMSE-LGHLQEAMQSIALVTKEPS 235
Cdd:pfam08397 156 LLEETVSQAVRAALIEERRRFCFLIEKLLPVSNTELQMLGEaITHLQNIVLLWKELTSEPH 216
I-BAR_IMD cd07605
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module ...
 10-223 1.36e-51

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module that binds and bends membranes; Inverse (I)-BAR (or IMD) is a member of the Bin/Amphiphysin/Rvs (BAR) domain family. It is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. IMD domains are found in Insulin Receptor tyrosine kinase Substrate p53 (IRSp53), Missing in Metastasis (MIM), and Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-like (BAIAP2L) proteins. These are multi-domain proteins that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. Most members contain an N-terminal IMD, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus, exccept for MIM which does not carry an SH3 domain. Some members contain additional domains and motifs. The IMD domain binds and bundles actin filaments, binds membranes and produces membrane protrusions, and interacts with the small GTPase Rac.


Pssm-ID: 153289 [Multi-domain]  Cd Length: 223  Bit Score: 179.48  E-value: 1.36e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597  10 SALGSLFQQII-NDMKNTSPLWEDFVAKAGKLHTCLRAAIQAIAAYLDAFQKIADAATNSRGaSKEIGTALTRVCLRHKA 88
Cdd:cd07605    1 EELNRLTENIYkNIKEQFNPVLRNLIKAGKKYQKALQALSQAAKVFFDALAKIGELASQSRG-SQELGEALKQIVDTHKS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597  89 VETRLKTFTSTIMDCLVQPLQERIEDWKRTVATIDKDHAKEYKRCRSELKKRSSDTLRLQKKARKGQTDGLQSLMDSHMQ 168
Cdd:cd07605   80 IEASLEQVAKAFHGELILPLEKKLELDQKVINKFEKDYKKEYKQKREDLDKARSELKKLQKKSQKSGTGKYQEKLDQALE 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 442622597 169 DVTLRRAELEEVEKKSLRAAMVEERLRYCSFVHMLQPVVHEECEVMS-ELGHLQEA 223
Cdd:cd07605  160 ELNDKQKELEAFVSQGLRDALLEERRRYCFLVDKHCSVAKHEIAYHAkAMTLLSTR 215
I-BAR_IMD_IRSp53 cd07646
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Insulin Receptor ...
 23-200 6.21e-10

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Insulin Receptor tyrosine kinase Substrate p53; The IMD domain, also called Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions. IRSp53 (Insulin Receptor tyrosine kinase Substrate p53) is also known as BAIAP2 (Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2). It is a scaffolding protein that takes part in many signaling pathways including Cdc42-induced filopodia formation, Rac-mediated lamellipodia extension, and spine morphogenesis. IRSp53 exists as multiple splicing variants that differ mainly at the C-termini. One variant (T-form) is expressed exclusively in human breast cancer cells. The gene encoding IRSp53 is a putative susceptibility gene for Gilles de la Tourette syndrome. IRSp53 contains an N-terminal IMD, a CRIB (Cdc42 and Rac interactive binding motif), an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. Its IMD domain binds and bundles actin filaments, binds membranes, and interacts with the small GTPase Rac.


Pssm-ID: 153330  Cd Length: 232  Bit Score: 60.33  E-value: 6.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597  23 MKNTSPLWEDFVAKAGKLHTCLRAAIQAIAAYLDAFQKIADAATNSRGaSKEIGTALTRVCLRHKAVETRLKTFTSTIMD 102
Cdd:cd07646   17 MEQFNPSLRNFIAMGKNYEKALASVTFAAKGYFDALVKMGELASESQG-SKELGDVLFQMAEVHRQIQNQLEEMLKSFHN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597 103 CLVQPLQERIEDWKRTVATIDKDHAKEYK-------RCRSELKKrssdtlrLQKKARKGQTDGLQSLMDS-HMQDVTLRR 174
Cdd:cd07646   96 ELLTQLEQKVELDSRYLTAALKKYQTEHRskgesleKCQAELKK-------LRKKSQGSKNPQKYSDKELqYIEAISNKQ 168

                        170       180
                 ....*....|....*....|....*.
gi 442622597 175 AELEEVEKKSLRAAMVEERLRYCSFV 200
Cdd:cd07646  169 GELENYVSDGYKTALTEERRRYCFLV 194
I-BAR_IMD_BAIAP2L1 cd07645
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Brain-specific ...
 21-200 1.11e-07

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 1; The IMD domain, also called Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions. BAIAP2L1 (Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 1) is also known as IRTKS (Insulin Receptor Tyrosine Kinase Substrate). It is widely expressed, serves as a substrate for the insulin receptor, and binds the small GTPase Rac. It plays a role in regulating the actin cytoskeleton and colocalizes with F-actin, cortactin, VASP, and vinculin. BAIAP2L1 expression leads to the formation of short actin bundles, distinct from filopodia-like protrusions induced by the expression of the related protein IRSp53. It contains an N-terminal IMD, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. The IMD domain of BAIAP2L1 binds and bundles actin filaments, and binds the small GTPase Rac.


Pssm-ID: 153329  Cd Length: 226  Bit Score: 53.38  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597  21 NDMKNTSPLWEDFVAKAGKLHTCLRAAIQAIAAYLDAFQKIADAATNSRgASKEIGTALTRVCLRHKAVETRLKTFTSTI 100
Cdd:cd07645   13 NVMEQFNPGLRNLINLGKNYEKAVNAMVLAGKAYYDGVAKIGEIAAVSP-VSKELGHVLMEISDVHKKLNDSLEENFKKF 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597 101 MDCLVQPLQERIE-DWKRTVATIdKDHAKEYKRCRSELKKRSSDTLRLQKKARKGQT-DGLQSLMDSHMQDVTLRRAELE 178
Cdd:cd07645   92 HREIIAELERKTDlDVKYMTATL-KRYQTEHKNKLDSLEKSQADLKKIRRKSQGRRNaSKYEHKENEYLETVTSRQSDIQ 170

                        170       180
                 ....*....|....*....|..
gi 442622597 179 EVEKKSLRAAMVEERLRYCSFV 200
Cdd:cd07645  171 KFIADGCREALLEEKRRFCFLV 192
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 39-179 2.93e-04

The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively.


Pssm-ID: 153271 [Multi-domain]  Cd Length: 194  Bit Score: 42.82  E-value: 2.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597  39 KLHTCLRAAIQAIAAYLDAFQKIADAATNSrgASKEIGTALTRVCLRHKAVETRLKTFTSTIMDCLVQPLQERI-EDWKR 117
Cdd:cd07307   18 KLLDSLKELPAAAEKLSEALQELGKELPDL--SNTDLGEALEKFGKIQKELEEFRDQLEQKLENKVIEPLKEYLkKDLKE 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622597 118 TvatidKDHAKEYKRCRSELKKRSSDTLRLQKKARKGQTD-GLQSLMDSHMQDVTLRRAELEE 179
Cdd:cd07307   96 I-----KKRRKKLDKARLDYDAAREKLKKLRKKKKDSSKLaEAEEELQEAKEKYEELREELIE 153
Pneumo_att_G pfam05539
Pneumovirinae attachment membrane glycoprotein G;
311-468 5.33e-04

Pneumovirinae attachment membrane glycoprotein G;


Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 43.11  E-value: 5.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597  311 PAIRLKPGESSDSGFCSSPALTTQTSNATNQTANVSTWPPhsqdgvdTLPPTADRPHTISTayekgHQRPPLTVYTFQNP 390
Cdd:pfam05539 232 PQTEPPPSQRGPSGSPQHPPSTTSQDQSTTGDGQEHTQRR-------KTPPATSNRRSPHS-----TATPPPTTKRQETG 299

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442622597  391 ETIHESGSCLNNGTAAPNGQPLSGQATPATQKSPAASLSRPPLPVRCSslerplsaqsnHRQGSGNNLLQRQCPSPIP 468
Cdd:pfam05539 300 RPTPRPTATTQSGSSPPHSSPPGVQANPTTQNLVDCKELDPPKPNSIC-----------YGVGIYNEALPRGCDIVVP 366
PHA03378 PHA03378
EBNA-3B; Provisional
 359-543 2.16e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.59  E-value: 2.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597 359 LPPTADRPHTISTAYEKGHQRPPLTVYTFQNPETIHESGSCLNNGTAAPNGQpLSGQATPATQKSPAASLSRPPLPVRCS 438
Cdd:PHA03378 633 MRPLRMQPITFNVLVFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPTGANTM-LPIQWAPGTMQPPPRAPTPMRPPAAPP 711

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597 439 SLERPLSAQSNHRQGSGNNLLQRQCPSPIPAHITKGGAAGGGStrigRRSSINQSKPPPPVRRSSSVTPSPNASVG--LQ 516
Cdd:PHA03378 712 GRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRA----RPPAAAPGRARPPAAAPGAPTPQPPPQAPpaPQ 787

                        170       180
                 ....*....|....*....|....*..
gi 442622597 517 QQPQHATLSQQNHQLSSSSEHLPPPPP 543
Cdd:PHA03378 788 QRPRGAPTPQPPPQAGPTSMQLMPRAA 814
Pneumo_att_G pfam05539
Pneumovirinae attachment membrane glycoprotein G;
320-543 9.51e-03

Pneumovirinae attachment membrane glycoprotein G;


Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 39.26  E-value: 9.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597  320 SSDSGFCSSPALTTQTSNATNQTANVSTWPPHSQDGVDTLPPTadRPHTISTAyekghqrppltvytfqnPETIHESGSC 399
Cdd:pfam05539 159 GKDVSCCKEPKTAVTTSKTTSWPTEVSHPTYPSQVTPQSQPAT--QGHQTATA-----------------NQRLSSTEPV 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597  400 LNNGTAAP-NGQPlsgQATPatqkspaaslsrPPLPVRCSSLERPLSAQSNHRQ---GSGNNLLQRQCPSPIPAHitkgg 475
Cdd:pfam05539 220 GTQGTTTSsNPEP---QTEP------------PPSQRGPSGSPQHPPSTTSQDQsttGDGQEHTQRRKTPPATSN----- 279

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442622597  476 aagggstrigRRSSINQSKPPPPVRRSSSVTPSPNASVGLQQQPQHATLS----QQN--HQLSSSSEHLPPPPP 543
Cdd:pfam05539 280 ----------RRSPHSTATPPPTTKRQETGRPTPRPTATTQSGSSPPHSSppgvQANptTQNLVDCKELDPPKP 343
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 300-577 9.97e-03

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 39.17  E-value: 9.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597  300 HYPRSlSQFVTPAIRLKPGESSDSGFCSSPALTTQTSNATNQTANVSTWPPHSQDGvdtlpPTADRPHTISTAYEKGHQR 379
Cdd:pfam17823  90 HTPHG-TDLSEPATREGAADGAASRALAAAASSSPSSAAQSLPAAIAALPSEAFSA-----PRAAACRANASAAPRAAIA 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597  380 PPLTVYTFQNPETIHESGSCLNNGTAAPNGQPLSGQATPATQKSPAASLSRPPLPVRCSSLERPLSAQSNHRQGSGNNLL 459
Cdd:pfam17823 164 AASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPARGISTAATATGHPAAGTALAAVGNSSPAAGTVTA 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622597  460 QRQCPSPIpahiTKGGAAGGGSTRIGRRSSINQSKP----PPPVRRSSSVTPSPNASVGLQQQPQHATLSQQNHQLSSSS 535
Cdd:pfam17823 244 AVGTVTPA----ALATLAAAAGTVASAAGTINMGDPharrLSPAKHMPSDTMARNPAAPMGAQAQGPIIQVSTDQPVHNT 319

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 442622597  536 EHLPPPPPFMLDAMPQIPSSALKVSETV--RALAAMRHQPASPV 577
Cdd:pfam17823 320 AGEPTPSPSNTTLEPNTPKSVASTNLAVvtTTKAQAKEPSASPV 363
 
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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