1WDZ


Conserved Protein Domain Family
IMD
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pfam08397: IMD 
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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.
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Statistics
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PSSM-Id: 429972
Aligned: 4 rows
Threshold Bit Score: 304.108
Created: 23-Mar-2022
Updated: 17-Oct-2022
Structure
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Program:
Drawing:
Aligned Rows:
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PubMed ReferencesClick to see Conserved Features Help
Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
1WDZ_B  20 YKTIMEQFN---PSLRNFIAMGKNYEKALAGVTYAAKGYFDALVKMGELASESQG-SKELGDVLFQMAEVHRQIQNQLEE 95  human
O43312  16 FQTIISDMKgsyPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGgTREIGSALTRMCMRHRSIEAKLRQ 95  human
Q765P7  15 FQAIVNDMKssyPIWEDFNSKATKLHSQLRTTVLAAVAFLDAFQKVADMATNTRGaTRDIGSALTRMCMRHRSIETKLRQ 94  human
Q6UXY1  16 YKSIMEQFN---PALENLVYLGNNYLRAFHALSEAAEVYFSAIQKIGERALQSPT-SQILGEILVQMSDTQRHLNSDLEV 91  human

1WDZ_B  96 MLKSFHNELLTQLEQKVELDSRYLSAALKKYQTEQRSKGDALDKCQAELKKLRKKSQG---SKNPQKYSDKELqyIDAIS 172 human
O43312  96 FSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKK---GRGDIQPQLDSA--LQDVN 170 human
Q765P7  95 FTNALLESLINPLQERIEDWKKAANQLDKDHAKEYKRARHEIKKKSSDTLKLQKKARKellGKGDLQPQLDSA--LQDVN 172 human
Q6UXY1  92 VVQTFHGGLLQHMEKNTKLDMQFIKDSRQHYELEYRHRAANLEKCMSELWRMERKRDK----------NVREM--KESVN 159 human

1WDZ_B 173 NKQGELENYVSDGYKTALTEERRRFCFLVEKQCAVAKNSAAYHSKgKELLAQKLPLWQQGVDSSGRI 239 human
O43312 171 DKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGE-ITHLQTISEDLKSLTMDPHKL 236 human
Q765P7 173 DMYLLLEETEKQAVRRALIEERGRFCTFITFLQPVVNGELTMLGE-ITHLQGIIDDLVVLTAEPHKL 238 human
Q6UXY1 160 RLHAQMQAFVSESQRAAELEEKRRYRFLAEKHLLLSNTFLQFFGRaRGMLQNRVLLWKEQ-SEASRS 225 human
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