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Conserved domains on  [gi|281362532|ref|NP_651342|]
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Band4.1 inhibitor LRP interactor, isoform B [Drosophila melanogaster]

Protein Classification

FERM_B-lobe and PH-like domain-containing protein( domain architecture ID 10448719)

FERM_B-lobe and PH-like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 537-663 1.51e-20

FERM central domain; This domain is the central structural domain of the FERM domain.


:

Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 87.71  E-value: 1.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362532  537 DEEKIKDHRILELLYEEARNNVLTGRYIMEPVHSLMLGGIQARIELGPYNSHTHTIGFFRenQARFLPPHVaksstwlwl 616
Cdd:pfam00373   2 LELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLS--LESFLPKQL--------- 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 281362532  617 pISQKNSAEVK--LLEQFKRV-PQTATtrKLMRKYLEFCWALPFYGAAYF 663
Cdd:pfam00373  71 -LRKMKSKELEkrVLEAHKNLrGLSAE--EAKLKYLQIAQSLPTYGVEFF 117
 
Name Accession Description Interval E-value
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 537-663 1.51e-20

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 87.71  E-value: 1.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362532  537 DEEKIKDHRILELLYEEARNNVLTGRYIMEPVHSLMLGGIQARIELGPYNSHTHTIGFFRenQARFLPPHVaksstwlwl 616
Cdd:pfam00373   2 LELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLS--LESFLPKQL--------- 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 281362532  617 pISQKNSAEVK--LLEQFKRV-PQTATtrKLMRKYLEFCWALPFYGAAYF 663
Cdd:pfam00373  71 -LRKMKSKELEkrVLEAHKNLrGLSAE--EAKLKYLQIAQSLPTYGVEFF 117
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 432-663 2.30e-16

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 78.49  E-value: 2.30e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362532   432 VYLMSRVAVHMEIEGTAQCpsQVMLAAAlgCEELGISNKLLaqsvFGLWMTSALLEMQlkahhcpyivrvAWPNLLQKFS 511
Cdd:smart00295   4 VYLLDGTTLEFEVDSSTTA--EELLETV--CRKLGIRESEY----FGLQFEDPDEDLR------------HWLDPAKTLL 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362532   512 NSspsDRKFdEPMIVLKRNVFFSKRDEEKIKDHRILELLYEEARNNVLTGRYIMEPVHSLMLGGIQARIELGPYNSHTHt 591
Cdd:smart00295  64 DQ---DVKS-EPLTLYFRVKFYPPDPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELH- 138

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281362532   592 IGFFRENQARFLPPHVAKSSTWLWLpisqknsaEVKLLEQFKRVpQTATTRKLMRKYLEFCWALPFYGAAYF 663
Cdd:smart00295 139 DLRGELSLKRFLPKQLLDSRKLKEW--------RERIVELHKEL-IGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 547-655 1.29e-09

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 56.10  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362532 547 LELLYEEARNNVLTGRYIMEPVHSLMLGGIQARIELGPYNSHTHTIGFFRENqaRFLPPHVAKSSTwlwlpisqKNSAEV 626
Cdd:cd14473    2 RYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLSLK--RFLPKQLLKQRK--------PEEWEK 71

                         90       100
                 ....*....|....*....|....*....
gi 281362532 627 KLLEQFKRVpQTATTRKLMRKYLEFCWAL 655
Cdd:cd14473   72 RIVELHKKL-RGLSPAEAKLKYLKIARKL 99
 
Name Accession Description Interval E-value
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 537-663 1.51e-20

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 87.71  E-value: 1.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362532  537 DEEKIKDHRILELLYEEARNNVLTGRYIMEPVHSLMLGGIQARIELGPYNSHTHTIGFFRenQARFLPPHVaksstwlwl 616
Cdd:pfam00373   2 LELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLS--LESFLPKQL--------- 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 281362532  617 pISQKNSAEVK--LLEQFKRV-PQTATtrKLMRKYLEFCWALPFYGAAYF 663
Cdd:pfam00373  71 -LRKMKSKELEkrVLEAHKNLrGLSAE--EAKLKYLQIAQSLPTYGVEFF 117
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 432-663 2.30e-16

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 78.49  E-value: 2.30e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362532   432 VYLMSRVAVHMEIEGTAQCpsQVMLAAAlgCEELGISNKLLaqsvFGLWMTSALLEMQlkahhcpyivrvAWPNLLQKFS 511
Cdd:smart00295   4 VYLLDGTTLEFEVDSSTTA--EELLETV--CRKLGIRESEY----FGLQFEDPDEDLR------------HWLDPAKTLL 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362532   512 NSspsDRKFdEPMIVLKRNVFFSKRDEEKIKDHRILELLYEEARNNVLTGRYIMEPVHSLMLGGIQARIELGPYNSHTHt 591
Cdd:smart00295  64 DQ---DVKS-EPLTLYFRVKFYPPDPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELH- 138

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281362532   592 IGFFRENQARFLPPHVAKSSTWLWLpisqknsaEVKLLEQFKRVpQTATTRKLMRKYLEFCWALPFYGAAYF 663
Cdd:smart00295 139 DLRGELSLKRFLPKQLLDSRKLKEW--------RERIVELHKEL-IGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 547-655 1.29e-09

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 56.10  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362532 547 LELLYEEARNNVLTGRYIMEPVHSLMLGGIQARIELGPYNSHTHTIGFFRENqaRFLPPHVAKSSTwlwlpisqKNSAEV 626
Cdd:cd14473    2 RYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLSLK--RFLPKQLLKQRK--------PEEWEK 71

                         90       100
                 ....*....|....*....|....*....
gi 281362532 627 KLLEQFKRVpQTATTRKLMRKYLEFCWAL 655
Cdd:cd14473   72 RIVELHKKL-RGLSPAEAKLKYLKIARKL 99
 
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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