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Conserved domains on  [gi|585866240|ref|NP_001276938|]
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bridging integrator 2 isoform 4 [Homo sapiens]

Protein Classification

BAR domain-containing protein( domain architecture ID 36964)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAR super family cl12013
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 1-116 1.15e-79

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.


The actual alignment was detected with superfamily member cd07612:

Pssm-ID: 472257  Cd Length: 211  Bit Score: 245.54  E-value: 1.15e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240   1 MEIYVAQFSEIKERIAKRGRKLVDYDSARHHLEAVQNAKKKDEAKTAKAEEEFNKAQTVFEDLNQELLEELPILYNSRIG 80
Cdd:cd07612   96 MESYMAQFPDVKERVAKRGRKLVDYDSARHHLEALQNAKKKDDAKIAKAEEEFNRAQVVFEDINRELREELPILYDSRIG 175

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 585866240  81 CYVTIFQNISNLRDVFYREMSKLNHNLYEVMSKLEK 116
Cdd:cd07612  176 CYVTVFQNISNLRDTFYKEMSKLNHDLYNVMKKLED 211
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 139-359 9.00e-05

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 9.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240  139 SPPVRTATVSSPLTSPTSPSTLSLKSESESVSATEDLAPDAAQGEDNSEIKELLEEEEIEKEGSEASSSEEDEPLPACNG 218
Cdd:PHA03307  207 PRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPAS 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240  219 PAQAQPSPTTERAKSQEEVLPSSTTPSPGGALSPSGQPSSSATevvlrtRTASEGSEQPKKRASIQRTSAPPSRPPPPRA 298
Cdd:PHA03307  287 SSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSST------SSSSESSRGAAVSPGPSPSRSPSPSRPPPPA 360

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 585866240  299 TASPRPSSGN---IPSSPTASgGGSPTSPRA-SLGTGTASPRTSLEVSPNPEPPEKPVRTPEAKE 359
Cdd:PHA03307  361 DPSSPRKRPRpsrAPSSPAAS-AGRPTRRRArAAVAGRARRRDATGRFPAGRPRPSPLDAGAASG 424
 
Name Accession Description Interval E-value
BAR_Bin2 cd07612
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 2; BAR domains are dimerization, ...
 1-116 1.15e-79

The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Bridging integrator 2 (Bin2) is a BAR domain containing protein that is mainly expressed in hematopoietic cells. It is upregulated during granulocyte differentiation and is thought to function primarily in this lineage. The BAR domain of Bin2 is closely related to the BAR domains of amphiphysins, which function primarily in endocytosis and other membrane remodeling events. Amphiphysins contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. Unlike amphiphysins, Bin2 does not appear to contain a C-terminal SH3 domain. Amphiphysin I proteins, enriched in the brain and nervous system, function in synaptic vesicle endocytosis. Some amphiphysin II isoforms, also called Bridging integrator 1 (Bin1), function in intracellular vessicle trafficking. Bin2 can form a stable complex with Bin1 in cells but cannot replace the function of Bin1, and thus, appears to harbor a nonredundant function. The N-BAR domain of amphiphysin forms a curved dimer with a positively-charged concave face that can drive membrane bending and curvature.


Pssm-ID: 153296  Cd Length: 211  Bit Score: 245.54  E-value: 1.15e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240   1 MEIYVAQFSEIKERIAKRGRKLVDYDSARHHLEAVQNAKKKDEAKTAKAEEEFNKAQTVFEDLNQELLEELPILYNSRIG 80
Cdd:cd07612   96 MESYMAQFPDVKERVAKRGRKLVDYDSARHHLEALQNAKKKDDAKIAKAEEEFNRAQVVFEDINRELREELPILYDSRIG 175

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 585866240  81 CYVTIFQNISNLRDVFYREMSKLNHNLYEVMSKLEK 116
Cdd:cd07612  176 CYVTVFQNISNLRDTFYKEMSKLNHDLYNVMKKLED 211
BAR smart00721
BAR domain;
1-113 2.43e-34

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 128.27  E-value: 2.43e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240     1 MEIYVAQFSEIKERIAKRGRKLVDYDSARHHLEAVQNAKKKDEA-KTAKAEEEFNKAQTVFEDLNQELLEELPILYNSRI 79
Cdd:smart00721 126 LNFLLGEFKEIKKARKKLERKLLDYDSARHKLKKAKKSKEKKKDeKLAKAEEELRKAKQEFEESNAQLVEELPQLVASRV 205

                           90       100       110
                   ....*....|....*....|....*....|....
gi 585866240    80 GCYVTIFQNISNLRDVFYREMSKLNHNLYEVMSK 113
Cdd:smart00721 206 DFFVNCLQALIEAQLNFHRESYKLLQQLQQQLDK 239
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
 1-113 3.54e-19

BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different protein families. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysin, endophilin, BRAP and Nadrin. BAR domains are also frequently found alongside domains that determine lipid specificity, like pfam00169 and pfam00787 domains in beta centaurins and sorting nexins respectively.


Pssm-ID: 460810 [Multi-domain]  Cd Length: 235  Bit Score: 86.24  E-value: 3.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240    1 MEIYVAQFSEIKERIAKRGRKLVDYDSARHHLEAVQNAKKKDEAKTAKAEEEFNKAQTVFEDLNQELLEELPILYNSRIG 80
Cdd:pfam03114 123 LRNLLKEFKEIQKHRKKLERKRLDYDAAKTRVKKAKKKKSSKAKDESQAEEELRKAQAKFEESNEQLKALLPNLLSLEVE 202

                          90       100       110
                  ....*....|....*....|....*....|...
gi 585866240   81 CYVTIFQNISNLRDVFYREMSKLNHNLYEVMSK 113
Cdd:pfam03114 203 FVVNQLVAFVEAQLDFHRQCYQLLEQLQQQLGK 235
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 139-359 9.00e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 9.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240  139 SPPVRTATVSSPLTSPTSPSTLSLKSESESVSATEDLAPDAAQGEDNSEIKELLEEEEIEKEGSEASSSEEDEPLPACNG 218
Cdd:PHA03307  207 PRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPAS 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240  219 PAQAQPSPTTERAKSQEEVLPSSTTPSPGGALSPSGQPSSSATevvlrtRTASEGSEQPKKRASIQRTSAPPSRPPPPRA 298
Cdd:PHA03307  287 SSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSST------SSSSESSRGAAVSPGPSPSRSPSPSRPPPPA 360

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 585866240  299 TASPRPSSGN---IPSSPTASgGGSPTSPRA-SLGTGTASPRTSLEVSPNPEPPEKPVRTPEAKE 359
Cdd:PHA03307  361 DPSSPRKRPRpsrAPSSPAAS-AGRPTRRRArAAVAGRARRRDATGRFPAGRPRPSPLDAGAASG 424
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 140-389 2.08e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 40.67  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240  140 PPVRTATVSSPL----TSPTSPSTlslKSESESVSATEDLAPDAAqgednseikELLEEEEIEKEGSEASSSEEDEPLPA 215
Cdd:pfam05109 466 PTVSTADVTSPTpagtTSGASPVT---PSPSPRDNGTESKAPDMT---------SPTSAVTTPTPNATSPTPAVTTPTPN 533

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240  216 CNGPAQAQPSPT---TERAKSQEEVLPSSTTPSPGGALSPSGQ--PSSSATEVVLRTRTASEGSEQPKKRASIQR----T 286
Cdd:pfam05109 534 ATSPTLGKTSPTsavTTPTPNATSPTPAVTTPTPNATIPTLGKtsPTSAVTTPTPNATSPTVGETSPQANTTNHTlggtS 613

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240  287 SAPPSRPPPPRATASPRPSSGNIPSSPTASGGGSPTSPRASLGTGTASPRTS---LEVSPNPEPPEKPVR-TPEAKENEN 362
Cdd:pfam05109 614 STPVVTSPPKNATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTShmpLLTSAHPTGGENITQvTPASTSTHH 693

                         250       260
                  ....*....|....*....|....*..
gi 585866240  363 IHNQNPeelctSPTLMTSQVASEPGEA 389
Cdd:pfam05109 694 VSTSSP-----APRPGTTSQASGPGNS 715
 
Name Accession Description Interval E-value
BAR_Bin2 cd07612
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 2; BAR domains are dimerization, ...
 1-116 1.15e-79

The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Bridging integrator 2 (Bin2) is a BAR domain containing protein that is mainly expressed in hematopoietic cells. It is upregulated during granulocyte differentiation and is thought to function primarily in this lineage. The BAR domain of Bin2 is closely related to the BAR domains of amphiphysins, which function primarily in endocytosis and other membrane remodeling events. Amphiphysins contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. Unlike amphiphysins, Bin2 does not appear to contain a C-terminal SH3 domain. Amphiphysin I proteins, enriched in the brain and nervous system, function in synaptic vesicle endocytosis. Some amphiphysin II isoforms, also called Bridging integrator 1 (Bin1), function in intracellular vessicle trafficking. Bin2 can form a stable complex with Bin1 in cells but cannot replace the function of Bin1, and thus, appears to harbor a nonredundant function. The N-BAR domain of amphiphysin forms a curved dimer with a positively-charged concave face that can drive membrane bending and curvature.


Pssm-ID: 153296  Cd Length: 211  Bit Score: 245.54  E-value: 1.15e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240   1 MEIYVAQFSEIKERIAKRGRKLVDYDSARHHLEAVQNAKKKDEAKTAKAEEEFNKAQTVFEDLNQELLEELPILYNSRIG 80
Cdd:cd07612   96 MESYMAQFPDVKERVAKRGRKLVDYDSARHHLEALQNAKKKDDAKIAKAEEEFNRAQVVFEDINRELREELPILYDSRIG 175

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 585866240  81 CYVTIFQNISNLRDVFYREMSKLNHNLYEVMSKLEK 116
Cdd:cd07612  176 CYVTVFQNISNLRDTFYKEMSKLNHDLYNVMKKLED 211
BAR_Amphiphysin cd07588
The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysins; BAR domains are dimerization, lipid ...
 1-116 4.67e-60

The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Amphiphysins function primarily in endocytosis and other membrane remodeling events. They contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. This subfamily is composed of different isoforms of amphiphysin and Bridging integrator 2 (Bin2). Amphiphysin I proteins, enriched in the brain and nervous system, contain domains that bind clathrin, Adaptor Protein complex 2 (AP2), dynamin and synaptojanin. They function in synaptic vesicle endocytosis. Some amphiphysin II isoforms, also called Bridging integrator 1 (Bin1), are localized in many different tissues and may function in intracellular vesicle trafficking. In skeletal muscle, Bin1 plays a role in the organization and maintenance of the T-tubule network. Bin2 is mainly expressed in hematopoietic cells and is upregulated during granulocyte differentiation. The N-BAR domains of amphiphysins form a curved dimer with a positively-charged concave face that can drive membrane bending and curvature.


Pssm-ID: 153272  Cd Length: 211  Bit Score: 194.88  E-value: 4.67e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240   1 MEIYVAQFSEIKERIAKRGRKLVDYDSARHHLEAVQNAKKKDEAKTAKAEEEFNKAQTVFEDLNQELLEELPILYNSRIG 80
Cdd:cd07588   96 LTAYQSQFPEVKKRIAKRGRKLVDYDSARHNLEALKAKKKVDDQKLTKAEEELQQAKKVYEELNTELHEELPALYDSRIA 175

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 585866240  81 CYVTIFQNISNLRDVFYREMSKLNHNLYEVMSKLEK 116
Cdd:cd07588  176 FYVDTLQSIFAAESVFHKEIGKVNTKLNDVMDGLAD 211
BAR_Amphiphysin_I_II cd07611
The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysin I and II; BAR domains are dimerization, ...
 1-116 5.36e-56

The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysin I and II; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Amphiphysins function primarily in endocytosis and other membrane remodeling events. They contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. Amphiphysin I proteins, enriched in the brain and nervous system, contain domains that bind clathrin, Adaptor Protein complex 2 (AP2), dynamin and synaptojanin. They function in synaptic vesicle endocytosis. Some amphiphysin II isoforms, also called Bridging integrator 1 (Bin1), are localized in many different tissues and may function in intracellular vesicle trafficking. In skeletal muscle, Bin1 plays a role in the organization and maintenance of the T-tubule network. The N-BAR domain of amphiphysin forms a curved dimer with a positively-charged concave face that can drive membrane bending and curvature. Human autoantibodies to amphiphysin-1 hinder GABAergic signaling and contribute to the pathogenesis of paraneoplastic stiff-person syndrome. Mutations in amphiphysin-2 (BIN1) are associated with autosomal recessive centronuclear myopathy.


Pssm-ID: 153295  Cd Length: 211  Bit Score: 184.37  E-value: 5.36e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240   1 MEIYVAQFSEIKERIAKRGRKLVDYDSARHHLEAVQNAKKKDEAKTAKAEEEFNKAQTVFEDLNQELLEELPILYNSRIG 80
Cdd:cd07611   96 LDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEALQTSKRKDEGRIAKAEEEFQKAQKVFEEFNVDLQEELPSLWSRRVG 175

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 585866240  81 CYVTIFQNISNLRDVFYREMSKLNHNLYEVMSKLEK 116
Cdd:cd07611  176 FYVNTFKNVSSLEAKFHKEISVLCHKLYEVMTKLGE 211
BAR smart00721
BAR domain;
1-113 2.43e-34

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 128.27  E-value: 2.43e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240     1 MEIYVAQFSEIKERIAKRGRKLVDYDSARHHLEAVQNAKKKDEA-KTAKAEEEFNKAQTVFEDLNQELLEELPILYNSRI 79
Cdd:smart00721 126 LNFLLGEFKEIKKARKKLERKLLDYDSARHKLKKAKKSKEKKKDeKLAKAEEELRKAKQEFEESNAQLVEELPQLVASRV 205

                           90       100       110
                   ....*....|....*....|....*....|....
gi 585866240    80 GCYVTIFQNISNLRDVFYREMSKLNHNLYEVMSK 113
Cdd:smart00721 206 DFFVNCLQALIEAQLNFHRESYKLLQQLQQQLDK 239
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
 1-113 3.54e-19

BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different protein families. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysin, endophilin, BRAP and Nadrin. BAR domains are also frequently found alongside domains that determine lipid specificity, like pfam00169 and pfam00787 domains in beta centaurins and sorting nexins respectively.


Pssm-ID: 460810 [Multi-domain]  Cd Length: 235  Bit Score: 86.24  E-value: 3.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240    1 MEIYVAQFSEIKERIAKRGRKLVDYDSARHHLEAVQNAKKKDEAKTAKAEEEFNKAQTVFEDLNQELLEELPILYNSRIG 80
Cdd:pfam03114 123 LRNLLKEFKEIQKHRKKLERKRLDYDAAKTRVKKAKKKKSSKAKDESQAEEELRKAQAKFEESNEQLKALLPNLLSLEVE 202

                          90       100       110
                  ....*....|....*....|....*....|...
gi 585866240   81 CYVTIFQNISNLRDVFYREMSKLNHNLYEVMSK 113
Cdd:pfam03114 203 FVVNQLVAFVEAQLDFHRQCYQLLEQLQQQLGK 235
BAR_Rvs161p cd07591
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon ...
 8-79 2.75e-14

The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon starvation protein 161 and similar proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of fungal proteins with similarity to Saccharomyces cerevisiae Reduced viability upon starvation protein 161 (Rvs161p) and Schizosaccharomyces pombe Hob3 (homolog of Bin3). S. cerevisiae Rvs161p plays a role in regulating cell polarity, actin cytoskeleton polarization, vesicle trafficking, endocytosis, bud formation, and the mating response. It forms a heterodimer with another BAR domain protein Rvs167p. Rvs161p and Rvs167p share common functions but are not interchangeable. Their BAR domains cannot be replaced with each other and the overexpression of one cannot suppress the mutant phenotypes of the other. S. pombe Hob3 is important in regulating filamentous actin localization and may be required in activating Cdc42 and recruiting it to cell division sites. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153275  Cd Length: 224  Bit Score: 71.99  E-value: 2.75e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 585866240   8 FSEIKERIAKRGRKLVDYDSARHHLEAVQNAKKKDEAKTAKAEEEFNKAQTVFEDLNQELLEELPILYNSRI 79
Cdd:cd07591  108 FPEINEAIKKRNHKLLDYDAARAKVRKLIDKPSEDPTKLPRAEKELDEAKEVYETLNDQLKTELPQLVDLRI 179
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 2-109 2.68e-13

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: 68.24  E-value: 2.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240   2 EIYVAQFSEIKERIAKRGRKLVDYDSARHHLEAVQNaKKKDEAKTAKAEEEFNKAQTVFEDLNQELLEELPILYNSRIGC 81
Cdd:cd07307   87 EYLKKDLKEIKKRRKKLDKARLDYDAAREKLKKLRK-KKKDSSKLAEAEEELQEAKEKYEELREELIEDLNKLEEKRKEL 165

                         90       100
                 ....*....|....*....|....*...
gi 585866240  82 YVTIFQNISNLRDVFYREMSKLNHNLYE 109
Cdd:cd07307  166 FLSLLLSFIEAQSEFFKEVLKILEQLLP 193
BAR_Rvs167p cd07599
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon ...
 11-74 3.36e-10

The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon starvation protein 167 and similar proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of fungal proteins with similarity to Saccharomyces cerevisiae Reduced viability upon starvation protein 167 (Rvs167p) and Schizosaccharomyces pombe Hob1 (homolog of Bin1). S. cerevisiae Rvs167p plays a role in regulation of the actin cytoskeleton, endocytosis, and sporulation. It forms a heterodimer with another BAR domain protein Rvs161p. Rvs161p and Rvs167p share common functions but are not interchangeable. Their BAR domains cannot be replaced with each other and the overexpression of one cannot suppress the mutant phenotypes of the other. Rvs167p also interacts with the GTPase activating protein (GAP) Gyp5p, which is involved in ER to Golgi vesicle trafficking. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153283 [Multi-domain]  Cd Length: 216  Bit Score: 59.58  E-value: 3.36e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 585866240  11 IKERIAKRGRKLVDYDSARHHLEAVQNAKK----KDEAKTAKAEEEFNKAQTVFEDLNQELLEELPIL 74
Cdd:cd07599  112 IRKTIKKRDHKKLDYDKLQNKLNKLLQKKKelslKDEKQLAKLERKLEEAKEEYEALNELLKSELPKL 179
BAR_DNMBP cd07589
The Bin/Amphiphysin/Rvs (BAR) domain of Dynamin Binding Protein; BAR domains are dimerization, ...
 15-75 2.36e-05

The Bin/Amphiphysin/Rvs (BAR) domain of Dynamin Binding Protein; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. DyNamin Binding Protein (DNMBP), also called Tuba, is a Cdc42-specific Guanine nucleotide Exchange Factor (GEF) that binds dynamin and various actin regulatory proteins. It serves as a link between dynamin function, Rho GTPase signaling, and actin dynamics. It plays an important role in regulating cell junction configuration. DNMBP contains BAR and SH3 domains as well as a Dbl Homology domain (DH domain), which harbors GEF activity. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of DNMBP may be involved in binding to membranes. The gene encoding DNMBP is a candidate gene for late onset Alzheimer's disease.


Pssm-ID: 153273  Cd Length: 195  Bit Score: 45.00  E-value: 2.36e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 585866240  15 IAKRGRKLVDYDSarhHLEAVQNAKKKDEAKTAKAEEefnkaqtvFEDLNQELLEELPILY 75
Cdd:cd07589  108 IQKRYDKLLDYER---YKEKKERGGKVDEELEEAANQ--------YEALNAQLKEELPKFN 157
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 139-359 9.00e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 9.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240  139 SPPVRTATVSSPLTSPTSPSTLSLKSESESVSATEDLAPDAAQGEDNSEIKELLEEEEIEKEGSEASSSEEDEPLPACNG 218
Cdd:PHA03307  207 PRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPAS 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240  219 PAQAQPSPTTERAKSQEEVLPSSTTPSPGGALSPSGQPSSSATevvlrtRTASEGSEQPKKRASIQRTSAPPSRPPPPRA 298
Cdd:PHA03307  287 SSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSST------SSSSESSRGAAVSPGPSPSRSPSPSRPPPPA 360

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 585866240  299 TASPRPSSGN---IPSSPTASgGGSPTSPRA-SLGTGTASPRTSLEVSPNPEPPEKPVRTPEAKE 359
Cdd:PHA03307  361 DPSSPRKRPRpsrAPSSPAAS-AGRPTRRRArAAVAGRARRRDATGRFPAGRPRPSPLDAGAASG 424
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 139-346 2.22e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240  139 SPPVRTATVSSPLTSPTSPSTLSLKSESESVSATEDLAPDAAQGEDNSEIKELLEEEEIEKEGSEASSSEEDEPLPACNG 218
Cdd:PHA03307  115 DPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPP 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240  219 PAQAQP--SPTTERAKSQEEVLPSSTTPSPG-GALSPSGQPSSSATEVVLRTRTASEGSEQPKKRASIQRTSAPPSRPPP 295
Cdd:PHA03307  195 PSTPPAaaSPRPPRRSSPISASASSPAPAPGrSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASG 274

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 585866240  296 PRATASPRPSSGniPSSPTASGGGSPTSPRASLGTGTASPRTSLEVSPNPE 346
Cdd:PHA03307  275 WNGPSSRPGPAS--SSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRE 323
BAR_Bin3 cd07590
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, ...
 8-102 6.70e-04

The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Bridging integrator 3 (Bin3) is widely expressed in many tissues except in the brain. It plays roles in regulating filamentous actin localization and in cell division. In humans, the Bin3 gene is located in chromosome 8p21.3, a region that is implicated in cancer suppression. Homozygous inactivation of the Bin3 gene in mice led to the development of cataracts and an increased likelihood of lymphomas during aging, suggesting a role for Bin3 in lens development and cancer suppression. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153274  Cd Length: 225  Bit Score: 40.81  E-value: 6.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240   8 FSEIKERIAKRGRKLVDYDSARHHLEAVQNAKKK--DEAKTAKAEEEFNKAQTVFEDLNQELLEELPILYNSRIGCYVTI 85
Cdd:cd07590  107 FPSVNAAIKRREQSLQEYERLQAKVEKLAEKEKTgpNLAKLEQAEKALAAARADFEKQNIKLLEELPKFYNGRTDYFQPC 186

                         90
                 ....*....|....*..
gi 585866240  86 FQNISNLRDVFYREMSK 102
Cdd:cd07590  187 FEALIKSQVLYYSQSTK 203
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 140-389 2.08e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 40.67  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240  140 PPVRTATVSSPL----TSPTSPSTlslKSESESVSATEDLAPDAAqgednseikELLEEEEIEKEGSEASSSEEDEPLPA 215
Cdd:pfam05109 466 PTVSTADVTSPTpagtTSGASPVT---PSPSPRDNGTESKAPDMT---------SPTSAVTTPTPNATSPTPAVTTPTPN 533

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240  216 CNGPAQAQPSPT---TERAKSQEEVLPSSTTPSPGGALSPSGQ--PSSSATEVVLRTRTASEGSEQPKKRASIQR----T 286
Cdd:pfam05109 534 ATSPTLGKTSPTsavTTPTPNATSPTPAVTTPTPNATIPTLGKtsPTSAVTTPTPNATSPTVGETSPQANTTNHTlggtS 613

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240  287 SAPPSRPPPPRATASPRPSSGNIPSSPTASGGGSPTSPRASLGTGTASPRTS---LEVSPNPEPPEKPVR-TPEAKENEN 362
Cdd:pfam05109 614 STPVVTSPPKNATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTShmpLLTSAHPTGGENITQvTPASTSTHH 693

                         250       260
                  ....*....|....*....|....*..
gi 585866240  363 IHNQNPeelctSPTLMTSQVASEPGEA 389
Cdd:pfam05109 694 VSTSSP-----APRPGTTSQASGPGNS 715
PHA03247 PHA03247
large tegument protein UL36; Provisional
 219-386 8.14e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 38.77  E-value: 8.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240  219 PAQAQPSPTTERAKSQEEVLPSSTT----PSPGGALSPSGQPSSSATEvvLRTRTASEGSEQPKKRASIQRTSAPPSRPP 294
Cdd:PHA03247 2673 AAQASSPPQRPRRRAARPTVGSLTSladpPPPPPTPEPAPHALVSATP--LPPGPAAARQASPALPAAPAPPAVPAGPAT 2750

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240  295 PPRATASPRPSSGNIPSSPTASGGGSPTSPRASLGTGTASPRTSLEVSP---NPEPPEKPVRTPEAKENENIHNQNPEEL 371
Cdd:PHA03247 2751 PGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPspwDPADPPAAVLAPAAALPPAASPAGPLPP 2830

                         170
                  ....*....|....*
gi 585866240  372 CTSPTLMTSQVASEP 386
Cdd:PHA03247 2831 PTSAQPTAPPPPPGP 2845
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
139-388 8.40e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 38.68  E-value: 8.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240 139 SPPVRTATVSSPLTSPTSPSTLSLKSESESVSATEDLAPDAAQGEDNSEIKELLEEEEIEKEGSEASSSEEDEPLPACNG 218
Cdd:PRK07003 374 ARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKA 453

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240 219 PAQAQPSPTTERAKSQEEVLPSSTTPSPGGAlsPSGQPSSSATEVVLRTRTASEGSEQPKKRASIQRTSAPPSrpppPRA 298
Cdd:PRK07003 454 NARASADSRCDERDAQPPADSGSASAPASDA--PPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAA----AAP 527

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585866240 299 TASPRPSSGNIPSSPTASGGGSP-------------TSPRASLGTGTASPRTSLEVSPNPEPPEKPVRTPEAKENENIHN 365
Cdd:PRK07003 528 PAPEARPPTPAAAAPAARAGGAAaaldvlrnagmrvSSDRGARAAAAAKPAAAPAAAPKPAAPRVAVQVPTPRARAATGD 607

                        250       260
                 ....*....|....*....|...
gi 585866240 366 QNPEELCTSPTLMTSQVASEPGE 388
Cdd:PRK07003 608 APPNGAARAEQAAESRGAPPPWE 630
 
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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