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Conserved domains on  [gi|568927292|ref|XP_006538275|]
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CBY1-interacting BAR domain-containing protein 1 isoform X3 [Mus musculus]

Protein Classification

BAR domain-containing protein( domain architecture ID 10166148)

BAR (Bin/Amphiphysin/Rvs) domain-containing protein, similar to human protein FAM92

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAR_FAM92 cd07598
The Bin/Amphiphysin/Rvs (BAR) domain of Family with sequence similarity 92 (FAM92); BAR ...
 77-257 6.62e-105

The Bin/Amphiphysin/Rvs (BAR) domain of Family with sequence similarity 92 (FAM92); 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. This group is composed of proteins from the family with sequence similarity 92 (FAM92), which were originally identified by the presence of the unknown domain DUF1208. This domain shows similarity to the BAR domains of sorting nexins. Mammals contain at least two member types, FAM92A and FAM92B, which may exist in many variants. The Xenopus homolog of FAM92A1, xVAP019, is essential for embryo survival and cell differentiation. FAM92A1 may be involved in regulating cell proliferation and apoptosis. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


:

Pssm-ID: 153282  Cd Length: 211  Bit Score: 303.08  E-value: 6.62e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927292  77 ERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEINLYASTETPNLKQGLKDFADEFAKLQDYRQAE 156
Cdd:cd07598    1 ARDNQTKFIQERITNVEKHFGELCQDFAAYTRKTARLRDKGDELAKSINAYADTENPSLKQGLKNFAECLAALQDYRQAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927292 157 mlmnmakVERLEAKVVEPLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTRQRNPSDRHVISQAETELQRATIDATR 236
Cdd:cd07598   81 -------VERLEAKVVQPLALYGTICKHARDDLKNTFTARNKELKQLKQLEKLRQKNPSDRQIISQAESELQKASVDANR 153

                        170       180
                 ....*....|....*....|.
gi 568927292 237 TSRHLEETIDNFEKQKIKDIK 257
Cdd:cd07598  154 STKELEEQMDNFEKQKIRDIK 174
 
Name Accession Description Interval E-value
BAR_FAM92 cd07598
The Bin/Amphiphysin/Rvs (BAR) domain of Family with sequence similarity 92 (FAM92); BAR ...
 77-257 6.62e-105

The Bin/Amphiphysin/Rvs (BAR) domain of Family with sequence similarity 92 (FAM92); 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. This group is composed of proteins from the family with sequence similarity 92 (FAM92), which were originally identified by the presence of the unknown domain DUF1208. This domain shows similarity to the BAR domains of sorting nexins. Mammals contain at least two member types, FAM92A and FAM92B, which may exist in many variants. The Xenopus homolog of FAM92A1, xVAP019, is essential for embryo survival and cell differentiation. FAM92A1 may be involved in regulating cell proliferation and apoptosis. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153282  Cd Length: 211  Bit Score: 303.08  E-value: 6.62e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927292  77 ERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEINLYASTETPNLKQGLKDFADEFAKLQDYRQAE 156
Cdd:cd07598    1 ARDNQTKFIQERITNVEKHFGELCQDFAAYTRKTARLRDKGDELAKSINAYADTENPSLKQGLKNFAECLAALQDYRQAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927292 157 mlmnmakVERLEAKVVEPLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTRQRNPSDRHVISQAETELQRATIDATR 236
Cdd:cd07598   81 -------VERLEAKVVQPLALYGTICKHARDDLKNTFTARNKELKQLKQLEKLRQKNPSDRQIISQAESELQKASVDANR 153

                        170       180
                 ....*....|....*....|.
gi 568927292 237 TSRHLEETIDNFEKQKIKDIK 257
Cdd:cd07598  154 STKELEEQMDNFEKQKIRDIK 174
FAM92 pfam06730
FAM92 protein; This family of proteins has a role in embryogenesis. During embryogenesis it is ...
 70-257 4.90e-94

FAM92 protein; This family of proteins has a role in embryogenesis. During embryogenesis it is essential for ectoderm and axial mesoderm development. It may regulate cell proliferation and apoptosis.


Pssm-ID: 284207  Cd Length: 225  Bit Score: 276.17  E-value: 4.90e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927292   70 MLRRN----LDERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEINLYASTETPNLK--QGLKDFA 143
Cdd:pfam06730   1 MFRRGklsfLENKDAQTKIINEAINITEKHFGELCQIFAAVTRKMAKLRDKADELAKEIKAYAADEEIHEKlcQGLKNFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927292  144 DEFAKLQDYRQAEmlmnmakVERLEAKVVEPLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTRQRNPSDRHVISQA 223
Cdd:pfam06730  81 DAFAILGDYMDAE-------VERLEAKIVEELAQFEQICKMKRDDLKAALIARDKEAKQLRQLEELKQKFPADNHVISAA 153

                         170       180       190
                  ....*....|....*....|....*....|....
gi 568927292  224 ETELQRATIDATRTSRHLEETIDNFEKQKIKDIK 257
Cdd:pfam06730 154 DSELFKAAMDAQRTNKEIDDIIGNFEQQKLKDIK 187
PTZ00121 PTZ00121
MAEBL; Provisional
 72-258 6.22e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 6.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927292   72 RRNLDERDAQ-TKQLQDA-VTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEinlyaSTETPNLKQGLKDFADEFAKL 149
Cdd:PTZ00121 1575 DKNMALRKAEeAKKAEEArIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-----EEEKKKVEQLKKKEAEEKKKA 1649

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927292  150 QDYRQAEMLMNMAKVErlEAKVVEPLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTRQRNPSDRHVISQAETELQR 229
Cdd:PTZ00121 1650 EELKKAEEENKIKAAE--EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE 1727

                         170       180
                  ....*....|....*....|....*....
gi 568927292  230 ATIDATRTSRHLEEtidnfEKQKIKDIKV 258
Cdd:PTZ00121 1728 NKIKAEEAKKEAEE-----DKKKAEEAKK 1751
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 71-237 1.74e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927292    71 LRRNLDERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARL-------RDKADLLVNEInLYASTETPNLKQGLKDFA 143
Cdd:TIGR02168  258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeqqkqilRERLANLERQL-EELEAQLEELESKLDELA 336

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927292   144 DEFAKLQDyrQAEMLMNM-----AKVERLEAKVVEPLKAYGTI------VKMKRDDLKATLTARNRE----AKQLSQLER 208
Cdd:TIGR02168  337 EELAELEE--KLEELKEElesleAELEELEAELEELESRLEELeeqletLRSKVAQLELQIASLNNEierlEARLERLED 414

                          170       180
                   ....*....|....*....|....*....
gi 568927292   209 TRQRNPSDrhvISQAETELQRATIDATRT 237
Cdd:TIGR02168  415 RRERLQQE---IEELLKKLEEAELKELQA 440
 
Name Accession Description Interval E-value
BAR_FAM92 cd07598
The Bin/Amphiphysin/Rvs (BAR) domain of Family with sequence similarity 92 (FAM92); BAR ...
 77-257 6.62e-105

The Bin/Amphiphysin/Rvs (BAR) domain of Family with sequence similarity 92 (FAM92); 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. This group is composed of proteins from the family with sequence similarity 92 (FAM92), which were originally identified by the presence of the unknown domain DUF1208. This domain shows similarity to the BAR domains of sorting nexins. Mammals contain at least two member types, FAM92A and FAM92B, which may exist in many variants. The Xenopus homolog of FAM92A1, xVAP019, is essential for embryo survival and cell differentiation. FAM92A1 may be involved in regulating cell proliferation and apoptosis. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153282  Cd Length: 211  Bit Score: 303.08  E-value: 6.62e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927292  77 ERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEINLYASTETPNLKQGLKDFADEFAKLQDYRQAE 156
Cdd:cd07598    1 ARDNQTKFIQERITNVEKHFGELCQDFAAYTRKTARLRDKGDELAKSINAYADTENPSLKQGLKNFAECLAALQDYRQAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927292 157 mlmnmakVERLEAKVVEPLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTRQRNPSDRHVISQAETELQRATIDATR 236
Cdd:cd07598   81 -------VERLEAKVVQPLALYGTICKHARDDLKNTFTARNKELKQLKQLEKLRQKNPSDRQIISQAESELQKASVDANR 153

                        170       180
                 ....*....|....*....|.
gi 568927292 237 TSRHLEETIDNFEKQKIKDIK 257
Cdd:cd07598  154 STKELEEQMDNFEKQKIRDIK 174
FAM92 pfam06730
FAM92 protein; This family of proteins has a role in embryogenesis. During embryogenesis it is ...
 70-257 4.90e-94

FAM92 protein; This family of proteins has a role in embryogenesis. During embryogenesis it is essential for ectoderm and axial mesoderm development. It may regulate cell proliferation and apoptosis.


Pssm-ID: 284207  Cd Length: 225  Bit Score: 276.17  E-value: 4.90e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927292   70 MLRRN----LDERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEINLYASTETPNLK--QGLKDFA 143
Cdd:pfam06730   1 MFRRGklsfLENKDAQTKIINEAINITEKHFGELCQIFAAVTRKMAKLRDKADELAKEIKAYAADEEIHEKlcQGLKNFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927292  144 DEFAKLQDYRQAEmlmnmakVERLEAKVVEPLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTRQRNPSDRHVISQA 223
Cdd:pfam06730  81 DAFAILGDYMDAE-------VERLEAKIVEELAQFEQICKMKRDDLKAALIARDKEAKQLRQLEELKQKFPADNHVISAA 153

                         170       180       190
                  ....*....|....*....|....*....|....
gi 568927292  224 ETELQRATIDATRTSRHLEETIDNFEKQKIKDIK 257
Cdd:pfam06730 154 DSELFKAAMDAQRTNKEIDDIIGNFEQQKLKDIK 187
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 74-256 4.80e-06

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: 45.90  E-value: 4.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927292  74 NLDERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNeinlyastetPNLKQGLKDFADEFAKLQDYR 153
Cdd:cd07307    1 KLDELEKLLKKLIKDTKKLLDSLKELPAAAEKLSEALQELGKELPDLSN----------TDLGEALEKFGKIQKELEEFR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927292 154 QAEmlmnmakVERLEAKVVEPLKAYgtivkmKRDDLKATLTARNREAKQLSQLERTRQRN------PSDRHVISQAETEL 227
Cdd:cd07307   71 DQL-------EQKLENKVIEPLKEY------LKKDLKEIKKRRKKLDKARLDYDAAREKLkklrkkKKDSSKLAEAEEEL 137

                        170       180
                 ....*....|....*....|....*....
gi 568927292 228 QRATIDATRTSRHLEETIDNFEKQKIKDI 256
Cdd:cd07307  138 QEAKEKYEELREELIEDLNKLEEKRKELF 166
PTZ00121 PTZ00121
MAEBL; Provisional
 72-258 6.22e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 6.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927292   72 RRNLDERDAQ-TKQLQDA-VTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEinlyaSTETPNLKQGLKDFADEFAKL 149
Cdd:PTZ00121 1575 DKNMALRKAEeAKKAEEArIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-----EEEKKKVEQLKKKEAEEKKKA 1649

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927292  150 QDYRQAEMLMNMAKVErlEAKVVEPLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTRQRNPSDRHVISQAETELQR 229
Cdd:PTZ00121 1650 EELKKAEEENKIKAAE--EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE 1727

                         170       180
                  ....*....|....*....|....*....
gi 568927292  230 ATIDATRTSRHLEEtidnfEKQKIKDIKV 258
Cdd:PTZ00121 1728 NKIKAEEAKKEAEE-----DKKKAEEAKK 1751
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 71-237 1.74e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927292    71 LRRNLDERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARL-------RDKADLLVNEInLYASTETPNLKQGLKDFA 143
Cdd:TIGR02168  258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeqqkqilRERLANLERQL-EELEAQLEELESKLDELA 336

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927292   144 DEFAKLQDyrQAEMLMNM-----AKVERLEAKVVEPLKAYGTI------VKMKRDDLKATLTARNRE----AKQLSQLER 208
Cdd:TIGR02168  337 EELAELEE--KLEELKEElesleAELEELEAELEELESRLEELeeqletLRSKVAQLELQIASLNNEierlEARLERLED 414

                          170       180
                   ....*....|....*....|....*....
gi 568927292   209 TRQRNPSDrhvISQAETELQRATIDATRT 237
Cdd:TIGR02168  415 RRERLQQE---IEELLKKLEEAELKELQA 440
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 77-257 8.49e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 36.56  E-value: 8.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927292  77 ERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEINLYASTETPN---LKQGLKDFADEFAKLQDyr 153
Cdd:cd07596    1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRRELGSALGEFGKALIKLAKCEEEVggeLGEALSKLGKAAEELSS-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927292 154 qaemlMNMAKVERLEAKVVEPLKAYGTIVKMkrddLKATLTARNREAKQLS-----------QLERTR-QRNPSDRHV-- 219
Cdd:cd07596   79 -----LSEAQANQELVKLLEPLKEYLRYCQA----VKETLDDRADALLTLQslkkdlaskkaQLEKLKaAPGIKPAKVee 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568927292 220 ----ISQAETELQRATIDATRTSRHLEETIDNFEKQKIKDIK 257
Cdd:cd07596  150 leeeLEEAESALEEARKRYEEISERLKEELKRFHEERARDLK 191
 
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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