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Conserved domains on  [gi|158749636|ref|NP_080834|]
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CBY1-interacting BAR domain-containing protein 1 isoform 1 [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 ...
 77-287 4.18e-134

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: 380.89  E-value: 4.18e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636  77 ERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEINLYASTETPNLKQGLKDFADEFAKLQDYRQAE 156
Cdd:cd07598    1 ARDNQTKFIQERITNVEKHFGELCQDFAAYTRKTARLRDKGDELAKSINAYADTENPSLKQGLKNFAECLAALQDYRQAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636 157 VERLEAKVVEPLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTRQRNPSDRHVISQAETELQRATIDATRTSRHLEE 236
Cdd:cd07598   81 VERLEAKVVQPLALYGTICKHARDDLKNTFTARNKELKQLKQLEKLRQKNPSDRQIISQAESELQKASVDANRSTKELEE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 158749636 237 TIDNFEKQKIKDIKNILSEFITIEMLFHGKALEVFTAAYQNIQNIDEDEDL 287
Cdd:cd07598  161 QMDNFEKQKIRDIKTIFSDFVLIEMLFHAKALEVYTAAYQDIQNIDEEEDL 211
 
Name Accession Description Interval E-value
BAR_FAM92 cd07598
The Bin/Amphiphysin/Rvs (BAR) domain of Family with sequence similarity 92 (FAM92); BAR ...
 77-287 4.18e-134

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: 380.89  E-value: 4.18e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636  77 ERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEINLYASTETPNLKQGLKDFADEFAKLQDYRQAE 156
Cdd:cd07598    1 ARDNQTKFIQERITNVEKHFGELCQDFAAYTRKTARLRDKGDELAKSINAYADTENPSLKQGLKNFAECLAALQDYRQAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636 157 VERLEAKVVEPLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTRQRNPSDRHVISQAETELQRATIDATRTSRHLEE 236
Cdd:cd07598   81 VERLEAKVVQPLALYGTICKHARDDLKNTFTARNKELKQLKQLEKLRQKNPSDRQIISQAESELQKASVDANRSTKELEE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 158749636 237 TIDNFEKQKIKDIKNILSEFITIEMLFHGKALEVFTAAYQNIQNIDEDEDL 287
Cdd:cd07598  161 QMDNFEKQKIRDIKTIFSDFVLIEMLFHAKALEVYTAAYQDIQNIDEEEDL 211
FAM92 pfam06730
FAM92 protein; This family of proteins has a role in embryogenesis. During embryogenesis it is ...
 70-288 3.87e-121

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: 348.59  E-value: 3.87e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636   70 MLRRN----LDERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEINLYASTETPNLK--QGLKDFA 143
Cdd:pfam06730   1 MFRRGklsfLENKDAQTKIINEAINITEKHFGELCQIFAAVTRKMAKLRDKADELAKEIKAYAADEEIHEKlcQGLKNFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636  144 DEFAKLQDYRQAEVERLEAKVVEPLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTRQRNPSDRHVISQAETELQRA 223
Cdd:pfam06730  81 DAFAILGDYMDAEVERLEAKIVEELAQFEQICKMKRDDLKAALIARDKEAKQLRQLEELKQKFPADNHVISAADSELFKA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158749636  224 TIDATRTSRHLEETIDNFEKQKIKDIKNILSEFITIEMLFHGKALEVFTAAYQNIQNIDEDEDLE 288
Cdd:pfam06730 161 AMDAQRTNKEIDDIIGNFEQQKLKDIKQIFSDFILIAMKFHGKALEILSAAYQDIGNIDEDDDFE 225
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 71-244 3.49e-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: 39.27  E-value: 3.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636    71 LRRNLDERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARL-------RDKADLLVNEInLYASTETPNLKQGLKDFA 143
Cdd:TIGR02168  258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeqqkqilRERLANLERQL-EELEAQLEELESKLDELA 336

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636   144 DEFAKLQdyrqAEVERLEAKVVEpLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTRQRNpsdrhvISQAETELQRA 223
Cdd:TIGR02168  337 EELAELE----EKLEELKEELES-LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ------IASLNNEIERL 405

                          170       180
                   ....*....|....*....|.
gi 158749636   224 TIDATRTSRHLEETIDNFEKQ 244
Cdd:TIGR02168  406 EARLERLEDRRERLQQEIEEL 426
PTZ00121 PTZ00121
MAEBL; Provisional
 72-250 4.35e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636   72 RRNLDERDAQ-TKQLQDA-VTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEinlyaSTETPNLKQGLKDFADEFAKL 149
Cdd:PTZ00121 1575 DKNMALRKAEeAKKAEEArIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-----EEEKKKVEQLKKKEAEEKKKA 1649

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636  150 QDYRQAEVERL-----EAKVVEPLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTRQRNPSDRHVISQAETELQRAT 224
Cdd:PTZ00121 1650 EELKKAEEENKikaaeEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENK 1729

                         170       180       190
                  ....*....|....*....|....*....|....
gi 158749636  225 IDATRTSRHLEE--------TIDNFEKQKIKDIK 250
Cdd:PTZ00121 1730 IKAEEAKKEAEEdkkkaeeaKKDEEEKKKIAHLK 1763
 
Name Accession Description Interval E-value
BAR_FAM92 cd07598
The Bin/Amphiphysin/Rvs (BAR) domain of Family with sequence similarity 92 (FAM92); BAR ...
 77-287 4.18e-134

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: 380.89  E-value: 4.18e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636  77 ERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEINLYASTETPNLKQGLKDFADEFAKLQDYRQAE 156
Cdd:cd07598    1 ARDNQTKFIQERITNVEKHFGELCQDFAAYTRKTARLRDKGDELAKSINAYADTENPSLKQGLKNFAECLAALQDYRQAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636 157 VERLEAKVVEPLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTRQRNPSDRHVISQAETELQRATIDATRTSRHLEE 236
Cdd:cd07598   81 VERLEAKVVQPLALYGTICKHARDDLKNTFTARNKELKQLKQLEKLRQKNPSDRQIISQAESELQKASVDANRSTKELEE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 158749636 237 TIDNFEKQKIKDIKNILSEFITIEMLFHGKALEVFTAAYQNIQNIDEDEDL 287
Cdd:cd07598  161 QMDNFEKQKIRDIKTIFSDFVLIEMLFHAKALEVYTAAYQDIQNIDEEEDL 211
FAM92 pfam06730
FAM92 protein; This family of proteins has a role in embryogenesis. During embryogenesis it is ...
 70-288 3.87e-121

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: 348.59  E-value: 3.87e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636   70 MLRRN----LDERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEINLYASTETPNLK--QGLKDFA 143
Cdd:pfam06730   1 MFRRGklsfLENKDAQTKIINEAINITEKHFGELCQIFAAVTRKMAKLRDKADELAKEIKAYAADEEIHEKlcQGLKNFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636  144 DEFAKLQDYRQAEVERLEAKVVEPLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTRQRNPSDRHVISQAETELQRA 223
Cdd:pfam06730  81 DAFAILGDYMDAEVERLEAKIVEELAQFEQICKMKRDDLKAALIARDKEAKQLRQLEELKQKFPADNHVISAADSELFKA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158749636  224 TIDATRTSRHLEETIDNFEKQKIKDIKNILSEFITIEMLFHGKALEVFTAAYQNIQNIDEDEDLE 288
Cdd:pfam06730 161 AMDAQRTNKEIDDIIGNFEQQKLKDIKQIFSDFILIAMKFHGKALEILSAAYQDIGNIDEDDDFE 225
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 74-277 4.29e-14

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: 70.17  E-value: 4.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636  74 NLDERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNeinlyastetPNLKQGLKDFADEFAKLQDYR 153
Cdd:cd07307    1 KLDELEKLLKKLIKDTKKLLDSLKELPAAAEKLSEALQELGKELPDLSN----------TDLGEALEKFGKIQKELEEFR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636 154 QAEVERLEAKVVEPLKAYgtivkmKRDDLKATLTARNREAKQLSQLERTRQRN------PSDRHVISQAETELQRATIDA 227
Cdd:cd07307   71 DQLEQKLENKVIEPLKEY------LKKDLKEIKKRRKKLDKARLDYDAAREKLkklrkkKKDSSKLAEAEEELQEAKEKY 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 158749636 228 TRTSRHLEETIDNFEKQKIKDIKNILSEFITIEMLFHGKALEVFTAAYQN 277
Cdd:cd07307  145 EELREELIEDLNKLEEKRKELFLSLLLSFIEAQSEFFKEVLKILEQLLPY 194
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 77-274 1.23e-08

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: 54.67  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636  77 ERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEINLYASTETPN---LKQGLKDFADEFAKLQDYR 153
Cdd:cd07596    1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRRELGSALGEFGKALIKLAKCEEEVggeLGEALSKLGKAAEELSSLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636 154 QAEVERLEAKVVEPLKAYGTIVKMkrddLKATLTARNREAKQLS-----------QLERTR-QRNPSDRHV------ISQ 215
Cdd:cd07596   81 EAQANQELVKLLEPLKEYLRYCQA----VKETLDDRADALLTLQslkkdlaskkaQLEKLKaAPGIKPAKVeeleeeLEE 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 158749636 216 AETELQRATIDATRTSRHLEETIDNFEKQKIKDIKNILSEFITIEMLFHGKALEVFTAA 274
Cdd:cd07596  157 AESALEEARKRYEEISERLKEELKRFHEERARDLKAALKEFARLQVQYAEKIAEAWESL 215
Vps5 pfam09325
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ...
 75-257 1.73e-04

Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is the C terminal dimerization domain.


Pssm-ID: 430527 [Multi-domain]  Cd Length: 236  Bit Score: 42.27  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636   75 LDERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTArlrdkadllvneiNLYASTETPNLKQGLKDFADEFAKLQDY-- 152
Cdd:pfam09325  33 IDSLESQLKKLYKALELLVSQRKELASATGEFAKSLA-------------SLASLELSTGLSRALSQLAEVEERIKELle 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636  153 RQAEVE--RLEAKVVEPLKAYGTI--VKMKRDDLKATLTARNRE-AKQLSQLERTRQRNPSDRHVISQAETELQRATIDA 227
Cdd:pfam09325 100 RQALQDvlTLGETIDEYLRLIGSVkaVFNQRVKAWQSWQNAEQElSKKKEQLEKLLRANKSQNDKLQQAKKEVEELERRV 179

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 158749636  228 TRTSRHLE---ETI----DNFEKQKIKDIKNILSEFI 257
Cdd:pfam09325 180 QQAEKEFEdisELIkkelERFELERVDDFKNSVEIYL 216
BAR_SNX2 cd07664
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 2; BAR domains are dimerization, lipid ...
 72-257 1.65e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 2; 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. SNX2 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153348 [Multi-domain]  Cd Length: 234  Bit Score: 39.65  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636  72 RRNLDERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRDKAD--LLVNEINLYASTETP----NLKQGLKDFADE 145
Cdd:cd07664   28 QQQFENLDQQLRKLHASVESLVCHRKELSANTAAFAKSAAMLGNSEDhtALSRALSQLAEVEEKidqlHQDQAFADFYLF 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636 146 FAKLQDYRQAeVERLEAKVVEPLKAYgtivkMKRDDLKATLTaRNREAKQLSQLERTRQRNPSDRHVISQAETELQRATI 225
Cdd:cd07664  108 SELLGDYIRL-IAAVKGVFDQRMKCW-----QKWQDAQVTLQ-KKREAEAKLQYANKPDKLQQAKDEIKEWEAKVQQGER 180

                        170       180       190
                 ....*....|....*....|....*....|..
gi 158749636 226 DATRTSRHLEETIDNFEKQKIKDIKNILSEFI 257
Cdd:cd07664  181 DFEQISKTIRKEVGRFEKERVKDFKTVIIKYL 212
BAR_SNX1_2 cd07623
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 1 and 2; BAR domains are dimerization, ...
 75-257 3.43e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 1 and 2; 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. This subfamily consists of SNX1, SNX2, and similar proteins. SNX1 and SNX2 are components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures efficient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153307  Cd Length: 224  Bit Score: 38.41  E-value: 3.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636  75 LDERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRdkadllvneinlyASTETPNLKQGLKDFADEFAKLQDYRQ 154
Cdd:cd07623   21 IENLDQQLRKLHASVESLVNHRKELALNTGSFAKSAAMLS-------------NCEEHTSLSRALSQLAEVEEKIEQLHG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636 155 AEVERLEAKVVEPLKAY----GTI-------VKMKRDDLKATLT-ARNREAK-QLSQLERTRQRNPSDRHVISqAETELQ 221
Cdd:cd07623   88 EQADTDFYILAELLKDYigliGAIkdvfherVKVWQNWQNAQQTlTKKREAKaKLELSGRTDKLDQAQQEIKE-WEAKVD 166

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 158749636 222 RATIDATRTSRHLEETIDNFEKQKIKDIKNILSEFI 257
Cdd:cd07623  167 RGQKEFEEISKTIKKEIERFEKNRVKDFKDIIIKYL 202
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 71-244 3.49e-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: 39.27  E-value: 3.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636    71 LRRNLDERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARL-------RDKADLLVNEInLYASTETPNLKQGLKDFA 143
Cdd:TIGR02168  258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeqqkqilRERLANLERQL-EELEAQLEELESKLDELA 336

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636   144 DEFAKLQdyrqAEVERLEAKVVEpLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTRQRNpsdrhvISQAETELQRA 223
Cdd:TIGR02168  337 EELAELE----EKLEELKEELES-LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ------IASLNNEIERL 405

                          170       180
                   ....*....|....*....|.
gi 158749636   224 TIDATRTSRHLEETIDNFEKQ 244
Cdd:TIGR02168  406 EARLERLEDRRERLQQEIEEL 426
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 78-258 4.25e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 38.50  E-value: 4.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636  78 RDAQTKQLQDAVTNVEKHFGELCQIFAayvRKTARLRDKADLLVNEINLYAsTETPNLKQGLKDFADEFAKL-----QDY 152
Cdd:cd22656  101 DDLADATDDEELEEAKKTIKALLDDLL---KEAKKYQDKAAKVVDKLTDFE-NQTEKDQTALETLEKALKDLltdegGAI 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636 153 RQAEVERLEAKVVEPLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTrqrnpsdrhvisqaeteLQRATIDATRTSR 232
Cdd:cd22656  177 ARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIAD-----------------LTAADTDLDNLLA 239

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 158749636 233 HLEETIDNFEK-----QKIKD----IKNILSEFIT 258
Cdd:cd22656  240 LIGPAIPALEKlqgawQAIATdldsLKDLLEDDIS 274
PTZ00121 PTZ00121
MAEBL; Provisional
 72-250 4.35e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636   72 RRNLDERDAQ-TKQLQDA-VTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEinlyaSTETPNLKQGLKDFADEFAKL 149
Cdd:PTZ00121 1575 DKNMALRKAEeAKKAEEArIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-----EEEKKKVEQLKKKEAEEKKKA 1649

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749636  150 QDYRQAEVERL-----EAKVVEPLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTRQRNPSDRHVISQAETELQRAT 224
Cdd:PTZ00121 1650 EELKKAEEENKikaaeEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENK 1729

                         170       180       190
                  ....*....|....*....|....*....|....
gi 158749636  225 IDATRTSRHLEE--------TIDNFEKQKIKDIK 250
Cdd:PTZ00121 1730 IKAEEAKKEAEEdkkkaeeaKKDEEEKKKIAHLK 1763
 
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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