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Conserved domains on  [gi|767989871|ref|XP_011521365|]
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CBY1-interacting BAR domain-containing protein 2 isoform X1 [Homo sapiens]

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 ...
 6-216 4.10e-106

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: 307.70  E-value: 4.10e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989871   6 SRDSQVRVMENTVANTEKYFGQFCSLLAAYTRKTARLRDKADQLVKQLIDFANSENPELRATMRGFAEDLAKVQDYRQAQ 85
Cdd:cd07598    1 ARDNQTKFIQERITNVEKHFGELCQDFAAYTRKTARLRDKGDELAKSINAYADTENPSLKQGLKNFAECLAALQDYRQAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989871  86 VERLETKVVNPLKLYGAQIKQTRAEIKKFKHVQNHEIKQLEKLEKLRQKSPSDQQMISQAETRVQRAAVDSSRTTLQLEE 165
Cdd:cd07598   81 VERLEAKVVQPLALYGTICKHARDDLKNTFTARNKELKQLKQLEKLRQKNPSDRQIISQAESELQKASVDANRSTKELEE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767989871 166 TVDGFQRQKLKDLQKFFCDFVTIEMVFHAKAVEVYSSAFQTLEKYDLERDL 216
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 ...
 6-216 4.10e-106

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: 307.70  E-value: 4.10e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989871   6 SRDSQVRVMENTVANTEKYFGQFCSLLAAYTRKTARLRDKADQLVKQLIDFANSENPELRATMRGFAEDLAKVQDYRQAQ 85
Cdd:cd07598    1 ARDNQTKFIQERITNVEKHFGELCQDFAAYTRKTARLRDKGDELAKSINAYADTENPSLKQGLKNFAECLAALQDYRQAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989871  86 VERLETKVVNPLKLYGAQIKQTRAEIKKFKHVQNHEIKQLEKLEKLRQKSPSDQQMISQAETRVQRAAVDSSRTTLQLEE 165
Cdd:cd07598   81 VERLEAKVVQPLALYGTICKHARDDLKNTFTARNKELKQLKQLEKLRQKNPSDRQIISQAESELQKASVDANRSTKELEE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767989871 166 TVDGFQRQKLKDLQKFFCDFVTIEMVFHAKAVEVYSSAFQTLEKYDLERDL 216
Cdd:cd07598  161 QMDNFEKQKIRDIKTIFSDFVLIEMLFHAKALEVYTAAYQDIQNIDEEEDL 211
FAM92 pfam06730
FAM92 protein; This family of proteins has a role in embryogenesis. During embryogenesis it is ...
 6-216 1.13e-68

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: 213.00  E-value: 1.13e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989871    6 SRDSQVRVMENTVANTEKYFGQFCSLLAAYTRKTARLRDKADQLVKQLIDFANSENP--ELRATMRGFAEDLAKVQDYRQ 83
Cdd:pfam06730  12 NKDAQTKIINEAINITEKHFGELCQIFAAVTRKMAKLRDKADELAKEIKAYAADEEIheKLCQGLKNFADAFAILGDYMD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989871   84 AQVERLETKVVNPLKLYGAQIKQTRAEIKKFKHVQNHEIKQLEKLEKLRQKSPSDQQMISQAETRVQRAAVDSSRTTLQL 163
Cdd:pfam06730  92 AEVERLEAKIVEELAQFEQICKMKRDDLKAALIARDKEAKQLRQLEELKQKFPADNHVISAADSELFKAAMDAQRTNKEI 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767989871  164 EETVDGFQRQKLKDLQKFFCDFVTIEMVFHAKAVEVYSSAFQTLEKYDLERDL 216
Cdd:pfam06730 172 DDIIGNFEQQKLKDIKQIFSDFILIAMKFHGKALEILSAAYQDIGNIDEDDDF 224
BAR smart00721
BAR domain;
71-207 7.76e-05

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 43.14  E-value: 7.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989871    71 FAEDLAKVQDYRQAQVERLETKVVNPLKLYGAQIKQTRAEIKKFKH-VQNHEIK--QLEKLEKLRQKSPSDQQMISQAET 147
Cdd:smart00721 100 LGEALKKLLQVEESLSQVKRTFILPLLNFLLGEFKEIKKARKKLERkLLDYDSArhKLKKAKKSKEKKKDEKLAKAEEEL 179

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989871   148 RVQRAAVDSSRTTLqLEETVDGFQRqKLKDLQKFFCDFVTIEMVFHAKAVEVYSSAFQTL 207
Cdd:smart00721 180 RKAKQEFEESNAQL-VEELPQLVAS-RVDFFVNCLQALIEAQLNFHRESYKLLQQLQQQL 237
 
Name Accession Description Interval E-value
BAR_FAM92 cd07598
The Bin/Amphiphysin/Rvs (BAR) domain of Family with sequence similarity 92 (FAM92); BAR ...
 6-216 4.10e-106

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: 307.70  E-value: 4.10e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989871   6 SRDSQVRVMENTVANTEKYFGQFCSLLAAYTRKTARLRDKADQLVKQLIDFANSENPELRATMRGFAEDLAKVQDYRQAQ 85
Cdd:cd07598    1 ARDNQTKFIQERITNVEKHFGELCQDFAAYTRKTARLRDKGDELAKSINAYADTENPSLKQGLKNFAECLAALQDYRQAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989871  86 VERLETKVVNPLKLYGAQIKQTRAEIKKFKHVQNHEIKQLEKLEKLRQKSPSDQQMISQAETRVQRAAVDSSRTTLQLEE 165
Cdd:cd07598   81 VERLEAKVVQPLALYGTICKHARDDLKNTFTARNKELKQLKQLEKLRQKNPSDRQIISQAESELQKASVDANRSTKELEE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767989871 166 TVDGFQRQKLKDLQKFFCDFVTIEMVFHAKAVEVYSSAFQTLEKYDLERDL 216
Cdd:cd07598  161 QMDNFEKQKIRDIKTIFSDFVLIEMLFHAKALEVYTAAYQDIQNIDEEEDL 211
FAM92 pfam06730
FAM92 protein; This family of proteins has a role in embryogenesis. During embryogenesis it is ...
 6-216 1.13e-68

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: 213.00  E-value: 1.13e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989871    6 SRDSQVRVMENTVANTEKYFGQFCSLLAAYTRKTARLRDKADQLVKQLIDFANSENP--ELRATMRGFAEDLAKVQDYRQ 83
Cdd:pfam06730  12 NKDAQTKIINEAINITEKHFGELCQIFAAVTRKMAKLRDKADELAKEIKAYAADEEIheKLCQGLKNFADAFAILGDYMD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989871   84 AQVERLETKVVNPLKLYGAQIKQTRAEIKKFKHVQNHEIKQLEKLEKLRQKSPSDQQMISQAETRVQRAAVDSSRTTLQL 163
Cdd:pfam06730  92 AEVERLEAKIVEELAQFEQICKMKRDDLKAALIARDKEAKQLRQLEELKQKFPADNHVISAADSELFKAAMDAQRTNKEI 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767989871  164 EETVDGFQRQKLKDLQKFFCDFVTIEMVFHAKAVEVYSSAFQTLEKYDLERDL 216
Cdd:pfam06730 172 DDIIGNFEQQKLKDIKQIFSDFILIAMKFHGKALEILSAAYQDIGNIDEDDDF 224
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 18-199 3.00e-12

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: 64.39  E-value: 3.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989871  18 VANTEKYFGQFCSLLAAYTRKTARLRDKADQLVKQLIDFA----NSENPELRATMRGFAEDLAKVQDYRQAQVERLETKV 93
Cdd:cd07307    2 LDELEKLLKKLIKDTKKLLDSLKELPAAAEKLSEALQELGkelpDLSNTDLGEALEKFGKIQKELEEFRDQLEQKLENKV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989871  94 VNPLKLYG-AQIKQTRAEIKKFKHVQNhEIKQ-LEKLEKLRQKSPsDQQMISQAETRVQRAAVDSSRTTLQLEETVDGFQ 171
Cdd:cd07307   82 IEPLKEYLkKDLKEIKKRRKKLDKARL-DYDAaREKLKKLRKKKK-DSSKLAEAEEELQEAKEKYEELREELIEDLNKLE 159

                        170       180
                 ....*....|....*....|....*...
gi 767989871 172 RQKLKDLQKFFCDFVTIEMVFHAKAVEV 199
Cdd:cd07307  160 EKRKELFLSLLLSFIEAQSEFFKEVLKI 187
BAR smart00721
BAR domain;
71-207 7.76e-05

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 43.14  E-value: 7.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989871    71 FAEDLAKVQDYRQAQVERLETKVVNPLKLYGAQIKQTRAEIKKFKH-VQNHEIK--QLEKLEKLRQKSPSDQQMISQAET 147
Cdd:smart00721 100 LGEALKKLLQVEESLSQVKRTFILPLLNFLLGEFKEIKKARKKLERkLLDYDSArhKLKKAKKSKEKKKDEKLAKAEEEL 179

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989871   148 RVQRAAVDSSRTTLqLEETVDGFQRqKLKDLQKFFCDFVTIEMVFHAKAVEVYSSAFQTL 207
Cdd:smart00721 180 RKAKQEFEESNAQL-VEELPQLVAS-RVDFFVNCLQALIEAQLNFHRESYKLLQQLQQQL 237
BAR_SNX4 cd07622
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 4; BAR domains are dimerization, lipid ...
 117-208 4.44e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 4; 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. SNX4 is involved in recycling traffic from the sorting endosome (post-Golgi endosome) back to the late Golgi. It is also implicated in the regulation of plasma membrane receptor trafficking and interacts with receptors for EGF, insulin, platelet-derived growth factor and leptin. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153306  Cd Length: 201  Bit Score: 37.75  E-value: 4.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989871 117 VQNHEIKQLEkLEKLRQKSPSDQQmisQAETRVQRAAVDSSRTTLQLEETVDGFQRQKLKDLQKFFCDFVTIEMVFHAKA 196
Cdd:cd07622  114 CKKHELLQYD-LEKAEDALANKKQ---QGEEAVKEAKDELNEFVKKALEDVERFKKQKVRDLKEILISYAKLQIKLAKKG 189

                         90
                 ....*....|..
gi 767989871 197 VEVYSSAFQTLE 208
Cdd:cd07622  190 LQTWTNIKECLQ 201
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 76-180 4.74e-03

Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.


Pssm-ID: 198139 [Multi-domain]  Cd Length: 154  Bit Score: 37.01  E-value: 4.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989871    76 AKVQDYRQAQVERLEtkvvnplklygaQIKQTRAEIKKFKHVqNHEIKQLEKL---EKLRQKSPSDQQMISQAETRVQRA 152
Cdd:smart01071  32 WKQRDIHQARVERME------------EIKNLKYELIMNDHL-NKRIDKLLKGlreEELSPETPTYNEMLAELQDQLKKE 98

                           90       100
                   ....*....|....*....|....*...
gi 767989871   153 AVDSSRTTLQLEETVDGfQRQKLKDLQK 180
Cdd:smart01071  99 LEEANGDSEGLLEELKK-HRDKLKKEQK 125
BAR_Bin3 cd07590
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, ...
 60-203 5.17e-03

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: 37.73  E-value: 5.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989871  60 ENPELRATMRGFAEDLAKVQDYRQAQVERLETKVVNPLKLYGAQIKQTRAEIKKF-KHVQNHEIKQ--LEKLEKLRQKSP 136
Cdd:cd07590   63 DNDELRNLVEALDSVTTQLDKTVQELVNLIQKTFIEPLKRLRSVFPSVNAAIKRReQSLQEYERLQakVEKLAEKEKTGP 142

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767989871 137 SDQQMiSQAETRVQRAAVDSSRTTLQLEETVDGFQRQKLKDLQKFFCDFVTIEMVFHAKAVEVYSSA 203
Cdd:cd07590  143 NLAKL-EQAEKALAAARADFEKQNIKLLEELPKFYNGRTDYFQPCFEALIKSQVLYYSQSTKIFTQL 208
BAR_SNX7_30 cd07624
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 7 and 30; BAR domains are dimerization, ...
 57-193 6.40e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 7 and 30; 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 SNX7, SNX30, and similar proteins. The specific functions of SNX7 and SNX30 have not been elucidated. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153308  Cd Length: 200  Bit Score: 36.97  E-value: 6.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989871  57 ANSEnPELRATMRGFAEDLAKVQDYRQAQVERLETKVVNPLK---LYGAQIKQTraeIKKFKHVQnheIKQLEKLEKLRQ 133
Cdd:cd07624   62 SASE-TELAPLLEGVSSAVERCTAALEVLLSDHEFVFLPPLReylLYSDAVKDV---LKRRDQFQ---IEYELSVEELNK 134

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767989871 134 KSPSDQQMISQAETRVQRAAVDssrttlqLEETVDGFQRQKLKDLQKFFCDFVTIEMVFH 193
Cdd:cd07624  135 KRLELLKEVEKLQDKLECANAD-------LKADLERWKQNKRQDLKKILLDMAEKQIQYY 187
 
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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