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Conserved domains on  [gi|1121947521|ref|XP_019486580|]
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PREDICTED: amphiphysin isoform X4 [Hipposideros armiger]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAR_Amphiphysin_I_II cd07611
The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysin I and II; BAR domains are dimerization, ...
 26-236 4.13e-155

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: 447.85  E-value: 4.13e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521  26 QKLGKADETKDEQFEEYVQNFKRQEAEGTRLQRELRGYLAAIKGMQEASMKLTESLHEVYEPDWYGREDVKMVGEKCDVL 105
Cdd:cd07611     1 QKLGKADETKDEQFEEYVQNFKRQETEGTRLQRELRAYLAAIKGMQEASKKLTESLHEVYEPDWYGRDDVKTIGEKCDLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521 106 WEDFHQKLVDGSLLTLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEALQSSKRKDESRISKAEEEFQKAQKVFEEFNV 185
Cdd:cd07611    81 WEDFHQKLVDGALLTLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEALQTSKRKDEGRIAKAEEEFQKAQKVFEEFNV 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1121947521 186 DLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEIAVLCHKLYEVMTKLGD 236
Cdd:cd07611   161 DLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEISVLCHKLYEVMTKLGE 211
SH3 super family cl17036
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 644-674 8.53e-12

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.


The actual alignment was detected with superfamily member cd12140:

Pssm-ID: 473055  Cd Length: 72  Bit Score: 61.07  E-value: 8.53e-12
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1121947521 644 LHDFEAANADELTLQRGDVVLVVPSDSEADQ 674
Cdd:cd12140     8 LHDFEAANSDELELKRGDIVLVVPSETAADQ 38
PHA02682 super family cl31817
ORF080 virion core protein; Provisional
 248-414 3.37e-06

ORF080 virion core protein; Provisional


The actual alignment was detected with superfamily member PHA02682:

Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 49.47  E-value: 3.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521 248 APSDSGPLRIAKTPSP------PEEASPIPSPTASP--NHTLAPAS--PAPVRPRS--PSQTRKGPPVPPLPKVTPTKE- 314
Cdd:PHA02682   83 APSPACAAPAPACPACapaapaPAVTCPAPAPACPPatAPTCPPPAvcPAPARPAPacPPSTRQCPPAPPLPTPKPAPAa 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521 315 ----LQQENIINFFEDNFVPEISvTTPSQNEVPEVKKEETLLDLDF---DPFKPEVAAAGSAGVTHSPMSQTLPWDLWTT 387
Cdd:PHA02682  163 kpifLHNQLPPPDYPAASCPTIE-TAPAASPVLEPRIPDKIIDADNddkDLIKKELADIADSVRDLNAESLSLTRDIENA 241

                         170       180
                  ....*....|....*....|....*...
gi 1121947521 388 -STDLAQPTDSSKSLSLCNLIMEETPDS 414
Cdd:PHA02682  242 kSTTQAAIDDLRRLLTGGGVARRDTPSA 269
 
Name Accession Description Interval E-value
BAR_Amphiphysin_I_II cd07611
The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysin I and II; BAR domains are dimerization, ...
 26-236 4.13e-155

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: 447.85  E-value: 4.13e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521  26 QKLGKADETKDEQFEEYVQNFKRQEAEGTRLQRELRGYLAAIKGMQEASMKLTESLHEVYEPDWYGREDVKMVGEKCDVL 105
Cdd:cd07611     1 QKLGKADETKDEQFEEYVQNFKRQETEGTRLQRELRAYLAAIKGMQEASKKLTESLHEVYEPDWYGRDDVKTIGEKCDLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521 106 WEDFHQKLVDGSLLTLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEALQSSKRKDESRISKAEEEFQKAQKVFEEFNV 185
Cdd:cd07611    81 WEDFHQKLVDGALLTLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEALQTSKRKDEGRIAKAEEEFQKAQKVFEEFNV 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1121947521 186 DLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEIAVLCHKLYEVMTKLGD 236
Cdd:cd07611   161 DLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEISVLCHKLYEVMTKLGE 211
BAR smart00721
BAR domain;
12-233 2.73e-66

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 218.79  E-value: 2.73e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521   12 NVQKRLNRAQEKVLQKLGKADETK-DEQFEEYVQNFKRQEAEGTRLQRELRGYL---AAIKGMQEASMKLTESLHEVYEP 87
Cdd:smart00721   1 GFKKQFNRAKQKVGEKVGKAEKTKlDEDFEELERRFDTTEAEIEKLQKDTKLYLqpnPAVRAKLASQKKLSKSLGEVYEG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521   88 --DWYGREDVKMVGEKCDVLWEDFHQKLV----------DGSLLTLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEAL 155
Cdd:smart00721  81 gdDGEGLGADSSYGKALDKLGEALKKLLQveeslsqvkrTFILPLLNFLLGEFKEIKKARKKLERKLLDYDSARHKLKKA 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1121947521  156 QSSKRKDE-SRISKAEEEFQKAQKVFEEFNVDLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEIAVLCHKLYEVMTK 233
Cdd:smart00721 161 KKSKEKKKdEKLAKAEEELRKAKQEFEESNAQLVEELPQLVASRVDFFVNCLQALIEAQLNFHRESYKLLQQLQQQLDK 239
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
 13-233 7.56e-61

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: 204.11  E-value: 7.56e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521  13 VQKRLNRAQEKVLQKLGKADETK-DEQFEEYVQNFKRQEAEGTRLQRELRGYLAAIKGMQEASM-------KLTESLHEV 84
Cdd:pfam03114   1 LKKQFNRASQLLGEKVGGAEKTKlDEDFEELERRFDTTEKEIKKLQKDTKGYLQPNPGARAKQTvleqpeeLLAESMIEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521  85 YEPDWYGR------EDVKMVGEKCDVLWEDFHQKLVDGSLLTLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEALQSS 158
Cdd:pfam03114  81 GKDLGEDSsfgkalEDYGEALKRLAQLLEQLDDRVETNFLDPLRNLLKEFKEIQKHRKKLERKRLDYDAAKTRVKKAKKK 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1121947521 159 KRKDESRISKAEEEFQKAQKVFEEFNVDLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEIAVLCHKLYEVMTK 233
Cdd:pfam03114 161 KSSKAKDESQAEEELRKAQAKFEESNEQLKALLPNLLSLEVEFVVNQLVAFVEAQLDFHRQCYQLLEQLQQQLGK 235
SH3_Amphiphysin_I cd12140
Src Homology 3 domain of Amphiphysin I; Amphiphysins function primarily in endocytosis and ...
 644-674 8.53e-12

Src Homology 3 domain of Amphiphysin I; Amphiphysins function primarily in endocytosis and other membrane remodeling events. They exist in several isoforms and mammals possess two amphiphysin proteins from distinct genes. 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. Human autoantibodies to amphiphysin I hinder GABAergic signaling and contribute to the pathogenesis of paraneoplastic stiff-person syndrome. 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. The SH3 domain of amphiphysins bind proline-rich motifs present in binding partners such as dynamin, synaptojanin, and nsP3. It also belongs to a subset of SH3 domains that bind ubiquitin in a site that overlaps with the peptide binding site. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 213016  Cd Length: 72  Bit Score: 61.07  E-value: 8.53e-12
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1121947521 644 LHDFEAANADELTLQRGDVVLVVPSDSEADQ 674
Cdd:cd12140     8 LHDFEAANSDELELKRGDIVLVVPSETAADQ 38
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 248-414 3.37e-06

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 49.47  E-value: 3.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521 248 APSDSGPLRIAKTPSP------PEEASPIPSPTASP--NHTLAPAS--PAPVRPRS--PSQTRKGPPVPPLPKVTPTKE- 314
Cdd:PHA02682   83 APSPACAAPAPACPACapaapaPAVTCPAPAPACPPatAPTCPPPAvcPAPARPAPacPPSTRQCPPAPPLPTPKPAPAa 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521 315 ----LQQENIINFFEDNFVPEISvTTPSQNEVPEVKKEETLLDLDF---DPFKPEVAAAGSAGVTHSPMSQTLPWDLWTT 387
Cdd:PHA02682  163 kpifLHNQLPPPDYPAASCPTIE-TAPAASPVLEPRIPDKIIDADNddkDLIKKELADIADSVRDLNAESLSLTRDIENA 241

                         170       180
                  ....*....|....*....|....*...
gi 1121947521 388 -STDLAQPTDSSKSLSLCNLIMEETPDS 414
Cdd:PHA02682  242 kSTTQAAIDDLRRLLTGGGVARRDTPSA 269
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 644-680 2.19e-04

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 39.44  E-value: 2.19e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1121947521  644 LHDFEAANADELTLQRGDVVLVVpSDSEADQVKAEVG 680
Cdd:smart00326   8 LYDYTAQDPDELSFKKGDIITVL-EKSDDGWWKGRLG 43
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 644-678 5.14e-04

SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 38.34  E-value: 5.14e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1121947521 644 LHDFEAANADELTLQRGDVVLVVpSDSEADQVKAE 678
Cdd:pfam00018   3 LYDYTAQEPDELSFKKGDIIIVL-EKSEDGWWKGR 36
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 11-190 7.82e-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: 7.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521   11 KNVQKRLNRAQEK------VLQKLGKADETKDEQFEEyVQNFKRQEAEGTRLQRELRG--YLAAIKGMQEASMKLTESLH 82
Cdd:TIGR02168  175 KETERKLERTRENldrledILNELERQLKSLERQAEK-AERYKELKAELRELELALLVlrLEELREELEELQEELKEAEE 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521   83 EVYEpdwyGREDVKMVGEKCDVLwEDFHQKLVDgsllTLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHL----EALQSS 158
Cdd:TIGR02168  254 ELEE----LTAELQELEEKLEEL-RLEVSELEE----EIEELQKELYALANEISRLEQQKQILRERLANLerqlEELEAQ 324

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1121947521  159 KRKDESRISKAEEEFQKAQKVFEEFNVDLQEE 190
Cdd:TIGR02168  325 LEELESKLDELAEELAELEEKLEELKEELESL 356
 
Name Accession Description Interval E-value
BAR_Amphiphysin_I_II cd07611
The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysin I and II; BAR domains are dimerization, ...
 26-236 4.13e-155

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: 447.85  E-value: 4.13e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521  26 QKLGKADETKDEQFEEYVQNFKRQEAEGTRLQRELRGYLAAIKGMQEASMKLTESLHEVYEPDWYGREDVKMVGEKCDVL 105
Cdd:cd07611     1 QKLGKADETKDEQFEEYVQNFKRQETEGTRLQRELRAYLAAIKGMQEASKKLTESLHEVYEPDWYGRDDVKTIGEKCDLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521 106 WEDFHQKLVDGSLLTLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEALQSSKRKDESRISKAEEEFQKAQKVFEEFNV 185
Cdd:cd07611    81 WEDFHQKLVDGALLTLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEALQTSKRKDEGRIAKAEEEFQKAQKVFEEFNV 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1121947521 186 DLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEIAVLCHKLYEVMTKLGD 236
Cdd:cd07611   161 DLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEISVLCHKLYEVMTKLGE 211
BAR_Amphiphysin cd07588
The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysins; BAR domains are dimerization, lipid ...
 26-236 1.26e-101

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: 310.44  E-value: 1.26e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521  26 QKLGKADETKDEQFEEYVQNFKRQEAEGTRLQRELRGYLAAIKGMQEASMKLTESLHEVYEPDWYGREDVKMVGEKCDVL 105
Cdd:cd07588     1 QKLGKADETRDEVFDEHVNNFNKQQASANRLQKDLKNYLNSVRAMKQASKTLSETLKELYEPDWPGREHLASIFEQLDLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521 106 WEDFHQKLVDGSLLTLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEALQSSKRKDESRISKAEEEFQKAQKVFEEFNV 185
Cdd:cd07588    81 WNDLEEKLSDQVLGPLTAYQSQFPEVKKRIAKRGRKLVDYDSARHNLEALKAKKKVDDQKLTKAEEELQQAKKVYEELNT 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1121947521 186 DLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEIAVLCHKLYEVMTKLGD 236
Cdd:cd07588   161 ELHEELPALYDSRIAFYVDTLQSIFAAESVFHKEIGKVNTKLNDVMDGLAD 211
BAR_Bin2 cd07612
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 2; BAR domains are dimerization, ...
 26-236 1.46e-91

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: 284.06  E-value: 1.46e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521  26 QKLGKADETKDEQFEEYVQNFKRQEAEGTRLQRELRGYLAAIKGMQEASMKLTESLHEVYEPDWYGREDVKMVGEKCDVL 105
Cdd:cd07612     1 QKLGKTVETKDEQFEQCAMNLNMQQSDGNRLYKDLKAYLNAVKVMHESSKRLSQTLQDIYEPDWDGHEDLGAIVEGEDLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521 106 WEDFHQKLVDGSLLTLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEALQSSKRKDESRISKAEEEFQKAQKVFEEFNV 185
Cdd:cd07612    81 WNDYEAKLHDQALRTMESYMAQFPDVKERVAKRGRKLVDYDSARHHLEALQNAKKKDDAKIAKAEEEFNRAQVVFEDINR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1121947521 186 DLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEIAVLCHKLYEVMTKLGD 236
Cdd:cd07612   161 ELREELPILYDSRIGCYVTVFQNISNLRDTFYKEMSKLNHDLYNVMKKLED 211
BAR smart00721
BAR domain;
12-233 2.73e-66

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 218.79  E-value: 2.73e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521   12 NVQKRLNRAQEKVLQKLGKADETK-DEQFEEYVQNFKRQEAEGTRLQRELRGYL---AAIKGMQEASMKLTESLHEVYEP 87
Cdd:smart00721   1 GFKKQFNRAKQKVGEKVGKAEKTKlDEDFEELERRFDTTEAEIEKLQKDTKLYLqpnPAVRAKLASQKKLSKSLGEVYEG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521   88 --DWYGREDVKMVGEKCDVLWEDFHQKLV----------DGSLLTLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEAL 155
Cdd:smart00721  81 gdDGEGLGADSSYGKALDKLGEALKKLLQveeslsqvkrTFILPLLNFLLGEFKEIKKARKKLERKLLDYDSARHKLKKA 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1121947521  156 QSSKRKDE-SRISKAEEEFQKAQKVFEEFNVDLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEIAVLCHKLYEVMTK 233
Cdd:smart00721 161 KKSKEKKKdEKLAKAEEELRKAKQEFEESNAQLVEELPQLVASRVDFFVNCLQALIEAQLNFHRESYKLLQQLQQQLDK 239
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
 13-233 7.56e-61

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: 204.11  E-value: 7.56e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521  13 VQKRLNRAQEKVLQKLGKADETK-DEQFEEYVQNFKRQEAEGTRLQRELRGYLAAIKGMQEASM-------KLTESLHEV 84
Cdd:pfam03114   1 LKKQFNRASQLLGEKVGGAEKTKlDEDFEELERRFDTTEKEIKKLQKDTKGYLQPNPGARAKQTvleqpeeLLAESMIEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521  85 YEPDWYGR------EDVKMVGEKCDVLWEDFHQKLVDGSLLTLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEALQSS 158
Cdd:pfam03114  81 GKDLGEDSsfgkalEDYGEALKRLAQLLEQLDDRVETNFLDPLRNLLKEFKEIQKHRKKLERKRLDYDAAKTRVKKAKKK 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1121947521 159 KRKDESRISKAEEEFQKAQKVFEEFNVDLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEIAVLCHKLYEVMTK 233
Cdd:pfam03114 161 KSSKAKDESQAEEELRKAQAKFEESNEQLKALLPNLLSLEVEFVVNQLVAFVEAQLDFHRQCYQLLEQLQQQLGK 235
BAR_Rvs161p cd07591
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon ...
 27-237 2.35e-26

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: 107.81  E-value: 2.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521  27 KLGKADETKDEQFEEYVQNFKRQEAEGTRLQRELRGYLAAIKGMQEASMKLTESLHEVYEPDwyGREDVKMVGEKCDVLW 106
Cdd:cd07591     1 KTGQVERTVDREFEFEERRYRTMEKASTKLQKEAKGYLDSLRALTSSQARIAETISSFYGDA--GDKDGAMLSQEYKQAV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521 107 EDFHQKLV---DGSLLT--------LDTYlgqFPDIKNRIAKRSRKLVDYDSARHHLEALQSSKRKDESRISKAEEEFQK 175
Cdd:cd07591    79 EELDAETVkelDGPYRQtvldpigrFNSY---FPEINEAIKKRNHKLLDYDAARAKVRKLIDKPSEDPTKLPRAEKELDE 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1121947521 176 AQKVFEEFNVDLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEIAvlcHKLYEVMTKLGDQ 237
Cdd:cd07591   156 AKEVYETLNDQLKTELPQLVDLRIPYLDPSFEAFVKIQLRFFTEGY---ERLAQVQRYLDAQ 214
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 45-221 7.36e-21

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: 90.97  E-value: 7.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521  45 NFKRQEAEGTRLQRELRGYLAAIKGMQEASMKLTESLHEVYE-----PDWYGREDVKMVGEKCDVL---WEDFHQKLVDG 116
Cdd:cd07307     1 KLDELEKLLKKLIKDTKKLLDSLKELPAAAEKLSEALQELGKelpdlSNTDLGEALEKFGKIQKELeefRDQLEQKLENK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521 117 SLLTLDTYL-GQFPDIKNRIAKRSRKLVDYDSARHHLEALQSsKRKDESRISKAEEEFQKAQKVFEEFNVDLQEELPSLW 195
Cdd:cd07307    81 VIEPLKEYLkKDLKEIKKRRKKLDKARLDYDAAREKLKKLRK-KKKDSSKLAEAEEELQEAKEKYEELREELIEDLNKLE 159

                         170       180
                  ....*....|....*....|....*.
gi 1121947521 196 SRRVGFYVNTFKNVSSLEAKFHKEIA 221
Cdd:cd07307   160 EKRKELFLSLLLSFIEAQSEFFKEVL 185
BAR_Rvs167p cd07599
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon ...
 36-194 2.96e-12

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: 66.51  E-value: 2.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521  36 DEQFEEYVQNFKRQEAEGTRLQRELRGYLAAIKGMQEASMKLTESLHEVYEPdwygredvkMVGEKCDVL---------- 105
Cdd:cd07599     1 DEQFEELEKDFKSLEKSLKKLIEQSKAFRDSWRSILTHQIAFAKEFAELYDP---------IVGPKESVGshpapestla 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521 106 ----WEDFHQKLVDGSLLTLDTY-----------LGQFPDIKNRIAKRSRKLVDYDSARHHLEALQSSKR----KDESRI 166
Cdd:cd07599    72 rlsrYVKALEELKKELLEELEFFeervilpakelKKYIKKIRKTIKKRDHKKLDYDKLQNKLNKLLQKKKelslKDEKQL 151

                         170       180
                  ....*....|....*....|....*...
gi 1121947521 167 SKAEEEFQKAQKVFEEFNVDLQEELPSL 194
Cdd:cd07599   152 AKLERKLEEAKEEYEALNELLKSELPKL 179
SH3_Amphiphysin_I cd12140
Src Homology 3 domain of Amphiphysin I; Amphiphysins function primarily in endocytosis and ...
 644-674 8.53e-12

Src Homology 3 domain of Amphiphysin I; Amphiphysins function primarily in endocytosis and other membrane remodeling events. They exist in several isoforms and mammals possess two amphiphysin proteins from distinct genes. 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. Human autoantibodies to amphiphysin I hinder GABAergic signaling and contribute to the pathogenesis of paraneoplastic stiff-person syndrome. 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. The SH3 domain of amphiphysins bind proline-rich motifs present in binding partners such as dynamin, synaptojanin, and nsP3. It also belongs to a subset of SH3 domains that bind ubiquitin in a site that overlaps with the peptide binding site. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 213016  Cd Length: 72  Bit Score: 61.07  E-value: 8.53e-12
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1121947521 644 LHDFEAANADELTLQRGDVVLVVPSDSEADQ 674
Cdd:cd12140     8 LHDFEAANSDELELKRGDIVLVVPSETAADQ 38
BAR_DNMBP cd07589
The Bin/Amphiphysin/Rvs (BAR) domain of Dynamin Binding Protein; BAR domains are dimerization, ...
 33-220 7.72e-10

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: 58.87  E-value: 7.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521  33 ETKDEQFEEYVQNFKRQEAEGTRLQRELRGYLAAIKGMQEASMKLTESLHEVYEPD--------WYGREDVKMVGEKcdv 104
Cdd:cd07589     1 QTKDKEFDELEKKFGSLEKQVQLVVRNVELYLQHVQESVLVKVLALEVVLDLYPSNhprleskwERFRRVVRGISSK--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521 105 LWEDFHQKLVDGSLLTLDTYLGQFPDIKNRIAKRSRKLVDYDSARhhlealqssKRKDESRisKAEEEFQKAQKVFEEFN 184
Cdd:cd07589    78 ALPEFKSRVRKLVIEPLSSLLKLFSGPQKLIQKRYDKLLDYERYK---------EKKERGG--KVDEELEEAANQYEALN 146

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1121947521 185 VDLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEI 220
Cdd:cd07589   147 AQLKEELPKFNQLTAQLLETCLKSFVELQRDLYDTL 182
SH3_Amphiphysin cd11790
Src Homology 3 domain of Amphiphysin and related domains; Amphiphysins function primarily in ...
 644-674 7.10e-08

Src Homology 3 domain of Amphiphysin and related domains; Amphiphysins function primarily in endocytosis and other membrane remodeling events. They exist in several isoforms and mammals possess two amphiphysin proteins from distinct genes. 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. Human autoantibodies to amphiphysin I hinder GABAergic signaling and contribute to the pathogenesis of paraneoplastic stiff-person syndrome. 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. Mutations in Bin1 are associated with autosomal recessive centronuclear myopathy. 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. The SH3 domain of amphiphysins bind proline-rich motifs present in binding partners such as dynamin, synaptojanin, and nsP3. It also belongs to a subset of SH3 domains that bind ubiquitin in a site that overlaps with the peptide binding site. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212724 [Multi-domain]  Cd Length: 64  Bit Score: 49.63  E-value: 7.10e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1121947521 644 LHDFEAANADELTLQRGDVVLVVPSDSEADQ 674
Cdd:cd11790     8 THDYTAEDTDELTFEKGDVILVIPFDDPEEQ 38
BAR_Bin3 cd07590
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, ...
 27-221 1.93e-07

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: 52.37  E-value: 1.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521  27 KLGKADETKDEQFEEYVQNFKRQEAEGTRLQRELRGYLAAIKGMQEASMKLTESL---HEVYEPDWYGR--EDVKMVGEK 101
Cdd:cd07590     1 KKPILSKTVDRELEREVQKLQQLESTTKKLYKDMKKYIEAVLALSKAEQRLSQDLasgPLCEDNDELRNlvEALDSVTTQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521 102 CDVLWED----FHQKLVDgsllTLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEALQSSKRKDES--RISKAEEEFQK 175
Cdd:cd07590    81 LDKTVQElvnlIQKTFIE----PLKRLRSVFPSVNAAIKRREQSLQEYERLQAKVEKLAEKEKTGPNlaKLEQAEKALAA 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1121947521 176 AQKVFEEFNVDLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEIA 221
Cdd:cd07590   157 ARADFEKQNIKLLEELPKFYNGRTDYFQPCFEALIKSQVLYYSQST 202
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 248-414 3.37e-06

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 49.47  E-value: 3.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521 248 APSDSGPLRIAKTPSP------PEEASPIPSPTASP--NHTLAPAS--PAPVRPRS--PSQTRKGPPVPPLPKVTPTKE- 314
Cdd:PHA02682   83 APSPACAAPAPACPACapaapaPAVTCPAPAPACPPatAPTCPPPAvcPAPARPAPacPPSTRQCPPAPPLPTPKPAPAa 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521 315 ----LQQENIINFFEDNFVPEISvTTPSQNEVPEVKKEETLLDLDF---DPFKPEVAAAGSAGVTHSPMSQTLPWDLWTT 387
Cdd:PHA02682  163 kpifLHNQLPPPDYPAASCPTIE-TAPAASPVLEPRIPDKIIDADNddkDLIKKELADIADSVRDLNAESLSLTRDIENA 241

                         170       180
                  ....*....|....*....|....*...
gi 1121947521 388 -STDLAQPTDSSKSLSLCNLIMEETPDS 414
Cdd:PHA02682  242 kSTTQAAIDDLRRLLTGGGVARRDTPSA 269
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 120-221 4.41e-05

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: 45.42  E-value: 4.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521 120 TLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEALQSSKRKD--------------ESRISKAEEEFQKAQKVFEEFNV 185
Cdd:cd07596    94 PLKEYLRYCQAVKETLDDRADALLTLQSLKKDLASKKAQLEKLkaapgikpakveelEEELEEAESALEEARKRYEEISE 173

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1121947521 186 DLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEIA 221
Cdd:cd07596   174 RLKEELKRFHEERARDLKAALKEFARLQVQYAEKIA 209
SH3_MLK cd11876
Src Homology 3 domain of Mixed Lineage Kinases; MLKs are Serine/Threonine Kinases (STKs), ...
 644-682 1.33e-04

Src Homology 3 domain of Mixed Lineage Kinases; MLKs are Serine/Threonine Kinases (STKs), catalyzing the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212809 [Multi-domain]  Cd Length: 58  Bit Score: 40.19  E-value: 1.33e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1121947521 644 LHDFEAANADELTLQRGDVVLVVPSDSEadqVKAEVGMW 682
Cdd:cd11876     5 LFDYDARGEDELTLRRGQPVEVLSKDAA---VSGDEGWW 40
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 644-680 2.19e-04

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 39.44  E-value: 2.19e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1121947521  644 LHDFEAANADELTLQRGDVVLVVpSDSEADQVKAEVG 680
Cdd:smart00326   8 LYDYTAQDPDELSFKKGDIITVL-EKSDDGWWKGRLG 43
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 644-671 2.36e-04

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.


Pssm-ID: 212690 [Multi-domain]  Cd Length: 51  Bit Score: 39.37  E-value: 2.36e-04
                          10        20
                  ....*....|....*....|....*...
gi 1121947521 644 LHDFEAANADELTLQRGDVVLVVPSDSE 671
Cdd:cd00174     5 LYDYEAQDDDELSFKKGDIITVLEKDDD 32
SH3_CD2AP-like_3 cd11875
Third Src Homology 3 domain (SH3C) of CD2-associated protein and similar proteins; This ...
 644-682 4.64e-04

Third Src Homology 3 domain (SH3C) of CD2-associated protein and similar proteins; This subfamily is composed of the third SH3 domain (SH3C) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3C of both proteins have been shown to bind to ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212808 [Multi-domain]  Cd Length: 55  Bit Score: 38.49  E-value: 4.64e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1121947521 644 LHDFEAANADELTLQRGDVVLVVPSDSEadqvkaEVGMW 682
Cdd:cd11875     5 LFDYEAENEDELTLREGDIVTILSKDCE------DKGWW 37
SH3_MLK1-3 cd12059
Src Homology 3 domain of Mixed Lineage Kinases 1, 2, and 3; MLKs 1, 2, and 3 are Serine ...
 646-682 4.93e-04

Src Homology 3 domain of Mixed Lineage Kinases 1, 2, and 3; MLKs 1, 2, and 3 are Serine/Threonine Kinases (STKs), catalyzing the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. Little is known about the specific function of MLK1, also called MAP3K9. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. MLK2, also called MAP3K10, is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK3, also called MAP3K11, is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. It also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and thus, impacts inflammation and immunity. MLKs contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212992 [Multi-domain]  Cd Length: 58  Bit Score: 38.59  E-value: 4.93e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1121947521 646 DFEAANADELTLQRGDVVLVVPSDSeadQVKAEVGMW 682
Cdd:cd12059     7 DYEASAEDELTLRRGDRVEVLSKDS---AVSGDEGWW 40
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 644-678 5.14e-04

SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 38.34  E-value: 5.14e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1121947521 644 LHDFEAANADELTLQRGDVVLVVpSDSEADQVKAE 678
Cdd:pfam00018   3 LYDYTAQEPDELSFKKGDIIIVL-EKSEDGWWKGR 36
SH3_MLK4 cd12058
Src Homology 3 domain of Mixed Lineage Kinase 4; MLK4 is a Serine/Threonine Kinase (STK), ...
 644-682 5.26e-04

Src Homology 3 domain of Mixed Lineage Kinase 4; MLK4 is a Serine/Threonine Kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. MLK4 contains an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212991 [Multi-domain]  Cd Length: 58  Bit Score: 38.77  E-value: 5.26e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1121947521 644 LHDFEAANADELTLQRGDVVLVVPSDSeadQVKAEVGMW 682
Cdd:cd12058     5 LYDYEASGEDELSLRRGDVVEVLSQDA---AVSGDDGWW 40
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 246-305 8.97e-04

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 42.43  E-value: 8.97e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521 246 QGAPSDSGPLRIAKTPSPPEEASPIPSPTASPnhtLAPASPAPVRPRSPSQTRKGPPVPP 305
Cdd:PLN02226  174 QVTPSQKIPETTDPKPSPPAEDKQKPKVESAP---VAEKPKAPSSPPPPKQSAKEPQLPP 230
BAR_SNX6 cd07662
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 6; BAR domains are dimerization, lipid ...
 121-218 9.19e-04

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 6; 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. SNX6 forms a stable complex with SNX1 and may be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It interacts with the receptor serine/threonine kinases from the transforming growth factor-beta family. It also plays roles in enhancing the degradation of EGFR and in regulating the activity of Na,K-ATPase through its interaction with Translationally Controlled Tumor Protein (TCTP). BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153346  Cd Length: 218  Bit Score: 41.18  E-value: 9.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521 121 LDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEALQsSKRKDesrISKAEEEFQKAQKVFEEFNVDLQEELPSLWSRRVG 200
Cdd:cd07662   111 LKYYLRESQAAKDLLYRRSRSLVDYENANKALDKAR-AKNKD---VLQAETTQQLCCQKFEKISESAKQELIDFKTRRVA 186

                          90
                  ....*....|....*...
gi 1121947521 201 FYVNTFKNVSSLEAKFHK 218
Cdd:cd07662   187 AFRKNLVELAELELKHAK 204
SH3_9 pfam14604
Variant SH3 domain;
644-671 1.60e-03

Variant SH3 domain;


Pssm-ID: 434066 [Multi-domain]  Cd Length: 49  Bit Score: 36.83  E-value: 1.60e-03
                          10        20
                  ....*....|....*....|....*...
gi 1121947521 644 LHDFEAANADELTLQRGDVVLVVPSDSE 671
Cdd:pfam14604   2 LYPYEPKDDDELSLQRGDVITVIEESED 29
SH3_Intersectin_1 cd11836
First Src homology 3 domain (or SH3A) of Intersectin; Intersectins (ITSNs) are adaptor ...
 644-665 3.58e-03

First Src homology 3 domain (or SH3A) of Intersectin; Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The first SH3 domain (or SH3A) of ITSN1 has been shown to bind many proteins including Sos1, dynamin1/2, CIN85, c-Cbl, PI3K-C2, SHIP2, N-WASP, and CdGAP, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212770 [Multi-domain]  Cd Length: 55  Bit Score: 36.18  E-value: 3.58e-03
                          10        20
                  ....*....|....*....|..
gi 1121947521 644 LHDFEAANADELTLQRGDVVLV 665
Cdd:cd11836     5 LYAFEARNPDEISFQPGDIIQV 26
PHA03247 PHA03247
large tegument protein UL36; Provisional
 261-396 4.87e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 4.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521  261 PSPPEEASPIPSPTASPNHTLAPASPAPVRPRSPSQTRKGPPVPPLPKVTPTKELQQENIINffednfVPEISVTTPSQN 340
Cdd:PHA03247  2899 ALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVP------QPWLGALVPGRV 2972

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1121947521  341 EVPEVKkeetlldldFDPFKPEVAAAGSAgvTHSPMSQTLP-WDLWTTSTDLAQPTD 396
Cdd:PHA03247  2973 AVPRFR---------VPQPAPSREAPASS--TPPLTGHSLSrVSSWASSLALHEETD 3018
PHA03247 PHA03247
large tegument protein UL36; Provisional
 242-503 5.92e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 5.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521  242 AFTIQGAPSDSGPLRIAKTPSPPEEASPIPSPTASPNHTLAPAspAPVRPRSPSqtRKGPPVPPLPKVTPTKELQQENII 321
Cdd:PHA03247  2817 ALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPG--GDVRRRPPS--RSPAAKPAAPARPPVRRLARPAVS 2892

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521  322 NFFEDNFVPEISVTTPSQNEVPEVKKEETLLDLDFDPFKPE----------------VAAAGSAGVTHSPMSQTL-PWDL 384
Cdd:PHA03247  2893 RSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPpppprpqpplapttdpAGAGEPSGAVPQPWLGALvPGRV 2972

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521  385 WTTSTDLAQPTDSSKSLSLCNLIMEETPDSG---------LAEEIQRSQIDLGAFIWGPDASTDSVSQEVTHSgsqeDSA 455
Cdd:PHA03247  2973 AVPRFRVPQPAPSREAPASSTPPLTGHSLSRvsswasslaLHEETDPPPVSLKQTLWPPDDTEDSDADSLFDS----DSE 3048

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1121947521  456 CLSEAEQDVGLSTGMLPSAD--GPTVVEQGDR-----LLGPTPPWGNEHLSPKPV 503
Cdd:PHA03247  3049 RSDLEALDPLPPEPHDPFAHepDPATPEAGARespssQFGPPPLSANAALSRRYV 3103
SH3_AHI-1 cd11812
Src Homology 3 domain of Abelson helper integration site-1 (AHI-1); AHI-1, also called ...
 644-671 6.15e-03

Src Homology 3 domain of Abelson helper integration site-1 (AHI-1); AHI-1, also called Jouberin, is expressed in high levels in the brain, gonad tissues, and skeletal muscle. It is an adaptor protein that interacts with the small GTPase Rab8a and regulates it distribution and function, affecting cilium formation and vesicle transport. Mutations in the AHI-1 gene can cause Joubert syndrome, a disorder characterized by brainstem malformations, cerebellar aplasia/hypoplasia, and retinal dystrophy. AHI-1 variation is also associated with susceptibility to schizophrenia and type 2 diabetes mellitus progression. AHI-1 contains WD40 and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212746 [Multi-domain]  Cd Length: 52  Bit Score: 35.56  E-value: 6.15e-03
                          10        20
                  ....*....|....*....|....*...
gi 1121947521 644 LHDFEAANADELTLQRGDVVLVVPSDSE 671
Cdd:cd11812     5 LYDYTANRSDELTIHRGDIIRVLYKDND 32
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 11-190 7.82e-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: 7.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521   11 KNVQKRLNRAQEK------VLQKLGKADETKDEQFEEyVQNFKRQEAEGTRLQRELRG--YLAAIKGMQEASMKLTESLH 82
Cdd:TIGR02168  175 KETERKLERTRENldrledILNELERQLKSLERQAEK-AERYKELKAELRELELALLVlrLEELREELEELQEELKEAEE 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121947521   83 EVYEpdwyGREDVKMVGEKCDVLwEDFHQKLVDgsllTLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHL----EALQSS 158
Cdd:TIGR02168  254 ELEE----LTAELQELEEKLEEL-RLEVSELEE----EIEELQKELYALANEISRLEQQKQILRERLANLerqlEELEAQ 324

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1121947521  159 KRKDESRISKAEEEFQKAQKVFEEFNVDLQEE 190
Cdd:TIGR02168  325 LEELESKLDELAEELAELEEKLEELKEELESL 356
PHA03301 PHA03301
envelope glycoprotein L; Provisional
 256-304 8.37e-03

envelope glycoprotein L; Provisional


Pssm-ID: 223037 [Multi-domain]  Cd Length: 226  Bit Score: 38.31  E-value: 8.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1121947521 256 RIAKTPSPP-EEASPIPSPTASPNHTLAPASPAPVRPRSPSQTRKGPPVP 304
Cdd:PHA03301  175 RTRRPLSAPdDEASPQPKSLATPPPVAAPSRRTPRPRRKPRGNRTRPSRP 224
SH3_STAM2 cd11963
Src homology 3 domain of Signal Transducing Adaptor Molecule 2; STAM2, also called EAST ...
 644-678 8.81e-03

Src homology 3 domain of Signal Transducing Adaptor Molecule 2; STAM2, also called EAST (Epidermal growth factor receptor-associated protein with SH3 and TAM domain) or Hbp (Hrs binding protein), is part of the endosomal sorting complex required for transport (ESCRT-0). It plays a role in sorting mono-ubiquinated endosomal cargo for trafficking to the lysosome for degradation. It is also involved in the regulation of exocytosis. STAMs were discovered as proteins that are highly phosphorylated following cytokine and growth factor stimulation. They function in cytokine signaling and surface receptor degradation, as well as regulate Golgi morphology. They associate with many proteins including Jak2 and Jak3 tyrosine kinases, Hrs, AMSH, and UBPY. STAM adaptor proteins contain VHS (Vps27, Hrs, STAM homology), ubiquitin interacting (UIM), and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212896 [Multi-domain]  Cd Length: 57  Bit Score: 34.99  E-value: 8.81e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1121947521 644 LHDFEAANADELTLQRGDVVLVVpSDSEADQVKAE 678
Cdd:cd11963     7 LYDFEAVEDNELTFKHGEIIIVL-DDSDANWWKGE 40
SH3_Bin1 cd12139
Src Homology 3 domain of Bridging integrator 1 (Bin1), also called Amphiphysin-2; Bin1 ...
 644-674 8.88e-03

Src Homology 3 domain of Bridging integrator 1 (Bin1), also called Amphiphysin-2; Bin1 isoforms are localized in many different tissues and may function in intracellular vesicle trafficking. It plays a role in the organization and maintenance of the T-tubule network in skeletal muscle. Mutations in Bin1 are associated with autosomal recessive centronuclear myopathy. Bin1 contains an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR) and a C-terminal SH3 domain. The SH3 domain of Bin1 forms transient complexes with actin, myosin filaments, and CDK5, to facilitate sarcomere organization and myofiber maturation. It also binds dynamin and prevents its self-assembly. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 213015  Cd Length: 72  Bit Score: 35.66  E-value: 8.88e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1121947521 644 LHDFEAANADELTLQRGDVVLVVPSDSEADQ 674
Cdd:cd12139     8 QHDYTATDTDELQLKAGDVVLVIPFQNPEEQ 38
PHA03247 PHA03247
large tegument protein UL36; Provisional
 244-312 9.92e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.54  E-value: 9.92e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1121947521  244 TIQGAPSDSGPlRIAKTPSPPEEASPIPSPTASpnhtlAPASPAPVRPRSPSQTRKGPPVPPLPKVTPT 312
Cdd:PHA03247  2715 LVSATPLPPGP-AAARQASPALPAAPAPPAVPA-----GPATPGGPARPARPPTTAGPPAPAPPAAPAA 2777
 
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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