NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|21536402|ref|NP_647594|]
View 

myc box-dependent-interacting protein 1 isoform 2 [Homo sapiens]

Protein Classification

myc box-dependent-interacting protein 1( domain architecture ID 12957181)

myc box-dependent-interacting protein 1 plays is localized in many different tissues and may function in intracellular vesicle trafficking; mutations in this protein are associated with autosomal recessive centronuclear myopathy

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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, ...
31-272 1.06e-142

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: 410.10  E-value: 1.06e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  31 QKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLNECLQEVYEPDWPGRDEANKIAENNDLL 110
Cdd:cd07611   1 QKLGKADETKDEQFEEYVQNFKRQETEGTRLQRELRAYLAAIKGMQEASKKLTESLHEVYEPDWYGRDDVKTIGEKCDLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402 111 WMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKpvsllekaapqwcqgkl 190
Cdd:cd07611  81 WEDFHQKLVDGALLTLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEALQTSKRKDEGRIAK----------------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402 191 qahlvaqtnllrnqAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVGL 270
Cdd:cd07611 144 --------------AEEEFQKAQKVFEEFNVDLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEISVLCHKLYEVMTKL 209

                ..
gi 21536402 271 EK 272
Cdd:cd07611 210 GE 211
SH3_Bin1 cd12139
Src Homology 3 domain of Bridging integrator 1 (Bin1), also called Amphiphysin-2; Bin1 ...
478-549 7.69e-46

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: 155.07  E-value: 7.69e-46
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536402 478 FMFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKELEKCRGVFPENFTERV 549
Cdd:cd12139   1 FLFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKKLEKCRGVFPENFTERV 72
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
260-448 5.47e-09

DNA polymerase III subunits gamma and tau; Validated


The actual alignment was detected with superfamily member PRK07764:

Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 58.84  E-value: 5.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  260 NQNLNDVLVGLEKQHGSNTFTVKAQPSDNAPAKGNKSPSPPDGSPAATPEirvnhePEPAGGATPGAtlPKSPSQFEAPG 339
Cdd:PRK07764 563 SPGNAEVLVTALAEELGGDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEA------ARPAAPAAPAA--PAAPAPAGAAA 634
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  340 PFSEQASLLDLDFDPLPPVTSPVKAPTPSGQSIPWDLWEPTESPAGSLPSGEPSAAEGTFAVSwPSQTAEPGPAQPAEAS 419
Cdd:PRK07764 635 APAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAA-PAQPAPAPAATPPAGQ 713
                        170       180
                 ....*....|....*....|....*....
gi 21536402  420 EVAGGTQPAAGAQEPGETAASEAASSSLP 448
Cdd:PRK07764 714 ADDPAAQPPQAAQGASAPSPAADDPVPLP 742
 
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, ...
31-272 1.06e-142

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: 410.10  E-value: 1.06e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  31 QKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLNECLQEVYEPDWPGRDEANKIAENNDLL 110
Cdd:cd07611   1 QKLGKADETKDEQFEEYVQNFKRQETEGTRLQRELRAYLAAIKGMQEASKKLTESLHEVYEPDWYGRDDVKTIGEKCDLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402 111 WMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKpvsllekaapqwcqgkl 190
Cdd:cd07611  81 WEDFHQKLVDGALLTLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEALQTSKRKDEGRIAK----------------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402 191 qahlvaqtnllrnqAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVGL 270
Cdd:cd07611 144 --------------AEEEFQKAQKVFEEFNVDLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEISVLCHKLYEVMTKL 209

                ..
gi 21536402 271 EK 272
Cdd:cd07611 210 GE 211
BAR smart00721
BAR domain;
17-269 4.42e-64

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 209.16  E-value: 4.42e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402     17 NVQKKLTRAQEKVLQKLGKADETK-DEQFEQCVQNFNKQLTEGTRLQKDLRTYL---ASVKAMHEASKKLNECLQEVYEP 92
Cdd:smart00721   1 GFKKQFNRAKQKVGEKVGKAEKTKlDEDFEELERRFDTTEAEIEKLQKDTKLYLqpnPAVRAKLASQKKLSKSLGEVYEG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402     93 --DWPGRDEANKIAENNDLLWMDYHQKLV----------DQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESL 160
Cdd:smart00721  81 gdDGEGLGADSSYGKALDKLGEALKKLLQveeslsqvkrTFILPLLNFLLGEFKEIKKARKKLERKLLDYDSARHKLKKA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402    161 QTAKKKDEAkiakpvsllEKAApqwcqgklqahlvaqtnllrnQAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVN 240
Cdd:smart00721 161 KKSKEKKKD---------EKLA---------------------KAEEELRKAKQEFEESNAQLVEELPQLVASRVDFFVN 210
                          250       260
                   ....*....|....*....|....*....
gi 21536402    241 TFQSIAGLEENFHKEMSKLNQNLNDVLVG 269
Cdd:smart00721 211 CLQALIEAQLNFHRESYKLLQQLQQQLDK 239
SH3_Bin1 cd12139
Src Homology 3 domain of Bridging integrator 1 (Bin1), also called Amphiphysin-2; Bin1 ...
478-549 7.69e-46

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: 155.07  E-value: 7.69e-46
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536402 478 FMFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKELEKCRGVFPENFTERV 549
Cdd:cd12139   1 FLFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKKLEKCRGVFPENFTERV 72
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
18-263 1.33e-40

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: 146.71  E-value: 1.33e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402    18 VQKKLTRAQEKVLQKLGKADETK-DEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAM--HEASKKLN-----ECLQEV 89
Cdd:pfam03114   1 LKKQFNRASQLLGEKVGGAEKTKlDEDFEELERRFDTTEKEIKKLQKDTKGYLQPNPGAraKQTVLEQPeellaESMIEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402    90 YEPDWPGRDEAN-----KIAENNDL-LWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTA 163
Cdd:pfam03114  81 GKDLGEDSSFGKaledyGEALKRLAqLLEQLDDRVETNFLDPLRNLLKEFKEIQKHRKKLERKRLDYDAAKTRVKKAKKK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402   164 KKKDEAKiakpvsllekaapqwcqgklqahlvaqtnllRNQAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQ 243
Cdd:pfam03114 161 KSSKAKD-------------------------------ESQAEEELRKAQAKFEESNEQLKALLPNLLSLEVEFVVNQLV 209
                         250       260
                  ....*....|....*....|....
gi 21536402   244 SIAGLEENFHKE----MSKLNQNL 263
Cdd:pfam03114 210 AFVEAQLDFHRQcyqlLEQLQQQL 233
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
480-547 7.26e-12

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: 60.24  E-value: 7.26e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536402    480 FKVQAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGVKESdwnqhkeleKCRGVFPENFTE 547
Cdd:smart00326   3 PQVRALYDYTAQDPDELSFKKGDIITVL-----EKSDDGWWKGRLGR---------GKEGLFPSNYVE 56
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
260-448 5.47e-09

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 58.84  E-value: 5.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  260 NQNLNDVLVGLEKQHGSNTFTVKAQPSDNAPAKGNKSPSPPDGSPAATPEirvnhePEPAGGATPGAtlPKSPSQFEAPG 339
Cdd:PRK07764 563 SPGNAEVLVTALAEELGGDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEA------ARPAAPAAPAA--PAAPAPAGAAA 634
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  340 PFSEQASLLDLDFDPLPPVTSPVKAPTPSGQSIPWDLWEPTESPAGSLPSGEPSAAEGTFAVSwPSQTAEPGPAQPAEAS 419
Cdd:PRK07764 635 APAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAA-PAQPAPAPAATPPAGQ 713
                        170       180
                 ....*....|....*....|....*....
gi 21536402  420 EVAGGTQPAAGAQEPGETAASEAASSSLP 448
Cdd:PRK07764 714 ADDPAAQPPQAAQGASAPSPAADDPVPLP 742
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
483-542 1.77e-07

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: 47.58  E-value: 1.77e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402   483 QAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGvkESDWNQhkelekcRGVFP 542
Cdd:pfam00018   1 VALYDYTAQEPDELSFKKGDIIIVL-----EKSEDGWWKG--RNKGGK-------EGLIP 46
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
320-503 4.76e-04

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


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 42.98  E-value: 4.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402   320 GGATPGAT--LPKS---PSQFEAPGPFSEQASLLDLDfDPLPPVT----SPVkAPTPSGQSIPWDLWEP-TESPAGSLPS 389
Cdd:pfam05109 438 GFAAPNTTtgLPSSthvPTNLTAPASTGPTVSTADVT-SPTPAGTtsgaSPV-TPSPSPRDNGTESKAPdMTSPTSAVTT 515
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402   390 GEPSAAEGTFAVSWPSQTA---------------EPGP----AQPAEASEVAGGTQPAAGAQEPGETAASEAASSSLPaV 450
Cdd:pfam05109 516 PTPNATSPTPAVTTPTPNAtsptlgktsptsavtTPTPnatsPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNATSP-T 594
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 21536402   451 VVETFPA--TVNGTVEGGSGAGRLDLPPGFMFK--VQAQHDYTATDTDELQLKAGDV 503
Cdd:pfam05109 595 VGETSPQanTTNHTLGGTSSTPVVTSPPKNATSavTTGQHNITSSSTSSMSLRPSSI 651
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
284-470 7.65e-03

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 38.89  E-value: 7.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402 284 QPSDNAPAKGNKSPSPPDGSPAATPEIRVNHEPEPAGGATPGATLPKSPSQFEAPGPFSEQaslldldfDPLPPVTSPVK 363
Cdd:COG5180 318 RPPGGARDPGTPRPGQPTERPAGVPEAASDAGQPPSAYPPAEEAVPGKPLEQGAPRPGSSG--------GDGAPFQPPNG 389
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402 364 APTPSGQSIPwDLWEPTESPAGSLPSGEPSAAEGTFAVSWPSQTAEPGPA--QPAEASEVAGGTQPAAGAQEPGETAASE 441
Cdd:COG5180 390 APQPGLGRRG-APGPPMGAGDLVQAALDGGGRETASLGGAAGGAGQGPKAdfVPGDAESVSGPAGLADQAGAAASTAMAD 468
                       170       180
                ....*....|....*....|....*....
gi 21536402 442 AASSSLPAVVVEtfPATVNGTVEGGSGAG 470
Cdd:COG5180 469 FVAPVTDATPVD--VADVLGVRPDAILGG 495
 
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, ...
31-272 1.06e-142

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: 410.10  E-value: 1.06e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  31 QKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLNECLQEVYEPDWPGRDEANKIAENNDLL 110
Cdd:cd07611   1 QKLGKADETKDEQFEEYVQNFKRQETEGTRLQRELRAYLAAIKGMQEASKKLTESLHEVYEPDWYGRDDVKTIGEKCDLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402 111 WMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKpvsllekaapqwcqgkl 190
Cdd:cd07611  81 WEDFHQKLVDGALLTLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEALQTSKRKDEGRIAK----------------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402 191 qahlvaqtnllrnqAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVGL 270
Cdd:cd07611 144 --------------AEEEFQKAQKVFEEFNVDLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEISVLCHKLYEVMTKL 209

                ..
gi 21536402 271 EK 272
Cdd:cd07611 210 GE 211
BAR_Amphiphysin cd07588
The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysins; BAR domains are dimerization, lipid ...
31-272 1.80e-122

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: 358.59  E-value: 1.80e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  31 QKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLNECLQEVYEPDWPGRDEANKIAENNDLL 110
Cdd:cd07588   1 QKLGKADETRDEVFDEHVNNFNKQQASANRLQKDLKNYLNSVRAMKQASKTLSETLKELYEPDWPGREHLASIFEQLDLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402 111 WMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIakpvsllekaapqwcqgkl 190
Cdd:cd07588  81 WNDLEEKLSDQVLGPLTAYQSQFPEVKKRIAKRGRKLVDYDSARHNLEALKAKKKVDDQKL------------------- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402 191 qahlvaqtnllrNQAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVGL 270
Cdd:cd07588 142 ------------TKAEEELQQAKKVYEELNTELHEELPALYDSRIAFYVDTLQSIFAAESVFHKEIGKVNTKLNDVMDGL 209

                ..
gi 21536402 271 EK 272
Cdd:cd07588 210 AD 211
BAR_Bin2 cd07612
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 2; BAR domains are dimerization, ...
31-272 5.07e-102

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: 306.40  E-value: 5.07e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  31 QKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLNECLQEVYEPDWPGRDEANKIAENNDLL 110
Cdd:cd07612   1 QKLGKTVETKDEQFEQCAMNLNMQQSDGNRLYKDLKAYLNAVKVMHESSKRLSQTLQDIYEPDWDGHEDLGAIVEGEDLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402 111 WMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKpvsllekaapqwcqgkl 190
Cdd:cd07612  81 WNDYEAKLHDQALRTMESYMAQFPDVKERVAKRGRKLVDYDSARHHLEALQNAKKKDDAKIAK----------------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402 191 qahlvaqtnllrnqAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVGL 270
Cdd:cd07612 144 --------------AEEEFNRAQVVFEDINRELREELPILYDSRIGCYVTVFQNISNLRDTFYKEMSKLNHDLYNVMKKL 209

                ..
gi 21536402 271 EK 272
Cdd:cd07612 210 ED 211
BAR smart00721
BAR domain;
17-269 4.42e-64

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 209.16  E-value: 4.42e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402     17 NVQKKLTRAQEKVLQKLGKADETK-DEQFEQCVQNFNKQLTEGTRLQKDLRTYL---ASVKAMHEASKKLNECLQEVYEP 92
Cdd:smart00721   1 GFKKQFNRAKQKVGEKVGKAEKTKlDEDFEELERRFDTTEAEIEKLQKDTKLYLqpnPAVRAKLASQKKLSKSLGEVYEG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402     93 --DWPGRDEANKIAENNDLLWMDYHQKLV----------DQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESL 160
Cdd:smart00721  81 gdDGEGLGADSSYGKALDKLGEALKKLLQveeslsqvkrTFILPLLNFLLGEFKEIKKARKKLERKLLDYDSARHKLKKA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402    161 QTAKKKDEAkiakpvsllEKAApqwcqgklqahlvaqtnllrnQAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVN 240
Cdd:smart00721 161 KKSKEKKKD---------EKLA---------------------KAEEELRKAKQEFEESNAQLVEELPQLVASRVDFFVN 210
                          250       260
                   ....*....|....*....|....*....
gi 21536402    241 TFQSIAGLEENFHKEMSKLNQNLNDVLVG 269
Cdd:smart00721 211 CLQALIEAQLNFHRESYKLLQQLQQQLDK 239
SH3_Bin1 cd12139
Src Homology 3 domain of Bridging integrator 1 (Bin1), also called Amphiphysin-2; Bin1 ...
478-549 7.69e-46

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: 155.07  E-value: 7.69e-46
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536402 478 FMFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKELEKCRGVFPENFTERV 549
Cdd:cd12139   1 FLFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKKLEKCRGVFPENFTERV 72
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
18-263 1.33e-40

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: 146.71  E-value: 1.33e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402    18 VQKKLTRAQEKVLQKLGKADETK-DEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAM--HEASKKLN-----ECLQEV 89
Cdd:pfam03114   1 LKKQFNRASQLLGEKVGGAEKTKlDEDFEELERRFDTTEKEIKKLQKDTKGYLQPNPGAraKQTVLEQPeellaESMIEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402    90 YEPDWPGRDEAN-----KIAENNDL-LWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTA 163
Cdd:pfam03114  81 GKDLGEDSSFGKaledyGEALKRLAqLLEQLDDRVETNFLDPLRNLLKEFKEIQKHRKKLERKRLDYDAAKTRVKKAKKK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402   164 KKKDEAKiakpvsllekaapqwcqgklqahlvaqtnllRNQAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQ 243
Cdd:pfam03114 161 KSSKAKD-------------------------------ESQAEEELRKAQAKFEESNEQLKALLPNLLSLEVEFVVNQLV 209
                         250       260
                  ....*....|....*....|....
gi 21536402   244 SIAGLEENFHKE----MSKLNQNL 263
Cdd:pfam03114 210 AFVEAQLDFHRQcyqlLEQLQQQL 233
SH3_Amphiphysin cd11790
Src Homology 3 domain of Amphiphysin and related domains; Amphiphysins function primarily in ...
478-549 2.36e-33

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: 121.28  E-value: 2.36e-33
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536402 478 FMFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDwnqhkeleKCRGVFPENFTERV 549
Cdd:cd11790   1 VLYKVRATHDYTAEDTDELTFEKGDVILVIPFDDPEEQDEGWLMGVKEST--------GCRGVFPENFTERI 64
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
50-265 1.66e-26

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: 106.76  E-value: 1.66e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  50 NFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLNECLQEVYEPDWP--------GRDEANKIAENNDLLWMDYHQKLVDQ 121
Cdd:cd07307   1 KLDELEKLLKKLIKDTKKLLDSLKELPAAAEKLSEALQELGKELPDlsntdlgeALEKFGKIQKELEEFRDQLEQKLENK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402 122 ALLTMDTYL-GQFPDIKSRIAKRGRKLVDYDSARHHYESLQTaKKKDEAKIAkpvsllekaapqwcqgklqahlvaqtnl 200
Cdd:cd07307  81 VIEPLKEYLkKDLKEIKKRRKKLDKARLDYDAAREKLKKLRK-KKKDSSKLA---------------------------- 131
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536402 201 lrnQAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLND 265
Cdd:cd07307 132 ---EAEEELQEAKEKYEELREELIEDLNKLEEKRKELFLSLLLSFIEAQSEFFKEVLKILEQLLP 193
SH3_Amphiphysin_I cd12140
Src Homology 3 domain of Amphiphysin I; Amphiphysins function primarily in endocytosis and ...
478-549 3.26e-25

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: 98.82  E-value: 3.26e-25
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536402 478 FMFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKELEKCRGVFPENFTERV 549
Cdd:cd12140   1 FLYKVETLHDFEAANSDELELKRGDIVLVVPSETAADQDAGWLTGVKESDWLQYRDASAYKGLFPENFTRRL 72
BAR_Rvs161p cd07591
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon ...
32-261 2.30e-18

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: 83.93  E-value: 2.30e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  32 KLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLNECLQEVYEpDWPGRDEANKIAEnndllw 111
Cdd:cd07591   1 KTGQVERTVDREFEFEERRYRTMEKASTKLQKEAKGYLDSLRALTSSQARIAETISSFYG-DAGDKDGAMLSQE------ 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402 112 mdYHQ---KLVDQALLTMDTYLGQ------------FPDIKSRIAKRGRKLVDYDSARHHYESLqtakkkdeakIAKPVS 176
Cdd:cd07591  74 --YKQaveELDAETVKELDGPYRQtvldpigrfnsyFPEINEAIKKRNHKLLDYDAARAKVRKL----------IDKPSE 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402 177 LLEKAApqwcqgklqahlvaqtnllrnQAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKE- 255
Cdd:cd07591 142 DPTKLP---------------------RAEKELDEAKEVYETLNDQLKTELPQLVDLRIPYLDPSFEAFVKIQLRFFTEg 200

                ....*.
gi 21536402 256 MSKLNQ 261
Cdd:cd07591 201 YERLAQ 206
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
480-547 7.26e-12

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: 60.24  E-value: 7.26e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536402    480 FKVQAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGVKESdwnqhkeleKCRGVFPENFTE 547
Cdd:smart00326   3 PQVRALYDYTAQDPDELSFKKGDIITVL-----EKSDDGWWKGRLGR---------GKEGLFPSNYVE 56
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
481-545 4.97e-11

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: 57.86  E-value: 4.97e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGVKESdwnqhkeleKCRGVFPENF 545
Cdd:cd00174   1 YARALYDYEAQDDDELSFKKGDIITVL-----EKDDDGWWEGELNG---------GREGLFPANY 51
BAR_Bin3 cd07590
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, ...
32-265 3.27e-10

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: 60.46  E-value: 3.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  32 KLGKADETKDEQFEQCVQNFNkQLTEGTR-LQKDLRTYLASVKAMHEASKKLNECLQEVyePDWPGRDEANKIAENNDLL 110
Cdd:cd07590   1 KKPILSKTVDRELEREVQKLQ-QLESTTKkLYKDMKKYIEAVLALSKAEQRLSQDLASG--PLCEDNDELRNLVEALDSV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402 111 WMDYH---QKLVDQALLT----MDTYLGQFPDIKSRIAKRGRKLVDYdsarhhyESLQTAKKKDEAKiakpvsllEKAAP 183
Cdd:cd07590  78 TTQLDktvQELVNLIQKTfiepLKRLRSVFPSVNAAIKRREQSLQEY-------ERLQAKVEKLAEK--------EKTGP 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402 184 QwcQGKLQahlvaqtnllrnQAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNL 263
Cdd:cd07590 143 N--LAKLE------------QAEKALAAARADFEKQNIKLLEELPKFYNGRTDYFQPCFEALIKSQVLYYSQSTKIFTQL 208

                ..
gi 21536402 264 ND 265
Cdd:cd07590 209 AP 210
SH3_UBASH3 cd11791
Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing proteins, also called ...
482-548 1.34e-09

Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing proteins, also called TULA (T cell Ubiquitin LigAnd) family of proteins; UBASH3 or TULA proteins are also referred to as Suppressor of T cell receptor Signaling (STS) proteins. They contain an N-terminal UBA domain, a central SH3 domain, and a C-terminal histidine phosphatase domain. They bind c-Cbl through the SH3 domain and to ubiquitin via UBA. In some vertebrates, there are two TULA family proteins, called UBASH3A (also called TULA or STS-2) and UBASH3B (also called TULA-2 or STS-1), which show partly overlapping as well as distinct functions. UBASH3B is widely expressed while UBASH3A is only found in lymphoid cells. UBASH3A facilitates apoptosis induced in T cells through its interaction with the apoptosis-inducing factor AIF. UBASH3B is an active phosphatase while UBASH3A is not. 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: 212725 [Multi-domain]  Cd Length: 59  Bit Score: 54.23  E-value: 1.34e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402 482 VQAQHDYTATDTDELQLKAGDVVLVipfqNPEEQD---EGWLMGVkesDWnqhkeLEKCRGVFPENFTER 548
Cdd:cd11791   2 LRVLYPYTPQEEDELELVPGDYIYV----SPEELDsssDGWVEGT---SW-----LTGCSGLLPENYTEK 59
SH3_CD2AP-like_3 cd11875
Third Src Homology 3 domain (SH3C) of CD2-associated protein and similar proteins; This ...
481-547 4.64e-09

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: 52.35  E-value: 4.64e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqNPEEQDEGWLMGvkesdwnqhkELEKCRGVFPENFTE 547
Cdd:cd11875   1 KARVLFDYEAENEDELTLREGDIVTIL---SKDCEDKGWWKG----------ELNGKRGVFPDNFVE 54
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
260-448 5.47e-09

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 58.84  E-value: 5.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  260 NQNLNDVLVGLEKQHGSNTFTVKAQPSDNAPAKGNKSPSPPDGSPAATPEirvnhePEPAGGATPGAtlPKSPSQFEAPG 339
Cdd:PRK07764 563 SPGNAEVLVTALAEELGGDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEA------ARPAAPAAPAA--PAAPAPAGAAA 634
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  340 PFSEQASLLDLDFDPLPPVTSPVKAPTPSGQSIPWDLWEPTESPAGSLPSGEPSAAEGTFAVSwPSQTAEPGPAQPAEAS 419
Cdd:PRK07764 635 APAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAA-PAQPAPAPAATPPAGQ 713
                        170       180
                 ....*....|....*....|....*....
gi 21536402  420 EVAGGTQPAAGAQEPGETAASEAASSSLP 448
Cdd:PRK07764 714 ADDPAAQPPQAAQGASAPSPAADDPVPLP 742
SH3_UBASH3A cd11937
Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing protein A; UBASH3A is ...
482-548 1.01e-08

Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing protein A; UBASH3A is also called Cbl-Interacting Protein 4 (CLIP4), T cell Ubiquitin LigAnd (TULA), or T cell receptor Signaling (STS)-2. It is only found in lymphoid cells and exhibits weak phosphatase activity. UBASH3A facilitates T cell-induced apoptosis through interaction with the apoptosis-inducing factor AIF. It is involved in regulating the level of phosphorylation of the zeta-associated protein (ZAP)-70 tyrosine kinase. TULA proteins contain an N-terminal UBA domain, a central SH3 domain, and a C-terminal histidine phosphatase domain. They bind c-Cbl through the SH3 domain and to ubiquitin via UBA. 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: 212870 [Multi-domain]  Cd Length: 60  Bit Score: 51.56  E-value: 1.01e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536402 482 VQAQHDYTATDTDELQLKAGDVVLVIPFQNpEEQDEGWLMGVKESdwnqhkelEKCRGVFPENFTER 548
Cdd:cd11937   3 LRALFQYKPQNIDELMLSPGDYIFVDPTQQ-SEASEGWVIGISHR--------TGCRGFLPENYTER 60
BAR_Rvs167p cd07599
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon ...
41-230 1.44e-08

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: 55.34  E-value: 1.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  41 DEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLNECLQEVYEP-----DWPGRDEAN--KIAENNDllWMD 113
Cdd:cd07599   1 DEQFEELEKDFKSLEKSLKKLIEQSKAFRDSWRSILTHQIAFAKEFAELYDPivgpkESVGSHPAPesTLARLSR--YVK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402 114 YHQKLVDQALLTMDTY-----------LGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKK----KDEAKIAKpvsll 178
Cdd:cd07599  79 ALEELKKELLEELEFFeervilpakelKKYIKKIRKTIKKRDHKKLDYDKLQNKLNKLLQKKKelslKDEKQLAK----- 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 21536402 179 ekaapqwcqgklqahlvaqtnllrnqAEEELIKAQKVFEEMNVDLQEELPSL 230
Cdd:cd07599 154 --------------------------LERKLEEAKEEYEALNELLKSELPKL 179
SH3_D21-like cd12142
Src Homology 3 domain of SH3 domain-containing protein 21 (SH3D21) and similar proteins; ...
487-547 1.65e-08

Src Homology 3 domain of SH3 domain-containing protein 21 (SH3D21) and similar proteins; N-terminal SH3 domain of the uncharacterized protein SH3 domain-containing protein 21, and similar uncharacterized domains, it belongs to the CD2AP-like_3 subfamily of proteins. The CD2AP-like_3 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: 213018 [Multi-domain]  Cd Length: 55  Bit Score: 50.93  E-value: 1.65e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536402 487 DYTATDTDELQLKAGDVVLVIpfqNPEEQDEGWLMGvkesdwnqhkELEKCRGVFPENFTE 547
Cdd:cd12142   7 DYNPVAPDELALKKGDVIEVI---SKETEDEGWWEG----------ELNGRRGFFPDNFVM 54
SH3_ephexin1_like cd11793
Src homology 3 domain of ephexin-1-like SH3 domain containing Rho guanine nucleotide exchange ...
482-547 3.63e-08

Src homology 3 domain of ephexin-1-like SH3 domain containing Rho guanine nucleotide exchange factors; Members of this family contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), and C-terminal SH3 domains. They include the Rho guanine nucleotide exchange factors ARHGEF5, ARHGEF16, ARHGEF19, ARHGEF26, ARHGEF27 (also called ephexin-1), and similar proteins, and are also called ephexins because they interact directly with ephrin A receptors. GEFs interact with Rho GTPases via their DH domains to catalyze nucleotide exchange by stabilizing the nucleotide-free GTPase intermediate. They play important roles in neuronal development. The SH3 domains of ARHGEFs play an autoinhibitory role through intramolecular interactions with a proline-rich region N-terminal to the DH domain. 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: 212727 [Multi-domain]  Cd Length: 55  Bit Score: 50.03  E-value: 3.63e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536402 482 VQAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGVKESDwnqhkeleKCRGVFPENFTE 547
Cdd:cd11793   2 VQCVHAYTAQQPDELTLEEGDVVNVL-----RKMPDGWYEGERLRD--------GERGWFPSSYTE 54
SH3_CD2AP-like_1 cd11873
First Src Homology 3 domain (SH3A) of CD2-associated protein and similar proteins; This ...
481-545 1.64e-07

First Src Homology 3 domain (SH3A) of CD2-associated protein and similar proteins; This subfamily is composed of the first SH3 domain (SH3A) 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. SH3A of both proteins bind to an atypical PXXXPR motif at the C-terminus of Cbl and the cytoplasmic domain of the cell adhesion protein CD2. CIN85 SH3A binds to internal proline-rich motifs within the proline-rich region; this intramolecular interaction serves as a regulatory mechanism to keep CIN85 in a closed conformation, preventing the recruitment of other proteins. CIN85 SH3A has also been shown to bind 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: 212806 [Multi-domain]  Cd Length: 53  Bit Score: 48.03  E-value: 1.64e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVlvipfQNPEEQDEGWLMGvkesdwnqhkELEKCRGVFPENF 545
Cdd:cd11873   1 EVIVEFDYDAEEPDELTLKVGDII-----TNVKKMEEGWWEG----------TLNGKRGMFPDNF 50
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
483-542 1.77e-07

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: 47.58  E-value: 1.77e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402   483 QAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGvkESDWNQhkelekcRGVFP 542
Cdd:pfam00018   1 VALYDYTAQEPDELSFKKGDIIIVL-----EKSEDGWWKG--RNKGGK-------EGLIP 46
SH3_9 pfam14604
Variant SH3 domain;
484-547 2.11e-07

Variant SH3 domain;


Pssm-ID: 434066 [Multi-domain]  Cd Length: 49  Bit Score: 47.61  E-value: 2.11e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536402   484 AQHDYTATDTDELQLKAGDVVLVIPfqnpeEQDEGWLMGvkesdwnqhkELEKCRGVFPENFTE 547
Cdd:pfam14604   1 ALYPYEPKDDDELSLQRGDVITVIE-----ESEDGWWEG----------INTGRTGLVPANYVE 49
SH3_Sdc25 cd11883
Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is ...
482-545 2.22e-07

Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is composed of the Saccharomyces cerevisiae guanine nucleotide exchange factors (GEFs) Sdc25 and Cdc25, and similar proteins. These GEFs regulate Ras by stimulating the GDP/GTP exchange on Ras. Cdc25 is involved in the Ras/PKA pathway that plays an important role in the regulation of metabolism, stress responses, and proliferation, depending on available nutrients and conditions. Proteins in this subfamily contain an N-terminal SH3 domain as well as REM (Ras exchanger motif) and RasGEF domains at the C-terminus. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212816  Cd Length: 55  Bit Score: 47.66  E-value: 2.22e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536402 482 VQAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGVKESDWNQHKelekcRGVFPENF 545
Cdd:cd11883   2 VVALYDFTPKSKNQLSFKAGDIIYVL-----NKDPSGWWDGVIISSSGKVK-----RGWFPSNY 55
SH3_CD2AP-like_2 cd11874
Second Src Homology 3 domain (SH3B) of CD2-associated protein and similar proteins; This ...
481-547 2.48e-07

Second Src Homology 3 domain (SH3B) of CD2-associated protein and similar proteins; This subfamily is composed of the second SH3 domain (SH3B) 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. SH3B of both proteins have been shown to bind to Cbl. In the case of CD2AP, its SH3B binds to Cbl at a site distinct from the c-Cbl/SH3A binding site. The CIN85 SH3B also binds 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: 212807 [Multi-domain]  Cd Length: 53  Bit Score: 47.33  E-value: 2.48e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGVKESdwnqhKElekcrGVFPENFTE 547
Cdd:cd11874   1 RCKVLFSYTPQNEDELELKVGDTIEVL-----GEVEEGWWEGKLNG-----KV-----GVFPSNFVK 52
SH3_Nebulin_family_C cd11789
C-terminal Src Homology 3 domain of the Nebulin family of proteins; Nebulin family proteins ...
481-525 6.25e-07

C-terminal Src Homology 3 domain of the Nebulin family of proteins; Nebulin family proteins contain multiple nebulin repeats, and may contain an N-terminal LIM domain and/or a C-terminal SH3 domain. They have molecular weights ranging from 34 to 900 kD, depending on the number of nebulin repeats, and they all bind actin. They are involved in the regulation of actin filament architecture and function as stabilizers and scaffolds for cytoskeletal structures with which they associate, such as long actin filaments or focal adhesions. Nebulin family proteins that contain a C-terminal SH3 domain include the giant filamentous protein nebulin, nebulette, Lasp1, and Lasp2. Lasp2, also called LIM-nebulette, is an alternatively spliced variant of nebulette. 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: 212723 [Multi-domain]  Cd Length: 55  Bit Score: 46.54  E-value: 6.25e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVvlvipFQNPEEQDEGWLMGVKE 525
Cdd:cd11789   1 RYRAMYDYAAADDDEVSFQEGDV-----IINVEIIDDGWMEGTVQ 40
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
282-434 6.53e-07

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 52.19  E-value: 6.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  282 KAQPSDNAPAKGNKSPSPPdgsPAATPEIRVNHEPEPAGGATPGATLPKSPSQFEAPgPFSEQASLLDLDFDPlPPVTSP 361
Cdd:PRK12323 411 AAAAAARAVAAAPARRSPA---PEALAAARQASARGPGGAPAPAPAPAAAPAAAARP-AAAGPRPVAAAAAAA-PARAAP 485
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536402  362 VKAPTPSGQSIPwdlwePTESPAGSLPSGEPSAAEGTFAVSWPSQTAEPGPAQPAEASEVAGGTQPAAGAQEP 434
Cdd:PRK12323 486 AAAPAPADDDPP-----PWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRA 553
SH3_Sorbs_3 cd11780
Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) ...
483-548 7.10e-07

Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) proteins and similar domains; This family, also called the vinexin family, is composed predominantly of adaptor proteins containing one sorbin homology (SoHo) and three SH3 domains. Members include the third SH3 domains of Sorbs1 (or ponsin), Sorbs2 (or ArgBP2), Vinexin (or Sorbs3), and similar domains. They are involved in the regulation of cytoskeletal organization, cell adhesion, and growth factor signaling. Members of this family bind multiple partners including signaling molecules like c-Abl, c-Arg, Sos, and c-Cbl, as well as cytoskeletal molecules such as vinculin and afadin. They may have overlapping functions. 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: 212714 [Multi-domain]  Cd Length: 55  Bit Score: 46.14  E-value: 7.10e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536402 483 QAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGVKESdwnqhkelEKCRGVFPENFTER 548
Cdd:cd11780   3 RALYSYTPQNEDELELREGDIVYVM-----EKCDDGWFVGTSER--------TGLFGTFPGNYVAR 55
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
315-476 9.54e-07

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 51.77  E-value: 9.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  315 EPEPAGGATPGATLPKS-PSQFEAPGPFSEQASLLDLDFDPLPPVTSPVKAPTPSGQSiPWDLWEPTESPAGSLPSGEPS 393
Cdd:PRK07003 359 EPAVTGGGAPGGGVPARvAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAA-AAAATRAEAPPAAPAPPATAD 437
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  394 AAEGTFAVSWPSQTAEPGPAQPAEASEVAGG---TQPAAGAQEPGETAASEAASSSLPAVVVETFPATVNGTVEGGSGAG 470
Cdd:PRK07003 438 RGDDAADGDAPVPAKANARASADSRCDERDAqppADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAAS 517

                 ....*.
gi 21536402  471 RLDLPP 476
Cdd:PRK07003 518 REDAPA 523
PHA03247 PHA03247
large tegument protein UL36; Provisional
282-471 1.28e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.48  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402   282 KAQPSDNAPAKGNKSPSPPDGSPAATPEIRVNHEPEPAGGATPGATLPKSPSQFEAPGPFSEQASLLDLDFDPLPPVTSP 361
Cdd:PHA03247 2686 RAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAG 2765
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402   362 VKAPTPSgqsipwdlweptESPAGSLPSGEPSAAEGTFAVSWPSQTAEPGPAQPAEASEVAGGTQPAAGAQEPGE--TAA 439
Cdd:PHA03247 2766 PPAPAPP------------AAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLppPTS 2833
                         170       180       190
                  ....*....|....*....|....*....|..
gi 21536402   440 SEAASSSLPAVVVETFPATVNGTVEGGSGAGR 471
Cdd:PHA03247 2834 AQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRR 2865
SH3_Nostrin cd11823
Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in ...
484-547 2.65e-06

Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in endothelial and epithelial cells and is involved in the regulation, trafficking and targeting of endothelial NOS (eNOS). It facilitates the endocytosis of eNOS by coordinating the functions of dynamin and the Wiskott-Aldrich syndrome protein (WASP). Increased expression of Nostrin may be correlated to preeclampsia. Nostrin contains an N-terminal F-BAR domain and a C-terminal SH3 domain. 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: 212757 [Multi-domain]  Cd Length: 53  Bit Score: 44.64  E-value: 2.65e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536402 484 AQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGvkesdwnqhkELEKCRGVFPENFTE 547
Cdd:cd11823   4 ALYSYTANREDELSLQPGDIIEVH-----EKQDDGWWLG----------ELNGKKGIFPATYVE 52
SH3_Eve1_5 cd11818
Fifth Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 ...
481-545 3.47e-06

Fifth Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 domain-containing protein 19 (SH3D19) or EEN-binding protein (EBP), exists in multiple alternatively spliced isoforms. The longest isoform contains five SH3 domain in the C-terminal region and seven proline-rich motifs in the N-terminal region. It is abundantly expressed in skeletal muscle and heart, and may be involved in regulating the activity of ADAMs (A disintegrin and metalloproteases). Eve-1 interacts with EEN, an endophilin involved in endocytosis and may be the target of the MLL-EEN fusion protein that is implicated in leukemogenesis. 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: 212752 [Multi-domain]  Cd Length: 50  Bit Score: 44.01  E-value: 3.47e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVlvipfQNPEEQDEGWLMGvkesdwnqhkELEKCRGVFPENF 545
Cdd:cd11818   1 KARALYDFTGENEDELSFKAGDII-----TELESIDEEWMSG----------ELRGKSGIFPKNF 50
SH3_CIN85_3 cd12057
Third Src Homology 3 domain (SH3C) of Cbl-interacting protein of 85 kDa; CIN85, also called ...
488-547 3.77e-06

Third Src Homology 3 domain (SH3C) of Cbl-interacting protein of 85 kDa; CIN85, also called SH3 domain-containing kinase-binding protein 1 (SH3KBP1) or CD2-binding protein 3 (CD2BP3) or Ruk, is an adaptor protein that is involved in the downregulation of receptor tyrosine kinases by facilitating endocytosis through interaction with endophilin-associated ubiquitin ligase Cbl proteins. It is also important in many other cellular processes including vesicle-mediated transport, cytoskeletal remodelling, apoptosis, cell adhesion and migration, and viral infection, among others. CIN85 exists as multiple variants from alternative splicing; the main variant contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the third SH3 domain (SH3C) of CIN85. SH3C has been shown to bind 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: 212990 [Multi-domain]  Cd Length: 56  Bit Score: 44.12  E-value: 3.77e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402 488 YTATDTDELQLKAGDVVLVIpfqNPEEQDEGWLMGvkesdwnqhkELEKCRGVFPENFTE 547
Cdd:cd12057   8 YEAQNEDELTIKEGDIVTLI---SKDCIDAGWWEG----------ELNGRRGVFPDNFVK 54
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
283-418 4.04e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.60  E-value: 4.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  283 AQPSDNAPAKGNKSPSPPDGSPAATPEirvnhEPEPAGGATPGATLPKSPSQfeAPGPFSEQASLLDLDFDPLPPVTSPV 362
Cdd:PRK07764 385 LGVAGGAGAPAAAAPSAAAAAPAAAPA-----PAAAAPAAAAAPAPAAAPQP--APAPAPAPAPPSPAGNAPAGGAPSPP 457
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 21536402  363 KAPTPSGQSIPWDlwEPTESPAGSLPSGEPSAAEGTFAVSWPSQTAEPGPAQPAEA 418
Cdd:PRK07764 458 PAAAPSAQPAPAP--AAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAAT 511
PHA03247 PHA03247
large tegument protein UL36; Provisional
276-476 4.74e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 4.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402   276 SNTFTVKAQPSDNAPAKGNKSPSPPDGS----PAATPEIRVNHEPEPAGGATPGATLP-------------KSPSQFEAP 338
Cdd:PHA03247 2595 SARPRAPVDDRGDPRGPAPPSPLPPDTHapdpPPPSPSPAANEPDPHPPPTVPPPERPrddpapgrvsrprRARRLGRAA 2674
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402   339 GPFSEQ------------ASLLDLDfDPLPPVTSPVKAPTPSGQSIPWDLWEPT---ESPAGSLPSGEPSAAEGTFAVSW 403
Cdd:PHA03247 2675 QASSPPqrprrraarptvGSLTSLA-DPPPPPPTPEPAPHALVSATPLPPGPAAarqASPALPAAPAPPAVPAGPATPGG 2753
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536402   404 PSQTAEP----GPAQPAEASEVAGGTQPAAGAQEPGETAASEAASSSLPAVVVETFPATVNGTVEGGSGAGRLDLPP 476
Cdd:PHA03247 2754 PARPARPpttaGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP 2830
SH3_PACSIN_like cd11999
Src homology 3 domain of an unknown subfamily of proteins with similarity to Protein kinase C ...
481-547 5.81e-06

Src homology 3 domain of an unknown subfamily of proteins with similarity to Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins; PACSINs, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. They bind both dynamin and Wiskott-Aldrich syndrome protein (WASP), and may provide direct links between the actin cytoskeletal machinery through WASP and dynamin-dependent endocytosis. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain and a C-terminal SH3 domain. 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: 212932 [Multi-domain]  Cd Length: 56  Bit Score: 43.77  E-value: 5.81e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqnPEEQDEGWLMGVKESDwnqhkelekCRGVFPENFTE 547
Cdd:cd11999   3 RVRAVYDYTGQEPDELSFKAGEELLKV----EDEDEQGWCKGVTDGG---------AVGLYPANYVE 56
SH3_Abi cd11826
Src homology 3 domain of Abl Interactor proteins; Abl interactor (Abi) proteins are adaptor ...
481-547 6.73e-06

Src homology 3 domain of Abl Interactor proteins; Abl interactor (Abi) proteins are adaptor proteins serving as binding partners and substrates of Abl tyrosine kinases. They are involved in regulating actin cytoskeletal reorganization and play important roles in membrane-ruffling, endocytosis, cell motility, and cell migration. They localize to sites of actin polymerization in epithelial adherens junction and immune synapses, as well as to the leading edge of lamellipodia. Vertebrates contain two Abi proteins, Abi1 and Abi2. Abi1 displays a wide expression pattern while Abi2 is highly expressed in the eye and brain. Abi proteins contain a homeobox homology domain, a proline-rich region, and a SH3 domain. The SH3 domain of Abi binds to a PxxP motif in Abl. 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: 212760 [Multi-domain]  Cd Length: 52  Bit Score: 43.46  E-value: 6.73e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGVkesdwnqhkeLEKCRGVFPENFTE 547
Cdd:cd11826   1 KVVALYDYTADKDDELSFQEGDIIYVT-----KKNDDGWYEGV----------LNGVTGLFPGNYVE 52
SH3_Lasp1_C cd11934
C-terminal Src Homology 3 domain of LIM and SH3 domain protein 1; Lasp1 is a cytoplasmic ...
481-549 7.25e-06

C-terminal Src Homology 3 domain of LIM and SH3 domain protein 1; Lasp1 is a cytoplasmic protein that binds focal adhesion proteins and is involved in cell signaling, migration, and proliferation. It is overexpressed in several cancer cells including breast, ovarian, bladder, and liver. In cancer cells, it can be found in the nucleus; its degree of nuclear localization correlates with tumor size and poor prognosis. Lasp1 is a 36kD protein containing an N-terminal LIM domain, two nebulin repeats, and a C-terminal SH3 domain. 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: 212867 [Multi-domain]  Cd Length: 59  Bit Score: 43.45  E-value: 7.25e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLvipfqNPEEQDEGWLMGVKESDWNQhkelekcrGVFPENFTERV 549
Cdd:cd11934   4 RYRAVYDYNAADEDEVSFQDGDTIV-----NVQQIDDGWMYGTVERTGDT--------GMLPANYVEAI 59
SH3_Bbc1 cd11887
Src Homology 3 domain of Bbc1 and similar domains; This subfamily is composed of Saccharomyces ...
480-548 1.27e-05

Src Homology 3 domain of Bbc1 and similar domains; This subfamily is composed of Saccharomyces cerevisiae Bbc1p, also called Mti1p (Myosin tail region-interacting protein), and similar proteins. Bbc1p interacts with and regulates type I myosins in yeast, Myo3p and Myo5p, which are involved in actin cytoskeletal reorganization. It also binds and inhibits Las17, a WASp family protein that functions as an activator of the Arp2/3 complex. Bbc1p contains an N-terminal SH3 domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212820 [Multi-domain]  Cd Length: 60  Bit Score: 42.72  E-value: 1.27e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536402 480 FKVQAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGVKESDWNQHKElekcrGVFPENFTER 548
Cdd:cd11887   2 FKVKALYPYESDHEDDLNFDVGQLITVT-----EEEDADWYFGEYVDSNGNTKE-----GIFPKNFVEV 60
PHA03247 PHA03247
large tegument protein UL36; Provisional
280-416 1.99e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 1.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402   280 TVKAQPSDNAPAkGNKSPSPPDGsPAATPEIRVNHEP-EPAGGATPGATLPKSPSqfEAPGPFSEQASLLDLDFDP---L 355
Cdd:PHA03247 2753 GPARPARPPTTA-GPPAPAPPAA-PAAGPPRRLTRPAvASLSESRESLPSPWDPA--DPPAAVLAPAAALPPAASPagpL 2828
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536402   356 PPVTSPVKA--PTPSGQSipwdlwEPTESPAGSLPSGepsaaeGTFAVSWPSQTAEPGPAQPA 416
Cdd:PHA03247 2829 PPPTSAQPTapPPPPGPP------PPSLPLGGSVAPG------GDVRRRPPSRSPAAKPAAPA 2879
SH3_Nebulin_C cd11933
C-terminal Src Homology 3 domain of Nebulin; Nebulin is a giant filamentous protein (600-900 ...
482-549 2.11e-05

C-terminal Src Homology 3 domain of Nebulin; Nebulin is a giant filamentous protein (600-900 kD) that is expressed abundantly in skeletal muscle. It binds to actin thin filaments and regulates its assembly and function. Nebulin was thought to be part of a molecular ruler complex that is critical in determining the lengths of actin thin filaments in skeletal muscle since its length, which varies due to alternative splicing, correlates with the length of thin filaments in various muscle types. Recent studies indicate that nebulin regulates thin filament length by stabilizing the filaments and preventing depolymerization. Mutations in nebulin can cause nemaline myopathy, characterized by muscle weakness which can be severe and can lead to neonatal lethality. Nebulin contains an N-terminal LIM domain, many nebulin repeats/super repeats, and a C-terminal SH3 domain. 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: 212866 [Multi-domain]  Cd Length: 58  Bit Score: 42.30  E-value: 2.11e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536402 482 VQAQHDYTATDTDELQLKAGDVVLvipfqNPEEQDEGWLMGVKESDWNQhkelekcrGVFPENFTERV 549
Cdd:cd11933   4 FRAMYDYRAADDDEVSFKDGDTIV-----NVQTIDEGWMYGTVQRTGKT--------GMLPANYVEAI 58
SH3_Irsp53_BAIAP2L cd11779
Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53, Brain-specific ...
481-547 2.15e-05

Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53, Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2 (BAIAP2)-Like proteins, and similar proteins; Proteins in this family include IRSp53, BAIAP2L1, BAIAP2L2, and similar proteins. They all contain an Inverse-Bin/Amphiphysin/Rvs (I-BAR) or IMD domain in addition to the SH3 domain. IRSp53, also known as BAIAP2, is a scaffolding protein that takes part in many signaling pathways including Cdc42-induced filopodia formation, Rac-mediated lamellipodia extension, and spine morphogenesis. IRSp53 exists as multiple splicing variants that differ mainly at the C-termini. BAIAP2L1, also called IRTKS (Insulin Receptor Tyrosine Kinase Substrate), serves as a substrate for the insulin receptor and binds the small GTPase Rac. It plays a role in regulating the actin cytoskeleton and colocalizes with F-actin, cortactin, VASP, and vinculin. IRSp53 and IRTKS also mediate the recruitment of effector proteins Tir and EspFu, which regulate host cell actin reorganization, to bacterial attachment sites. BAIAP2L2 co-localizes with clathrin plaques but its function has not been determined. The SH3 domains of IRSp53 and IRTKS have been shown to bind the proline-rich C-terminus of EspFu. 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: 212713 [Multi-domain]  Cd Length: 57  Bit Score: 42.31  E-value: 2.15e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqNPEEQDeGWLMGvkesdwnqHKELEKCRGVFPENFTE 547
Cdd:cd11779   2 RVKALYPHAAGGETQLSFEEGDVITLL---GPEPRD-GWHYG--------ENERSGRRGWFPIAYTE 56
SH3_MLK4 cd12058
Src Homology 3 domain of Mixed Lineage Kinase 4; MLK4 is a Serine/Threonine Kinase (STK), ...
484-548 2.85e-05

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: 41.85  E-value: 2.85e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536402 484 AQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGvkesdwnqhkELEKCRGVFPENFTER 548
Cdd:cd12058   4 ALYDYEASGEDELSLRRGDVVEVLSQDAAVSGDDGWWAG----------KIRHRLGIFPANYVTR 58
SH3_Sorbs1_3 cd11916
Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing 1 (Sorbs1), ...
479-549 3.02e-05

Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing 1 (Sorbs1), also called ponsin; Sorbs1 is also called ponsin, SH3P12, or CAP (c-Cbl associated protein). It is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. It binds Cbl and plays a major role in regulating the insulin signaling pathway by enhancing insulin-induced phosphorylation of Cbl. Sorbs1, like vinexin, localizes at cell-ECM and cell-cell adhesion sites where it binds vinculin, paxillin, and afadin. It may function in the control of cell motility. Other interaction partners of Sorbs1 include c-Abl, Sos, flotillin, Grb4, ataxin-7, filamin C, 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: 212849 [Multi-domain]  Cd Length: 59  Bit Score: 41.90  E-value: 3.02e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536402 479 MFKVQAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGVKESdwnqhkelEKCRGVFPENFTERV 549
Cdd:cd11916   1 AYSYQALYSYAPQNDDELELRDGDIVDVM-----EKCDDGWFVGTSRR--------TKQFGTFPGNYVKLL 58
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
289-415 3.62e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 46.60  E-value: 3.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  289 APAKGNKSPSPPDGSPAA--TPEIRVNHEPEPAGGATPGATLPKSPSQFEAPGPfseqasllDLDFDPLPPvtspvkAPT 366
Cdd:PRK14959 379 SAPSGSAAEGPASGGAATipTPGTQGPQGTAPAAGMTPSSAAPATPAPSAAPSP--------RVPWDDAPP------APP 444
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 21536402  367 PSGQSIPWDLWEPTESPAGSLPSGEPSAAEGTFAVSWPSQTAEPGPAQP 415
Cdd:PRK14959 445 RSGIPPRPAPRMPEASPVPGAPDSVASASDAPPTLGDPSDTAEHTPSGP 493
SH3_PACSIN cd11843
Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) ...
482-547 3.89e-05

Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins; PACSINs, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. They bind both dynamin and Wiskott-Aldrich syndrome protein (WASP), and may provide direct links between the actin cytoskeletal machinery through WASP and dynamin-dependent endocytosis. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain and a C-terminal SH3 domain. 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: 212777 [Multi-domain]  Cd Length: 53  Bit Score: 41.25  E-value: 3.89e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536402 482 VQAQHDYTATDTDELQLKAGDVVLVIpfqnPEEQDEGWLMGVKESDwnqhkelekcRGVFPENFTE 547
Cdd:cd11843   2 VRALYDYEGQESDELSFKAGDILTKL----EEEDEQGWCKGRLDGR----------VGLYPANYVE 53
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
285-431 4.54e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 4.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402   285 PSDNAPAKGNKSPSPP--DGSPAATPEIRVNHEPEPAGGATPGATLPKSPSqFEAPGPFSEQASLLDLDFDPLP------ 356
Cdd:PHA03307  179 PEETARAPSSPPAEPPpsTPPAAASPRPPRRSSPISASASSPAPAPGRSAA-DDAGASSSDSSSSESSGCGWGPenecpl 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402   357 PVTSPVKAPTPSGQSIPWDLWEPTESPAGSLPS-------------GEPSAAEGTFAVSWPSQTAEPGPAQPAEASEVAG 423
Cdd:PHA03307  258 PRPAPITLPTRIWEASGWNGPSSRPGPASSSSSprerspspspsspGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSR 337

                  ....*...
gi 21536402   424 GTQPAAGA 431
Cdd:PHA03307  338 GAAVSPGP 345
SH3_Sorbs2_3 cd11917
Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing 2 (Sorbs2), ...
483-549 4.80e-05

Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing 2 (Sorbs2), also called Arg-binding protein 2 (ArgBP2); Sorbs2 or ArgBP2 is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. It regulates actin-dependent processes including cell adhesion, morphology, and migration. It is expressed in many tissues and is abundant in the heart. Like vinexin, it is found in focal adhesion where it interacts with vinculin and afadin. It also localizes in epithelial cell stress fibers and in cardiac muscle cell Z-discs. Sorbs2 has been implicated to play roles in the signaling of c-Arg, Akt, and Pyk2. Other interaction partners of Sorbs2 include c-Abl, flotillin, spectrin, dynamin 1/2, synaptojanin, PTP-PEST, 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: 212850 [Multi-domain]  Cd Length: 61  Bit Score: 41.13  E-value: 4.80e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536402 483 QAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGVKESdwnqhkelEKCRGVFPENFTERV 549
Cdd:cd11917   8 QALYNYMPRNEDELELREGDVIDVM-----EKCDDGWFVGTSRR--------TKFFGTFPGNYVKRL 61
SH3_Bzz1_2 cd11778
Second Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP ...
481-545 5.20e-05

Second Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP/Las17-interacting protein involved in endocytosis and trafficking to the vacuole. It physically interacts with type I myosins and functions in the early steps of endocytosis. Together with other proteins, it induces membrane scission in yeast. Bzz1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. This model represents the second C-terminal SH3 domain. 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: 212712 [Multi-domain]  Cd Length: 51  Bit Score: 40.94  E-value: 5.20e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqnPEEQDEGWLMGvkesdwnqhkELEKCRGVFPENF 545
Cdd:cd11778   1 YVEALYDYEAQGDDEISIRVGDRIAVI----RGDDGSGWTYG----------EINGVKGLFPTSY 51
SH3_MLK cd11876
Src Homology 3 domain of Mixed Lineage Kinases; MLKs are Serine/Threonine Kinases (STKs), ...
484-545 5.54e-05

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: 40.96  E-value: 5.54e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536402 484 AQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGvkesdwnqhkELEKCRGVFPENF 545
Cdd:cd11876   4 ALFDYDARGEDELTLRRGQPVEVLSKDAAVSGDEGWWTG----------KIGDKVGIFPSNY 55
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
264-437 5.87e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 5.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402   264 NDVLVGLEKQHGSNTFTVKAQPSDNAPAKGNKSPS---PPDGSPAATPEIRVNHEP-------EPAGGATPGATLPKSPS 333
Cdd:PHA03307   33 DDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPptgPPPGPGTEAPANESRSTPtwslstlAPASPAREGSPTPPGPS 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402   334 QFEAPGPFSEQASlldldfdPLPPVTSPVKAPTPSGQSiPWDLWEPTESPAGSLP----SGEPSAAEGTFAVSWPSQTAE 409
Cdd:PHA03307  113 SPDPPPPTPPPAS-------PPPSPAPDLSEMLRPVGS-PGPPPAASPPAAGASPaavaSDAASSRQAALPLSSPEETAR 184
                         170       180
                  ....*....|....*....|....*...
gi 21536402   410 PGPAQPAEASEVAGGTQPAAGAQEPGET 437
Cdd:PHA03307  185 APSSPPAEPPPSTPPAAASPRPPRRSSP 212
PHA03247 PHA03247
large tegument protein UL36; Provisional
280-434 6.72e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 6.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402   280 TVKAQPSDNAPAKGNKSPSPPDGSPAAT----PEIRVNHEPEPAGG-ATPGATLPKSPSQfeAPGPFSEQASLLDL---- 350
Cdd:PHA03247 2782 RLTRPAVASLSESRESLPSPWDPADPPAavlaPAAALPPAASPAGPlPPPTSAQPTAPPP--PPGPPPPSLPLGGSvapg 2859
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402   351 -DFDPLPPVTSPVKAPTpsgqsipwdlwEPTESPAGSLPSGEPSAAEGTFAVSWPSQTAEPGPAQPAEASEVAGGTQPAA 429
Cdd:PHA03247 2860 gDVRRRPPSRSPAAKPA-----------APARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ 2928

                  ....*
gi 21536402   430 GAQEP 434
Cdd:PHA03247 2929 PQPPP 2933
SH3_GRB2_like_C cd11805
C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related ...
481-548 7.93e-05

C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related proteins; This family includes the adaptor protein GRB2 and related proteins including Drosophila melanogaster Downstream of receptor kinase (DRK), Caenorhabditis elegans Sex muscle abnormal protein 5 (Sem-5), GRB2-related adaptor protein (GRAP), GRAP2, and similar proteins. Family members contain an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. GRB2/Sem-5/DRK is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. GRAP2 plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. GRAP acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. The C-terminal SH3 domains (SH3c) of GRB2 and GRAP2 have been shown to bind to classical PxxP motif ligands, as well as to non-classical motifs. GRB2 SH3c binds Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, while the SH3c of GRAP2 binds to the phosphatase-like protein HD-PTP via a RxxxxK motif. SH3 domains are protein interaction domains that typically 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: 212739 [Multi-domain]  Cd Length: 53  Bit Score: 40.30  E-value: 7.93e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGvkesdwnqhkELEKCRGVFPENFTER 548
Cdd:cd11805   1 RVQALYDFNPQEPGELEFRRGDIITVL-----DSSDPDWWKG----------ELRGRVGIFPANYVQP 53
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
281-473 8.34e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 45.64  E-value: 8.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  281 VKAQPSDNAPAKGNKSPSPPDGSPAATpeirvnhePEPAGGATPGATLPKSPSQFEAPGPFSEQASLLDLDFDPLP---P 357
Cdd:PRK12323 383 AQPAPAAAAPAAAAPAPAAPPAAPAAA--------PAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPapaP 454
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  358 VTSPVKAPTPSGQSIPWDLWEPTESPAGSLPSGEPSAAEGTFAvSW---PSQTAEPGPAQ--PAEASEVAGGTQPAAGAQ 432
Cdd:PRK12323 455 AAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPP-PWeelPPEFASPAPAQpdAAPAGWVAESIPDPATAD 533
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 21536402  433 EPGETAASEAASSSLPAVVVETFPATVNGTVEGGSGAGRLD 473
Cdd:PRK12323 534 PDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLP 574
SH3_STAM1 cd11964
Src homology 3 domain of Signal Transducing Adaptor Molecule 1; STAM1 is part of the endosomal ...
481-545 8.83e-05

Src homology 3 domain of Signal Transducing Adaptor Molecule 1; STAM1 is part of the endosomal sorting complex required for transport (ESCRT-0) and is involved in sorting ubiquitinated cargo proteins from the endosome. It may also be involved in the regulation of IL2 and GM-CSF mediated signaling, and has been implicated in neural cell survival. 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: 212897 [Multi-domain]  Cd Length: 55  Bit Score: 40.32  E-value: 8.83e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGvkesdwnqhkELEKCRGVFPENF 545
Cdd:cd11964   2 KVRAIYDFEAAEDNELTFKAGDIITIL-----DDSDPNWWKG----------ETPQGTGLFPSNF 51
SH3_CD2AP_3 cd12056
Third Src Homology 3 domain (SH3C) of CD2-associated protein; CD2AP, also called CMS (Cas ...
483-545 1.00e-04

Third Src Homology 3 domain (SH3C) of CD2-associated protein; CD2AP, also called CMS (Cas ligand with Multiple SH3 domains) or METS1 (Mesenchyme-to-Epithelium Transition protein with SH3 domains), is a cytosolic adaptor protein that plays a role in regulating the cytoskeleton. It is critical in cell-to-cell union necessary for kidney function. It also stabilizes the contact between a T cell and antigen-presenting cells. It is primarily expressed in podocytes at the cytoplasmic face of the slit diaphragm and serves as a linker anchoring podocin and nephrin to the actin cytoskeleton. CD2AP contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the third SH3 domain (SH3C) of CD2AP. SH3C has been shown to bind 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: 212989 [Multi-domain]  Cd Length: 57  Bit Score: 40.19  E-value: 1.00e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536402 483 QAQHDYTATDTDELQLKAGDVVLVIpfqNPEEQDEGWLMGvkesdwnqhkELEKCRGVFPENF 545
Cdd:cd12056   5 KALFHYEGTNEDELDFKEGEIILII---SKDTGEPGWWKG----------ELNGKEGVFPDNF 54
SH3_CD2AP_1 cd12053
First Src Homology 3 domain (SH3A) of CD2-associated protein; CD2AP, also called CMS (Cas ...
485-549 1.03e-04

First Src Homology 3 domain (SH3A) of CD2-associated protein; CD2AP, also called CMS (Cas ligand with Multiple SH3 domains) or METS1 (Mesenchyme-to-Epithelium Transition protein with SH3 domains), is a cytosolic adaptor protein that plays a role in regulating the cytoskeleton. It is critical in cell-to-cell union necessary for kidney function. It also stabilizes the contact between a T cell and antigen-presenting cells. It is primarily expressed in podocytes at the cytoplasmic face of the slit diaphragm and serves as a linker anchoring podocin and nephrin to the actin cytoskeleton. CD2AP contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the first SH3 domain (SH3A) of CD2AP. SH3A binds to the PXXXPR motif present in c-Cbl and the cytoplasmic domain of cell adhesion protein CD2. Its interaction with CD2 anchors CD2 at sites of cell contact. 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: 212986  Cd Length: 56  Bit Score: 40.21  E-value: 1.03e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536402 485 QHDYTATDTDELQLKAGDVVlvipfQNPEE-QDEGWLMGvkesdwnqhkELEKCRGVFPENFTERV 549
Cdd:cd12053   5 EYDYDAVHEDELTIRVGEII-----RNVKKlEEEGWLEG----------ELNGRRGMFPDNFVKEI 55
SH3_MyoIe_If_like cd11827
Src homology 3 domain of Myosins Ie, If, and similar proteins; Myosins Ie (MyoIe) and If ...
481-548 1.46e-04

Src homology 3 domain of Myosins Ie, If, and similar proteins; Myosins Ie (MyoIe) and If (MyoIf) are nonmuscle, unconventional, long tailed, class I myosins containing an N-terminal motor domain and a myosin tail with TH1, TH2, and SH3 domains. MyoIe interacts with the endocytic proteins, dynamin and synaptojanin-1, through its SH3 domain; it may play a role in clathrin-dependent endocytosis. In the kidney, MyoIe is critical for podocyte function and normal glomerular filtration. Mutations in MyoIe is associated with focal segmental glomerulosclerosis, a disease characterized by massive proteinuria and progression to end-stage kidney disease. MyoIf is predominantly expressed in the immune system; it plays a role in immune cell motility and innate immunity. Mutations in MyoIf may be associated with the loss of hearing. The MyoIf gene has also been found to be fused to the MLL (Mixed lineage leukemia) gene in infant acute myeloid leukemias (AML). 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: 212761 [Multi-domain]  Cd Length: 53  Bit Score: 39.71  E-value: 1.46e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGvkesdwnqhkELEKCRGVFPENFTER 548
Cdd:cd11827   1 QCKALYAYDAQDTDELSFNEGDIIEIL-----KEDPSGWWTG----------RLRGKEGLFPGNYVEK 53
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
292-436 1.49e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 44.67  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  292 KGNKSPSPPDGSPAatpeirvnhepePAGGATPGATLPkspsqfeAPGPFSEQASLLDLDFDP---LPPVTSPVKAPTPS 368
Cdd:PRK14959 373 PSGGGASAPSGSAA------------EGPASGGAATIP-------TPGTQGPQGTAPAAGMTPssaAPATPAPSAAPSPR 433
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536402  369 gqsIPWDLWEPTESPAGSLPSGEPSAAEgtfavswpsqtAEPGPAQPAEASEVAGGTQPAAGAQEPGE 436
Cdd:PRK14959 434 ---VPWDDAPPAPPRSGIPPRPAPRMPE-----------ASPVPGAPDSVASASDAPPTLGDPSDTAE 487
SH3_PACSIN3 cd11997
Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 3 (PACSIN3); ...
481-547 1.51e-04

Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 3 (PACSIN3); PACSIN 3 or Syndapin III (Synaptic dynamin-associated protein III) is expressed ubiquitously and regulates glucose uptake in adipocytes through its role in GLUT1 trafficking. It also modulates the subcellular localization and stimulus-specific function of the cation channel TRPV4. PACSINs act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain and a C-terminal SH3 domain. 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: 212930 [Multi-domain]  Cd Length: 56  Bit Score: 39.94  E-value: 1.51e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqnPEEQDEGWLMGvkesdwnqhkELEKCR-GVFPENFTE 547
Cdd:cd11997   3 RVRALYDYTGQEADELSFKAGEELLKI----GEEDEQGWCKG----------RLLSGRiGLYPANYVE 56
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
318-434 1.53e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 1.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  318 PAGGATPGATLPKSPSQFEAPGPFSEQASlldldfDPLPPVTSPVKAPTPSGQSIPwdlwEPTESPAGSLPSGEPSAAEG 397
Cdd:PRK07764 386 GVAGGAGAPAAAAPSAAAAAPAAAPAPAA------AAPAAAAAPAPAAAPQPAPAP----APAPAPPSPAGNAPAGGAPS 455
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 21536402  398 TFAVSWPSQTAEPGPAQPAEASEVAGGTQPAAGAQEP 434
Cdd:PRK07764 456 PPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAA 492
SH3_Nebulette_C cd11935
C-terminal Src Homology 3 domain of Nebulette and LIM-nebulette (or Lasp2); Nebulette is a ...
483-549 1.57e-04

C-terminal Src Homology 3 domain of Nebulette and LIM-nebulette (or Lasp2); Nebulette is a cardiac-specific protein that localizes to the Z-disc. It interacts with tropomyosin and is important in stabilizing actin thin filaments in cardiac muscles. Polymorphisms in the nebulette gene are associated with dilated cardiomyopathy, with some mutations resulting in severe heart failure. Nebulette is a 107kD protein that contains an N-terminal acidic region, multiple nebulin repeats, and a C-terminal SH3 domain. LIM-nebulette, also called Lasp2 (LIM and SH3 domain protein 2), is an alternatively spliced variant of nebulette. Although it shares a gene with nebulette, Lasp2 is not transcribed from a muscle-specific promoter, giving rise to its multiple tissue expression pattern with highest amounts in the brain. It can crosslink actin filaments and it affects cell spreading. Lasp2 is a 34kD protein containing an N-terminal LIM domain, three nebulin repeats, and a C-terminal SH3 domain. 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: 212868 [Multi-domain]  Cd Length: 58  Bit Score: 39.60  E-value: 1.57e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536402 483 QAQHDYTATDTDELQLKAGDVVlvipfQNPEEQDEGWLMG-VKESDWNqhkelekcrGVFPENFTERV 549
Cdd:cd11935   4 RAMYDYSAQDEDEVSFRDGDYI-----VNVQPIDEGWMYGtVQRTGRT---------GMLPANYIEFV 57
SH3_STAM cd11820
Src homology 3 domain of Signal Transducing Adaptor Molecules; STAMs were discovered as ...
481-545 1.70e-04

Src homology 3 domain of Signal Transducing Adaptor Molecules; 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. There are two vertebrate STAMs, STAM1 and STAM2, which may be functionally redundant; vertebrate STAMs contain ITAM motifs. They are part of the endosomal sorting complex required for transport (ESCRT-0). STAM2 deficiency in mice did not cause any obvious abnormality, while STAM1 deficiency resulted in growth retardation. Loss of both STAM1 and STAM2 in mice proved lethal, indicating that STAMs are important for embryonic development. 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: 212754 [Multi-domain]  Cd Length: 54  Bit Score: 39.37  E-value: 1.70e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGvkesdwnqhkELEKCRGVFPENF 545
Cdd:cd11820   2 KVRALYDFEAAEDNELTFKAGEIITVL-----DDSDPNWWKG----------SNHRGEGLFPANF 51
SH3_PIX cd11877
Src Homology 3 domain of Pak Interactive eXchange factors; PIX proteins are Rho guanine ...
481-547 2.00e-04

Src Homology 3 domain of Pak Interactive eXchange factors; PIX proteins are Rho guanine nucleotide exchange factors (GEFs), which activate small GTPases by exchanging bound GDP for free GTP. They act as GEFs for both Cdc42 and Rac 1, and have been implicated in cell motility, adhesion, neurite outgrowth, and cell polarity. Vertebrates contain two proteins from the PIX subfamily, alpha-PIX and beta-PIX. Alpha-PIX, also called ARHGEF6, is localized in dendritic spines where it regulates spine morphogenesis. Mutations in the ARHGEF6 gene cause X-linked intellectual disability in humans. Beta-PIX play roles in regulating neuroendocrine exocytosis, focal adhesion maturation, cell migration, synaptic vesicle localization, and insulin secretion. PIX proteins contain an N-terminal SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains, and a C-terminal leucine-zipper domain for dimerization. The SH3 domain of PIX binds to an atypical PxxxPR motif in p21-activated kinases (PAKs) with high affinity. The binding of PAKs to PIX facilitate the localization of PAKs to focal complexes and also localizes PAKs to PIX targets Cdc43 and Rac, leading to the activation of PAKs. 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: 212810 [Multi-domain]  Cd Length: 53  Bit Score: 39.22  E-value: 2.00e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGVkesdwnqhkeLEKCRGVFPENFTE 547
Cdd:cd11877   1 LVRAKFNFEGTNEDELSFDKGDIITVT-----QVVEGGWWEGT----------LNGKTGWFPSNYVK 52
SH3_BOI cd11886
Src Homology 3 domain of fungal BOI-like proteins; This subfamily includes the Saccharomyces ...
486-545 2.09e-04

Src Homology 3 domain of fungal BOI-like proteins; This subfamily includes the Saccharomyces cerevisiae proteins BOI1 and BOI2, and similar proteins. They contain an N-terminal SH3 domain, a Sterile alpha motif (SAM), and a Pleckstrin homology (PH) domain at the C-terminus. BOI1 and BOI2 interact with the SH3 domain of Bem1p, a protein involved in bud formation. They promote polarized cell growth and participates in the NoCut signaling pathway, which is involved in the control of cytokinesis. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212819  Cd Length: 55  Bit Score: 39.24  E-value: 2.09e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536402 486 HDYTATDTDELQLKAGDVVLVIpfQNPEEQDEGWLMGvkesdwnqhKELEKCR-GVFPENF 545
Cdd:cd11886   6 HDFNARSEDELTLKPGDKIELI--EDDEEFGDGWYLG---------RNLRTGEtGLFPVVF 55
SH3_SNX9_like cd11763
Src Homology 3 domain of Sorting Nexin 9 and similar proteins; Sorting nexins (SNXs) are Phox ...
481-547 2.34e-04

Src Homology 3 domain of Sorting Nexin 9 and similar proteins; 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. This subfamily consists of SH3 domain containing SNXs including SNX9, SNX18, SNX33, and similar proteins. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis, while SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1. 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: 212697 [Multi-domain]  Cd Length: 55  Bit Score: 39.23  E-value: 2.34e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqnPEEQDEGWLMGVkesdwNQHKElekcRGVFPENFTE 547
Cdd:cd11763   1 KVRALYDFDSQPSGELSLRAGEVLTIT----RQDVGDGWLEGR-----NSRGE----VGLFPSSYVE 54
SH3_CIN85_2 cd12055
Second Src Homology 3 domain (SH3B) of Cbl-interacting protein of 85 kDa; CIN85, also called ...
481-547 2.60e-04

Second Src Homology 3 domain (SH3B) of Cbl-interacting protein of 85 kDa; CIN85, also called SH3 domain-containing kinase-binding protein 1 (SH3KBP1) or CD2-binding protein 3 (CD2BP3) or Ruk, is an adaptor protein that is involved in the downregulation of receptor tyrosine kinases by facilitating endocytosis through interaction with endophilin-associated ubiquitin ligase Cbl proteins. It is also important in many other cellular processes including vesicle-mediated transport, cytoskeletal remodelling, apoptosis, cell adhesion and migration, and viral infection, among others. CIN85 exists as multiple variants from alternative splicing; the main variant contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the second SH3 domain (SH3B) of CIN85. SH3B has been shown to bind Cbl proline-rich peptides and 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: 212988 [Multi-domain]  Cd Length: 53  Bit Score: 38.82  E-value: 2.60e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIPfqnpeEQDEGWLMGVkesdwnqhkeLEKCRGVFPENFTE 547
Cdd:cd12055   1 RCQVAFSYLPQNEDELELKVGDIIEVVG-----EVEEGWWEGV----------LNGKTGMFPSNFIK 52
SH3_MLK1-3 cd12059
Src Homology 3 domain of Mixed Lineage Kinases 1, 2, and 3; MLKs 1, 2, and 3 are Serine ...
484-545 2.77e-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: 38.98  E-value: 2.77e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536402 484 AQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGvkesdwnqhkELEKCRGVFPENF 545
Cdd:cd12059   4 AVFDYEASAEDELTLRRGDRVEVLSKDSAVSGDEGWWTG----------KINDRVGIFPSNY 55
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
283-457 2.99e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 2.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  283 AQPSDNAPAKGNKSPSPPDGSPAATPEIRVNHEPEPAGGATPGATLPksPSQFEAPGPFSEQASLLDLDFDPLPPVTSPV 362
Cdd:PRK07764 637 AEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPP--APAPAAPAAPAGAAPAQPAPAPAATPPAGQA 714
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  363 KAPTPSGQSIPWDLWEPTESPAGSLPS-GEPSAAEGTFAVSWPSQTAEPGPAQPAEASEVAGGTQPAAG------AQEPG 435
Cdd:PRK07764 715 DDPAAQPPQAAQGASAPSPAADDPVPLpPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEemaeddAPSMD 794
                        170       180
                 ....*....|....*....|....*....
gi 21536402  436 ETAASEAAS-------SSLPAVVVETFPA 457
Cdd:PRK07764 795 DEDRRDAEEvamelleEELGAKKIEEFAA 823
SH3_p47phox_like cd11856
Src homology 3 domains of the p47phox subunit of NADPH oxidase and similar domains; This ...
484-519 3.00e-04

Src homology 3 domains of the p47phox subunit of NADPH oxidase and similar domains; This family is composed of the tandem SH3 domains of p47phox subunit of NADPH oxidase and Nox Organizing protein 1 (NoxO1), the four SH3 domains of Tks4 (Tyr kinase substrate with four SH3 domains), the five SH3 domains of Tks5, the SH3 domain of obscurin, Myosin-I, and similar domains. Most members of this group also contain Phox homology (PX) domains, except for obscurin and Myosin-I. p47phox and NoxO1 are regulators of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) and nonphagocytic NADPH oxidase Nox1, respectively. They play roles in the activation of their respective NADPH oxidase, which catalyzes the transfer of electrons from NADPH to molecular oxygen to form superoxide. Tks proteins are Src substrates and scaffolding proteins that play important roles in the formation of podosomes and invadopodia, the dynamic actin-rich structures that are related to cell migration and cancer cell invasion. Obscurin is a giant muscle protein that plays important roles in the organization and assembly of the myofibril and the sarcoplasmic reticulum. Type I myosins (Myosin-I) are actin-dependent motors in endocytic actin structures and actin patches. They play roles in membrane traffic in endocytic and secretory pathways, cell motility, and mechanosensing. Myosin-I contains an N-terminal actin-activated ATPase, a phospholipid-binding TH1 (tail homology 1) domain, and a C-terminal extension which includes an F-actin-binding TH2 domain, an SH3 domain, and an acidic peptide that participates in activating the Arp2/3complex. The SH3 domain of myosin-I is required for myosin-I-induced actin polymerization. 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: 212790 [Multi-domain]  Cd Length: 53  Bit Score: 38.77  E-value: 3.00e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 21536402 484 AQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGW 519
Cdd:cd11856   4 AIADYEAQGDDEISLQEGEVVEVL-----EKNDSGW 34
SH3_Cortactin_like cd11819
Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, ...
484-547 3.22e-04

Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, Abp1 (actin-binding protein 1), hematopoietic lineage cell-specific protein 1 (HS1), and similar proteins. These proteins are involved in regulating actin dynamics through direct or indirect interaction with the Arp2/3 complex, which is required to initiate actin polymerization. They all contain at least one C-terminal SH3 domain. Cortactin and HS1 bind Arp2/3 and actin through an N-terminal region that contains an acidic domain and several copies of a repeat domain found in cortactin and HS1. Abp1 binds actin via an N-terminal actin-depolymerizing factor (ADF) homology domain. Yeast Abp1 binds Arp2/3 directly through two acidic domains. Mammalian Abp1 does not directly interact with Arp2/3; instead, it regulates actin dynamics indirectly by interacting with dynamin and WASP family proteins. The C-terminal region of these proteins acts as an adaptor or scaffold that can connect membrane trafficking and signaling proteins that bind the SH3 domain within the actin network. 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: 212753 [Multi-domain]  Cd Length: 54  Bit Score: 38.83  E-value: 3.22e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536402 484 AQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGVKESdwNQhkelekcRGVFPENFTE 547
Cdd:cd11819   4 ALYDYQAAEDNEISFVEGDIITQI-----EQIDEGWWLGVNAK--GQ-------KGLFPANYVE 53
PHA03379 PHA03379
EBNA-3A; Provisional
289-464 3.97e-04

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 43.51  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  289 APAKGNKSPSPPDGSPaaTPEIRVNHEPEPAGGATPGATLPksPSQFEAPGPFSEQASLLDLDFDPLPPvtSPVKAPTPs 368
Cdd:PHA03379 408 ASEPTYGTPRPPVEKP--RPEVPQSLETATSHGSAQVPEPP--PVHDLEPGPLHDQHSMAPCPVAQLPP--GPLQDLEP- 480
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  369 GQSIPWDLWEPTESPAgslPSGEPSaaeGTFAVSWpsqtaEPGPAQPAEASEVAGGTQPAAGAQEPGETAASEAASSSLP 448
Cdd:PHA03379 481 GDQLPGVVQDGRPACA---PVPAPA---GPIVRPW-----EASLSQVPGVAFAPVMPQPMPVEPVPVPTVALERPVCPAP 549
                        170
                 ....*....|....*.
gi 21536402  449 AVVVETFPATVNGTVE 464
Cdd:PHA03379 550 PLIAMQGPGETSGIVR 565
SH3_CIN85_1 cd12052
First Src Homology 3 domain (SH3A) of Cbl-interacting protein of 85 kDa; CIN85, also called ...
480-545 4.65e-04

First Src Homology 3 domain (SH3A) of Cbl-interacting protein of 85 kDa; CIN85, also called SH3 domain-containing kinase-binding protein 1 (SH3KBP1) or CD2-binding protein 3 (CD2BP3) or Ruk, is an adaptor protein that is involved in the downregulation of receptor tyrosine kinases by facilitating endocytosis through interaction with endophilin-associated ubiquitin ligase Cbl proteins. It is also important in many other cellular processes including vesicle-mediated transport, cytoskeletal remodelling, apoptosis, cell adhesion and migration, and viral infection, among others. CIN85 exists as multiple variants from alternative splicing; the main variant contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the first SH3 domain (SH3A) of CIN85; SH3A binds to internal proline-rich motifs within the proline-rich region. This intramolecular interaction serves as a regulatory mechanism to keep CIN85 in a closed conformation, preventing the recruitment of other proteins. SH3A has also been shown to bind ubiquitin and to an atypical PXXXPR motif at the C-terminus of Cbl and the cytoplasmic end of the cell adhesion protein CD2. 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: 212985 [Multi-domain]  Cd Length: 53  Bit Score: 38.34  E-value: 4.65e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536402 480 FKVQAQHDytatdtDELQLKAGDVVLVIpfqnpEEQDEGWLMGvkesdwnqhkELEKCRGVFPENF 545
Cdd:cd12052   6 FDYKAQHE------DELTITVGDIITKI-----KKDDGGWWEG----------EIKGRRGLFPDNF 50
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
320-503 4.76e-04

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


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 42.98  E-value: 4.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402   320 GGATPGAT--LPKS---PSQFEAPGPFSEQASLLDLDfDPLPPVT----SPVkAPTPSGQSIPWDLWEP-TESPAGSLPS 389
Cdd:pfam05109 438 GFAAPNTTtgLPSSthvPTNLTAPASTGPTVSTADVT-SPTPAGTtsgaSPV-TPSPSPRDNGTESKAPdMTSPTSAVTT 515
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402   390 GEPSAAEGTFAVSWPSQTA---------------EPGP----AQPAEASEVAGGTQPAAGAQEPGETAASEAASSSLPaV 450
Cdd:pfam05109 516 PTPNATSPTPAVTTPTPNAtsptlgktsptsavtTPTPnatsPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNATSP-T 594
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 21536402   451 VVETFPA--TVNGTVEGGSGAGRLDLPPGFMFK--VQAQHDYTATDTDELQLKAGDV 503
Cdd:pfam05109 595 VGETSPQanTTNHTLGGTSSTPVVTSPPKNATSavTTGQHNITSSSTSSMSLRPSSI 651
SH3_ephexin1 cd11939
Src homology 3 domain of the Rho guanine nucleotide exchange factor, ephexin-1 (also called ...
481-547 4.86e-04

Src homology 3 domain of the Rho guanine nucleotide exchange factor, ephexin-1 (also called NGEF or ARHGEF27); Ephexin-1, also called NGEF (neuronal GEF) or ARHGEF27, activates RhoA, Tac1, and Cdc42 by exchanging bound GDP for free GTP. It is expressed mainly in the brain in a region associated with movement control. It regulates the stability of postsynaptic acetylcholine receptor (AChR) clusters and thus, plays a critical role in the maturation and neurotransmission of neuromuscular junctions. Ephexin-1 directly interacts with the ephrin receptor EphA4 and their coexpression enhances the ability of ephexin-1 to activate RhoA. It is required for normal axon growth and EphA-induced growth cone collapse. Ephexin-1 contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), and SH3 domains. The SH3 domains of ARHGEFs play an autoinhibitory role through intramolecular interactions with a proline-rich region N-terminal to the DH domain. 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: 212872 [Multi-domain]  Cd Length: 55  Bit Score: 38.39  E-value: 4.86e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGVKESDWNqhkelekcRGVFPENFTE 547
Cdd:cd11939   1 QVQCVHPYVSQEPDELSLELADVLNIL-----DKTDDGWIFGERLHDQE--------RGWFPSSVVE 54
SH3_PSTPIP1 cd11824
Src homology 3 domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; PSTPIP1, ...
481-521 5.03e-04

Src homology 3 domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; PSTPIP1, also called CD2 Binding Protein 1 (CD2BP1), is mainly expressed in hematopoietic cells. It is a binding partner of the cell surface receptor CD2 and PTP-PEST, a tyrosine phosphatase which functions in cell motility and Rac1 regulation. It also plays a role in the activation of the Wiskott-Aldrich syndrome protein (WASP), which couples actin rearrangement and T cell activation. Mutations in the gene encoding PSTPIP1 cause the autoinflammatory disorder known as PAPA (pyogenic sterile arthritis, pyoderma gangrenosum, and acne) syndrome. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain. 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: 212758 [Multi-domain]  Cd Length: 53  Bit Score: 38.12  E-value: 5.03e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLM 521
Cdd:cd11824   1 KYSVLYDYTAQEDDELSISKGDVVAVI-----EKGEDGWWT 36
PHA02682 PHA02682
ORF080 virion core protein; Provisional
285-395 5.18e-04

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 42.16  E-value: 5.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  285 PSDNAPAKGNKSPSPPDGSPAATPeirvnhePEPAgGATPGATLPKSPSQFEAPGPFSEQASL--LDLDFDPLPPVTSPV 362
Cdd:PHA02682  86 PACAAPAPACPACAPAAPAPAVTC-------PAPA-PACPPATAPTCPPPAVCPAPARPAPACppSTRQCPPAPPLPTPK 157
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 21536402  363 KAPT--PS--GQSIPwdlwePTESPAGSLPSGEPSAA 395
Cdd:PHA02682 158 PAPAakPIflHNQLP-----PPDYPAASCPTIETAPA 189
PHA03269 PHA03269
envelope glycoprotein C; Provisional
284-408 5.29e-04

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 42.79  E-value: 5.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  284 QPSDNAPAKGNKSPSPPDgsPAATPEIRVNHEPEPAGGATPGATlpkspSQFEaPGPFSEQASLLDLDfdplppvtsPVK 363
Cdd:PHA03269  38 QKPDPAPAPHQAASRAPD--PAVAPTSAASRKPDLAQAPTPAAS-----EKFD-PAPAPHQAASRAPD---------PAV 100
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 21536402  364 APTPSGQSIPwdlwEPTESPAGSLPSGEPSAAEGTFAVSWPSQTA 408
Cdd:PHA03269 101 APQLAAAPKP----DAAEAFTSAAQAHEAPADAGTSAASKKPDPA 141
SH3_Abi2 cd11972
Src homology 3 domain of Abl Interactor 2; Abi2 is highly expressed in the brain and eye. It ...
478-549 5.33e-04

Src homology 3 domain of Abl Interactor 2; Abi2 is highly expressed in the brain and eye. It regulates actin cytoskeletal reorganization at adherens junctions and dendritic spines, which is important in cell morphogenesis, migration, and cognitive function. Mice deficient with Abi2 show defects in orientation and migration of lens fibers, neuronal migration, dendritic spine morphology, as well as deficits in learning and memory. Abi proteins are adaptor proteins serving as binding partners and substrates of Abl tyrosine kinases. They are involved in regulating actin cytoskeletal reorganization and play important roles in membrane-ruffling, endocytosis, cell motility, and cell migration. Abi proteins contain a homeobox homology domain, a proline-rich region, and a SH3 domain. The SH3 domain of Abi binds to a PxxP motif in Abl. 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: 212905 [Multi-domain]  Cd Length: 61  Bit Score: 38.45  E-value: 5.33e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536402 478 FMFKVQAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGVkesdwnqhkeLEKCRGVFPENFTERV 549
Cdd:cd11972   1 YLEKVVAIYDYTKDKEDELSFQEGAIIYVI-----KKNDDGWYEGV----------MNGVTGLFPGNYVESI 57
SH3_ASAP cd11821
Src homology 3 domain of ArfGAP with SH3 domain, ankyrin repeat and PH domain containing ...
481-545 5.72e-04

Src homology 3 domain of ArfGAP with SH3 domain, ankyrin repeat and PH domain containing proteins; ASAPs are Arf GTPase activating proteins (GAPs) and they function in regulating cell growth, migration, and invasion. They contain an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, ankyrin (ANK) repeats, and a C-terminal SH3 domain. Vertebrates contain at least three members, ASAP1, ASAP2, and ASAP3, but some ASAP3 proteins do not seem to harbor a C-terminal SH3 domain. ASAP1 and ASAP2 show GTPase activating protein (GAP) activity towards Arf1 and Arf5. They do not show GAP activity towards Arf6, but are able to mediate Arf6 signaling by binding stably to GTP-Arf6. ASAP3 is an Arf6-specific GAP. 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: 212755 [Multi-domain]  Cd Length: 53  Bit Score: 38.06  E-value: 5.72e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGVKESDWNQhkelekcRGVFPENF 545
Cdd:cd11821   1 RVRALYDCQADNDDELTFSEGEIIVVT-----GEEDDEWWEGHIEGDPSR-------RGVFPVSF 53
SH3_ARHGEF16_26 cd11938
Src homology 3 domain of the Rho guanine nucleotide exchange factors ARHGEF16 and ARHGEF26; ...
481-547 6.04e-04

Src homology 3 domain of the Rho guanine nucleotide exchange factors ARHGEF16 and ARHGEF26; ARHGEF16, also called ephexin-4, acts as a GEF for RhoG, activating it by exchanging bound GDP for free GTP. RhoG is a small GTPase that is a crucial regulator of Rac in migrating cells. ARHGEF16 interacts directly with the ephrin receptor EphA2 and mediates cell migration and invasion in breast cancer cells by activating RhoG. ARHGEF26, also called SGEF (SH3 domain-containing guanine exchange factor), also activates RhoG. It is highly expressed in liver and may play a role in regulating membrane dynamics. ARHGEF16 and ARHGEF26 contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), and SH3 domains. The SH3 domains of ARHGEFs play an autoinhibitory role through intramolecular interactions with a proline-rich region N-terminal to the DH domain. 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: 212871  Cd Length: 55  Bit Score: 37.90  E-value: 6.04e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGVKESDwnqhkeleKCRGVFPENFTE 547
Cdd:cd11938   1 QVEIIKAYTAKQPDELSLQQADVVLVL-----QTESDGWYYGERLRD--------GERGWFPSSCAK 54
PHA03379 PHA03379
EBNA-3A; Provisional
284-434 7.62e-04

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 42.35  E-value: 7.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  284 QPSDNAPAKGN-KSPSPPDGSPAATPEIRVNH--EPEPAGGATPGATLPKSPSQFEaPGPFSeqaslldldfDPLPpvtS 360
Cdd:PHA03379 429 QSLETATSHGSaQVPEPPPVHDLEPGPLHDQHsmAPCPVAQLPPGPLQDLEPGDQL-PGVVQ----------DGRP---A 494
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  361 PVKAPTPSGQSI-PWD---LWEPTESPAGSLP---SGE----PSAAEGTFAVSWPSQTAEPGPAQPAEASEVAGGTQPAA 429
Cdd:PHA03379 495 CAPVPAPAGPIVrPWEaslSQVPGVAFAPVMPqpmPVEpvpvPTVALERPVCPAPPLIAMQGPGETSGIVRVRERWRPAP 574

                 ....*
gi 21536402  430 GAQEP 434
Cdd:PHA03379 575 WTPNP 579
SH3_DNMBP_N3 cd11796
Third N-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba; DNMBP or ...
494-545 8.02e-04

Third N-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba; DNMBP or Tuba is a cdc42-specific guanine nucleotide exchange factor (GEF) that contains four N-terminal SH3 domains, a central RhoGEF [or Dbl homology (DH)] domain followed by a Bin/Amphiphysin/Rvs (BAR) domain, and two C-terminal SH3 domains. It provides a functional link between dynamin and key regulatory proteins of the actin cytoskeleton. It plays an important role in regulating cell junction configuration. The four N-terminal SH3 domains of DNMBP binds the GTPase dynamin, which plays an important role in the fission of endocytic vesicles. 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: 212730  Cd Length: 51  Bit Score: 37.33  E-value: 8.02e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 21536402 494 DELQLKAGDVVLVIpfqnpEEQDEGWLMGvkesdwnqhkELEKCRGVFPENF 545
Cdd:cd11796  14 EELDLREGDVVTIT-----GILDKGWFRG----------ELNGRRGIFPEGF 50
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
481-520 8.39e-04

Variant 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: 429575 [Multi-domain]  Cd Length: 54  Bit Score: 37.58  E-value: 8.39e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 21536402   481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqnPEEQDEGWL 520
Cdd:pfam07653   1 YGRVIFDYVGTDKNGLTLKKGDVVKVL----GKDNDGWWE 36
SH3_STAM2 cd11963
Src homology 3 domain of Signal Transducing Adaptor Molecule 2; STAM2, also called EAST ...
481-545 8.75e-04

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: 37.69  E-value: 8.75e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGvkesdwnqhkELEKCRGVFPENF 545
Cdd:cd11963   3 KVRALYDFEAVEDNELTFKHGEIIIVL-----DDSDANWWKG----------ENHRGVGLFPSNF 52
SH3_Pex13p_fungal cd11771
Src Homology 3 domain of fungal peroxisomal membrane protein Pex13p; Pex13p, located in the ...
482-547 9.02e-04

Src Homology 3 domain of fungal peroxisomal membrane protein Pex13p; Pex13p, located in the peroxisomal membrane, contains two transmembrane regions and a C-terminal SH3 domain. It binds to the peroxisomal targeting type I (PTS1) receptor Pex5p and the docking factor Pex14p through its SH3 domain. It is essential for both PTS1 and PTS2 protein import pathways into the peroxisomal matrix. Pex13p binds Pex14p, which contains a PxxP motif, in a classical fashion to the proline-rich ligand binding site of its SH3 domain. It binds the WxxxF/Y motif of Pex5p in a novel site that does not compete with Pex14p binding. 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: 212705 [Multi-domain]  Cd Length: 60  Bit Score: 37.64  E-value: 9.02e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536402 482 VQAQHDYT-ATDTDELQLKAGDVVLVIPFQNPEEQDEGWlmgvkesdWnqhkeleKCR------GVFPENFTE 547
Cdd:cd11771   2 CRALYDFTpENPEMELSLKKGDIVAVLSKTDPLGRDSEW--------W-------KGRtrdgriGWFPSNYVE 59
SH3_Intersectin_1 cd11836
First Src homology 3 domain (or SH3A) of Intersectin; Intersectins (ITSNs) are adaptor ...
481-548 9.18e-04

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: 37.34  E-value: 9.18e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVipfqnPEEQD--EGWLMGvkesdwnqhkELEKCRGVFPENFTER 548
Cdd:cd11836   1 KYRALYAFEARNPDEISFQPGDIIQV-----DESQVaePGWLAG----------ELKGKTGWFPANYVEK 55
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
281-435 9.44e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.14  E-value: 9.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  281 VKAQPSDNAPAKGNKSPSPP---DGSPAATPEIRVNHEPEPAGGATPGATLPKSPSQFEAPGPFSEQASLLDLDFDPLP- 356
Cdd:PRK07003 372 VPARVAGAVPAPGARAAAAVgasAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPa 451
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  357 --PVTSPVKAPTPSGQSIPWDLWEPTESPAGSLPSG-----EPSAAEGTFAVSWPSQTAEPgPAQPAEASEVAGGTQPAA 429
Cdd:PRK07003 452 kaNARASADSRCDERDAQPPADSGSASAPASDAPPDaafepAPRAAAPSAATPAAVPDARA-PAAASREDAPAAAAPPAP 530

                 ....*.
gi 21536402  430 GAQEPG 435
Cdd:PRK07003 531 EARPPT 536
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
281-429 1.01e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.14  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  281 VKAQPSDNAPAKGNKSPSPPDGSPAATPEIRVnhEPEPAGGATPGATLPKSPSQFEAPGPFSEQASLLDLDFDPlppVTS 360
Cdd:PRK07003 399 VTAVTGAAGAALAPKAAAAAAATRAEAPPAAP--APPATADRGDDAADGDAPVPAKANARASADSRCDERDAQP---PAD 473
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536402  361 PVKAPTPSGQSIPWDLWEPT-----ESPAGSLPSGEPSAAEGTFAVSWPSQTAEPGPA----QPAEASEVAGGTQPAA 429
Cdd:PRK07003 474 SGSASAPASDAPPDAAFEPApraaaPSAATPAAVPDARAPAAASREDAPAAAAPPAPEarppTPAAAAPAARAGGAAA 551
SH3_ARHGEF9_like cd11828
Src homology 3 domain of ARHGEF9-like Rho guanine nucleotide exchange factors; Members of this ...
481-520 1.54e-03

Src homology 3 domain of ARHGEF9-like Rho guanine nucleotide exchange factors; Members of this family contain a SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains. They include the Rho guanine nucleotide exchange factors ARHGEF9, ASEF (also called ARHGEF4), ASEF2, and similar proteins. GEFs activate small GTPases by exchanging bound GDP for free GTP. ARHGEF9 specifically activates Cdc42, while both ASEF and ASEF2 can activate Rac1 and Cdc42. ARHGEF9 is highly expressed in the brain and it interacts with gephyrin, a postsynaptic protein associated with GABA and glycine receptors. ASEF plays a role in angiogenesis and cell migration. ASEF2 is important in cell migration and adhesion dynamics. ASEF exists in an autoinhibited form and is activated upon binding of the tumor suppressor APC (adenomatous polyposis coli), leading to the activation of Rac1 or Cdc42. In its autoinhibited form, the SH3 domain of ASEF forms an extensive interface with the DH and PH domains, blocking the Rac 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: 212762 [Multi-domain]  Cd Length: 53  Bit Score: 36.98  E-value: 1.54e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIPFQNPE------EQDEGWL 520
Cdd:cd11828   1 LAEALWDHVTMDPEELGFKAGDVIEVLDMSDKDwwwgsiRDEEGWF 46
SH3_Sla1p_3 cd11775
Third Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p; Sla1p facilitates ...
481-548 1.61e-03

Third Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p; Sla1p facilitates endocytosis by playing a role as an adaptor protein in coupling components of the actin cytoskeleton to the endocytic machinery. It interacts with Abp1p, Las17p and Pan1p, which are activator proteins of actin-related protein 2/3 (Arp2/3). Sla1p contains multiple domains including three SH3 domains, a SAM (sterile alpha motif) domain, and a Sla1 homology domain 1 (SHD1), which binds to the NPFXD motif that is found in many integral membrane proteins such as the Golgi-localized Arf-binding protein Lsb5p and the P4-ATPases, Drs2p and Dnf1p. The third SH3 domain of Sla1p can bind ubiquitin while retaining the ability to bind proline-rich ligands; monoubiquitination of target proteins signals internalization and sorting through the endocytic pathway. 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: 212709 [Multi-domain]  Cd Length: 57  Bit Score: 36.91  E-value: 1.61e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqNPEEQDEGWLmgVKESDWNQhkelekcRGVFPENFTER 548
Cdd:cd11775   2 RGKVLYDFDAQSDDELTVKEGDVVYIL---DDKKSKDWWM--VENVSTGK-------EGVVPASYIEI 57
SH3_Abi1 cd11971
Src homology 3 domain of Abl Interactor 1; Abi1, also called e3B1, is a central regulator of ...
481-549 1.71e-03

Src homology 3 domain of Abl Interactor 1; Abi1, also called e3B1, is a central regulator of actin cytoskeletal reorganization through interactions with many protein complexes. It is part of WAVE, a nucleation-promoting factor complex, that links Rac 1 activation to actin polymerization causing lamellipodia protrusion at the plasma membrane. Abi1 interact with formins to promote protrusions at the leading edge of motile cells. It also is a target of alpha4 integrin, regulating membrane protrusions at sites of integrin engagement. Abi proteins are adaptor proteins serving as binding partners and substrates of Abl tyrosine kinases. They are involved in regulating actin cytoskeletal reorganization and play important roles in membrane-ruffling, endocytosis, cell motility, and cell migration. Abi proteins contain a homeobox homology domain, a proline-rich region, and a SH3 domain. The SH3 domain of Abi binds to a PxxP motif in Abl. 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: 212904 [Multi-domain]  Cd Length: 59  Bit Score: 36.92  E-value: 1.71e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGVkesdwnqhkeLEKCRGVFPENFTERV 549
Cdd:cd11971   1 KVVAIYDYSKDKDDELSFMEGAIIYVI-----KKNDDGWYEGV----------CNGVTGLFPGNYVESI 54
SH3_Cortactin cd11959
Src homology 3 domain of Cortactin; Cortactin was originally identified as a substrate of Src ...
484-547 1.76e-03

Src homology 3 domain of Cortactin; Cortactin was originally identified as a substrate of Src kinase. It is an actin regulatory protein that binds to the Arp2/3 complex and stabilizes branched actin filaments. It is involved in cellular processes that affect cell motility, adhesion, migration, endocytosis, and invasion. It is expressed ubiquitously except in hematopoietic cells, where the homolog hematopoietic lineage cell-specific 1 (HS1) is expressed instead. Cortactin contains an N-terminal acidic domain, several copies of a repeat domain found in cortactin and HS1, a proline-rich region, and a C-terminal SH3 domain. The N-terminal region interacts with the Arp2/3 complex and F-actin, and is crucial in regulating branched actin assembly. Cortactin also serves as a scaffold and provides a bridge to the actin cytoskeleton for membrane trafficking and signaling proteins that bind to its SH3 domain. Binding partners for the SH3 domain of cortactin include dynamin2, N-WASp, MIM, FGD1, 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: 212892 [Multi-domain]  Cd Length: 53  Bit Score: 36.63  E-value: 1.76e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536402 484 AQHDYTATDTDELQLKAGDVVlvipfQNPEEQDEGWLMGVkesdwnqhkelekCR---GVFPENFTE 547
Cdd:cd11959   4 ALYDYQAADDDEISFDPDDII-----TNIEMIDEGWWRGV-------------CRgkyGLFPANYVE 52
SH3_p67phox-like_C cd11870
C-terminal Src Homology 3 domain of the p67phox subunit of NADPH oxidase and similar proteins; ...
481-547 1.85e-03

C-terminal Src Homology 3 domain of the p67phox subunit of NADPH oxidase and similar proteins; This subfamily is composed of p67phox, NADPH oxidase activator 1 (Noxa1), and similar proteins. p67phox, also called Neutrophil cytosol factor 2 (NCF-2), and Noxa1 are homologs and are the cytosolic subunits of the phagocytic (Nox2) and nonphagocytic (Nox1) NADPH oxidase complexes, respectively. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p67phox and Noxa1 play regulatory roles. p67phox contains N-terminal TPR, first SH3 (or N-terminal or central SH3), PB1, and C-terminal SH3 domains. Noxa1 has a similar domain architecture except it is lacking the N-terminal SH3 domain. The TPR domain of both binds activated GTP-bound Rac, while the C-terminal SH3 domain of p67phox and Noxa1 binds the polyproline motif found at the C-terminus of p47phox and Noxo1, respectively. 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: 212803 [Multi-domain]  Cd Length: 53  Bit Score: 36.74  E-value: 1.85e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGvkESDWNQhkelekcrGVFPENFTE 547
Cdd:cd11870   1 QVVALHRYEAQGPEDLGFREGDTIDVL-----SEVNEAWLEG--HSDGRV--------GIFPKCFVV 52
SH3_Abp1_eu cd11960
Src homology 3 domain of eumetazoan Actin-binding protein 1; Abp1, also called drebrin-like ...
481-547 2.13e-03

Src homology 3 domain of eumetazoan Actin-binding protein 1; Abp1, also called drebrin-like protein, is an adaptor protein that functions in receptor-mediated endocytosis and vesicle trafficking. It contains an N-terminal actin-binding module, the actin-depolymerizing factor (ADF) homology domain, a helical domain, and a C-terminal SH3 domain. Mammalian Abp1, unlike yeast Abp1, does not contain an acidic domain that interacts with the Arp2/3 complex. It regulates actin dynamics indirectly by interacting with dynamin and WASP family proteins. Abp1 deficiency causes abnormal organ structure and function of the spleen, heart, and lung of mice. 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: 212893 [Multi-domain]  Cd Length: 54  Bit Score: 36.61  E-value: 2.13e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGVKESDWNqhkelekcrGVFPENFTE 547
Cdd:cd11960   1 RARALYDYQAADDTEISFDPGDIITDI-----EQIDEGWWRGTGPDGTY---------GLFPANYVE 53
SH3_CD2AP_2 cd12054
Second Src Homology 3 domain (SH3B) of CD2-associated protein; CD2AP, also called CMS (Cas ...
487-549 2.40e-03

Second Src Homology 3 domain (SH3B) of CD2-associated protein; CD2AP, also called CMS (Cas ligand with Multiple SH3 domains) or METS1 (Mesenchyme-to-Epithelium Transition protein with SH3 domains), is a cytosolic adaptor protein that plays a role in regulating the cytoskeleton. It is critical in cell-to-cell union necessary for kidney function. It also stabilizes the contact between a T cell and antigen-presenting cells. It is primarily expressed in podocytes at the cytoplasmic face of the slit diaphragm and serves as a linker anchoring podocin and nephrin to the actin cytoskeleton. CD2AP contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the second SH3 domain (SH3B) of CD2AP. SH3B binds to c-Cbl in a site (TPSSRPLR is the core binding motif) distinct from the c-Cbl/SH3A 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: 212987 [Multi-domain]  Cd Length: 55  Bit Score: 36.48  E-value: 2.40e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536402 487 DYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGvkesdwnqhkELEKCRGVFPENFTERV 549
Cdd:cd12054   8 EYVPQNEDELELKVGDIIDIN-----EEVEEGWWSG----------TLNGKSGLFPSNFVKEL 55
DUF959 pfam06121
Domain of Unknown Function (DUF959); This N-terminal domain is not expressed in the 'Short' ...
278-420 2.52e-03

Domain of Unknown Function (DUF959); This N-terminal domain is not expressed in the 'Short' isoform of Collagen A.


Pssm-ID: 399255 [Multi-domain]  Cd Length: 192  Bit Score: 39.43  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402   278 TFTVKAQPSDNAPAKGNKSPS----PPDG-----SPAATPEIRVnHEPEPAGGATPGAtlPKSPSQFEAPgpfseqASLL 348
Cdd:pfam06121  28 EDTLASEPQGGLAVQPAAAPAthvaPQDDpaeqaTAAASPELPL-EELEAAPGRAPGA--PISAAAPAAL------AARP 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536402   349 DLDFDPLPPVTSPVKAPTPSGQSIP--WDLWEPTESPAGSlPSGEPSAAEGTFAVSWPSQTAE-----PGPAQPAEASE 420
Cdd:pfam06121  99 DMREENVAGVGAKILNIAQGIQSFIqlWNDAAPTESPAGA-GTLAASAPTDPLALAEPSGPAAesgtaLGPHRGALSSL 176
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
285-434 2.53e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 40.47  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  285 PSDNAPAKGNKSPSPPDGSPAATPEirVNHEPEPAGGATPGATLPKSPSQFEAPGPFSEQASLldldfdPLPPVTSPVKA 364
Cdd:PRK14951 366 PAAAAEAAAPAEKKTPARPEAAAPA--AAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPV------AAPAAAAPAAA 437
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536402  365 PTPSGQSIPwdLWEPTESPAGSLPSGEPSAAEGTFAVSWPSQTAEPGPAQ----PAEASEVAGGTQPAAGAQEP 434
Cdd:PRK14951 438 PAAAPAAVA--LAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAarltPTEEGDVWHATVQQLAAAEA 509
PHA03247 PHA03247
large tegument protein UL36; Provisional
281-502 2.57e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402   281 VKAQPSDNAPAKGNKSPSPPDGSPAATPEIRVNHEPEPAGGATPGATLPKSPSQFEAPGPFSEQASLLDLDfDPLPPVTS 360
Cdd:PHA03247  260 VVGEGADRAPETARGATGPPPPPEAAAPNGAAAPPDGVWGAALAGAPLALPAPPDPPPPAPAGDAEEEDDE-DGAMEVVS 338
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402   361 PVKAPT---PSGQSipwDLWEPTESPAGS---LPSGEPSAAEGTFAVSwpSQTAEPGPAQPAeASEVAGGTQPAAGAQEP 434
Cdd:PHA03247  339 PLPRPRqhyPLGFP---KRRRPTWTPPSSledLSAGRHHPKRASLPTR--KRRSARHAATPF-ARGPGGDDQTRPAAPVP 412
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536402   435 GETaaSEAASSSLPAVVVETfPATVNGTVEGGSGAGRldLPPGFMFKVQAQHDYTATDTDELQLKAGD 502
Cdd:PHA03247  413 ASV--PTPAPTPVPASAPPP-PATPLPSAEPGSDDGP--APPPERQPPAPATEPAPDDPDDATRKALD 475
PHA03247 PHA03247
large tegument protein UL36; Provisional
285-432 2.90e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402   285 PSDNAPAKGNKSPSPPDGSPAATPEIRVNHEPEPAGGATPGATLPKS-PSQFEAPGPFSEQASLLDLDFDPLPPVTSPVK 363
Cdd:PHA03247 2575 PRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDThAPDPPPPSPSPAANEPDPHPPPTVPPPERPRD 2654
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536402   364 APTPSGQSIPWDLWEPTESPAGSLP-------SGEPSAAEGTFAVSWPSQTAEPGPAQPAEASEVAGGTQPAAGAQ 432
Cdd:PHA03247 2655 DPAPGRVSRPRRARRLGRAAQASSPpqrprrrAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQ 2730
SH3_PACSIN1-2 cd11998
Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1) ...
481-547 2.98e-03

Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1) and PACSIN 2; PACSIN 1 or Syndapin I (Synaptic dynamin-associated protein I) is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. PACSIN 2 or Syndapin II is expressed ubiquitously and is involved in the regulation of tubulin polymerization. It associates with Golgi membranes and forms a complex with dynamin II which is crucial in promoting vesicle formation from the trans-Golgi network. PACSINs act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain and a C-terminal SH3 domain. 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: 212931 [Multi-domain]  Cd Length: 56  Bit Score: 36.08  E-value: 2.98e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqnPEEQDEGWLMGVKESDWnqhkelekcRGVFPENFTE 547
Cdd:cd11998   2 RVRALYDYDGQEQDELSFKAGDELTKL----EDEDEQGWCKGRLDSGQ---------VGLYPANYVE 55
SH3_Vinexin_3 cd11918
Third (or C-terminal) Src Homology 3 domain of Vinexin, also called Sorbin and SH3 domain ...
483-549 3.27e-03

Third (or C-terminal) Src Homology 3 domain of Vinexin, also called Sorbin and SH3 domain containing 3 (Sorbs3); Vinexin is also called Sorbs3, SH3P3, and SH3-containing adapter molecule 1 (SCAM-1). It is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. Vinexin was first identified as a vinculin binding protein; it is co-localized with vinculin at cell-ECM and cell-cell adhesion sites. There are several splice variants of vinexin: alpha, which contains the SoHo and three SH3 domains and displays tissue-specific expression; and beta, which contains only the three SH3 domains and is widely expressed. Vinexin alpha stimulates the accumulation of F-actin at focal contact sites. Vinexin also promotes keratinocyte migration and wound healing. The SH3 domains of vinexin have been reported to bind a number of ligands including vinculin, WAVE2, DLG5, Abl, and Cbl. 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: 212851 [Multi-domain]  Cd Length: 58  Bit Score: 36.09  E-value: 3.27e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536402 483 QAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGVKESdwnqhkelEKCRGVFPENFTERV 549
Cdd:cd11918   5 KAVYQYRPQNEDELELREGDRVDVM-----QQCDDGWFVGVSRR--------TQKFGTFPGNYVAPV 58
SH3_DNMBP_C2_like cd11800
Second C-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba, and ...
484-545 3.51e-03

Second C-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba, and similar domains; DNMBP or Tuba is a cdc42-specific guanine nucleotide exchange factor (GEF) that contains four N-terminal SH3 domains, a central RhoGEF [or Dbl homology (DH)] domain followed by a Bin/Amphiphysin/Rvs (BAR) domain, and two C-terminal SH3 domains. It provides a functional link between dynamin, Rho GTPase signaling, and actin dynamics. It plays an important role in regulating cell junction configuration. The C-terminal SH3 domains of DNMBP bind to N-WASP and Ena/VASP proteins, which are key regulatory proteins of the actin cytoskeleton. Also included in this subfamily is the second C-terminal SH3 domain of Rho guanine nucleotide exchange factor 37 (ARHGEF37), whose function is still unknown. 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: 212734 [Multi-domain]  Cd Length: 57  Bit Score: 35.81  E-value: 3.51e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536402 484 AQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMgvkesdwnqhkELEKCRGVFPENF 545
Cdd:cd11800   4 ALYTFEARSPGELSVTEGQVVTVLEKHDLKGNPEWWLV-----------EDRGKQGYVPSNY 54
SH3_FCHSD_2 cd11762
Second Src Homology 3 domain of FCH and double SH3 domains proteins; This group is composed of ...
482-542 3.58e-03

Second Src Homology 3 domain of FCH and double SH3 domains proteins; This group is composed of FCH and double SH3 domains protein 1 (FCHSD1) and FCHSD2. These proteins have a common domain structure consisting of an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), two SH3, and C-terminal proline-rich domains. They have only been characterized in silico and their functions remain unknown. This group also includes the insect protein, nervous wreck, which acts as a regulator of synaptic growth signaling. 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: 212696 [Multi-domain]  Cd Length: 57  Bit Score: 35.84  E-value: 3.58e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536402 482 VQAQHDYTATDTDELQLKAGDVVLVIPfQNPEEQDEGWLMGvkesdwnqhkELEKCRGVFP 542
Cdd:cd11762   2 VRALYDYEAQSDEELSFPEGAIIRILR-KDDNGVDDGWWEG----------EFNGRVGVFP 51
SH3_GRAF-like cd11882
Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase and similar ...
481-547 4.15e-03

Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase and similar proteins; This subfamily is composed of Rho GTPase activating proteins (GAPs) with similarity to GRAF. Members contain an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. Although vertebrates harbor four Rho GAPs in the GRAF subfamily including GRAF, GRAF2, GRAF3, and Oligophrenin-1 (OPHN1), only three are included in this model. OPHN1 contains the BAR, PH and GAP domains, but not the C-terminal SH3 domain. GRAF and GRAF2 show GAP activity towards RhoA and Cdc42. GRAF influences Rho-mediated cytoskeletal rearrangements and binds focal adhesion kinase. GRAF2 regulates caspase-activated p21-activated protein kinase-2. The SH3 domain of GRAF and GRAF2 binds PKNbeta, a target of the small GTPase Rho. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212815 [Multi-domain]  Cd Length: 54  Bit Score: 35.73  E-value: 4.15e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVvlvipFQNPEEQDE-GWLMGVkesdwnqhkeLEKCRGVFPENFTE 547
Cdd:cd11882   1 RARALYACKAEDESELSFEPGQI-----ITNVQPSDEpGWLEGT----------LNGRTGLIPENYVE 53
PHA03247 PHA03247
large tegument protein UL36; Provisional
280-424 5.58e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 5.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402   280 TVKAQPSDNAPAKGNKSPSPPDGSPAATP--EIRVNHEPEPAGGATPGA-TLPKSPSQFEAPGPFSEQASlLDLDFDPLP 356
Cdd:PHA03247 2723 PGPAAARQASPALPAAPAPPAVPAGPATPggPARPARPPTTAGPPAPAPpAAPAAGPPRRLTRPAVASLS-ESRESLPSP 2801
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536402   357 PVTSPVKAPTPSgqsiPWDLWEPTESPAGSLPSgePSAaegtfavswPSQTAEPGPAQPAEASEVAGG 424
Cdd:PHA03247 2802 WDPADPPAAVLA----PAAALPPAASPAGPLPP--PTS---------AQPTAPPPPPGPPPPSLPLGG 2854
PHA03264 PHA03264
envelope glycoprotein D; Provisional
297-431 5.58e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 39.22  E-value: 5.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402  297 PSPPDGSPAATPEIRVNHEPEPaGGATPGAtlPKSPSQFEAPGPfseqaslldldfDPLPPVTSPVKAPTPSgqsipwdl 376
Cdd:PHA03264 268 PAPSGGSPAPPGDDRPEAKPEP-GPVEDGA--PGRETGGEGEGP------------EPAGRDGAAGGEPKPG-------- 324
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536402  377 wEPTESPAGSLPSGepsaaegtfavsWPSQTAE----PGPAQPA--EASEVAGGTQPAAGA 431
Cdd:PHA03264 325 -PPRPAPDADRPEG------------WPSLEAItfppPTPATPAvpRARPVIVGTGIAAAA 372
SH3_Intersectin_5 cd11840
Fifth Src homology 3 domain (or SH3E) of Intersectin; Intersectins (ITSNs) are adaptor ...
481-547 6.72e-03

Fifth Src homology 3 domain (or SH3E) 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 fifth SH3 domain (or SH3E) of ITSN1 has been shown to bind many protein partners including SGIP1, Sos1, dynamin1/2, CIN85, c-Cbl, SHIP2, N-WASP, and synaptojanin-1, 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: 212774 [Multi-domain]  Cd Length: 53  Bit Score: 35.08  E-value: 6.72e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqNPEEQDegWLMGvkesdwnqhkELEKCRGVFPENFTE 547
Cdd:cd11840   1 QVIALFPYTAQNEDELSFQKGDIINVL---SKDDPD--WWRG----------ELNGQTGLFPSNYVE 52
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
284-470 7.65e-03

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 38.89  E-value: 7.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402 284 QPSDNAPAKGNKSPSPPDGSPAATPEIRVNHEPEPAGGATPGATLPKSPSQFEAPGPFSEQaslldldfDPLPPVTSPVK 363
Cdd:COG5180 318 RPPGGARDPGTPRPGQPTERPAGVPEAASDAGQPPSAYPPAEEAVPGKPLEQGAPRPGSSG--------GDGAPFQPPNG 389
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536402 364 APTPSGQSIPwDLWEPTESPAGSLPSGEPSAAEGTFAVSWPSQTAEPGPA--QPAEASEVAGGTQPAAGAQEPGETAASE 441
Cdd:COG5180 390 APQPGLGRRG-APGPPMGAGDLVQAALDGGGRETASLGGAAGGAGQGPKAdfVPGDAESVSGPAGLADQAGAAASTAMAD 468
                       170       180
                ....*....|....*....|....*....
gi 21536402 442 AASSSLPAVVVEtfPATVNGTVEGGSGAG 470
Cdd:COG5180 469 FVAPVTDATPVD--VADVLGVRPDAILGG 495
SH3_GRAP2_C cd11950
C-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS ...
482-547 8.17e-03

C-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS (GRB2-related adapter downstream of Shc), GrpL, GRB2L, Mona, or GRID (Grb2-related protein with insert domain). It is expressed specifically in the hematopoietic system. It plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. It also has roles in antigen-receptor and tyrosine kinase mediated signaling. GRAP2 is unique from other GRB2-like adaptor proteins in that it can be regulated by caspase cleavage. It contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domain of GRAP2 binds to different motifs found in substrate peptides including the typical PxxP motif in hematopoietic progenitor kinase 1 (HPK1), the RxxK motif in SLP-76 and HPK1, and the RxxxxK motif in phosphatase-like protein HD-PTP. SH3 domains are protein interaction domains that typically 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: 212883 [Multi-domain]  Cd Length: 53  Bit Score: 34.80  E-value: 8.17e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536402 482 VQAQHDYTATDTDELQLKAGDVVLVIPFQNPEeqdegWLMGvkesdwnqhkELEKCRGVFPENFTE 547
Cdd:cd11950   2 VRALYDFEALEDDELGFNSGDVIEVLDSSNPS-----WWKG----------RLHGKLGLFPANYVA 52
SH3_Nck_2 cd11766
Second Src Homology 3 domain of Nck adaptor proteins; Nck adaptor proteins regulate actin ...
481-548 9.27e-03

Second Src Homology 3 domain of Nck adaptor proteins; Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4), which show partly overlapping functions but also bind distinct targets. Their SH3 domains are involved in recruiting downstream effector molecules, such as the N-WASP/Arp2/3 complex, which when activated induces actin polymerization that results in the production of pedestals, or protrusions of the plasma membrane. The second SH3 domain of Nck appears to prefer ligands containing the APxxPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. 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: 212700 [Multi-domain]  Cd Length: 53  Bit Score: 34.55  E-value: 9.27e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536402 481 KVQAQHDYTATDTDELQLKAGDVVLVIpfqnpEEQDEGWLMGvkeSDWNQhkelekcRGVFPENFTER 548
Cdd:cd11766   1 PAVVKFNYEAQREDELSLRKGDRVLVL-----EKSSDGWWRG---ECNGQ-------VGWFPSNYVTE 53
SH3_GRB2_like_N cd11804
N-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related ...
484-519 9.74e-03

N-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related proteins; This family includes the adaptor protein GRB2 and related proteins including Drosophila melanogaster Downstream of receptor kinase (DRK), Caenorhabditis elegans Sex muscle abnormal protein 5 (Sem-5), GRB2-related adaptor protein (GRAP), GRAP2, and similar proteins. Family members contain an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. GRB2/Sem-5/DRK is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. GRAP2 plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. GRAP acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. The N-terminal SH3 domain of GRB2 binds to Sos and Sos-derived proline-rich peptides. 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: 212738 [Multi-domain]  Cd Length: 52  Bit Score: 34.64  E-value: 9.74e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 21536402 484 AQHDYTATDTDELQLKAGDVVLVIpfqnPEEQDEGW 519
Cdd:cd11804   4 AKHDFKATAEDELSFKKGSILKVL----NMEDDPNW 35
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH