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Conserved domains on  [gi|1519313032|ref|NP_061859|]
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SH3 domain and tetratricopeptide repeat-containing protein 1 isoform 1 [Homo sapiens]

Protein Classification

tetratricopeptide repeat protein( domain architecture ID 11591114)

tetratricopeptide repeat (TPR) protein may adopt a right-handed helical structure with an amphipathic channel and may function as an interaction scaffold in the formation of multi-protein complexes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SH3_SH3TC cd11885
Src Homology 3 domain of SH3 domain and tetratricopeptide repeat-containing (SH3TC) proteins ...
 309-363 5.65e-23

Src Homology 3 domain of SH3 domain and tetratricopeptide repeat-containing (SH3TC) proteins and similar domains; This subfamily is composed of vertebrate SH3TC proteins and hypothetical fungal proteins containing BAR and SH3 domains. Mammals contain two SH3TC proteins, SH3TC1 and SH3TC2. The function of SH3TC1 is unknown. SH3TC2 is localized in Schwann cells in the peripheral nervous system, where it interacts with Rab11 and plays a role in peripheral nerve myelination. Mutations in SH3TC2 are associated with Charcot-Marie-Tooth disease type 4C, a severe hereditary peripheral neuropathy with symptoms that include progressive scoliosis, delayed age of walking, muscular atrophy, distal weakness, and reduced nerve conduction velocity. 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: 212818  Cd Length: 55  Bit Score: 93.15  E-value: 5.65e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1519313032  309 LASALADFQGSGPEEMTFRGGDLIEILGAQVPSLPWCVGRHAASGRVGFVRSSLI 363
Cdd:cd11885      1 SCTAKMDFEGVEPGELSFRQGDSIEIIGDLIPGLQWFVGRSKSSGRVGFVPTNHF 55
COG3899 super family cl28481
Predicted ATPase [General function prediction only];
552-938 2.19e-03

Predicted ATPase [General function prediction only];


The actual alignment was detected with superfamily member COG3899:

Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 42.54  E-value: 2.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313032  552 KAGLLMALARLCFLLGRLCSRRLKLSQARVYFEEALGALEGSFGDLFLVvAVYANLASIYRKQKNREKCAQVVPKAMALL 631
Cdd:COG3899    697 RAGERDRAARLLLRAARRALARGAYAEALRYLERALELLPPDPEEEYRL-ALLLELAEALYLAGRFEEAEALLERALAAR 775

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313032  632 L---------GTPDHICST------------EAEGELLQLALRRAVGGQSLQAEARACFLLARHHVHLKQPEEALPFLER 690
Cdd:COG3899    776 AlaalaalrhGNPPASARAyanlgllllgdyEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLRE 855

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313032  691 LLLLHRDSGAPEAAWLSDCYLLLADIYSRkcLPHLVLSCVKVASLRTRGSLAGSLRSVNLVLQNAPQPHSLPAQTSHYLR 770
Cdd:COG3899    856 ALEAGLETGDAALALLALAAAAAAAAAAA--ALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALAL 933

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313032  771 QALASLTPGTGQALRGPLYTSLAQLYSHHGCHGPAITFMTQAVEASAIAGVRAIVDHLVALAWLHVLHGQSPVALDILQS 850
Cdd:COG3899    934 AAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAA 1013

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313032  851 VRDAVVASEDQEGVIANMVAVALKRTGRTRQAAESYYRALRVARDLGQQRNQAVGLANFGALCLHAGASRLAQHYLLEAV 930
Cdd:COG3899   1014 ALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALA 1093


                   ....*...
gi 1519313032  931 RLFSRLPL 938
Cdd:COG3899   1094 AAALAAAA 1101
TPR_12 pfam13424
Tetratricopeptide repeat;
1156-1224 3.34e-03

Tetratricopeptide repeat;


:

Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 37.75  E-value: 3.34e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519313032 1156 NKLVALLATLEEPQEGLEFAHMALALSITL--GDRLNERVAYHRLAALQHRLGHGELAEHFYLKALSLCNS 1224
Cdd:pfam13424    7 NNLAAVLRRLGRYDEALELLEKALEIARRLlgPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1063-1304 4.52e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 40.48  E-value: 4.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313032 1063 LQKKEKEAHAWLQAGKIYyilRQSELVDLYIQVAQNvaLYTGDPNLGLELFEAAGDIFFDGAWERekAVSFYRDralplA 1142
Cdd:COG2956     35 LELDPETVEAHLALGNLY---RRRGEYDRAIRIHQK--LLERDPDRAEALLELAQDYLKAGLLDR--AEELLEK-----L 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313032 1143 VTTGNRKAELRLcnKLVALLATLEEPQEGLEFAHMALALSitlgdrLNERVAYHRLAALQHRLGHGELAEHFYLKALSLC 1222
Cdd:COG2956    103 LELDPDDAEALR--LLAEIYEQEGDWEKAIEVLERLLKLG------PENAHAYCELAELYLEQGDYDEAIEALEKALKLD 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313032 1223 NSplefdeetlyYVKVYLVLGDiIFYDLKDPFDAAGYYQLALAAAVDlgnkkaQLKIYTRLATIYHNfLLDREKSLFFYQ 1302
Cdd:COG2956    175 PD----------CARALLLLAE-LYLEQGDYEEAIAALERALEQDPD------YLPALPRLAELYEK-LGDPEEALELLR 236


                   ..
gi 1519313032 1303 KA 1304
Cdd:COG2956    237 KA 238
 
Name Accession Description Interval E-value
SH3_SH3TC cd11885
Src Homology 3 domain of SH3 domain and tetratricopeptide repeat-containing (SH3TC) proteins ...
 309-363 5.65e-23

Src Homology 3 domain of SH3 domain and tetratricopeptide repeat-containing (SH3TC) proteins and similar domains; This subfamily is composed of vertebrate SH3TC proteins and hypothetical fungal proteins containing BAR and SH3 domains. Mammals contain two SH3TC proteins, SH3TC1 and SH3TC2. The function of SH3TC1 is unknown. SH3TC2 is localized in Schwann cells in the peripheral nervous system, where it interacts with Rab11 and plays a role in peripheral nerve myelination. Mutations in SH3TC2 are associated with Charcot-Marie-Tooth disease type 4C, a severe hereditary peripheral neuropathy with symptoms that include progressive scoliosis, delayed age of walking, muscular atrophy, distal weakness, and reduced nerve conduction velocity. 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: 212818  Cd Length: 55  Bit Score: 93.15  E-value: 5.65e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1519313032  309 LASALADFQGSGPEEMTFRGGDLIEILGAQVPSLPWCVGRHAASGRVGFVRSSLI 363
Cdd:cd11885      1 SCTAKMDFEGVEPGELSFRQGDSIEIIGDLIPGLQWFVGRSKSSGRVGFVPTNHF 55
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 312-361 1.09e-05

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: 44.07  E-value: 1.09e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1519313032   312 ALADFQGSGPEEMTFRGGDLIEILGAQVPSlpWCVGRHaASGRVGFVRSS 361
Cdd:smart00326    7 ALYDYTAQDPDELSFKKGDIITVLEKSDDG--WWKGRL-GRGKEGLFPSN 53
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 312-358 1.50e-03

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: 37.57  E-value: 1.50e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1519313032  312 ALADFQGSGPEEMTFRGGDLIEILgAQVPSlPWCVGRhAASGRVGFV 358
Cdd:pfam00018    2 ALYDYTAQEPDELSFKKGDIIIVL-EKSED-GWWKGR-NKGGKEGLI 45
COG3899 COG3899
Predicted ATPase [General function prediction only];
552-938 2.19e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 42.54  E-value: 2.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313032  552 KAGLLMALARLCFLLGRLCSRRLKLSQARVYFEEALGALEGSFGDLFLVvAVYANLASIYRKQKNREKCAQVVPKAMALL 631
Cdd:COG3899    697 RAGERDRAARLLLRAARRALARGAYAEALRYLERALELLPPDPEEEYRL-ALLLELAEALYLAGRFEEAEALLERALAAR 775

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313032  632 L---------GTPDHICST------------EAEGELLQLALRRAVGGQSLQAEARACFLLARHHVHLKQPEEALPFLER 690
Cdd:COG3899    776 AlaalaalrhGNPPASARAyanlgllllgdyEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLRE 855

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313032  691 LLLLHRDSGAPEAAWLSDCYLLLADIYSRkcLPHLVLSCVKVASLRTRGSLAGSLRSVNLVLQNAPQPHSLPAQTSHYLR 770
Cdd:COG3899    856 ALEAGLETGDAALALLALAAAAAAAAAAA--ALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALAL 933

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313032  771 QALASLTPGTGQALRGPLYTSLAQLYSHHGCHGPAITFMTQAVEASAIAGVRAIVDHLVALAWLHVLHGQSPVALDILQS 850
Cdd:COG3899    934 AAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAA 1013

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313032  851 VRDAVVASEDQEGVIANMVAVALKRTGRTRQAAESYYRALRVARDLGQQRNQAVGLANFGALCLHAGASRLAQHYLLEAV 930
Cdd:COG3899   1014 ALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALA 1093


                   ....*...
gi 1519313032  931 RLFSRLPL 938
Cdd:COG3899   1094 AAALAAAA 1101
TPR_12 pfam13424
Tetratricopeptide repeat;
1156-1224 3.34e-03

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 37.75  E-value: 3.34e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519313032 1156 NKLVALLATLEEPQEGLEFAHMALALSITL--GDRLNERVAYHRLAALQHRLGHGELAEHFYLKALSLCNS 1224
Cdd:pfam13424    7 NNLAAVLRRLGRYDEALELLEKALEIARRLlgPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1063-1304 4.52e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 40.48  E-value: 4.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313032 1063 LQKKEKEAHAWLQAGKIYyilRQSELVDLYIQVAQNvaLYTGDPNLGLELFEAAGDIFFDGAWERekAVSFYRDralplA 1142
Cdd:COG2956     35 LELDPETVEAHLALGNLY---RRRGEYDRAIRIHQK--LLERDPDRAEALLELAQDYLKAGLLDR--AEELLEK-----L 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313032 1143 VTTGNRKAELRLcnKLVALLATLEEPQEGLEFAHMALALSitlgdrLNERVAYHRLAALQHRLGHGELAEHFYLKALSLC 1222
Cdd:COG2956    103 LELDPDDAEALR--LLAEIYEQEGDWEKAIEVLERLLKLG------PENAHAYCELAELYLEQGDYDEAIEALEKALKLD 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313032 1223 NSplefdeetlyYVKVYLVLGDiIFYDLKDPFDAAGYYQLALAAAVDlgnkkaQLKIYTRLATIYHNfLLDREKSLFFYQ 1302
Cdd:COG2956    175 PD----------CARALLLLAE-LYLEQGDYEEAIAALERALEQDPD------YLPALPRLAELYEK-LGDPEEALELLR 236


                   ..
gi 1519313032 1303 KA 1304
Cdd:COG2956    237 KA 238
 
Name Accession Description Interval E-value
SH3_SH3TC cd11885
Src Homology 3 domain of SH3 domain and tetratricopeptide repeat-containing (SH3TC) proteins ...
 309-363 5.65e-23

Src Homology 3 domain of SH3 domain and tetratricopeptide repeat-containing (SH3TC) proteins and similar domains; This subfamily is composed of vertebrate SH3TC proteins and hypothetical fungal proteins containing BAR and SH3 domains. Mammals contain two SH3TC proteins, SH3TC1 and SH3TC2. The function of SH3TC1 is unknown. SH3TC2 is localized in Schwann cells in the peripheral nervous system, where it interacts with Rab11 and plays a role in peripheral nerve myelination. Mutations in SH3TC2 are associated with Charcot-Marie-Tooth disease type 4C, a severe hereditary peripheral neuropathy with symptoms that include progressive scoliosis, delayed age of walking, muscular atrophy, distal weakness, and reduced nerve conduction velocity. 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: 212818  Cd Length: 55  Bit Score: 93.15  E-value: 5.65e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1519313032  309 LASALADFQGSGPEEMTFRGGDLIEILGAQVPSLPWCVGRHAASGRVGFVRSSLI 363
Cdd:cd11885      1 SCTAKMDFEGVEPGELSFRQGDSIEIIGDLIPGLQWFVGRSKSSGRVGFVPTNHF 55
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 312-361 1.09e-05

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: 44.07  E-value: 1.09e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1519313032   312 ALADFQGSGPEEMTFRGGDLIEILGAQVPSlpWCVGRHaASGRVGFVRSS 361
Cdd:smart00326    7 ALYDYTAQDPDELSFKKGDIITVLEKSDDG--WWKGRL-GRGKEGLFPSN 53
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 312-358 7.83e-05

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: 41.29  E-value: 7.83e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1519313032  312 ALADFQGSGPEEMTFRGGDLIEILGAQVPSlpWCVGRHaASGRVGFV 358
Cdd:cd00174      4 ALYDYEAQDDDELSFKKGDIITVLEKDDDG--WWEGEL-NGGREGLF 47
SH3_SKAP1-like cd11866
Src Homology 3 domain of Src Kinase-Associated Phosphoprotein 1 and similar proteins; This ...
 312-358 9.01e-04

Src Homology 3 domain of Src Kinase-Associated Phosphoprotein 1 and similar proteins; This subfamily is composed of SKAP1, SKAP2, and similar proteins. SKAP1 and SKAP2 are immune cell-specific adaptor proteins that play roles in T- and B-cell adhesion, respectively, and are thus important in the migration of T- and B-cells to sites of inflammation and for movement during T-cell conjugation with antigen-presenting cells. Both SKAP1 and SKAP2 bind to ADAP (adhesion and degranulation-promoting adaptor protein), among many other binding partners. They contain a pleckstrin homology (PH) domain, a C-terminal SH3 domain, and several tyrosine phosphorylation sites. The SH3 domain of SKAP1 is necessary for its ability to regulate T-cell conjugation with antigen-presenting cells and the formation of LFA-1 clusters. SKAP1 binds primarily to a proline-rich region of ADAP through its SH3 domain; its degradation is regulated by ADAP. A secondary interaction occurs via the ADAP SH3 domain and the RKxxYxxY motif in SKAP1. 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: 212800  Cd Length: 53  Bit Score: 38.57  E-value: 9.01e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1519313032  312 ALADFQGSGPEEMTFRGGDLIEILGAQVPSLPWCVGRhaASGRVGFV 358
Cdd:cd11866      4 GLWDCSGNEPDELSFKRGDLIYIISKEYDSFGWWVGE--LNGKVGLV 48
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 312-358 1.50e-03

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: 37.57  E-value: 1.50e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1519313032  312 ALADFQGSGPEEMTFRGGDLIEILgAQVPSlPWCVGRhAASGRVGFV 358
Cdd:pfam00018    2 ALYDYTAQEPDELSFKKGDIIIVL-EKSED-GWWKGR-NKGGKEGLI 45
SH3_SH3YL1_like cd11841
Src homology 3 domain of SH3 domain containing Ysc84-like 1 (SH3YL1) protein; SH3YL1 localizes ...
 310-356 1.75e-03

Src homology 3 domain of SH3 domain containing Ysc84-like 1 (SH3YL1) protein; SH3YL1 localizes to the plasma membrane and is required for dorsal ruffle formation. It binds phosphoinositides (PIs) with high affinity through its N-terminal SYLF domain (also called DUF500). In addition, SH3YL1 contains a C-terminal SH3 domain which has been reported to bind to N-WASP, dynamin 2, and SHIP2 (a PI 5-phosphatase). 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: 212775  Cd Length: 54  Bit Score: 37.76  E-value: 1.75e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1519313032  310 ASALADFQGSGPEEMTFRGGDLIEILGAQVPSLPWCVGRHaaSGRVG 356
Cdd:cd11841      2 VTALYSFEGQQPCDLSFQAGDRITVLTRTDSQFDWWEGRL--RGRVG 46
COG3899 COG3899
Predicted ATPase [General function prediction only];
552-938 2.19e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 42.54  E-value: 2.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313032  552 KAGLLMALARLCFLLGRLCSRRLKLSQARVYFEEALGALEGSFGDLFLVvAVYANLASIYRKQKNREKCAQVVPKAMALL 631
Cdd:COG3899    697 RAGERDRAARLLLRAARRALARGAYAEALRYLERALELLPPDPEEEYRL-ALLLELAEALYLAGRFEEAEALLERALAAR 775

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313032  632 L---------GTPDHICST------------EAEGELLQLALRRAVGGQSLQAEARACFLLARHHVHLKQPEEALPFLER 690
Cdd:COG3899    776 AlaalaalrhGNPPASARAyanlgllllgdyEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLRE 855

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313032  691 LLLLHRDSGAPEAAWLSDCYLLLADIYSRkcLPHLVLSCVKVASLRTRGSLAGSLRSVNLVLQNAPQPHSLPAQTSHYLR 770
Cdd:COG3899    856 ALEAGLETGDAALALLALAAAAAAAAAAA--ALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALAL 933

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313032  771 QALASLTPGTGQALRGPLYTSLAQLYSHHGCHGPAITFMTQAVEASAIAGVRAIVDHLVALAWLHVLHGQSPVALDILQS 850
Cdd:COG3899    934 AAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAA 1013

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313032  851 VRDAVVASEDQEGVIANMVAVALKRTGRTRQAAESYYRALRVARDLGQQRNQAVGLANFGALCLHAGASRLAQHYLLEAV 930
Cdd:COG3899   1014 ALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALA 1093


                   ....*...
gi 1519313032  931 RLFSRLPL 938
Cdd:COG3899   1094 AAALAAAA 1101
SH3_GRAP_C cd11951
C-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor ...
 310-357 2.43e-03

C-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor protein that is highly expressed in lymphoid tissues. It acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. It has been identified as a regulator of TGFbeta signaling in diabetic kidney tubules and may have a role in the pathogenesis of the disease. GRAP contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domains (SH3c) of the related proteins, 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: 212884  Cd Length: 53  Bit Score: 37.47  E-value: 2.43e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1519313032  310 ASALADFQGSGPEEMTFRGGDLIEILGAQVPSlpWCVGRhaASGRVGF 357
Cdd:cd11951      2 VQAQYDFSAEDPSQLSFRRGDIIEVLDCPDPN--WWRGR--ISGRVGF 45
TPR_12 pfam13424
Tetratricopeptide repeat;
1156-1224 3.34e-03

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 37.75  E-value: 3.34e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519313032 1156 NKLVALLATLEEPQEGLEFAHMALALSITL--GDRLNERVAYHRLAALQHRLGHGELAEHFYLKALSLCNS 1224
Cdd:pfam13424    7 NNLAAVLRRLGRYDEALELLEKALEIARRLlgPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1063-1304 4.52e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 40.48  E-value: 4.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313032 1063 LQKKEKEAHAWLQAGKIYyilRQSELVDLYIQVAQNvaLYTGDPNLGLELFEAAGDIFFDGAWERekAVSFYRDralplA 1142
Cdd:COG2956     35 LELDPETVEAHLALGNLY---RRRGEYDRAIRIHQK--LLERDPDRAEALLELAQDYLKAGLLDR--AEELLEK-----L 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313032 1143 VTTGNRKAELRLcnKLVALLATLEEPQEGLEFAHMALALSitlgdrLNERVAYHRLAALQHRLGHGELAEHFYLKALSLC 1222
Cdd:COG2956    103 LELDPDDAEALR--LLAEIYEQEGDWEKAIEVLERLLKLG------PENAHAYCELAELYLEQGDYDEAIEALEKALKLD 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519313032 1223 NSplefdeetlyYVKVYLVLGDiIFYDLKDPFDAAGYYQLALAAAVDlgnkkaQLKIYTRLATIYHNfLLDREKSLFFYQ 1302
Cdd:COG2956    175 PD----------CARALLLLAE-LYLEQGDYEEAIAALERALEQDPD------YLPALPRLAELYEK-LGDPEEALELLR 236


                   ..
gi 1519313032 1303 KA 1304
Cdd:COG2956    237 KA 238
SH3_EFS cd12003
Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding protein family member, ...
 309-358 4.89e-03

Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding protein family member, Embryonal Fyn-associated Substrate; EFS is also called HEFS, CASS3 (Cas scaffolding protein family member 3) or SIN (Src-interacting protein). It was identified based on interactions with the Src kinases, Fyn and Yes. It plays a role in thymocyte development and acts as a negative regulator of T cell proliferation. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes. They share a common domain structure that includes an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain. The SH3 domain of CAS proteins binds to diverse partners including FAK, FRNK, Pyk2, PTP-PEST, DOCK180, 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: 212936  Cd Length: 62  Bit Score: 36.79  E-value: 4.89e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1519313032  309 LASALADFQGSGPEEMTFRGGDLIEILGAQVPSLP-WCvgRHAASGRVGFV 358
Cdd:cd12003      2 LAKALYDNAAESPEELSFRRGDVLMVLKREHGSLPgWW--LCSLHGQQGIA 50
SH3_GRAP2_C cd11950
C-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS ...
 310-356 6.03e-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: 36.34  E-value: 6.03e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1519313032  310 ASALADFQGSGPEEMTFRGGDLIEILGAQVPSlpWCVGRhaASGRVG 356
Cdd:cd11950      2 VRALYDFEALEDDELGFNSGDVIEVLDSSNPS--WWKGR--LHGKLG 44
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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