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Conserved domains on  [gi|148368971|ref|NP_919325|]
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SH3 domain and tetratricopeptide repeat-containing protein 1 [Mus musculus]

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 ...
 313-367 7.60e-20

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: 84.29  E-value: 7.60e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 148368971  313 LASAIADFQGSGPEEMSFSVGDVIEILGAQVPGLPWCVGRHMASGQVGFVRTGLV 367
Cdd:cd11885     1 SCTAKMDFEGVEPGELSFRQGDSIEIIGDLIPGLQWFVGRSKSSGRVGFVPTNHF 55
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 667-901 1.10e-04

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: 45.49  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971  667 EARACFLLARHYTHLKQPEEALPYLERLLRLNRDAgspqaswpEDCYLLLADIYGRKCLPHLALSCLRvsslwtrcslpg 746
Cdd:COG2956    75 RAEALLELAQDYLKAGLLDRAEELLEKLLELDPDD--------AEALRLLAEIYEQEGDWEKAIEVLE------------ 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971  747 slrsvdlvlqnvpgpnsqrRAGHSLPSQIAYYLRQALASLAPG-TGQALR------------GPLYASLAQLYSHHQQYS 813
Cdd:COG2956   135 -------------------RLLKLGPENAHAYCELAELYLEQGdYDEAIEalekalkldpdcARALLLLAELYLEQGDYE 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971  814 QAIAFMSQAAEADTAAGVHpvvdrLVALAWLHMLCGNSLVAMDILKcisdaAVANKDQECVMMNMVAMALKRMGRTRQAA 893
Cdd:COG2956   196 EAIAALERALEQDPDYLPA-----LPRLAELYEKLGDPEEALELLR-----KALELDPSDDLLLALADLLERKEGLEAAL 265


                  ....*...
gi 148368971  894 EGYFRALH 901
Cdd:COG2956   266 ALLERQLR 273
TPR_12 pfam13424
Tetratricopeptide repeat;
1166-1231 5.86e-04

Tetratricopeptide repeat;


:

Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 39.68  E-value: 5.86e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148368971  1166 NKLVALLSALEAPQEGLEFAHEALALSITL--GDRLNERVAYHRLATLHHRLGHGELAEHFFLKALSL 1231
Cdd:pfam13424    7 NNLAAVLRRLGRYDEALELLEKALEIARRLlgPDHPLTATTLLNLGRLYLELGRYEEALELLERALAL 74
 
Name Accession Description Interval E-value
SH3_SH3TC cd11885
Src Homology 3 domain of SH3 domain and tetratricopeptide repeat-containing (SH3TC) proteins ...
 313-367 7.60e-20

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: 84.29  E-value: 7.60e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 148368971  313 LASAIADFQGSGPEEMSFSVGDVIEILGAQVPGLPWCVGRHMASGQVGFVRTGLV 367
Cdd:cd11885     1 SCTAKMDFEGVEPGELSFRQGDSIEIIGDLIPGLQWFVGRSKSSGRVGFVPTNHF 55
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 316-362 5.64e-08

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: 50.61  E-value: 5.64e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 148368971    316 AIADFQGSGPEEMSFSVGDVIEILGAQVPGlpWCVGRHMaSGQVGFV 362
Cdd:smart00326    7 ALYDYTAQDPDELSFKKGDIITVLEKSDDG--WWKGRLG-RGKEGLF 50
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 316-362 2.22e-05

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: 42.96  E-value: 2.22e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 148368971   316 AIADFQGSGPEEMSFSVGDVIEILGAQVPGlpWCVGRhMASGQVGFV 362
Cdd:pfam00018    2 ALYDYTAQEPDELSFKKGDIIIVLEKSEDG--WWKGR-NKGGKEGLI 45
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 667-901 1.10e-04

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: 45.49  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971  667 EARACFLLARHYTHLKQPEEALPYLERLLRLNRDAgspqaswpEDCYLLLADIYGRKCLPHLALSCLRvsslwtrcslpg 746
Cdd:COG2956    75 RAEALLELAQDYLKAGLLDRAEELLEKLLELDPDD--------AEALRLLAEIYEQEGDWEKAIEVLE------------ 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971  747 slrsvdlvlqnvpgpnsqrRAGHSLPSQIAYYLRQALASLAPG-TGQALR------------GPLYASLAQLYSHHQQYS 813
Cdd:COG2956   135 -------------------RLLKLGPENAHAYCELAELYLEQGdYDEAIEalekalkldpdcARALLLLAELYLEQGDYE 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971  814 QAIAFMSQAAEADTAAGVHpvvdrLVALAWLHMLCGNSLVAMDILKcisdaAVANKDQECVMMNMVAMALKRMGRTRQAA 893
Cdd:COG2956   196 EAIAALERALEQDPDYLPA-----LPRLAELYEKLGDPEEALELLR-----KALELDPSDDLLLALADLLERKEGLEAAL 265


                  ....*...
gi 148368971  894 EGYFRALH 901
Cdd:COG2956   266 ALLERQLR 273
TPR_12 pfam13424
Tetratricopeptide repeat;
1166-1231 5.86e-04

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 39.68  E-value: 5.86e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148368971  1166 NKLVALLSALEAPQEGLEFAHEALALSITL--GDRLNERVAYHRLATLHHRLGHGELAEHFFLKALSL 1231
Cdd:pfam13424    7 NNLAAVLRRLGRYDEALELLEKALEIARRLlgPDHPLTATTLLNLGRLYLELGRYEEALELLERALAL 74
COG3899 COG3899
Predicted ATPase [General function prediction only];
657-1213 1.20e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 43.31  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971  657 RVICGLSPQAEARACFLLARHYTHLKQPEEALPYLERLLRLNRDAGSPQASwpEDCYLLLADIYGRKCLPH--LALSCLR 734
Cdd:COG3899   674 RALEARGPEPLEERLFELAHHLNRAGERDRAARLLLRAARRALARGAYAEA--LRYLERALELLPPDPEEEyrLALLLEL 751

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971  735 VSSLWTRCSLPGSLRSVDLVLQ-NVPGPNSQRRAGHSLPSQIAY----------------YLRQALASLAPGTGQALRGP 797
Cdd:COG3899   752 AEALYLAGRFEEAEALLERALAaRALAALAALRHGNPPASARAYanlgllllgdyeeayeFGELALALAERLGDRRLEAR 831

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971  798 LYASLAQLYSHHQQYSQAIAFMSQAAEADTAAGVHPVVDRLVALAWLHMLCGNSL--VAMDILKCISDAAVANKDQECVM 875
Cdd:COG3899   832 ALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALaaAAAAAARLLAAAAAALAAAAAAA 911

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971  876 MNMVAMALKRMGRTRQAAEGYFRALHMAYAQGHLQSQAVVLANFGALCLQAGARSLAQHYLREAVGLFSQvpsgvCGRDF 955
Cdd:COG3899   912 ALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAA-----AAAAA 986

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971  956 TQVLLWLGQLCTRRALPQQAKCYYEWAFLVAVETDHLESQLQAVQKLCLFYSKVMPNEVRCVIYHEFQLALARKTANKVL 1035
Cdd:COG3899   987 AAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAA 1066

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971 1036 EGQLLEAISQLYLSLGTERAYKSALDYTKRSLGIFIDLQQKEKEARAWLQAGKIYYILRQNELVDLYIQVAQNAALYTGD 1115
Cdd:COG3899  1067 ALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALAL 1146

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971 1116 PKLGLELFEAAGDIFFNGTWEREKAVSFYRDRALPLAVTVGDQEVELRLCNKLVALLSALEAPQEGLEFAHEALALSITL 1195
Cdd:COG3899  1147 AALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLL 1226

                         570
                  ....*....|....*...
gi 148368971 1196 GDRLNERVAYHRLATLHH 1213
Cdd:COG3899  1227 LLAALALAAALLALRLLA 1244
TPR_12 pfam13424
Tetratricopeptide repeat;
673-734 4.83e-03

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 37.37  E-value: 4.83e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148368971   673 LLARHYTHLKQPEEALPYLERLLRLNRDAGSPQASWPEDCYLLLADIYGRKCLPHLALSCLR 734
Cdd:pfam13424    8 NLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLE 69
 
Name Accession Description Interval E-value
SH3_SH3TC cd11885
Src Homology 3 domain of SH3 domain and tetratricopeptide repeat-containing (SH3TC) proteins ...
 313-367 7.60e-20

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: 84.29  E-value: 7.60e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 148368971  313 LASAIADFQGSGPEEMSFSVGDVIEILGAQVPGLPWCVGRHMASGQVGFVRTGLV 367
Cdd:cd11885     1 SCTAKMDFEGVEPGELSFRQGDSIEIIGDLIPGLQWFVGRSKSSGRVGFVPTNHF 55
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 316-362 5.64e-08

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: 50.61  E-value: 5.64e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 148368971    316 AIADFQGSGPEEMSFSVGDVIEILGAQVPGlpWCVGRHMaSGQVGFV 362
Cdd:smart00326    7 ALYDYTAQDPDELSFKKGDIITVLEKSDDG--WWKGRLG-RGKEGLF 50
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 316-362 3.05e-07

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: 48.23  E-value: 3.05e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 148368971  316 AIADFQGSGPEEMSFSVGDVIEILGAQVPGlpWCVGRHmASGQVGFV 362
Cdd:cd00174     4 ALYDYEAQDDDELSFKKGDIITVLEKDDDG--WWEGEL-NGGREGLF 47
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 316-362 2.22e-05

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: 42.96  E-value: 2.22e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 148368971   316 AIADFQGSGPEEMSFSVGDVIEILGAQVPGlpWCVGRhMASGQVGFV 362
Cdd:pfam00018    2 ALYDYTAQEPDELSFKKGDIIIVLEKSEDG--WWKGR-NKGGKEGLI 45
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 667-901 1.10e-04

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: 45.49  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971  667 EARACFLLARHYTHLKQPEEALPYLERLLRLNRDAgspqaswpEDCYLLLADIYGRKCLPHLALSCLRvsslwtrcslpg 746
Cdd:COG2956    75 RAEALLELAQDYLKAGLLDRAEELLEKLLELDPDD--------AEALRLLAEIYEQEGDWEKAIEVLE------------ 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971  747 slrsvdlvlqnvpgpnsqrRAGHSLPSQIAYYLRQALASLAPG-TGQALR------------GPLYASLAQLYSHHQQYS 813
Cdd:COG2956   135 -------------------RLLKLGPENAHAYCELAELYLEQGdYDEAIEalekalkldpdcARALLLLAELYLEQGDYE 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971  814 QAIAFMSQAAEADTAAGVHpvvdrLVALAWLHMLCGNSLVAMDILKcisdaAVANKDQECVMMNMVAMALKRMGRTRQAA 893
Cdd:COG2956   196 EAIAALERALEQDPDYLPA-----LPRLAELYEKLGDPEEALELLR-----KALELDPSDDLLLALADLLERKEGLEAAL 265


                  ....*...
gi 148368971  894 EGYFRALH 901
Cdd:COG2956   266 ALLERQLR 273
TPR_12 pfam13424
Tetratricopeptide repeat;
1166-1231 5.86e-04

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 39.68  E-value: 5.86e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148368971  1166 NKLVALLSALEAPQEGLEFAHEALALSITL--GDRLNERVAYHRLATLHHRLGHGELAEHFFLKALSL 1231
Cdd:pfam13424    7 NNLAAVLRRLGRYDEALELLEKALEIARRLlgPDHPLTATTLLNLGRLYLELGRYEEALELLERALAL 74
COG3899 COG3899
Predicted ATPase [General function prediction only];
657-1213 1.20e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 43.31  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971  657 RVICGLSPQAEARACFLLARHYTHLKQPEEALPYLERLLRLNRDAGSPQASwpEDCYLLLADIYGRKCLPH--LALSCLR 734
Cdd:COG3899   674 RALEARGPEPLEERLFELAHHLNRAGERDRAARLLLRAARRALARGAYAEA--LRYLERALELLPPDPEEEyrLALLLEL 751

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971  735 VSSLWTRCSLPGSLRSVDLVLQ-NVPGPNSQRRAGHSLPSQIAY----------------YLRQALASLAPGTGQALRGP 797
Cdd:COG3899   752 AEALYLAGRFEEAEALLERALAaRALAALAALRHGNPPASARAYanlgllllgdyeeayeFGELALALAERLGDRRLEAR 831

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971  798 LYASLAQLYSHHQQYSQAIAFMSQAAEADTAAGVHPVVDRLVALAWLHMLCGNSL--VAMDILKCISDAAVANKDQECVM 875
Cdd:COG3899   832 ALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALaaAAAAAARLLAAAAAALAAAAAAA 911

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971  876 MNMVAMALKRMGRTRQAAEGYFRALHMAYAQGHLQSQAVVLANFGALCLQAGARSLAQHYLREAVGLFSQvpsgvCGRDF 955
Cdd:COG3899   912 ALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAA-----AAAAA 986

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971  956 TQVLLWLGQLCTRRALPQQAKCYYEWAFLVAVETDHLESQLQAVQKLCLFYSKVMPNEVRCVIYHEFQLALARKTANKVL 1035
Cdd:COG3899   987 AAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAA 1066

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971 1036 EGQLLEAISQLYLSLGTERAYKSALDYTKRSLGIFIDLQQKEKEARAWLQAGKIYYILRQNELVDLYIQVAQNAALYTGD 1115
Cdd:COG3899  1067 ALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALAL 1146

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971 1116 PKLGLELFEAAGDIFFNGTWEREKAVSFYRDRALPLAVTVGDQEVELRLCNKLVALLSALEAPQEGLEFAHEALALSITL 1195
Cdd:COG3899  1147 AALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLL 1226

                         570
                  ....*....|....*...
gi 148368971 1196 GDRLNERVAYHRLATLHH 1213
Cdd:COG3899  1227 LLAALALAAALLALRLLA 1244
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
778-939 2.69e-03

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 41.15  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971  778 YLRQALAsLAPGTGQAlrgplYASLAQLYSHHQQYSQAIAFMSQAAEADTAagvhpVVDRLVALAWLHMLCGNSLVAMDI 857
Cdd:COG0457    30 DYEKALE-LDPDDAEA-----LYNLGLAYLRLGRYEEALADYEQALELDPD-----DAEALNNLGLALQALGRYEEALED 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971  858 LkcisDAAVANKDQECVMMNMVAMALKRMGRTRQAAEGYFRALHMAyaqghlQSQAVVLANFGALCLQAGARSLAQHYLR 937
Cdd:COG0457    99 Y----DKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELD------PDDADALYNLGIALEKLGRYEEALELLE 168


                  ..
gi 148368971  938 EA 939
Cdd:COG0457   169 KL 170
SH3_SH3YL1_like cd11841
Src homology 3 domain of SH3 domain containing Ysc84-like 1 (SH3YL1) protein; SH3YL1 localizes ...
 314-360 3.76e-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: 36.99  E-value: 3.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 148368971  314 ASAIADFQGSGPEEMSFSVGDVIEILGAQVPGLPWCVGRHmaSGQVG 360
Cdd:cd11841     2 VTALYSFEGQQPCDLSFQAGDRITVLTRTDSQFDWWEGRL--RGRVG 46
TPR_12 pfam13424
Tetratricopeptide repeat;
673-734 4.83e-03

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 37.37  E-value: 4.83e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148368971   673 LLARHYTHLKQPEEALPYLERLLRLNRDAGSPQASWPEDCYLLLADIYGRKCLPHLALSCLR 734
Cdd:pfam13424    8 NLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLE 69
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 632-826 5.50e-03

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 41.13  E-value: 5.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971  632 AAALLLGTPGHSCNADAELLKYALRRVICGLSPQAEARACFLLARHYTHLKQPEEALPYLERLLRLNRDagSPQAswped 711
Cdd:COG3914    42 GLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNPD--NAEA----- 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148368971  712 cYLLLADIYGRKCLPHLALSCLRvsslwtrcslpgslRSVDLVLQNVPGPNSQRRAGHSL--PSQIAYYLRQALAsLAPG 789
Cdd:COG3914   115 -LFNLGNLLLALGRLEEALAALR--------------RALALNPDFAEAYLNLGEALRRLgrLEEAIAALRRALE-LDPD 178

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 148368971  790 TGQALRgplyaSLAQLYSHHQQYSQAIAFMSQAAEAD 826
Cdd:COG3914   179 NAEALN-----NLGNALQDLGRLEEAIAAYRRALELD 210
SH3_BOI cd11886
Src Homology 3 domain of fungal BOI-like proteins; This subfamily includes the Saccharomyces ...
 315-360 6.85e-03

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: 36.16  E-value: 6.85e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 148368971  315 SAIADFQGSGPEEMSFSVGDVIEIL--------GaqvpglpWCVGRHMASGQVG 360
Cdd:cd11886     3 IVIHDFNARSEDELTLKPGDKIELIeddeefgdG-------WYLGRNLRTGETG 49
TPR_2 pfam07719
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ...
 668-700 8.33e-03

Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by pfam00515.


Pssm-ID: 429619 [Multi-domain]  Cd Length: 33  Bit Score: 35.19  E-value: 8.33e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 148368971   668 ARACFLLARHYTHLKQPEEALPYLERLLRLNRD 700
Cdd:pfam07719    1 AEALYNLGLAYYKLGDYEEALEAYEKALELDPN 33
 
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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