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Conserved domains on  [gi|1958676061|ref|XP_038947889|]
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SH3 domain and tetratricopeptide repeat-containing protein 1 isoform X4 [Rattus norvegicus]

Protein Classification

tetratricopeptide repeat protein( domain architecture ID 11683153)

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 super family cl17036
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
312-366 1.08e-18

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


The actual alignment was detected with superfamily member cd11885:

Pssm-ID: 473055  Cd Length: 55  Bit Score: 80.44  E-value: 1.08e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958676061  312 LASAIADFQGSGPEEMSFSVGDVIEIVGAQVPGLPWCLGQHMASGQVGFVRTGLV 366
Cdd:cd11885      1 SCTAKMDFEGVEPGELSFRQGDSIEIIGDLIPGLQWFVGRSKSSGRVGFVPTNHF 55
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
666-900 2.46e-05

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: 47.42  E-value: 2.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676061  666 EARACFLLARHYTHLKQPEEALPYLERLLRLNRDVgtpqaswpEDCYLLLADIYGRKCLPHLALSCLK------VSSLWT 739
Cdd:COG2956     75 RAEALLELAQDYLKAGLLDRAEELLEKLLELDPDD--------AEALRLLAEIYEQEGDWEKAIEVLErllklgPENAHA 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676061  740 RCSLAgslrsvdlvlqnapgpnsQRSTGHSLPSQIAHYLRQALASLPpgtgQTLRgpLYASLAQLYSYHQQYGQAIAFMS 819
Cdd:COG2956    147 YCELA------------------ELYLEQGDYDEAIEALEKALKLDP----DCAR--ALLLLAELYLEQGDYEEAIAALE 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676061  820 QAAEADTAAGVHpvvdrLVALAWLHLLCGKSLVAMDILKcvsdaAVANKDQECVMMNMVAMALKRMGRTRQAAEGYFRAL 899
Cdd:COG2956    203 RALEQDPDYLPA-----LPRLAELYEKLGDPEEALELLR-----KALELDPSDDLLLALADLLERKEGLEAALALLERQL 272

                   .
gi 1958676061  900 H 900
Cdd:COG2956    273 R 273
TPR super family cl33886
Tetratricopeptide (TPR) repeat [General function prediction only];
798-1047 4.52e-03

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


The actual alignment was detected with superfamily member COG0457:

Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 39.99  E-value: 4.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676061  798 YASLAQLYSYHQQYGQAIAFMSQAAEADTAagvhpVVDRLVALAWLHLLCGKSLVAMDILkcvsDAAVANKDQECVMMNM 877
Cdd:COG0457     11 YNNLGLAYRRLGRYEEAIEDYEKALELDPD-----DAEALYNLGLAYLRLGRYEEALADY----EQALELDPDDAEALNN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676061  878 VAMALKRMGRTRQAAEGYFRALHMAYsqghlqSQAVVLANFGALCLQAGARSLAQHYLREAVGLFSqlpsgvcgrDFTQV 957
Cdd:COG0457     82 LGLALQALGRYEEALEDYDKALELDP------DDAEALYNLGLALLELGRYDEAIEAYERALELDP---------DDADA 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676061  958 LLWLGQLCTRRTLPQQAKCYYEWAFLVAVETDHLESQLQAVQKLCHFYSKVMPNEVRCVIYHEFQLALARKTADKVLEGQ 1037
Cdd:COG0457    147 LYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLA 226
                          250
                   ....*....|
gi 1958676061 1038 LLEAISQLYL 1047
Cdd:COG0457    227 LALLLALRLA 236
 
Name Accession Description Interval E-value
SH3_SH3TC cd11885
Src Homology 3 domain of SH3 domain and tetratricopeptide repeat-containing (SH3TC) proteins ...
312-366 1.08e-18

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: 80.44  E-value: 1.08e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958676061  312 LASAIADFQGSGPEEMSFSVGDVIEIVGAQVPGLPWCLGQHMASGQVGFVRTGLV 366
Cdd:cd11885      1 SCTAKMDFEGVEPGELSFRQGDSIEIIGDLIPGLQWFVGRSKSSGRVGFVPTNHF 55
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
315-361 2.29e-07

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: 48.30  E-value: 2.29e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1958676061   315 AIADFQGSGPEEMSFSVGDVIEIVGAQVPGlpWCLGQHMaSGQVGFV 361
Cdd:smart00326    7 ALYDYTAQDPDELSFKKGDIITVLEKSDDG--WWKGRLG-RGKEGLF 50
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
666-900 2.46e-05

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: 47.42  E-value: 2.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676061  666 EARACFLLARHYTHLKQPEEALPYLERLLRLNRDVgtpqaswpEDCYLLLADIYGRKCLPHLALSCLK------VSSLWT 739
Cdd:COG2956     75 RAEALLELAQDYLKAGLLDRAEELLEKLLELDPDD--------AEALRLLAEIYEQEGDWEKAIEVLErllklgPENAHA 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676061  740 RCSLAgslrsvdlvlqnapgpnsQRSTGHSLPSQIAHYLRQALASLPpgtgQTLRgpLYASLAQLYSYHQQYGQAIAFMS 819
Cdd:COG2956    147 YCELA------------------ELYLEQGDYDEAIEALEKALKLDP----DCAR--ALLLLAELYLEQGDYEEAIAALE 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676061  820 QAAEADTAAGVHpvvdrLVALAWLHLLCGKSLVAMDILKcvsdaAVANKDQECVMMNMVAMALKRMGRTRQAAEGYFRAL 899
Cdd:COG2956    203 RALEQDPDYLPA-----LPRLAELYEKLGDPEEALELLR-----KALELDPSDDLLLALADLLERKEGLEAALALLERQL 272

                   .
gi 1958676061  900 H 900
Cdd:COG2956    273 R 273
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
315-361 4.57e-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: 41.81  E-value: 4.57e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958676061  315 AIADFQGSGPEEMSFSVGDVIEIVGAQVPGlpWCLGQhMASGQVGFV 361
Cdd:pfam00018    2 ALYDYTAQEPDELSFKKGDIIIVLEKSEDG--WWKGR-NKGGKEGLI 45
TPR_12 pfam13424
Tetratricopeptide repeat;
672-733 1.12e-03

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 38.91  E-value: 1.12e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958676061  672 LLARHYTHLKQPEEALPYLERLLRLNRDVGTPQASWPEDCYLLLADIYGRKCLPHLALSCLK 733
Cdd:pfam13424    8 NLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLE 69
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
798-1047 4.52e-03

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 39.99  E-value: 4.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676061  798 YASLAQLYSYHQQYGQAIAFMSQAAEADTAagvhpVVDRLVALAWLHLLCGKSLVAMDILkcvsDAAVANKDQECVMMNM 877
Cdd:COG0457     11 YNNLGLAYRRLGRYEEAIEDYEKALELDPD-----DAEALYNLGLAYLRLGRYEEALADY----EQALELDPDDAEALNN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676061  878 VAMALKRMGRTRQAAEGYFRALHMAYsqghlqSQAVVLANFGALCLQAGARSLAQHYLREAVGLFSqlpsgvcgrDFTQV 957
Cdd:COG0457     82 LGLALQALGRYEEALEDYDKALELDP------DDAEALYNLGLALLELGRYDEAIEAYERALELDP---------DDADA 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676061  958 LLWLGQLCTRRTLPQQAKCYYEWAFLVAVETDHLESQLQAVQKLCHFYSKVMPNEVRCVIYHEFQLALARKTADKVLEGQ 1037
Cdd:COG0457    147 LYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLA 226
                          250
                   ....*....|
gi 1958676061 1038 LLEAISQLYL 1047
Cdd:COG0457    227 LALLLALRLA 236
 
Name Accession Description Interval E-value
SH3_SH3TC cd11885
Src Homology 3 domain of SH3 domain and tetratricopeptide repeat-containing (SH3TC) proteins ...
312-366 1.08e-18

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: 80.44  E-value: 1.08e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958676061  312 LASAIADFQGSGPEEMSFSVGDVIEIVGAQVPGLPWCLGQHMASGQVGFVRTGLV 366
Cdd:cd11885      1 SCTAKMDFEGVEPGELSFRQGDSIEIIGDLIPGLQWFVGRSKSSGRVGFVPTNHF 55
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
315-361 2.29e-07

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: 48.30  E-value: 2.29e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1958676061   315 AIADFQGSGPEEMSFSVGDVIEIVGAQVPGlpWCLGQHMaSGQVGFV 361
Cdd:smart00326    7 ALYDYTAQDPDELSFKKGDIITVLEKSDDG--WWKGRLG-RGKEGLF 50
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
315-361 6.77e-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: 47.07  E-value: 6.77e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958676061  315 AIADFQGSGPEEMSFSVGDVIEIVGAQVPGlpWCLGQHmASGQVGFV 361
Cdd:cd00174      4 ALYDYEAQDDDELSFKKGDIITVLEKDDDG--WWEGEL-NGGREGLF 47
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
666-900 2.46e-05

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: 47.42  E-value: 2.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676061  666 EARACFLLARHYTHLKQPEEALPYLERLLRLNRDVgtpqaswpEDCYLLLADIYGRKCLPHLALSCLK------VSSLWT 739
Cdd:COG2956     75 RAEALLELAQDYLKAGLLDRAEELLEKLLELDPDD--------AEALRLLAEIYEQEGDWEKAIEVLErllklgPENAHA 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676061  740 RCSLAgslrsvdlvlqnapgpnsQRSTGHSLPSQIAHYLRQALASLPpgtgQTLRgpLYASLAQLYSYHQQYGQAIAFMS 819
Cdd:COG2956    147 YCELA------------------ELYLEQGDYDEAIEALEKALKLDP----DCAR--ALLLLAELYLEQGDYEEAIAALE 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676061  820 QAAEADTAAGVHpvvdrLVALAWLHLLCGKSLVAMDILKcvsdaAVANKDQECVMMNMVAMALKRMGRTRQAAEGYFRAL 899
Cdd:COG2956    203 RALEQDPDYLPA-----LPRLAELYEKLGDPEEALELLR-----KALELDPSDDLLLALADLLERKEGLEAALALLERQL 272

                   .
gi 1958676061  900 H 900
Cdd:COG2956    273 R 273
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
315-361 4.57e-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: 41.81  E-value: 4.57e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958676061  315 AIADFQGSGPEEMSFSVGDVIEIVGAQVPGlpWCLGQhMASGQVGFV 361
Cdd:pfam00018    2 ALYDYTAQEPDELSFKKGDIIIVLEKSEDG--WWKGR-NKGGKEGLI 45
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
777-938 6.43e-04

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 42.69  E-value: 6.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676061  777 YLRQALAsLPPGTGQTlrgplYASLAQLYSYHQQYGQAIAFMSQAAEADTAagvhpVVDRLVALAWLHLLCGKSLVAMDI 856
Cdd:COG0457     30 DYEKALE-LDPDDAEA-----LYNLGLAYLRLGRYEEALADYEQALELDPD-----DAEALNNLGLALQALGRYEEALED 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676061  857 LkcvsDAAVANKDQECVMMNMVAMALKRMGRTRQAAEGYFRALHMAysqghlQSQAVVLANFGALCLQAGARSLAQHYLR 936
Cdd:COG0457     99 Y----DKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELD------PDDADALYNLGIALEKLGRYEEALELLE 168

                   ..
gi 1958676061  937 EA 938
Cdd:COG0457    169 KL 170
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
579-825 8.15e-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: 42.41  E-value: 8.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676061  579 KLSQARVYFEEALGALEGSfgdlslvAAVYSSLATVYLKQKNGEKCVQlapkaaalllgtpghscstdaellkyALRRVV 658
Cdd:COG2956     91 LLDRAEELLEKLLELDPDD-------AEALRLLAEIYEQEGDWEKAIE--------------------------VLERLL 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676061  659 cGLSPQaEARACFLLARHYTHLKQPEEALPYLERLLRLNRDvgtpqaswPEDCYLLLADIYGRKCLPHLALSCLKvsslw 738
Cdd:COG2956    138 -KLGPE-NAHAYCELAELYLEQGDYDEAIEALEKALKLDPD--------CARALLLLAELYLEQGDYEEAIAALE----- 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676061  739 TRCSLAGSLRSVDLVLQNApgpnsQRSTGHslPSQIAHYLRQALASLPpgtgqtlRGPLYASLAQLYSYHQQYGQAIAFM 818
Cdd:COG2956    203 RALEQDPDYLPALPRLAEL-----YEKLGD--PEEALELLRKALELDP-------SDDLLLALADLLERKEGLEAALALL 268

                   ....*..
gi 1958676061  819 SQAAEAD 825
Cdd:COG2956    269 ERQLRRH 275
TPR_12 pfam13424
Tetratricopeptide repeat;
672-733 1.12e-03

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 38.91  E-value: 1.12e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958676061  672 LLARHYTHLKQPEEALPYLERLLRLNRDVGTPQASWPEDCYLLLADIYGRKCLPHLALSCLK 733
Cdd:pfam13424    8 NLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLE 69
TPR_2 pfam07719
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ...
667-699 1.41e-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: 37.12  E-value: 1.41e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1958676061  667 ARACFLLARHYTHLKQPEEALPYLERLLRLNRD 699
Cdd:pfam07719    1 AEALYNLGLAYYKLGDYEEALEAYEKALELDPN 33
SH3_9 pfam14604
Variant SH3 domain;
315-361 3.95e-03

Variant SH3 domain;


Pssm-ID: 434066 [Multi-domain]  Cd Length: 49  Bit Score: 36.44  E-value: 3.95e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958676061  315 AIADFQGSGPEEMSFSVGDVIEIVGAQVPGlpWCLGQHmaSGQVGFV 361
Cdd:pfam14604    1 ALYPYEPKDDDELSLQRGDVITVIEESEDG--WWEGIN--TGRTGLV 43
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
798-1047 4.52e-03

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 39.99  E-value: 4.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676061  798 YASLAQLYSYHQQYGQAIAFMSQAAEADTAagvhpVVDRLVALAWLHLLCGKSLVAMDILkcvsDAAVANKDQECVMMNM 877
Cdd:COG0457     11 YNNLGLAYRRLGRYEEAIEDYEKALELDPD-----DAEALYNLGLAYLRLGRYEEALADY----EQALELDPDDAEALNN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676061  878 VAMALKRMGRTRQAAEGYFRALHMAYsqghlqSQAVVLANFGALCLQAGARSLAQHYLREAVGLFSqlpsgvcgrDFTQV 957
Cdd:COG0457     82 LGLALQALGRYEEALEDYDKALELDP------DDAEALYNLGLALLELGRYDEAIEAYERALELDP---------DDADA 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676061  958 LLWLGQLCTRRTLPQQAKCYYEWAFLVAVETDHLESQLQAVQKLCHFYSKVMPNEVRCVIYHEFQLALARKTADKVLEGQ 1037
Cdd:COG0457    147 LYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLA 226
                          250
                   ....*....|
gi 1958676061 1038 LLEAISQLYL 1047
Cdd:COG0457    227 LALLLALRLA 236
TPR_7 pfam13176
Tetratricopeptide repeat;
669-703 9.08e-03

Tetratricopeptide repeat;


Pssm-ID: 433012 [Multi-domain]  Cd Length: 36  Bit Score: 34.82  E-value: 9.08e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1958676061  669 ACFLLARHYTHLKQPEEALPYLERLLRLNRDVGTP 703
Cdd:pfam13176    1 ALLNLGRIYRKLGDYDEAISLYEQALALAKDPYDR 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.
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