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Conserved domains on  [gi|46396348|sp|Q80VA5|]
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RecName: Full=SH3 domain and tetratricopeptide repeat-containing protein 2

Protein Classification

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 ...
 271-325 2.11e-24

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: 97.00  E-value: 2.11e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 46396348  271 RCKALMDYEQEERDELCFLQGESIDVIGFVIPGLQWFIGKSVSSGEVGFVPTRSI 325
Cdd:cd11885    1 SCTAKMDFEGVEPGELSFRQGDSIEIIGDLIPGLQWFVGRSKSSGRVGFVPTNHF 55
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 180-237 1.15e-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: 41.04  E-value: 1.15e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 46396348    180 FCRAVCSVAqPADKEGeyLTLCKNELISVLSG-GESECEAMslVTGQRGLVPMSALEPL 237
Cdd:pfam07653    1 YGRVIFDYV-GTDKNG--LTLKKGDVVKVLGKdNDGWWEGE--TGGRVGLVPSTAVEEI 54
TPR super family cl33886
Tetratricopeptide (TPR) repeat [General function prediction only];
1045-1235 6.38e-04

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: 43.07  E-value: 6.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46396348 1045 AEAWLGAGRLHYLMQEdelvelyLQEAIQTALRseepslALKLYEEAGDVFFNgtrhrhRAVEYYRAGAVPLARRM--KA 1122
Cdd:COG0457    8 AEAYNNLGLAYRRLGR-------YEEAIEDYEK------ALELDPDDAEALYN------LGLAYLRLGRYEEALADyeQA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46396348 1123 LRTELR---IFNKLTELQISLEGYEKALEFATLAARLsvltgdQKQELVAFHRLATVYFSLNMYEMAEDCYLKTLSLCPp 1199
Cdd:COG0457   69 LELDPDdaeALNNLGLALQALGRYEEALEDYDKALEL------DPDDAEALYNLGLALLELGRYDEAIEAYERALELDP- 141

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 46396348 1200 wlqspkealYYAKVYCRLGRLtFYQLKDAHDATEYF 1235
Cdd:COG0457  142 ---------DDADALYNLGIA-LEKLGRYEEALELL 167
COG3899 super family cl28481
Predicted ATPase [General function prediction only];
814-1176 2.06e-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: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46396348  814 EKALEILEPLLCSLRETECVTQRGVVHNLLGLAFEDEGRTSRAAKSYLRALIRAREMGNIRNQAVSMANLGHLTLKscMQ 893
Cdd:COG3899  729 ERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLG--DY 806

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46396348  894 QSARGYLLQAVRLYSELQAsketDMELVQVLLWLGQASVSGHQLVHSRLCYEMALLFGLRHQHLSSqlqvtkSLCHFYSS 973
Cdd:COG3899  807 EEAYEFGELALALAERLGD----RRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAAL------ALLALAAA 876

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46396348  974 VSPNPDACITYHEHWLAL-AQQLRDREMEGQLLESLGQLYRNLNTSRSLRRSLACIKESLRIFVDLGERDKAAEAWLGAG 1052
Cdd:COG3899  877 AAAAAAAAALAAAAAAAArLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAA 956

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46396348 1053 RLHYLMQEDELVELYLQEAIQTALRSEEPSLALKLYEEAGDVffnGTRHRHRAVEYYRAGAVPLARRMKALRTELRIFNK 1132
Cdd:COG3899  957 ALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAAL---LALLAAAAAAAAAAAALAAALLAAALAALAAAAAA 1033

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 46396348 1133 LTELQISLEGYEKALEFATLAARLSVLTGDQKQELVAFHRLATV 1176
Cdd:COG3899 1034 AALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAA 1077
 
Name Accession Description Interval E-value
SH3_SH3TC cd11885
Src Homology 3 domain of SH3 domain and tetratricopeptide repeat-containing (SH3TC) proteins ...
 271-325 2.11e-24

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: 97.00  E-value: 2.11e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 46396348  271 RCKALMDYEQEERDELCFLQGESIDVIGFVIPGLQWFIGKSVSSGEVGFVPTRSI 325
Cdd:cd11885    1 SCTAKMDFEGVEPGELSFRQGDSIEIIGDLIPGLQWFVGRSKSSGRVGFVPTNHF 55
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 268-322 6.52e-06

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: 44.45  E-value: 6.52e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 46396348     268 GRGRCKALMDYEQEERDELCFLQGESIDVIGFVIPGlqWFIGKsVSSGEVGFVPT 322
Cdd:smart00326    1 EGPQVRALYDYTAQDPDELSFKKGDIITVLEKSDDG--WWKGR-LGRGKEGLFPS 52
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 273-322 5.97e-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: 41.42  E-value: 5.97e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 46396348    273 KALMDYEQEERDELCFLQGESIDVIGFVIPGlqWFIGKSvSSGEVGFVPT 322
Cdd:pfam00018    1 VALYDYTAQEPDELSFKKGDIIIVLEKSEDG--WWKGRN-KGGKEGLIPS 47
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 180-237 1.15e-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: 41.04  E-value: 1.15e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 46396348    180 FCRAVCSVAqPADKEGeyLTLCKNELISVLSG-GESECEAMslVTGQRGLVPMSALEPL 237
Cdd:pfam07653    1 YGRVIFDYV-GTDKNG--LTLKKGDVVKVLGKdNDGWWEGE--TGGRVGLVPSTAVEEI 54
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1045-1235 6.38e-04

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 43.07  E-value: 6.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46396348 1045 AEAWLGAGRLHYLMQEdelvelyLQEAIQTALRseepslALKLYEEAGDVFFNgtrhrhRAVEYYRAGAVPLARRM--KA 1122
Cdd:COG0457    8 AEAYNNLGLAYRRLGR-------YEEAIEDYEK------ALELDPDDAEALYN------LGLAYLRLGRYEEALADyeQA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46396348 1123 LRTELR---IFNKLTELQISLEGYEKALEFATLAARLsvltgdQKQELVAFHRLATVYFSLNMYEMAEDCYLKTLSLCPp 1199
Cdd:COG0457   69 LELDPDdaeALNNLGLALQALGRYEEALEDYDKALEL------DPDDAEALYNLGLALLELGRYDEAIEAYERALELDP- 141

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 46396348 1200 wlqspkealYYAKVYCRLGRLtFYQLKDAHDATEYF 1235
Cdd:COG0457  142 ---------DDADALYNLGIA-LEKLGRYEEALELL 167
TPR_1 pfam00515
Tetratricopeptide repeat;
1169-1198 8.74e-04

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 37.79  E-value: 8.74e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 46396348   1169 AFHRLATVYFSLNMYEMAEDCYLKTLSLCP 1198
Cdd:pfam00515    3 ALYNLGNAYFKLGKYDEALEYYEKALELNP 32
COG3899 COG3899
Predicted ATPase [General function prediction only];
814-1176 2.06e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 42.54  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46396348  814 EKALEILEPLLCSLRETECVTQRGVVHNLLGLAFEDEGRTSRAAKSYLRALIRAREMGNIRNQAVSMANLGHLTLKscMQ 893
Cdd:COG3899  729 ERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLG--DY 806

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46396348  894 QSARGYLLQAVRLYSELQAsketDMELVQVLLWLGQASVSGHQLVHSRLCYEMALLFGLRHQHLSSqlqvtkSLCHFYSS 973
Cdd:COG3899  807 EEAYEFGELALALAERLGD----RRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAAL------ALLALAAA 876

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46396348  974 VSPNPDACITYHEHWLAL-AQQLRDREMEGQLLESLGQLYRNLNTSRSLRRSLACIKESLRIFVDLGERDKAAEAWLGAG 1052
Cdd:COG3899  877 AAAAAAAAALAAAAAAAArLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAA 956

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46396348 1053 RLHYLMQEDELVELYLQEAIQTALRSEEPSLALKLYEEAGDVffnGTRHRHRAVEYYRAGAVPLARRMKALRTELRIFNK 1132
Cdd:COG3899  957 ALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAAL---LALLAAAAAAAAAAAALAAALLAAALAALAAAAAA 1033

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 46396348 1133 LTELQISLEGYEKALEFATLAARLSVLTGDQKQELVAFHRLATV 1176
Cdd:COG3899 1034 AALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAA 1077
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 1169-1198 3.24e-03

Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.


Pssm-ID: 197478 [Multi-domain]  Cd Length: 34  Bit Score: 36.27  E-value: 3.24e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 46396348    1169 AFHRLATVYFSLNMYEMAEDCYLKTLSLCP 1198
Cdd:smart00028    3 ALYNLGNAYLKLGDYDEALEYYEKALELDP 32
 
Name Accession Description Interval E-value
SH3_SH3TC cd11885
Src Homology 3 domain of SH3 domain and tetratricopeptide repeat-containing (SH3TC) proteins ...
 271-325 2.11e-24

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: 97.00  E-value: 2.11e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 46396348  271 RCKALMDYEQEERDELCFLQGESIDVIGFVIPGLQWFIGKSVSSGEVGFVPTRSI 325
Cdd:cd11885    1 SCTAKMDFEGVEPGELSFRQGDSIEIIGDLIPGLQWFVGRSKSSGRVGFVPTNHF 55
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 271-321 4.13e-06

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: 45.15  E-value: 4.13e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 46396348  271 RCKALMDYEQEERDELCFLQGESIDVIGFVIPGlqWFIGKSVsSGEVGFVP 321
Cdd:cd00174    1 YARALYDYEAQDDDELSFKKGDIITVLEKDDDG--WWEGELN-GGREGLFP 48
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 268-322 6.52e-06

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: 44.45  E-value: 6.52e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 46396348     268 GRGRCKALMDYEQEERDELCFLQGESIDVIGFVIPGlqWFIGKsVSSGEVGFVPT 322
Cdd:smart00326    1 EGPQVRALYDYTAQDPDELSFKKGDIITVLEKSDDG--WWKGR-LGRGKEGLFPS 52
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 273-322 5.97e-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: 41.42  E-value: 5.97e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 46396348    273 KALMDYEQEERDELCFLQGESIDVIGFVIPGlqWFIGKSvSSGEVGFVPT 322
Cdd:pfam00018    1 VALYDYTAQEPDELSFKKGDIIIVLEKSEDG--WWKGRN-KGGKEGLIPS 47
SH3_Eve1_3 cd11816
Third Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 ...
 271-321 1.11e-04

Third 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: 212750 [Multi-domain]  Cd Length: 51  Bit Score: 40.85  E-value: 1.11e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 46396348  271 RCKALMDYEQEERDELCFLQGESIDVIGFVipGLQWfiGKSVSSGEVGFVP 321
Cdd:cd11816    1 RCVARFDFEGEQEDELSFSEGDVITLKEYV--GEEW--AKGELNGKIGIFP 47
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 180-237 1.15e-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: 41.04  E-value: 1.15e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 46396348    180 FCRAVCSVAqPADKEGeyLTLCKNELISVLSG-GESECEAMslVTGQRGLVPMSALEPL 237
Cdd:pfam07653    1 YGRVIFDYV-GTDKNG--LTLKKGDVVKVLGKdNDGWWEGE--TGGRVGLVPSTAVEEI 54
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1045-1235 6.38e-04

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 43.07  E-value: 6.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46396348 1045 AEAWLGAGRLHYLMQEdelvelyLQEAIQTALRseepslALKLYEEAGDVFFNgtrhrhRAVEYYRAGAVPLARRM--KA 1122
Cdd:COG0457    8 AEAYNNLGLAYRRLGR-------YEEAIEDYEK------ALELDPDDAEALYN------LGLAYLRLGRYEEALADyeQA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46396348 1123 LRTELR---IFNKLTELQISLEGYEKALEFATLAARLsvltgdQKQELVAFHRLATVYFSLNMYEMAEDCYLKTLSLCPp 1199
Cdd:COG0457   69 LELDPDdaeALNNLGLALQALGRYEEALEDYDKALEL------DPDDAEALYNLGLALLELGRYDEAIEAYERALELDP- 141

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 46396348 1200 wlqspkealYYAKVYCRLGRLtFYQLKDAHDATEYF 1235
Cdd:COG0457  142 ---------DDADALYNLGIA-LEKLGRYEEALELL 167
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1030-1219 6.39e-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: 43.18  E-value: 6.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46396348 1030 ESLRIFVDLGERD-KAAEAWLGAGRLHYLMQEDELVELYLQEAIQTALRSEEPSLAL-KLYEEAGDVffngtrhrHRAVE 1107
Cdd:COG2956   26 KAIDLLEEALELDpETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELaQDYLKAGLL--------DRAEE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46396348 1108 YYRAGAVPLARRMKALRTELRIFNKLTElqislegYEKALEFATLAARLSvltgdqKQELVAFHRLATVYFSLNMYEMAE 1187
Cdd:COG2956   98 LLEKLLELDPDDAEALRLLAEIYEQEGD-------WEKAIEVLERLLKLG------PENAHAYCELAELYLEQGDYDEAI 164

                        170       180       190
                 ....*....|....*....|....*....|..
gi 46396348 1188 DCYLKTLSLCPpwlQSPKEALYYAKVYCRLGR 1219
Cdd:COG2956  165 EALEKALKLDP---DCARALLLLAELYLEQGD 193
COG3899 COG3899
Predicted ATPase [General function prediction only];
1039-1197 7.62e-04

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 44.08  E-value: 7.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46396348 1039 GERDKAAEAWLGAGRLHYLMQEDELVELYLQEAIQTALRSEEPSLALKLYEEAGDVFFNGTRHRHRAVEYYRAGAVPLAR 1118
Cdd:COG3899  699 GERDRAARLLLRAARRALARGAYAEALRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALA 778

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46396348 1119 RMKALR---TELRIFNKLTELQISLEGYEKALEFATLAARLSVLTGDQKQELVAFHRLATVYFSLNMYEMAEDCYLKTLS 1195
Cdd:COG3899  779 ALAALRhgnPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALE 858


                 ..
gi 46396348 1196 LC 1197
Cdd:COG3899  859 AG 860
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 1045-1235 7.98e-04

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 43.83  E-value: 7.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46396348 1045 AEAWLGAGRLHYLMQEDELVELYLQEAIQTALRSEEPSLALKLYEEAGDVFF--NGTRHRHRAVEYYRAGAVPLARRMKA 1122
Cdd:COG3914    1 AAAAALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAeaAAAALLALAAGEAAAAAAALLLLAAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46396348 1123 LRTELRIFNKLTELQISLEGYEKALEFATLAArlsvltgdqkqelVAFHRLATVYFSLNMYEMAEDCYLKTLSLCPPwlq 1202
Cdd:COG3914   81 LELAALLLQALGRYEEALALYRRALALNPDNA-------------EALFNLGNLLLALGRLEEALAALRRALALNPD--- 144

                        170       180       190
                 ....*....|....*....|....*....|...
gi 46396348 1203 spkealyYAKVYCRLGRLtFYQLKDAHDATEYF 1235
Cdd:COG3914  145 -------FAEAYLNLGEA-LRRLGRLEEAIAAL 169
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1044-1235 8.42e-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: 42.79  E-value: 8.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46396348 1044 AAEAWLGAGRLHYLMQEDELVELYLQEAIQTALRSEEPSLAL-KLYEEAGDVffngtrhrHRAVEYYRagavplaRRMKA 1122
Cdd:COG2956    7 AALGWYFKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALgNLYRRRGEY--------DRAIRIHQ-------KLLER 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46396348 1123 LRTELRIFNKLTELQISLEGYEKALEFATLAARLSvltgdqKQELVAFHRLATVYFSLNMYEMAEDCYLKTLSLCPpwlq 1202
Cdd:COG2956   72 DPDRAEALLELAQDYLKAGLLDRAEELLEKLLELD------PDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGP---- 141

                        170       180       190
                 ....*....|....*....|....*....|...
gi 46396348 1203 spkealYYAKVYCRLGRLtFYQLKDAHDATEYF 1235
Cdd:COG2956  142 ------ENAHAYCELAEL-YLEQGDYDEAIEAL 167
TPR_1 pfam00515
Tetratricopeptide repeat;
1169-1198 8.74e-04

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 37.79  E-value: 8.74e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 46396348   1169 AFHRLATVYFSLNMYEMAEDCYLKTLSLCP 1198
Cdd:pfam00515    3 ALYNLGNAYFKLGKYDEALEYYEKALELNP 32
SH3_FCHSD_1 cd11761
First Src Homology 3 domain of FCH and double SH3 domains proteins; This group is composed of ...
 272-327 1.54e-03

First 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: 212695 [Multi-domain]  Cd Length: 57  Bit Score: 38.11  E-value: 1.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 46396348  272 CKALMDYEQEERDELCFLQGESIDVI--GfviPGLQWFIGKSvSSGEVGFVPTRSIDL 327
Cdd:cd11761    4 CKVLYSYEAQRPDELTITEGEELEVIedG---DGDGWVKARN-KSGEVGYVPENYLQF 57
SH3_CD2AP-like_2 cd11874
Second Src Homology 3 domain (SH3B) of CD2-associated protein and similar proteins; This ...
 271-322 1.61e-03

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: 37.70  E-value: 1.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 46396348  271 RCKALMDYEQEERDELCFLQGESIDVIGFVIPGlqWFIGKsvSSGEVGFVPT 322
Cdd:cd11874    1 RCKVLFSYTPQNEDELELKVGDTIEVLGEVEEG--WWEGK--LNGKVGVFPS 48
COG3899 COG3899
Predicted ATPase [General function prediction only];
814-1176 2.06e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 42.54  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46396348  814 EKALEILEPLLCSLRETECVTQRGVVHNLLGLAFEDEGRTSRAAKSYLRALIRAREMGNIRNQAVSMANLGHLTLKscMQ 893
Cdd:COG3899  729 ERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLG--DY 806

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46396348  894 QSARGYLLQAVRLYSELQAsketDMELVQVLLWLGQASVSGHQLVHSRLCYEMALLFGLRHQHLSSqlqvtkSLCHFYSS 973
Cdd:COG3899  807 EEAYEFGELALALAERLGD----RRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAAL------ALLALAAA 876

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46396348  974 VSPNPDACITYHEHWLAL-AQQLRDREMEGQLLESLGQLYRNLNTSRSLRRSLACIKESLRIFVDLGERDKAAEAWLGAG 1052
Cdd:COG3899  877 AAAAAAAAALAAAAAAAArLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAA 956

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46396348 1053 RLHYLMQEDELVELYLQEAIQTALRSEEPSLALKLYEEAGDVffnGTRHRHRAVEYYRAGAVPLARRMKALRTELRIFNK 1132
Cdd:COG3899  957 ALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAAL---LALLAAAAAAAAAAAALAAALLAAALAALAAAAAA 1033

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 46396348 1133 LTELQISLEGYEKALEFATLAARLSVLTGDQKQELVAFHRLATV 1176
Cdd:COG3899 1034 AALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAA 1077
SH3_SNX9_like cd11763
Src Homology 3 domain of Sorting Nexin 9 and similar proteins; Sorting nexins (SNXs) are Phox ...
 271-322 2.20e-03

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: 37.31  E-value: 2.20e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 46396348  271 RCKALMDYEQEERDELCFLQGESIDVIGF-VIPGlqWFIGKSvSSGEVGFVPT 322
Cdd:cd11763    1 KVRALYDFDSQPSGELSLRAGEVLTITRQdVGDG--WLEGRN-SRGEVGLFPS 50
SH3_Cortactin_like cd11819
Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, ...
 271-327 2.89e-03

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: 36.91  E-value: 2.89e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 46396348  271 RCKALMDYEQEERDELCFLQGESIDVIGFVIPGlqWFIGKSvSSGEVGFVPTRSIDL 327
Cdd:cd11819    1 RAKALYDYQAAEDNEISFVEGDIITQIEQIDEG--WWLGVN-AKGQKGLFPANYVEL 54
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 1169-1198 3.24e-03

Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.


Pssm-ID: 197478 [Multi-domain]  Cd Length: 34  Bit Score: 36.27  E-value: 3.24e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 46396348    1169 AFHRLATVYFSLNMYEMAEDCYLKTLSLCP 1198
Cdd:smart00028    3 ALYNLGNAYLKLGDYDEALEYYEKALELDP 32
SH3_GRB2_like_C cd11805
C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related ...
 271-323 5.08e-03

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: 36.45  E-value: 5.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 46396348  271 RCKALMDYEQEERDELCFLQGESIDVIGFVIPglQWFIGKsvSSGEVGFVPTR 323
Cdd:cd11805    1 RVQALYDFNPQEPGELEFRRGDIITVLDSSDP--DWWKGE--LRGRVGIFPAN 49
SH3_Amphiphysin cd11790
Src Homology 3 domain of Amphiphysin and related domains; Amphiphysins function primarily in ...
 271-325 5.36e-03

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: 36.54  E-value: 5.36e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46396348  271 RCKALMDYEQEERDELCFLQGESIDVIGFVIPGLQ---WFIGKSVSSGEVGFVP---TRSI 325
Cdd:cd11790    4 KVRATHDYTAEDTDELTFEKGDVILVIPFDDPEEQdegWLMGVKESTGCRGVFPenfTERI 64
SH3_MyoIe_If_like cd11827
Src homology 3 domain of Myosins Ie, If, and similar proteins; Myosins Ie (MyoIe) and If ...
 271-297 7.83e-03

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: 35.85  E-value: 7.83e-03
                         10        20
                 ....*....|....*....|....*..
gi 46396348  271 RCKALMDYEQEERDELCFLQGESIDVI 297
Cdd:cd11827    1 QCKALYAYDAQDTDELSFNEGDIIEIL 27
 
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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