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Conserved domains on  [gi|564393707|ref|XP_006254879|]
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SH3 domain and tetratricopeptide repeat-containing protein 2 isoform X2 [Rattus norvegicus]

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 ...
 294-348 6.75e-22

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: 90.07  E-value: 6.75e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564393707  294 RCKALMDYQQEERDELGFLQGESIDVIGFVIPGLRWFIGKSMSSGKVGFVPTRSI 348
Cdd:cd11885     1 SCTAKMDFEGVEPGELSFRQGDSIEIIGDLIPGLQWFVGRSKSSGRVGFVPTNHF 55
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 203-260 1.07e-05

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: 44.12  E-value: 1.07e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 564393707   203 FCRAMCSVTqPADKEGeyLTLCKNELISVLSGGESD-WEGMslVTGQRGLVPVSALEPL 260
Cdd:pfam07653    1 YGRVIFDYV-GTDKNG--LTLKKGDVVKVLGKDNDGwWEGE--TGGRVGLVPSTAVEEI 54
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1052-1241 7.13e-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: 46.26  E-value: 7.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393707 1052 ESLRIFVDLGERD-KAAEAWLGAGRLHYLMQEDELVEVYLQEAIQTALRSEELSLAL-KLYEEAGDvfFNgtrhrhRAVE 1129
Cdd:COG2956    26 KAIDLLEEALELDpETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELaQDYLKAGL--LD------RAEE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393707 1130 YYRAGAVPLARRMKALRtelrifnKLTELQISLRGYEKALEFATLAARLSvltgdqKQELVAFHRLATVYFSLNMYEMAE 1209
Cdd:COG2956    98 LLEKLLELDPDDAEALR-------LLAEIYEQEGDWEKAIEVLERLLKLG------PENAHAYCELAELYLEQGDYDEAI 164

                         170       180       190
                  ....*....|....*....|....*....|..
gi 564393707 1210 DCYLKTLSLCPpwlQSPKEALYYAKVYCRLGR 1241
Cdd:COG2956   165 EALEKALKLDP---DCARALLLLAELYLEQGD 193
COG3899 super family cl28481
Predicted ATPase [General function prediction only];
832-1198 7.30e-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: 41.00  E-value: 7.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393707  832 ARQTKKALEILEPLLCSLRETECVTQRGVVHNLLGLAFQDEGRTSRAAKSYLRALIRAREMGNIRNQAVSMANLGHLTLK 911
Cdd:COG3899   725 LRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLG 804

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393707  912 scMQQSARGYLLQAVRLYSEIQAsketDMELVQVLLWLGQALVSGHQLVHSRLCYEMALLFGLRHRHLNSqlqvtkSLCH 991
Cdd:COG3899   805 --DYEEAYEFGELALALAERLGD----RRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAAL------ALLA 872

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393707  992 FYSSVSPNPDACITYHEHWLAL-AQQLRDREMEGRLLESLGQLYRNLNTSRSLRRSLACIKESLRIFVDLGERDKAAEAW 1070
Cdd:COG3899   873 LAAAAAAAAAAAALAAAAAAAArLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAA 952

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393707 1071 LGAGRLHYLMQEDELVEVYLQEAIQTALRSEELSLALKLYEEAGDVffnGTRHRHRAVEYYRAGAVPLARRMKALRTELR 1150
Cdd:COG3899   953 ALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAAL---LALLAAAAAAAAAAAALAAALLAAALAALAA 1029

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 564393707 1151 IFNKLTELQISLRGYEKALEFATLAARLSVLTGDQKQELVAFHRLATV 1198
Cdd:COG3899  1030 AAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAA 1077
 
Name Accession Description Interval E-value
SH3_SH3TC cd11885
Src Homology 3 domain of SH3 domain and tetratricopeptide repeat-containing (SH3TC) proteins ...
 294-348 6.75e-22

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: 90.07  E-value: 6.75e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564393707  294 RCKALMDYQQEERDELGFLQGESIDVIGFVIPGLRWFIGKSMSSGKVGFVPTRSI 348
Cdd:cd11885     1 SCTAKMDFEGVEPGELSFRQGDSIEIIGDLIPGLQWFVGRSKSSGRVGFVPTNHF 55
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 291-345 2.45e-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: 45.99  E-value: 2.45e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 564393707    291 GRGRCKALMDYQQEERDELGFLQGESIDVIGFVIPGlrWFIGKSMsSGKVGFVPT 345
Cdd:smart00326    1 EGPQVRALYDYTAQDPDELSFKKGDIITVLEKSDDG--WWKGRLG-RGKEGLFPS 52
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 296-345 4.66e-06

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: 44.89  E-value: 4.66e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 564393707   296 KALMDYQQEERDELGFLQGESIDVIGFVIPGlrWFIGKSMsSGKVGFVPT 345
Cdd:pfam00018    1 VALYDYTAQEPDELSFKKGDIIIVLEKSEDG--WWKGRNK-GGKEGLIPS 47
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 203-260 1.07e-05

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: 44.12  E-value: 1.07e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 564393707   203 FCRAMCSVTqPADKEGeyLTLCKNELISVLSGGESD-WEGMslVTGQRGLVPVSALEPL 260
Cdd:pfam07653    1 YGRVIFDYV-GTDKNG--LTLKKGDVVKVLGKDNDGwWEGE--TGGRVGLVPSTAVEEI 54
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1052-1241 7.13e-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: 46.26  E-value: 7.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393707 1052 ESLRIFVDLGERD-KAAEAWLGAGRLHYLMQEDELVEVYLQEAIQTALRSEELSLAL-KLYEEAGDvfFNgtrhrhRAVE 1129
Cdd:COG2956    26 KAIDLLEEALELDpETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELaQDYLKAGL--LD------RAEE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393707 1130 YYRAGAVPLARRMKALRtelrifnKLTELQISLRGYEKALEFATLAARLSvltgdqKQELVAFHRLATVYFSLNMYEMAE 1209
Cdd:COG2956    98 LLEKLLELDPDDAEALR-------LLAEIYEQEGDWEKAIEVLERLLKLG------PENAHAYCELAELYLEQGDYDEAI 164

                         170       180       190
                  ....*....|....*....|....*....|..
gi 564393707 1210 DCYLKTLSLCPpwlQSPKEALYYAKVYCRLGR 1241
Cdd:COG2956   165 EALEKALKLDP---DCARALLLLAELYLEQGD 193
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 202-258 1.90e-04

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: 40.60  E-value: 1.90e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 564393707    202 FFCRAMCSVTqpADKEGEyLTLCKNELISVLSGGESDW-EGMsLVTGQRGLVPVSALE 258
Cdd:smart00326    3 PQVRALYDYT--AQDPDE-LSFKKGDIITVLEKSDDGWwKGR-LGRGKEGLFPSNYVE 56
TPR_1 pfam00515
Tetratricopeptide repeat;
1191-1220 7.20e-04

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 38.17  E-value: 7.20e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 564393707  1191 AFHRLATVYFSLNMYEMAEDCYLKTLSLCP 1220
Cdd:pfam00515    3 ALYNLGNAYFKLGKYDEALEYYEKALELNP 32
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 1191-1220 2.70e-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: 36.66  E-value: 2.70e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 564393707   1191 AFHRLATVYFSLNMYEMAEDCYLKTLSLCP 1220
Cdd:smart00028    3 ALYNLGNAYLKLGDYDEALEYYEKALELDP 32
COG3899 COG3899
Predicted ATPase [General function prediction only];
832-1198 7.30e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 41.00  E-value: 7.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393707  832 ARQTKKALEILEPLLCSLRETECVTQRGVVHNLLGLAFQDEGRTSRAAKSYLRALIRAREMGNIRNQAVSMANLGHLTLK 911
Cdd:COG3899   725 LRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLG 804

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393707  912 scMQQSARGYLLQAVRLYSEIQAsketDMELVQVLLWLGQALVSGHQLVHSRLCYEMALLFGLRHRHLNSqlqvtkSLCH 991
Cdd:COG3899   805 --DYEEAYEFGELALALAERLGD----RRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAAL------ALLA 872

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393707  992 FYSSVSPNPDACITYHEHWLAL-AQQLRDREMEGRLLESLGQLYRNLNTSRSLRRSLACIKESLRIFVDLGERDKAAEAW 1070
Cdd:COG3899   873 LAAAAAAAAAAAALAAAAAAAArLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAA 952

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393707 1071 LGAGRLHYLMQEDELVEVYLQEAIQTALRSEELSLALKLYEEAGDVffnGTRHRHRAVEYYRAGAVPLARRMKALRTELR 1150
Cdd:COG3899   953 ALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAAL---LALLAAAAAAAAAAAALAAALLAAALAALAA 1029

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 564393707 1151 IFNKLTELQISLRGYEKALEFATLAARLSVLTGDQKQELVAFHRLATV 1198
Cdd:COG3899  1030 AAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAA 1077
 
Name Accession Description Interval E-value
SH3_SH3TC cd11885
Src Homology 3 domain of SH3 domain and tetratricopeptide repeat-containing (SH3TC) proteins ...
 294-348 6.75e-22

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: 90.07  E-value: 6.75e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564393707  294 RCKALMDYQQEERDELGFLQGESIDVIGFVIPGLRWFIGKSMSSGKVGFVPTRSI 348
Cdd:cd11885     1 SCTAKMDFEGVEPGELSFRQGDSIEIIGDLIPGLQWFVGRSKSSGRVGFVPTNHF 55
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 291-345 2.45e-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: 45.99  E-value: 2.45e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 564393707    291 GRGRCKALMDYQQEERDELGFLQGESIDVIGFVIPGlrWFIGKSMsSGKVGFVPT 345
Cdd:smart00326    1 EGPQVRALYDYTAQDPDELSFKKGDIITVLEKSDDG--WWKGRLG-RGKEGLFPS 52
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 294-344 2.69e-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: 45.53  E-value: 2.69e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564393707  294 RCKALMDYQQEERDELGFLQGESIDVIGFVIPGlrWFIGKSMsSGKVGFVP 344
Cdd:cd00174     1 YARALYDYEAQDDDELSFKKGDIITVLEKDDDG--WWEGELN-GGREGLFP 48
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 296-345 4.66e-06

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: 44.89  E-value: 4.66e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 564393707   296 KALMDYQQEERDELGFLQGESIDVIGFVIPGlrWFIGKSMsSGKVGFVPT 345
Cdd:pfam00018    1 VALYDYTAQEPDELSFKKGDIIIVLEKSEDG--WWKGRNK-GGKEGLIPS 47
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 203-260 1.07e-05

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: 44.12  E-value: 1.07e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 564393707   203 FCRAMCSVTqPADKEGeyLTLCKNELISVLSGGESD-WEGMslVTGQRGLVPVSALEPL 260
Cdd:pfam07653    1 YGRVIFDYV-GTDKNG--LTLKKGDVVKVLGKDNDGwWEGE--TGGRVGLVPSTAVEEI 54
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1052-1241 7.13e-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: 46.26  E-value: 7.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393707 1052 ESLRIFVDLGERD-KAAEAWLGAGRLHYLMQEDELVEVYLQEAIQTALRSEELSLAL-KLYEEAGDvfFNgtrhrhRAVE 1129
Cdd:COG2956    26 KAIDLLEEALELDpETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELaQDYLKAGL--LD------RAEE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393707 1130 YYRAGAVPLARRMKALRtelrifnKLTELQISLRGYEKALEFATLAARLSvltgdqKQELVAFHRLATVYFSLNMYEMAE 1209
Cdd:COG2956    98 LLEKLLELDPDDAEALR-------LLAEIYEQEGDWEKAIEVLERLLKLG------PENAHAYCELAELYLEQGDYDEAI 164

                         170       180       190
                  ....*....|....*....|....*....|..
gi 564393707 1210 DCYLKTLSLCPpwlQSPKEALYYAKVYCRLGR 1241
Cdd:COG2956   165 EALEKALKLDP---DCARALLLLAELYLEQGD 193
SH3_CD2AP-like_2 cd11874
Second Src Homology 3 domain (SH3B) of CD2-associated protein and similar proteins; This ...
 294-345 1.18e-04

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: 41.17  E-value: 1.18e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564393707  294 RCKALMDYQQEERDELGFLQGESIDVIGFVIPGlrWFIGKsmSSGKVGFVPT 345
Cdd:cd11874     1 RCKVLFSYTPQNEDELELKVGDTIEVLGEVEEG--WWEGK--LNGKVGVFPS 48
SH3_Eve1_3 cd11816
Third Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 ...
 294-344 1.29e-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: 1.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564393707  294 RCKALMDYQQEERDELGFLQGESIDVIGFVipGLRWfiGKSMSSGKVGFVP 344
Cdd:cd11816     1 RCVARFDFEGEQEDELSFSEGDVITLKEYV--GEEW--AKGELNGKIGIFP 47
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 202-258 1.90e-04

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: 40.60  E-value: 1.90e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 564393707    202 FFCRAMCSVTqpADKEGEyLTLCKNELISVLSGGESDW-EGMsLVTGQRGLVPVSALE 258
Cdd:smart00326    3 PQVRALYDYT--AQDPDE-LSFKKGDIITVLEKSDDGWwKGR-LGRGKEGLFPSNYVE 56
SH3_Cortactin_like cd11819
Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, ...
 294-350 5.17e-04

Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, Abp1 (actin-binding protein 1), hematopoietic lineage cell-specific protein 1 (HS1), and similar proteins. These proteins are involved in regulating actin dynamics through direct or indirect interaction with the Arp2/3 complex, which is required to initiate actin polymerization. They all contain at least one C-terminal SH3 domain. Cortactin and HS1 bind Arp2/3 and actin through an N-terminal region that contains an acidic domain and several copies of a repeat domain found in cortactin and HS1. Abp1 binds actin via an N-terminal actin-depolymerizing factor (ADF) homology domain. Yeast Abp1 binds Arp2/3 directly through two acidic domains. Mammalian Abp1 does not directly interact with Arp2/3; instead, it regulates actin dynamics indirectly by interacting with dynamin and WASP family proteins. The C-terminal region of these proteins acts as an adaptor or scaffold that can connect membrane trafficking and signaling proteins that bind the SH3 domain within the actin network. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212753 [Multi-domain]  Cd Length: 54  Bit Score: 39.22  E-value: 5.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564393707  294 RCKALMDYQQEERDELGFLQGESIDVIGFVIPGlrWFIGKSmSSGKVGFVPTRSIDL 350
Cdd:cd11819     1 RAKALYDYQAAEDNEISFVEGDIITQIEQIDEG--WWLGVN-AKGQKGLFPANYVEL 54
COG3899 COG3899
Predicted ATPase [General function prediction only];
1061-1219 7.15e-04

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 44.08  E-value: 7.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393707 1061 GERDKAAEAWLGAGRLHYLMQEDELVEVYLQEAIQTALRSEELSLALKLYEEAGDVFFNGTRHRHRAVEYYRAGAVPLAR 1140
Cdd:COG3899   699 GERDRAARLLLRAARRALARGAYAEALRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALA 778

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393707 1141 RMKALR---TELRIFNKLTELQISLRGYEKALEFATLAARLSVLTGDQKQELVAFHRLATVYFSLNMYEMAEDCYLKTLS 1217
Cdd:COG3899   779 ALAALRhgnPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALE 858


                  ..
gi 564393707 1218 LC 1219
Cdd:COG3899   859 AG 860
TPR_1 pfam00515
Tetratricopeptide repeat;
1191-1220 7.20e-04

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 38.17  E-value: 7.20e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 564393707  1191 AFHRLATVYFSLNMYEMAEDCYLKTLSLCP 1220
Cdd:pfam00515    3 ALYNLGNAYFKLGKYDEALEYYEKALELNP 32
SH3_Cyk3p-like cd11889
Src Homology 3 domain of Cytokinesis protein 3 and similar proteins; Cytokinesis protein 3 ...
 294-344 7.85e-04

Src Homology 3 domain of Cytokinesis protein 3 and similar proteins; Cytokinesis protein 3 (Cyk3 or Cyk3p) is a component of the actomyosin ring independent cytokinesis pathway in yeast. It interacts with Inn1 and facilitates its recruitment to the bud neck, thereby promoting cytokinesis. Cyk3p contains an N-terminal SH3 domain and a C-terminal transglutaminase-like domain. The Cyk3p SH3 domain binds to the C-terminal proline-rich region of Inn1. 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: 212822  Cd Length: 53  Bit Score: 38.63  E-value: 7.85e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564393707  294 RCKALMDYQQEERDELGFLQGESIDVIGFVIPglRWFIGKSMSSGKVGFVP 344
Cdd:cd11889     1 KVKAVYSWAGETEGDLGFLEGDLIEVLSIGDG--SWWSGKLRRNGAEGIFP 49
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1067-1241 1.28e-03

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 41.92  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393707 1067 AEAWLGAGRLHYLMQEdelvevyLQEAIQTALRseelslALKLYEEAGDVFFNgtrhrhRAVEYYRAGAVPLARRM--KA 1144
Cdd:COG0457     8 AEAYNNLGLAYRRLGR-------YEEAIEDYEK------ALELDPDDAEALYN------LGLAYLRLGRYEEALADyeQA 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393707 1145 LRTELR---IFNKLTELQISLRGYEKALEFATLAARLsvltgdQKQELVAFHRLATVYFSLNMYEMAEDCYLKTLSLCPp 1221
Cdd:COG0457    69 LELDPDdaeALNNLGLALQALGRYEEALEDYDKALEL------DPDDAEALYNLGLALLELGRYDEAIEAYERALELDP- 141

                         170       180
                  ....*....|....*....|.
gi 564393707 1222 wlqSPKEALYY-AKVYCRLGR 1241
Cdd:COG0457   142 ---DDADALYNlGIALEKLGR 159
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 1067-1242 1.38e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 43.06  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393707 1067 AEAWLGAGRLHYLMQEDELVEVYLQEAIQTALRSEELSLALKLYEEAGDVFF--NGTRHRHRAVEYYRAGAVPLARRMKA 1144
Cdd:COG3914     1 AAAAALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAeaAAAALLALAAGEAAAAAAALLLLAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393707 1145 LRTELRIFNKLTELQISLRGYEKALEFATLAArlsvltgdqkqelVAFHRLATVYFSLNMYEMAEDCYLKTLSLCPPWLQ 1224
Cdd:COG3914    81 LELAALLLQALGRYEEALALYRRALALNPDNA-------------EALFNLGNLLLALGRLEEALAALRRALALNPDFAE 147

                         170
                  ....*....|....*...
gi 564393707 1225 SpkeALYYAKVYCRLGRL 1242
Cdd:COG3914   148 A---YLNLGEALRRLGRL 162
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 1191-1220 2.70e-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: 36.66  E-value: 2.70e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 564393707   1191 AFHRLATVYFSLNMYEMAEDCYLKTLSLCP 1220
Cdd:smart00028    3 ALYNLGNAYLKLGDYDEALEYYEKALELDP 32
SH3_SH3RF_3 cd11783
Third Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), SH3RF3, and ...
 297-344 3.07e-03

Third Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), SH3RF3, and similar domains; SH3RF1 (or POSH) and SH3RF3 (or POSH2) are scaffold proteins that function as E3 ubiquitin-protein ligases. They contain an N-terminal RING finger domain and four SH3 domains. This model represents the third SH3 domain, located in the middle of SH3RF1 and SH3RF3, and similar domains. SH3RF1 plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF3 interacts with p21-activated kinase 2 (PAK2) and GTP-loaded Rac1. It may play a role in regulating JNK mediated apoptosis in certain conditions. 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: 212717 [Multi-domain]  Cd Length: 55  Bit Score: 36.99  E-value: 3.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 564393707  297 ALMDYQQEERDELGFLQGESIDVIGFVIPGlrWFIGKSMSSGKVGFVP 344
Cdd:cd11783     4 ALYPYKPQKPDELELRKGEMYTVTEKCQDG--WFKGTSLRTGQSGVFP 49
SH3_MyoIe_If_like cd11827
Src homology 3 domain of Myosins Ie, If, and similar proteins; Myosins Ie (MyoIe) and If ...
 294-344 3.75e-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: 36.62  E-value: 3.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564393707  294 RCKALMDYQQEERDELGFLQGESIDVIGFVIPGlrWFIGKsmSSGKVGFVP 344
Cdd:cd11827     1 QCKALYAYDAQDTDELSFNEGDIIEILKEDPSG--WWTGR--LRGKEGLFP 47
SH3_Endophilin_A cd11803
Src homology 3 domain of Endophilin-A; Endophilins play roles in synaptic vesicle formation, ...
 295-350 3.83e-03

Src homology 3 domain of Endophilin-A; Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. They are classified into two types, A and B. Vertebrates contain three endophilin-A isoforms (A1, A2, and A3). Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. They tubulate membranes and regulate calcium influx into neurons to trigger the activation of the endocytic machinery. They are also involved in the sorting of plasma membrane proteins, actin filament assembly, and the uncoating of clathrin-coated vesicles for fusion with endosomes. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212737 [Multi-domain]  Cd Length: 55  Bit Score: 36.85  E-value: 3.83e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564393707  295 CKALMDYQQEERDELGFLQGESIDVIGFVipGLRWFIGksMSSGKVGFVPTRSIDL 350
Cdd:cd11803     3 CRALYDFEPENEGELGFKEGDIITLTNQI--DENWYEG--MVNGQSGFFPVNYVEV 54
SH3_9 pfam14604
Variant SH3 domain;
297-344 5.33e-03

Variant SH3 domain;


Pssm-ID: 434066 [Multi-domain]  Cd Length: 49  Bit Score: 36.06  E-value: 5.33e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 564393707   297 ALMDYQQEERDELGFLQGESIDVIGFVIPGlrWFIGKsmSSGKVGFVP 344
Cdd:pfam14604    1 ALYPYEPKDDDELSLQRGDVITVIEESEDG--WWEGI--NTGRTGLVP 44
COG3899 COG3899
Predicted ATPase [General function prediction only];
832-1198 7.30e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 41.00  E-value: 7.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393707  832 ARQTKKALEILEPLLCSLRETECVTQRGVVHNLLGLAFQDEGRTSRAAKSYLRALIRAREMGNIRNQAVSMANLGHLTLK 911
Cdd:COG3899   725 LRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLG 804

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393707  912 scMQQSARGYLLQAVRLYSEIQAsketDMELVQVLLWLGQALVSGHQLVHSRLCYEMALLFGLRHRHLNSqlqvtkSLCH 991
Cdd:COG3899   805 --DYEEAYEFGELALALAERLGD----RRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAAL------ALLA 872

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393707  992 FYSSVSPNPDACITYHEHWLAL-AQQLRDREMEGRLLESLGQLYRNLNTSRSLRRSLACIKESLRIFVDLGERDKAAEAW 1070
Cdd:COG3899   873 LAAAAAAAAAAAALAAAAAAAArLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAA 952

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393707 1071 LGAGRLHYLMQEDELVEVYLQEAIQTALRSEELSLALKLYEEAGDVffnGTRHRHRAVEYYRAGAVPLARRMKALRTELR 1150
Cdd:COG3899   953 ALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAAL---LALLAAAAAAAAAAAALAAALLAAALAALAA 1029

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 564393707 1151 IFNKLTELQISLRGYEKALEFATLAARLSVLTGDQKQELVAFHRLATV 1198
Cdd:COG3899  1030 AAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAA 1077
SH3_GRAP2_C cd11950
C-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS ...
 296-344 7.39e-03

C-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS (GRB2-related adapter downstream of Shc), GrpL, GRB2L, Mona, or GRID (Grb2-related protein with insert domain). It is expressed specifically in the hematopoietic system. It plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. It also has roles in antigen-receptor and tyrosine kinase mediated signaling. GRAP2 is unique from other GRB2-like adaptor proteins in that it can be regulated by caspase cleavage. It contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domain of GRAP2 binds to different motifs found in substrate peptides including the typical PxxP motif in hematopoietic progenitor kinase 1 (HPK1), the RxxK motif in SLP-76 and HPK1, and the RxxxxK motif in phosphatase-like protein HD-PTP. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212883 [Multi-domain]  Cd Length: 53  Bit Score: 35.96  E-value: 7.39e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 564393707  296 KALMDYQQEERDELGFLQGESIDVIGFVIPGlrWFIGKsmSSGKVGFVP 344
Cdd:cd11950     3 RALYDFEALEDDELGFNSGDVIEVLDSSNPS--WWKGR--LHGKLGLFP 47
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 1126-1242 8.42e-03

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 38.25  E-value: 8.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393707 1126 RAVEYYRAGAVPLARRM--KALRTE---LRIFNKLTELQISLRGYEKALEFATLAARLsvltgdQKQELVAFHRLATVYF 1200
Cdd:COG4783    10 LAQALLLAGDYDEAEALleKALELDpdnPEAFALLGEILLQLGDLDEAIVLLHEALEL------DPDEPEARLNLGLALL 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 564393707 1201 SLNMYEMAEDCYLKTLSLCPpwlQSPKEALYYAKVYCRLGRL 1242
Cdd:COG4783    84 KAGDYDEALALLEKALKLDP---EHPEAYLRLARAYRALGRP 122
 
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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