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Conserved domains on  [gi|569003756|ref|XP_006525947|]
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SH3 domain and tetratricopeptide repeat-containing protein 2 isoform X4 [Mus musculus]

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 ...
 1-50 9.39e-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: 89.30  E-value: 9.39e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 569003756    1 MDYEQEERDELCFLQGESIDVIGFVIPGLQWFIGKSVSSGEVGFVPTRSI 50
Cdd:cd11885     6 MDFEGVEPGELSFRQGDSIEIIGDLIPGLQWFVGRSKSSGRVGFVPTNHF 55
TPR_1 pfam00515
Tetratricopeptide repeat;
894-923 1.13e-03

Tetratricopeptide repeat;


:

Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 37.40  E-value: 1.13e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 569003756   894 AFHRLATVYFSLNMYEMAEDCYLKTLSLCP 923
Cdd:pfam00515    3 ALYNLGNAYFKLGKYDEALEYYEKALELNP 32
Spy super family cl27809
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 770-945 1.20e-03

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


The actual alignment was detected with superfamily member COG3914:

Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 42.67  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003756  770 AEAWLGAGRLHYLMQEDELVELYLQEAIQTALRSEEPSLALKLYEEAGDVFF--NGTRHRHRAVEYYRAGAVPLARRMKA 847
Cdd:COG3914     1 AAAAALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAeaAAAALLALAAGEAAAAAAALLLLAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003756  848 LRTELRIFNKLTELQISLEGYEKALEFATLAArlsvltgdqkqelVAFHRLATVYFSLNMYEMAEDCYLKTLSLCPPWLQ 927
Cdd:COG3914    81 LELAALLLQALGRYEEALALYRRALALNPDNA-------------EALFNLGNLLLALGRLEEALAALRRALALNPDFAE 147

                         170
                  ....*....|....*...
gi 569003756  928 SpkeALYYAKVYCRLGRL 945
Cdd:COG3914   148 A---YLNLGEALRRLGRL 162
 
Name Accession Description Interval E-value
SH3_SH3TC cd11885
Src Homology 3 domain of SH3 domain and tetratricopeptide repeat-containing (SH3TC) proteins ...
 1-50 9.39e-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: 89.30  E-value: 9.39e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 569003756    1 MDYEQEERDELCFLQGESIDVIGFVIPGLQWFIGKSVSSGEVGFVPTRSI 50
Cdd:cd11885     6 MDFEGVEPGELSFRQGDSIEIIGDLIPGLQWFVGRSKSSGRVGFVPTNHF 55
TPR_1 pfam00515
Tetratricopeptide repeat;
894-923 1.13e-03

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 37.40  E-value: 1.13e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 569003756   894 AFHRLATVYFSLNMYEMAEDCYLKTLSLCP 923
Cdd:pfam00515    3 ALYNLGNAYFKLGKYDEALEYYEKALELNP 32
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 2-47 1.19e-03

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: 37.90  E-value: 1.19e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 569003756      2 DYEQEERDELCFLQGESIDVIGFVIPGlqWFIGKsVSSGEVGFVPT 47
Cdd:smart00326   10 DYTAQDPDELSFKKGDIITVLEKSDDG--WWKGR-LGRGKEGLFPS 52
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 770-945 1.20e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 42.67  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003756  770 AEAWLGAGRLHYLMQEDELVELYLQEAIQTALRSEEPSLALKLYEEAGDVFF--NGTRHRHRAVEYYRAGAVPLARRMKA 847
Cdd:COG3914     1 AAAAALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAeaAAAALLALAAGEAAAAAAALLLLAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003756  848 LRTELRIFNKLTELQISLEGYEKALEFATLAArlsvltgdqkqelVAFHRLATVYFSLNMYEMAEDCYLKTLSLCPPWLQ 927
Cdd:COG3914    81 LELAALLLQALGRYEEALALYRRALALNPDNA-------------EALFNLGNLLLALGRLEEALAALRRALALNPDFAE 147

                         170
                  ....*....|....*...
gi 569003756  928 SpkeALYYAKVYCRLGRL 945
Cdd:COG3914   148 A---YLNLGEALRRLGRL 162
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 2-47 1.57e-03

SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 37.18  E-value: 1.57e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 569003756     2 DYEQEERDELCFLQGESIDVIGFVIPGlqWFIGKSvSSGEVGFVPT 47
Cdd:pfam00018    5 DYTAQEPDELSFKKGDIIIVLEKSEDG--WWKGRN-KGGKEGLIPS 47
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 894-923 4.17e-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: 35.89  E-value: 4.17e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 569003756    894 AFHRLATVYFSLNMYEMAEDCYLKTLSLCP 923
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 ...
 1-50 9.39e-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: 89.30  E-value: 9.39e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 569003756    1 MDYEQEERDELCFLQGESIDVIGFVIPGLQWFIGKSVSSGEVGFVPTRSI 50
Cdd:cd11885     6 MDFEGVEPGELSFRQGDSIEIIGDLIPGLQWFVGRSKSSGRVGFVPTNHF 55
TPR_1 pfam00515
Tetratricopeptide repeat;
894-923 1.13e-03

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 37.40  E-value: 1.13e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 569003756   894 AFHRLATVYFSLNMYEMAEDCYLKTLSLCP 923
Cdd:pfam00515    3 ALYNLGNAYFKLGKYDEALEYYEKALELNP 32
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 2-47 1.19e-03

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: 37.90  E-value: 1.19e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 569003756      2 DYEQEERDELCFLQGESIDVIGFVIPGlqWFIGKsVSSGEVGFVPT 47
Cdd:smart00326   10 DYTAQDPDELSFKKGDIITVLEKSDDG--WWKGR-LGRGKEGLFPS 52
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 770-945 1.20e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 42.67  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003756  770 AEAWLGAGRLHYLMQEDELVELYLQEAIQTALRSEEPSLALKLYEEAGDVFF--NGTRHRHRAVEYYRAGAVPLARRMKA 847
Cdd:COG3914     1 AAAAALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAeaAAAALLALAAGEAAAAAAALLLLAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003756  848 LRTELRIFNKLTELQISLEGYEKALEFATLAArlsvltgdqkqelVAFHRLATVYFSLNMYEMAEDCYLKTLSLCPPWLQ 927
Cdd:COG3914    81 LELAALLLQALGRYEEALALYRRALALNPDNA-------------EALFNLGNLLLALGRLEEALAALRRALALNPDFAE 147

                         170
                  ....*....|....*...
gi 569003756  928 SpkeALYYAKVYCRLGRL 945
Cdd:COG3914   148 A---YLNLGEALRRLGRL 162
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 2-47 1.57e-03

SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 37.18  E-value: 1.57e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 569003756     2 DYEQEERDELCFLQGESIDVIGFVIPGlqWFIGKSvSSGEVGFVPT 47
Cdd:pfam00018    5 DYTAQEPDELSFKKGDIIIVLEKSEDG--WWKGRN-KGGKEGLIPS 47
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 2-46 1.64e-03

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: 37.44  E-value: 1.64e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 569003756    2 DYEQEERDELCFLQGESIDVIGFVIPGlqWFIGKSVsSGEVGFVP 46
Cdd:cd00174     7 DYEAQDDDELSFKKGDIITVLEKDDDG--WWEGELN-GGREGLFP 48
COG3899 COG3899
Predicted ATPase [General function prediction only];
764-922 2.95e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 41.77  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003756  764 GERDKAAEAWLGAGRLHYLMQEDELVELYLQEAIQTALRSEEPSLALKLYEEAGDVFFNGTRHRHRAVEYYRAGAVPLAR 843
Cdd:COG3899   699 GERDRAARLLLRAARRALARGAYAEALRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALA 778

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003756  844 RMKALR---TELRIFNKLTELQISLEGYEKALEFATLAARLSVLTGDQKQELVAFHRLATVYFSLNMYEMAEDCYLKTLS 920
Cdd:COG3899   779 ALAALRhgnPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALE 858


                  ..
gi 569003756  921 LC 922
Cdd:COG3899   859 AG 860
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 755-944 3.82e-03

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 40.48  E-value: 3.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003756  755 ESLRIFVDLGERD-KAAEAWLGAGRLHYLMQEDELVELYLQEAIQTALRSEEPSLAL-KLYEEAGDVffngtrhrHRAVE 832
Cdd:COG2956    26 KAIDLLEEALELDpETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELaQDYLKAGLL--------DRAEE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003756  833 YYRAGAVPLARRMKALRTELRIFNKLTElqislegYEKALEFATLAARLSvltgdqKQELVAFHRLATVYFSLNMYEMAE 912
Cdd:COG2956    98 LLEKLLELDPDDAEALRLLAEIYEQEGD-------WEKAIEVLERLLKLG------PENAHAYCELAELYLEQGDYDEAI 164

                         170       180       190
                  ....*....|....*....|....*....|..
gi 569003756  913 DCYLKTLSLCPpwlQSPKEALYYAKVYCRLGR 944
Cdd:COG2956   165 EALEKALKLDP---DCARALLLLAELYLEQGD 193
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 894-923 4.17e-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: 35.89  E-value: 4.17e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 569003756    894 AFHRLATVYFSLNMYEMAEDCYLKTLSLCP 923
Cdd:smart00028    3 ALYNLGNAYLKLGDYDEALEYYEKALELDP 32
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 769-960 5.07e-03

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 40.10  E-value: 5.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003756  769 AAEAWLGAGRLHYLMQEDELVELYLQEAIQTALRSEEPSLAL-KLYEEAGDVffngtrhrHRAVEYYRagavplaRRMKA 847
Cdd:COG2956     7 AALGWYFKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALgNLYRRRGEY--------DRAIRIHQ-------KLLER 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003756  848 LRTELRIFNKLTELQISLEGYEKALEFATLAARLSvltgdqKQELVAFHRLATVYFSLNMYEMAEDCYLKTLSLCPpwlq 927
Cdd:COG2956    72 DPDRAEALLELAQDYLKAGLLDRAEELLEKLLELD------PDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGP---- 141

                         170       180       190
                  ....*....|....*....|....*....|...
gi 569003756  928 spkealYYAKVYCRLGRLtFYQLKDAHDATEYF 960
Cdd:COG2956   142 ------ENAHAYCELAEL-YLEQGDYDEAIEAL 167
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
770-960 8.09e-03

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 39.22  E-value: 8.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003756  770 AEAWLGAGRLHYLMQEdelvelyLQEAIQTALRseepslALKLYEEAGDVFFNgtrhrhRAVEYYRAGAVPLARRM--KA 847
Cdd:COG0457     8 AEAYNNLGLAYRRLGR-------YEEAIEDYEK------ALELDPDDAEALYN------LGLAYLRLGRYEEALADyeQA 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003756  848 LRTELR---IFNKLTELQISLEGYEKALEFATLAARLsvltgdQKQELVAFHRLATVYFSLNMYEMAEDCYLKTLSLCPp 924
Cdd:COG0457    69 LELDPDdaeALNNLGLALQALGRYEEALEDYDKALEL------DPDDAEALYNLGLALLELGRYDEAIEAYERALELDP- 141

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 569003756  925 wlqspkealYYAKVYCRLGRLtFYQLKDAHDATEYF 960
Cdd:COG0457   142 ---------DDADALYNLGIA-LEKLGRYEEALELL 167
 
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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