NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|189533885|ref|XP_001923593|]
View 

FYN-binding protein-like isoform X2 [Danio rerio]

Protein Classification

FYN-binding protein 1( domain architecture ID 10983874)

FYN-binding protein 1 acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells

CATH:  2.30.30.40
Gene Ontology:  GO:0005515|GO:0070064|GO:0050852|GO:0044877|GO:0007229|GO:0008289
PubMed:  28510178|1639195|11256992
SCOP:  4000369

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
hSH3 pfam14603
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ...
 645-723 6.06e-40

Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion and de-granulation promoting adapter protein. It shows homology to SH3 domains; however, conserved residues of the fold are absent. It thus represents an altered SH3 domain fold. An N-terminal, amphipathic, helix makes extensive contacts to residues of the regular SH3 domain fold thereby creating a composite surface with unusual surface properties. The domain can no longer bind conventional proline-rich peptides. There are key phosphorylation sites within the two hSH3 domains and it would appear that binding at these sites does not materially affect the folding of these regions although the equilibrium towards the unfolded state may be slightly altered. The binding partners of the hSH3 domains are still unknown.


:

Pssm-ID: 464216  Cd Length: 89  Bit Score: 141.66  E-value: 6.06e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885  645 YDGEIQVLHQATI---ATSKKGSGKDLAVQAGETVDVISKSDPDKFICRNKEGKFGYVSLSNI-QTDDEVYDDIGDDCIY 720
Cdd:pfam14603   7 YDGEIKVLYSMTVdpnLTIKKWGGKDLPVKPGEVLDVIQKTDDTKVLCRNEEGKYGYVLRSNLlQNDGEIYDDIGDDCIY 86


                  ...
gi 189533885  721 DND 723
Cdd:pfam14603  87 DND 89
hSH3 super family cl48258
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ...
 419-510 3.47e-12

Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion and de-granulation promoting adapter protein. It shows homology to SH3 domains; however, conserved residues of the fold are absent. It thus represents an altered SH3 domain fold. An N-terminal, amphipathic, helix makes extensive contacts to residues of the regular SH3 domain fold thereby creating a composite surface with unusual surface properties. The domain can no longer bind conventional proline-rich peptides. There are key phosphorylation sites within the two hSH3 domains and it would appear that binding at these sites does not materially affect the folding of these regions although the equilibrium towards the unfolded state may be slightly altered. The binding partners of the hSH3 domains are still unknown.


The actual alignment was detected with superfamily member pfam14603:

Pssm-ID: 464216  Cd Length: 89  Bit Score: 62.70  E-value: 3.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885  419 KKFKITPPFQVMHQVKAKSDC---KGGKNDLSIKKGESIDIIRITDnpEGKWLGRNQDGLFGYVKTemvqinfSALknqa 495
Cdd:pfam14603   3 KKFKYDGEIKVLYSMTVDPNLtikKWGGKDLPVKPGEVLDVIQKTD--DTKVLCRNEEGKYGYVLR-------SNL---- 69

                          90
                  ....*....|....*.
gi 189533885  496 qsphgLENE-EVYDDV 510
Cdd:pfam14603  70 -----LQNDgEIYDDI 80
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 32-357 8.53e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 8.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885   32 PVQPTLSSGPVVPSKKPvletslSGGATSTSTPPKPNFLKNTVNTARSAPDMPDPPKPKAFGNRFENMSENKGNKVPVKP 111
Cdd:PHA03247 2592 PPQSARPRAPVDDRGDP------RGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPR 2665

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885  112 KPPDSSLDPEPSKVP-FPKVPLQKPPSSIFANDTKDTSPKPLVSTTKPSWIKDIPK---AEVNGPTTPKMPSAPKPKSTM 187
Cdd:PHA03247 2666 RARRLGRAAQASSPPqRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLppgPAAARQASPALPAAPAPPAVP 2745

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885  188 AMLRQQPEENSNTESTVRSSPVSNVKPSSFRAKNSFTKLEEGVKDGAKASSTNESVSKPVAPIKPNFPKKAHGPPAQTvn 267
Cdd:PHA03247 2746 AGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAS-- 2823

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885  268 ddPSAPKKktlPNTYALGSAPSKPNRPPKVNLE---------KFKKGPevPTESPGPKNVTPPPPPAAHPSN-QVPPALP 337
Cdd:PHA03247 2824 --PAGPLP---PPTSAQPTAPPPPPGPPPPSLPlggsvapggDVRRRP--PSRSPAAKPAAPARPPVRRLARpAVSRSTE 2896

                         330       340
                  ....*....|....*....|
gi 189533885  338 SQPLPPSLPPRHPGPPIQDE 357
Cdd:PHA03247 2897 SFALPPDQPERPPQPQAPPP 2916
 
Name Accession Description Interval E-value
hSH3 pfam14603
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ...
 645-723 6.06e-40

Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion and de-granulation promoting adapter protein. It shows homology to SH3 domains; however, conserved residues of the fold are absent. It thus represents an altered SH3 domain fold. An N-terminal, amphipathic, helix makes extensive contacts to residues of the regular SH3 domain fold thereby creating a composite surface with unusual surface properties. The domain can no longer bind conventional proline-rich peptides. There are key phosphorylation sites within the two hSH3 domains and it would appear that binding at these sites does not materially affect the folding of these regions although the equilibrium towards the unfolded state may be slightly altered. The binding partners of the hSH3 domains are still unknown.


Pssm-ID: 464216  Cd Length: 89  Bit Score: 141.66  E-value: 6.06e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885  645 YDGEIQVLHQATI---ATSKKGSGKDLAVQAGETVDVISKSDPDKFICRNKEGKFGYVSLSNI-QTDDEVYDDIGDDCIY 720
Cdd:pfam14603   7 YDGEIKVLYSMTVdpnLTIKKWGGKDLPVKPGEVLDVIQKTDDTKVLCRNEEGKYGYVLRSNLlQNDGEIYDDIGDDCIY 86


                  ...
gi 189533885  721 DND 723
Cdd:pfam14603  87 DND 89
hSH3_ADAP cd11867
Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor ...
 645-706 5.54e-16

Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor Protein; ADAP, also called Fyn T-binding protein (FYB) or SLP-76-associated protein (SLAP), is expressed mainly in hematopoietic cells but not in B cells. It is required for the proliferation of mature T-cells and plays an important role in T-cell activation, TCR-induced integrin clustering, and T-cell adhesion. ADAP has been shown to bind many partners including SLP-76, Fyn, Src, SKAP1, SKAP2, dynein, Ena/VASP, Carma1, among others. It is connected to cytoskeleton via its binding to Ena and VASP, which impacts actin cytoskeletal remodeling upon TCR ligation. The SH3 domain of ADAP adopts an altered fold referred to as a helically extended SH3 (hSH3) domain characterized by clusters of positive charges. The hSH3 domain can no longer bind conventional proline-rich peptides, instead, it functions as a novel lipid interaction domain and can bind acidic lipids such as phosphatidylserine, phosphatidylinositol, phosphatidic acid, and polyphosphoinositides.


Pssm-ID: 212801  Cd Length: 77  Bit Score: 73.32  E-value: 5.54e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189533885 645 YDGEIQVLHQATIA---TSKKGSGKDLAVQAGETVDVISKSDPDKFICRNKEGKFGYVSLSNIQT 706
Cdd:cd11867   13 YNGEIKVLYSTTVLqtlTIKKFGSKDLQVKPGESLEVIQHTDDTKVLCRNEEGKYGYVLRSNLEP 77
hSH3 pfam14603
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ...
 419-510 3.47e-12

Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion and de-granulation promoting adapter protein. It shows homology to SH3 domains; however, conserved residues of the fold are absent. It thus represents an altered SH3 domain fold. An N-terminal, amphipathic, helix makes extensive contacts to residues of the regular SH3 domain fold thereby creating a composite surface with unusual surface properties. The domain can no longer bind conventional proline-rich peptides. There are key phosphorylation sites within the two hSH3 domains and it would appear that binding at these sites does not materially affect the folding of these regions although the equilibrium towards the unfolded state may be slightly altered. The binding partners of the hSH3 domains are still unknown.


Pssm-ID: 464216  Cd Length: 89  Bit Score: 62.70  E-value: 3.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885  419 KKFKITPPFQVMHQVKAKSDC---KGGKNDLSIKKGESIDIIRITDnpEGKWLGRNQDGLFGYVKTemvqinfSALknqa 495
Cdd:pfam14603   3 KKFKYDGEIKVLYSMTVDPNLtikKWGGKDLPVKPGEVLDVIQKTD--DTKVLCRNEEGKYGYVLR-------SNL---- 69

                          90
                  ....*....|....*.
gi 189533885  496 qsphgLENE-EVYDDV 510
Cdd:pfam14603  70 -----LQNDgEIYDDI 80
hSH3_ADAP cd11867
Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor ...
 411-479 3.95e-10

Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor Protein; ADAP, also called Fyn T-binding protein (FYB) or SLP-76-associated protein (SLAP), is expressed mainly in hematopoietic cells but not in B cells. It is required for the proliferation of mature T-cells and plays an important role in T-cell activation, TCR-induced integrin clustering, and T-cell adhesion. ADAP has been shown to bind many partners including SLP-76, Fyn, Src, SKAP1, SKAP2, dynein, Ena/VASP, Carma1, among others. It is connected to cytoskeleton via its binding to Ena and VASP, which impacts actin cytoskeletal remodeling upon TCR ligation. The SH3 domain of ADAP adopts an altered fold referred to as a helically extended SH3 (hSH3) domain characterized by clusters of positive charges. The hSH3 domain can no longer bind conventional proline-rich peptides, instead, it functions as a novel lipid interaction domain and can bind acidic lipids such as phosphatidylserine, phosphatidylinositol, phosphatidic acid, and polyphosphoinositides.


Pssm-ID: 212801  Cd Length: 77  Bit Score: 56.38  E-value: 3.95e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189533885 411 EKKEKDAIKKFKITPPFQVMHQVKAKSDC---KGGKNDLSIKKGESIDIIRITDnpEGKWLGRNQDGLFGYV 479
Cdd:cd11867    1 EKEEKEFRKKFKYNGEIKVLYSTTVLQTLtikKFGSKDLQVKPGESLEVIQHTD--DTKVLCRNEEGKYGYV 70
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 431-479 6.49e-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: 44.07  E-value: 6.49e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 189533885   431 HQVKAKSDCKG-GKNDLSIKKGESIDIIRITDnpEGKWLGRNQDGLFGYV 479
Cdd:smart00326   3 PQVRALYDYTAqDPDELSFKKGDIITVLEKSD--DGWWKGRLGRGKEGLF 50
PHA03247 PHA03247
large tegument protein UL36; Provisional
 32-357 8.53e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 8.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885   32 PVQPTLSSGPVVPSKKPvletslSGGATSTSTPPKPNFLKNTVNTARSAPDMPDPPKPKAFGNRFENMSENKGNKVPVKP 111
Cdd:PHA03247 2592 PPQSARPRAPVDDRGDP------RGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPR 2665

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885  112 KPPDSSLDPEPSKVP-FPKVPLQKPPSSIFANDTKDTSPKPLVSTTKPSWIKDIPK---AEVNGPTTPKMPSAPKPKSTM 187
Cdd:PHA03247 2666 RARRLGRAAQASSPPqRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLppgPAAARQASPALPAAPAPPAVP 2745

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885  188 AMLRQQPEENSNTESTVRSSPVSNVKPSSFRAKNSFTKLEEGVKDGAKASSTNESVSKPVAPIKPNFPKKAHGPPAQTvn 267
Cdd:PHA03247 2746 AGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAS-- 2823

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885  268 ddPSAPKKktlPNTYALGSAPSKPNRPPKVNLE---------KFKKGPevPTESPGPKNVTPPPPPAAHPSN-QVPPALP 337
Cdd:PHA03247 2824 --PAGPLP---PPTSAQPTAPPPPPGPPPPSLPlggsvapggDVRRRP--PSRSPAAKPAAPARPPVRRLARpAVSRSTE 2896

                         330       340
                  ....*....|....*....|
gi 189533885  338 SQPLPPSLPPRHPGPPIQDE 357
Cdd:PHA03247 2897 SFALPPDQPERPPQPQAPPP 2916
 
Name Accession Description Interval E-value
hSH3 pfam14603
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ...
 645-723 6.06e-40

Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion and de-granulation promoting adapter protein. It shows homology to SH3 domains; however, conserved residues of the fold are absent. It thus represents an altered SH3 domain fold. An N-terminal, amphipathic, helix makes extensive contacts to residues of the regular SH3 domain fold thereby creating a composite surface with unusual surface properties. The domain can no longer bind conventional proline-rich peptides. There are key phosphorylation sites within the two hSH3 domains and it would appear that binding at these sites does not materially affect the folding of these regions although the equilibrium towards the unfolded state may be slightly altered. The binding partners of the hSH3 domains are still unknown.


Pssm-ID: 464216  Cd Length: 89  Bit Score: 141.66  E-value: 6.06e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885  645 YDGEIQVLHQATI---ATSKKGSGKDLAVQAGETVDVISKSDPDKFICRNKEGKFGYVSLSNI-QTDDEVYDDIGDDCIY 720
Cdd:pfam14603   7 YDGEIKVLYSMTVdpnLTIKKWGGKDLPVKPGEVLDVIQKTDDTKVLCRNEEGKYGYVLRSNLlQNDGEIYDDIGDDCIY 86


                  ...
gi 189533885  721 DND 723
Cdd:pfam14603  87 DND 89
hSH3_ADAP cd11867
Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor ...
 645-706 5.54e-16

Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor Protein; ADAP, also called Fyn T-binding protein (FYB) or SLP-76-associated protein (SLAP), is expressed mainly in hematopoietic cells but not in B cells. It is required for the proliferation of mature T-cells and plays an important role in T-cell activation, TCR-induced integrin clustering, and T-cell adhesion. ADAP has been shown to bind many partners including SLP-76, Fyn, Src, SKAP1, SKAP2, dynein, Ena/VASP, Carma1, among others. It is connected to cytoskeleton via its binding to Ena and VASP, which impacts actin cytoskeletal remodeling upon TCR ligation. The SH3 domain of ADAP adopts an altered fold referred to as a helically extended SH3 (hSH3) domain characterized by clusters of positive charges. The hSH3 domain can no longer bind conventional proline-rich peptides, instead, it functions as a novel lipid interaction domain and can bind acidic lipids such as phosphatidylserine, phosphatidylinositol, phosphatidic acid, and polyphosphoinositides.


Pssm-ID: 212801  Cd Length: 77  Bit Score: 73.32  E-value: 5.54e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189533885 645 YDGEIQVLHQATIA---TSKKGSGKDLAVQAGETVDVISKSDPDKFICRNKEGKFGYVSLSNIQT 706
Cdd:cd11867   13 YNGEIKVLYSTTVLqtlTIKKFGSKDLQVKPGESLEVIQHTDDTKVLCRNEEGKYGYVLRSNLEP 77
hSH3 pfam14603
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ...
 419-510 3.47e-12

Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion and de-granulation promoting adapter protein. It shows homology to SH3 domains; however, conserved residues of the fold are absent. It thus represents an altered SH3 domain fold. An N-terminal, amphipathic, helix makes extensive contacts to residues of the regular SH3 domain fold thereby creating a composite surface with unusual surface properties. The domain can no longer bind conventional proline-rich peptides. There are key phosphorylation sites within the two hSH3 domains and it would appear that binding at these sites does not materially affect the folding of these regions although the equilibrium towards the unfolded state may be slightly altered. The binding partners of the hSH3 domains are still unknown.


Pssm-ID: 464216  Cd Length: 89  Bit Score: 62.70  E-value: 3.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885  419 KKFKITPPFQVMHQVKAKSDC---KGGKNDLSIKKGESIDIIRITDnpEGKWLGRNQDGLFGYVKTemvqinfSALknqa 495
Cdd:pfam14603   3 KKFKYDGEIKVLYSMTVDPNLtikKWGGKDLPVKPGEVLDVIQKTD--DTKVLCRNEEGKYGYVLR-------SNL---- 69

                          90
                  ....*....|....*.
gi 189533885  496 qsphgLENE-EVYDDV 510
Cdd:pfam14603  70 -----LQNDgEIYDDI 80
hSH3_ADAP cd11867
Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor ...
 411-479 3.95e-10

Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor Protein; ADAP, also called Fyn T-binding protein (FYB) or SLP-76-associated protein (SLAP), is expressed mainly in hematopoietic cells but not in B cells. It is required for the proliferation of mature T-cells and plays an important role in T-cell activation, TCR-induced integrin clustering, and T-cell adhesion. ADAP has been shown to bind many partners including SLP-76, Fyn, Src, SKAP1, SKAP2, dynein, Ena/VASP, Carma1, among others. It is connected to cytoskeleton via its binding to Ena and VASP, which impacts actin cytoskeletal remodeling upon TCR ligation. The SH3 domain of ADAP adopts an altered fold referred to as a helically extended SH3 (hSH3) domain characterized by clusters of positive charges. The hSH3 domain can no longer bind conventional proline-rich peptides, instead, it functions as a novel lipid interaction domain and can bind acidic lipids such as phosphatidylserine, phosphatidylinositol, phosphatidic acid, and polyphosphoinositides.


Pssm-ID: 212801  Cd Length: 77  Bit Score: 56.38  E-value: 3.95e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189533885 411 EKKEKDAIKKFKITPPFQVMHQVKAKSDC---KGGKNDLSIKKGESIDIIRITDnpEGKWLGRNQDGLFGYV 479
Cdd:cd11867    1 EKEEKEFRKKFKYNGEIKVLYSTTVLQTLtikKFGSKDLQVKPGESLEVIQHTD--DTKVLCRNEEGKYGYV 70
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 431-479 6.49e-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: 44.07  E-value: 6.49e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 189533885   431 HQVKAKSDCKG-GKNDLSIKKGESIDIIRITDnpEGKWLGRNQDGLFGYV 479
Cdd:smart00326   3 PQVRALYDYTAqDPDELSFKKGDIITVLEKSD--DGWWKGRLGRGKEGLF 50
PHA03247 PHA03247
large tegument protein UL36; Provisional
 32-357 8.53e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 8.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885   32 PVQPTLSSGPVVPSKKPvletslSGGATSTSTPPKPNFLKNTVNTARSAPDMPDPPKPKAFGNRFENMSENKGNKVPVKP 111
Cdd:PHA03247 2592 PPQSARPRAPVDDRGDP------RGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPR 2665

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885  112 KPPDSSLDPEPSKVP-FPKVPLQKPPSSIFANDTKDTSPKPLVSTTKPSWIKDIPK---AEVNGPTTPKMPSAPKPKSTM 187
Cdd:PHA03247 2666 RARRLGRAAQASSPPqRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLppgPAAARQASPALPAAPAPPAVP 2745

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885  188 AMLRQQPEENSNTESTVRSSPVSNVKPSSFRAKNSFTKLEEGVKDGAKASSTNESVSKPVAPIKPNFPKKAHGPPAQTvn 267
Cdd:PHA03247 2746 AGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAS-- 2823

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885  268 ddPSAPKKktlPNTYALGSAPSKPNRPPKVNLE---------KFKKGPevPTESPGPKNVTPPPPPAAHPSN-QVPPALP 337
Cdd:PHA03247 2824 --PAGPLP---PPTSAQPTAPPPPPGPPPPSLPlggsvapggDVRRRP--PSRSPAAKPAAPARPPVRRLARpAVSRSTE 2896

                         330       340
                  ....*....|....*....|
gi 189533885  338 SQPLPPSLPPRHPGPPIQDE 357
Cdd:PHA03247 2897 SFALPPDQPERPPQPQAPPP 2916
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 113-407 9.02e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 45.84  E-value: 9.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885 113 PPDSsldPEPSKVPfPKVPLQKPPSSIFANDTKDT----------SPKPLVSTTKPSWIKDIPKAEVngPTTPKMPSAPK 182
Cdd:PTZ00449 510 PPEG---PEASGLP-PKAPGDKEGEEGEHEDSKESdepkeggkpgETKEGEVGKKPGPAKEHKPSKI--PTLSKKPEFPK 583

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885 183 -PKSTmamlrQQPEENSNTESTVrsSPVSNVKPSSFRAKNSFTkleegVKDGAKASSTNESVSKPVAPIKPNFPKKAHGP 261
Cdd:PTZ00449 584 dPKHP-----KDPEEPKKPKRPR--SAQRPTRPKSPKLPELLD-----IPKSPKRPESPKSPKRPPPPQRPSSPERPEGP 651

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885 262 PAQTVNDDPSAPK-------KKTLPNTYALGSAPSKPNRPPKVNLEKFKKG-PEVPTESPGPKNVTPPPppaahpsnqVP 333
Cdd:PTZ00449 652 KIIKSPKPPKSPKppfdpkfKEKFYDDYLDAAAKSKETKTTVVLDESFESIlKETLPETPGTPFTTPRP---------LP 722

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885 334 PALPSQPLPPSLPPRHPGPPIQDENY-----DDVDCFRDQTNEGSGSDGEIYEDL--DDSRSSAAEPSQPQKKPEKDVKN 406
Cdd:PTZ00449 723 PKLPRDEEFPFEPIGDPDAEQPDDIEfftppEEERTFFHETPADTPLPDILAEEFkeEDIHAETGEPDEAMKRPDSPSEH 802


                 .
gi 189533885 407 Q 407
Cdd:PTZ00449 803 E 803
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 432-479 1.00e-04

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: 40.52  E-value: 1.00e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 189533885 432 QVKAKSDCKGGK-NDLSIKKGESIDIIRITDnpEGKWLGRNQDGLFGYV 479
Cdd:cd00174    1 YARALYDYEAQDdDELSFKKGDIITVLEKDD--DGWWEGELNGGREGLF 47
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 95-417 1.45e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 45.45  E-value: 1.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885  95 RFENMSENKGNKVPVKPKPPDSSLDPEPSKVPFPKVPLQKPpssifandtkdTSPKPLVSTTKPSWIK--DIPKAevngP 172
Cdd:PTZ00449 590 DPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESP-----------KSPKRPPPPQRPSSPErpEGPKI----I 654

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885 173 TTPKMPSAPKPKSTMAMLRQQPEENSNTESTVRSSPVSNVKPSSFRAKNSFTKLEegvkdgakASSTNESVSKPVAPIKP 252
Cdd:PTZ00449 655 KSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPE--------TPGTPFTTPRPLPPKLP 726

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885 253 NFPKKAHGPPAQTVNDDPSAPKKKTLPNTYALGSAPSKPNRP-PKVNLEKFK---------------KGPEVPTE-SPGP 315
Cdd:PTZ00449 727 RDEEFPFEPIGDPDAEQPDDIEFFTPPEEERTFFHETPADTPlPDILAEEFKeedihaetgepdeamKRPDSPSEhEDKP 806

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885 316 KNVTPPPPPAAHPSNQVPPALPSQPLPPSLPPRHP-GPPI---QDENYDDVDCFRDQT------------NEGSGSDGEI 379
Cdd:PTZ00449 807 PGDHPSLPKKRHRLDGLALSTTDLESDAGRIAKDAsGKIVklkRSKSFDDLTTVEEAEemgaearkivvdDDGTEADDED 886

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 189533885 380 YEDLDDSRSSAAEPSQPQKKPEKDVKNQKDREKKEKDA 417
Cdd:PTZ00449 887 THPPEEKHKSEVRRRRPPKKPSKPKKPSKPKKPKKPDS 924
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 64-247 8.36e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 8.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885   64 PPKPNFLKNTVNTARSAPDMPDPPKPKAFGNRFENMSENKGNKVPVKPKPPDSSLDPEPS-------KVPFPKVPLQKPP 136
Cdd:PRK10263  402 QPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTyqteqtyQQPAAQEPLYQQP 481

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885  137 SSIFANDTkdTSPKPLVSTTKPS-----WIKDIPKAEVNGPTTPKMPSAPKPKSTmamlrQQPEENSNTESTVRSSPVSN 211
Cdd:PRK10263  482 QPVEQQPV--VEPEPVVEETKPArpplyYFEEVEEKRAREREQLAAWYQPIPEPV-----KEPEPIKSSLKAPSVAAVPP 554

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 189533885  212 VKPSSfraknSFTKLEEGVKDGAKASSTNESVSKPV 247
Cdd:PRK10263  555 VEAAA-----AVSPLASGVKKATLATGAAATVAAPV 585
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 106-331 1.09e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 42.22  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885 106 KVPVK-PKPPDSSLDPEPSKVPfPKVPLQKPPSSIFAND---TKDTSPKPLVSTTKPSWIKDiPKAEVNGPTTPKMPSAP 181
Cdd:PLN03209 322 KIPSQrVPPKESDAADGPKPVP-TKPVTPEAPSPPIEEEppqPKAVVPRPLSPYTAYEDLKP-PTSPIPTPPSSSPASSK 399

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885 182 KPKSTMAMLRQQPEENSNTESTVRSSPVSNVKPSSFRAKNSFTKLEEgVKDGAKASSTNESVSKPVAPIKPNFPKKAHGP 261
Cdd:PLN03209 400 SVDAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRPLSPYARYED-LKPPTSPSPTAPTGVSPSVSSTSSVPAVPDTA 478

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885 262 PAQTVNDDPSAPKKKTLPNTYALGSAPSKPNRPPKvnlEKFKKGPEVPTESPGPKNVTPPPPPAAHPSNQ 331
Cdd:PLN03209 479 PATAATDAAAPPPANMRPLSPYAVYDDLKPPTSPS---PAAPVGKVAPSSTNEVVKVGNSAPPTALADEQ 545
PHA03247 PHA03247
large tegument protein UL36; Provisional
 112-353 1.83e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885  112 KPPDSSLDPEPSKVPF-PKVPLQKPPSSIFANdtkdTSPKPLVSTTKPSWIKDIPKAEVNGPTTPKMPSAPkPKSTMAML 190
Cdd:PHA03247 2700 DPPPPPPTPEPAPHALvSATPLPPGPAAARQA----SPALPAAPAPPAVPAGPATPGGPARPARPPTTAGP-PAPAPPAA 2774

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885  191 RQQPEENSNTESTVRSSPVSNVKPSSFRAKNSFTKLEEGVKDGAKASSTNESVSKPVAPIKPNFPKKAHGPPAQTVNDD- 269
Cdd:PHA03247 2775 PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGg 2854

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189533885  270 ---PSAPKKKTLPNtyalGSAPSKPNRPPKVNLEKFKK-GPEVPTES-PGPKNVTPPPPPAAHPSNQVPPALPSQPLPPS 344
Cdd:PHA03247 2855 svaPGGDVRRRPPS----RSPAAKPAAPARPPVRRLARpAVSRSTESfALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQ 2930


                  ....*....
gi 189533885  345 LPPRHPGPP 353
Cdd:PHA03247 2931 PPPPPPPRP 2939
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 434-479 3.51e-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: 36.03  E-value: 3.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 189533885  434 KAKSD-CKGGKNDLSIKKGESIDIIRitDNPEGKWLGRNQDGLFGYV 479
Cdd:pfam00018   1 VALYDyTAQEPDELSFKKGDIIIVLE--KSEDGWWKGRNKGGKEGLI 45
SH3_SNX9 cd11898
Src Homology 3 domain of Sorting nexin 9; Sorting nexin 9 (SNX9), also known as SH3PX1, is a ...
 428-487 3.74e-03

Src Homology 3 domain of Sorting nexin 9; Sorting nexin 9 (SNX9), also known as SH3PX1, is a cytosolic protein that interacts with proteins associated with clathrin-coated pits such as Cdc-42-associated tyrosine kinase 2 (ACK2). It binds class I polyproline sequences found in dynamin 1/2 and the WASP/N-WASP actin regulators. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis. Its array of interacting partners suggests that SNX9 functions at the interface between endocytosis and actin cytoskeletal organization. SNXs are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNX9 also contains BAR and SH3 domains. 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: 212831  Cd Length: 57  Bit Score: 36.38  E-value: 3.74e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189533885 428 QVMHQVKAKSdckgGKNDLSIKKGEsidIIRITD-NPEGKWL-GRNQDGLFGYVKTEMVQIN 487
Cdd:cd11898    3 RVLYDFAAEP----GNNELTVKEGE---IITVTNpNVGGGWIeAKNSQGERGLVPTDYVEIV 57
SH3_SH3TC cd11885
Src Homology 3 domain of SH3 domain and tetratricopeptide repeat-containing (SH3TC) proteins ...
 432-484 4.36e-03

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: 35.75  E-value: 4.36e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 189533885 432 QVKAKSDCKG-GKNDLSIKKGESIDIIRITdNPEGKWL-GRN-QDGLFGYVKTEMV 484
Cdd:cd11885    1 SCTAKMDFEGvEPGELSFRQGDSIEIIGDL-IPGLQWFvGRSkSSGRVGFVPTNHF 55
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 667-699 4.53e-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: 35.52  E-value: 4.53e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 189533885 667 DLAVQAGETVDVISKSDPDKFICRNKEGKFGYV 699
Cdd:cd00174   15 ELSFKKGDIITVLEKDDDGWWEGELNGGREGLF 47
SH3_Nck_3 cd11767
Third Src Homology 3 domain of Nck adaptor proteins; This group contains the third SH3 domain ...
 667-699 5.10e-03

Third Src Homology 3 domain of Nck adaptor proteins; This group contains the third SH3 domain of Nck, the first SH3 domain of Caenorhabditis elegans Ced-2 (Cell death abnormality protein 2), and similar domains. Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4), which show partly overlapping functions but also bind distinct targets. Their SH3 domains are involved in recruiting downstream effector molecules, such as the N-WASP/Arp2/3 complex, which when activated induces actin polymerization that results in the production of pedestals, or protrusions of the plasma membrane. The third SH3 domain of Nck appears to prefer ligands with a PxAPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. Ced-2 is a cell corpse engulfment protein that interacts with Ced-5 in a pathway that regulates the activation of Ced-10, a Rac small GTPase.


Pssm-ID: 212701 [Multi-domain]  Cd Length: 56  Bit Score: 35.75  E-value: 5.10e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 189533885 667 DLAVQAGETVDVISK--SDPDKFICRNKEGKFGYV 699
Cdd:cd11767   15 ELSFEKGERLEIIEKpeDDPDWWKARNALGTTGLV 49
SH3_Nck_3 cd11767
Third Src Homology 3 domain of Nck adaptor proteins; This group contains the third SH3 domain ...
 445-486 5.15e-03

Third Src Homology 3 domain of Nck adaptor proteins; This group contains the third SH3 domain of Nck, the first SH3 domain of Caenorhabditis elegans Ced-2 (Cell death abnormality protein 2), and similar domains. Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4), which show partly overlapping functions but also bind distinct targets. Their SH3 domains are involved in recruiting downstream effector molecules, such as the N-WASP/Arp2/3 complex, which when activated induces actin polymerization that results in the production of pedestals, or protrusions of the plasma membrane. The third SH3 domain of Nck appears to prefer ligands with a PxAPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. Ced-2 is a cell corpse engulfment protein that interacts with Ced-5 in a pathway that regulates the activation of Ced-10, a Rac small GTPase.


Pssm-ID: 212701 [Multi-domain]  Cd Length: 56  Bit Score: 35.75  E-value: 5.15e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 189533885 445 DLSIKKGESIDIIRITDNPEGKWLGRNQDGLFGYVKTEMVQI 486
Cdd:cd11767   15 ELSFEKGERLEIIEKPEDDPDWWKARNALGTTGLVPRNYVEV 56
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH