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Conserved domains on  [gi|688605399|ref|XP_009293646|]
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FYN-binding protein-like isoform X1 [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

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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 ...
 658-736 6.35e-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: 6.35e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399  658 YDGEIQVLHQATI---ATSKKGSGKDLAVQAGETVDVISKSDPDKFICRNKEGKFGYVSLSNI-QTDDEVYDDIGDDCIY 733
Cdd:pfam14603   7 YDGEIKVLYSMTVdpnLTIKKWGGKDLPVKPGEVLDVIQKTDDTKVLCRNEEGKYGYVLRSNLlQNDGEIYDDIGDDCIY 86


                  ...
gi 688605399  734 DND 736
Cdd:pfam14603  87 DND 89
hSH3 super family cl48258
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ...
 432-523 3.54e-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: 3.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399  432 KKFKITPPFQVMHQVKAKSDC---KGGKNDLSIKKGESIDIIRITDnpEGKWLGRNQDGLFGYVKTemvqinfSALknqa 508
Cdd:pfam14603   3 KKFKYDGEIKVLYSMTVDPNLtikKWGGKDLPVKPGEVLDVIQKTD--DTKVLCRNEEGKYGYVLR-------SNL---- 69

                          90
                  ....*....|....*.
gi 688605399  509 qsphgLENE-EVYDDV 523
Cdd:pfam14603  70 -----LQNDgEIYDDI 80
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 45-370 6.44e-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: 46.86  E-value: 6.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399   45 PVQPTLSSGPVVPSKKPvletslSGGATSTSTPPKPNFLKNTVNTARSAPDMPDPPKPKAFGNRFENMSENKGNKVPVKP 124
Cdd:PHA03247 2592 PPQSARPRAPVDDRGDP------RGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPR 2665

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399  125 KPPDSSLDPEPSKVP-FPKVPLQKPPSSIFANDTKDTSPKPLVSTTKPSWIKDIP---KAEVNGPTTPKMPSAPKPKSTM 200
Cdd:PHA03247 2666 RARRLGRAAQASSPPqRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPlppGPAAARQASPALPAAPAPPAVP 2745

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399  201 AMLRQQPEENSNTESTVRSSPVSNVKPSSFRAKNSFTKLEEGVKDGAKASSTNESVSKPVAPIKPNFPKKAHGPPAQTvn 280
Cdd:PHA03247 2746 AGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAS-- 2823

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399  281 ddPSAPKKktlPNTYALGSAPSKPNRPPKVNLE---------KFKKGPevPTESPGPKNVTPPPPPAAHPSN-QVPPALP 350
Cdd:PHA03247 2824 --PAGPLP---PPTSAQPTAPPPPPGPPPPSLPlggsvapggDVRRRP--PSRSPAAKPAAPARPPVRRLARpAVSRSTE 2896

                         330       340
                  ....*....|....*....|
gi 688605399  351 SQPLPPSLPPRHPGPPIQDE 370
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 ...
 658-736 6.35e-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: 6.35e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399  658 YDGEIQVLHQATI---ATSKKGSGKDLAVQAGETVDVISKSDPDKFICRNKEGKFGYVSLSNI-QTDDEVYDDIGDDCIY 733
Cdd:pfam14603   7 YDGEIKVLYSMTVdpnLTIKKWGGKDLPVKPGEVLDVIQKTDDTKVLCRNEEGKYGYVLRSNLlQNDGEIYDDIGDDCIY 86


                  ...
gi 688605399  734 DND 736
Cdd:pfam14603  87 DND 89
hSH3_ADAP cd11867
Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor ...
 658-719 6.73e-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: 72.94  E-value: 6.73e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688605399 658 YDGEIQVLHQATIA---TSKKGSGKDLAVQAGETVDVISKSDPDKFICRNKEGKFGYVSLSNIQT 719
Cdd:cd11867   13 YNGEIKVLYSTTVLqtlTIKKFGSKDLQVKPGESLEVIQHTDDTKVLCRNEEGKYGYVLRSNLEP 77
hSH3 pfam14603
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ...
 432-523 3.54e-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: 3.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399  432 KKFKITPPFQVMHQVKAKSDC---KGGKNDLSIKKGESIDIIRITDnpEGKWLGRNQDGLFGYVKTemvqinfSALknqa 508
Cdd:pfam14603   3 KKFKYDGEIKVLYSMTVDPNLtikKWGGKDLPVKPGEVLDVIQKTD--DTKVLCRNEEGKYGYVLR-------SNL---- 69

                          90
                  ....*....|....*.
gi 688605399  509 qsphgLENE-EVYDDV 523
Cdd:pfam14603  70 -----LQNDgEIYDDI 80
hSH3_ADAP cd11867
Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor ...
 424-492 4.52e-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: 4.52e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688605399 424 EKKEKDAIKKFKITPPFQVMHQVKAKSDC---KGGKNDLSIKKGESIDIIRITDnpEGKWLGRNQDGLFGYV 492
Cdd:cd11867    1 EKEEKEFRKKFKYNGEIKVLYSTTVLQTLtikKFGSKDLQVKPGESLEVIQHTD--DTKVLCRNEEGKYGYV 70
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 444-492 6.60e-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: 6.60e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 688605399   444 HQVKAKSDCKG-GKNDLSIKKGESIDIIRITDnpEGKWLGRNQDGLFGYV 492
Cdd:smart00326   3 PQVRALYDYTAqDPDELSFKKGDIITVLEKSD--DGWWKGRLGRGKEGLF 50
PHA03247 PHA03247
large tegument protein UL36; Provisional
 45-370 6.44e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 6.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399   45 PVQPTLSSGPVVPSKKPvletslSGGATSTSTPPKPNFLKNTVNTARSAPDMPDPPKPKAFGNRFENMSENKGNKVPVKP 124
Cdd:PHA03247 2592 PPQSARPRAPVDDRGDP------RGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPR 2665

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399  125 KPPDSSLDPEPSKVP-FPKVPLQKPPSSIFANDTKDTSPKPLVSTTKPSWIKDIP---KAEVNGPTTPKMPSAPKPKSTM 200
Cdd:PHA03247 2666 RARRLGRAAQASSPPqRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPlppGPAAARQASPALPAAPAPPAVP 2745

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399  201 AMLRQQPEENSNTESTVRSSPVSNVKPSSFRAKNSFTKLEEGVKDGAKASSTNESVSKPVAPIKPNFPKKAHGPPAQTvn 280
Cdd:PHA03247 2746 AGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAS-- 2823

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399  281 ddPSAPKKktlPNTYALGSAPSKPNRPPKVNLE---------KFKKGPevPTESPGPKNVTPPPPPAAHPSN-QVPPALP 350
Cdd:PHA03247 2824 --PAGPLP---PPTSAQPTAPPPPPGPPPPSLPlggsvapggDVRRRP--PSRSPAAKPAAPARPPVRRLARpAVSRSTE 2896

                         330       340
                  ....*....|....*....|
gi 688605399  351 SQPLPPSLPPRHPGPPIQDE 370
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 ...
 658-736 6.35e-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: 6.35e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399  658 YDGEIQVLHQATI---ATSKKGSGKDLAVQAGETVDVISKSDPDKFICRNKEGKFGYVSLSNI-QTDDEVYDDIGDDCIY 733
Cdd:pfam14603   7 YDGEIKVLYSMTVdpnLTIKKWGGKDLPVKPGEVLDVIQKTDDTKVLCRNEEGKYGYVLRSNLlQNDGEIYDDIGDDCIY 86


                  ...
gi 688605399  734 DND 736
Cdd:pfam14603  87 DND 89
hSH3_ADAP cd11867
Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor ...
 658-719 6.73e-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: 72.94  E-value: 6.73e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688605399 658 YDGEIQVLHQATIA---TSKKGSGKDLAVQAGETVDVISKSDPDKFICRNKEGKFGYVSLSNIQT 719
Cdd:cd11867   13 YNGEIKVLYSTTVLqtlTIKKFGSKDLQVKPGESLEVIQHTDDTKVLCRNEEGKYGYVLRSNLEP 77
hSH3 pfam14603
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ...
 432-523 3.54e-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: 3.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399  432 KKFKITPPFQVMHQVKAKSDC---KGGKNDLSIKKGESIDIIRITDnpEGKWLGRNQDGLFGYVKTemvqinfSALknqa 508
Cdd:pfam14603   3 KKFKYDGEIKVLYSMTVDPNLtikKWGGKDLPVKPGEVLDVIQKTD--DTKVLCRNEEGKYGYVLR-------SNL---- 69

                          90
                  ....*....|....*.
gi 688605399  509 qsphgLENE-EVYDDV 523
Cdd:pfam14603  70 -----LQNDgEIYDDI 80
hSH3_ADAP cd11867
Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor ...
 424-492 4.52e-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: 4.52e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688605399 424 EKKEKDAIKKFKITPPFQVMHQVKAKSDC---KGGKNDLSIKKGESIDIIRITDnpEGKWLGRNQDGLFGYV 492
Cdd:cd11867    1 EKEEKEFRKKFKYNGEIKVLYSTTVLQTLtikKFGSKDLQVKPGESLEVIQHTD--DTKVLCRNEEGKYGYV 70
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 444-492 6.60e-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: 6.60e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 688605399   444 HQVKAKSDCKG-GKNDLSIKKGESIDIIRITDnpEGKWLGRNQDGLFGYV 492
Cdd:smart00326   3 PQVRALYDYTAqDPDELSFKKGDIITVLEKSD--DGWWKGRLGRGKEGLF 50
PHA03247 PHA03247
large tegument protein UL36; Provisional
 45-370 6.44e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 6.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399   45 PVQPTLSSGPVVPSKKPvletslSGGATSTSTPPKPNFLKNTVNTARSAPDMPDPPKPKAFGNRFENMSENKGNKVPVKP 124
Cdd:PHA03247 2592 PPQSARPRAPVDDRGDP------RGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPR 2665

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399  125 KPPDSSLDPEPSKVP-FPKVPLQKPPSSIFANDTKDTSPKPLVSTTKPSWIKDIP---KAEVNGPTTPKMPSAPKPKSTM 200
Cdd:PHA03247 2666 RARRLGRAAQASSPPqRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPlppGPAAARQASPALPAAPAPPAVP 2745

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399  201 AMLRQQPEENSNTESTVRSSPVSNVKPSSFRAKNSFTKLEEGVKDGAKASSTNESVSKPVAPIKPNFPKKAHGPPAQTvn 280
Cdd:PHA03247 2746 AGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAS-- 2823

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399  281 ddPSAPKKktlPNTYALGSAPSKPNRPPKVNLE---------KFKKGPevPTESPGPKNVTPPPPPAAHPSN-QVPPALP 350
Cdd:PHA03247 2824 --PAGPLP---PPTSAQPTAPPPPPGPPPPSLPlggsvapggDVRRRP--PSRSPAAKPAAPARPPVRRLARpAVSRSTE 2896

                         330       340
                  ....*....|....*....|
gi 688605399  351 SQPLPPSLPPRHPGPPIQDE 370
Cdd:PHA03247 2897 SFALPPDQPERPPQPQAPPP 2916
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 126-420 6.80e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 46.61  E-value: 6.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399 126 PPDSsldPEPSKVPfPKVPLQKPPSSIFANDTKDT----------SPKPLVSTTKPSWIKDIPKAEVngPTTPKMPSAPK 195
Cdd:PTZ00449 510 PPEG---PEASGLP-PKAPGDKEGEEGEHEDSKESdepkeggkpgETKEGEVGKKPGPAKEHKPSKI--PTLSKKPEFPK 583

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399 196 -PKSTmamlrQQPEENSNTESTVrsSPVSNVKPSSFRAKNSFTkleegVKDGAKASSTNESVSKPVAPIKPNFPKKAHGP 274
Cdd:PTZ00449 584 dPKHP-----KDPEEPKKPKRPR--SAQRPTRPKSPKLPELLD-----IPKSPKRPESPKSPKRPPPPQRPSSPERPEGP 651

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399 275 PAQTVNDDPSAPK-------KKTLPNTYALGSAPSKPNRPPKVNLEKFKKG-PEVPTESPGPKNVTPPPppaahpsnqVP 346
Cdd:PTZ00449 652 KIIKSPKPPKSPKppfdpkfKEKFYDDYLDAAAKSKETKTTVVLDESFESIlKETLPETPGTPFTTPRP---------LP 722

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399 347 PALPSQPLPPSLPPRHPGPPIQDENY-----DDVDCFRDQTNEGSGSDGEIYEDL--DDSRSSAAEPSQPQKKPEKDVKN 419
Cdd:PTZ00449 723 PKLPRDEEFPFEPIGDPDAEQPDDIEfftppEEERTFFHETPADTPLPDILAEEFkeEDIHAETGEPDEAMKRPDSPSEH 802


                 .
gi 688605399 420 Q 420
Cdd:PTZ00449 803 E 803
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 445-492 1.02e-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: 1.02e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 688605399 445 QVKAKSDCKGGK-NDLSIKKGESIDIIRITDnpEGKWLGRNQDGLFGYV 492
Cdd:cd00174    1 YARALYDYEAQDdDELSFKKGDIITVLEKDD--DGWWEGELNGGREGLF 47
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 108-430 1.29e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 45.45  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399 108 RFENMSENKGNKVPVKPKPPDSSLDPEPSKVPFPKVPLQKPpssifandtkdTSPKPLVSTTKPSWIK--DIPKAevngP 185
Cdd:PTZ00449 590 DPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESP-----------KSPKRPPPPQRPSSPErpEGPKI----I 654

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399 186 TTPKMPSAPKPKSTMAMLRQQPEENSNTESTVRSSPVSNVKPSSFRAKNSFTKLEegvkdgakASSTNESVSKPVAPIKP 265
Cdd:PTZ00449 655 KSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPE--------TPGTPFTTPRPLPPKLP 726

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399 266 NFPKKAHGPPAQTVNDDPSAPKKKTLPNTYALGSAPSKPNRP-PKVNLEKFK---------------KGPEVPTE-SPGP 328
Cdd:PTZ00449 727 RDEEFPFEPIGDPDAEQPDDIEFFTPPEEERTFFHETPADTPlPDILAEEFKeedihaetgepdeamKRPDSPSEhEDKP 806

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399 329 KNVTPPPPPAAHPSNQVPPALPSQPLPPSLPPRHP-GPPI---QDENYDDVDCFRDQT------------NEGSGSDGEI 392
Cdd:PTZ00449 807 PGDHPSLPKKRHRLDGLALSTTDLESDAGRIAKDAsGKIVklkRSKSFDDLTTVEEAEemgaearkivvdDDGTEADDED 886

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 688605399 393 YEDLDDSRSSAAEPSQPQKKPEKDVKNQKDREKKEKDA 430
Cdd:PTZ00449 887 THPPEEKHKSEVRRRRPPKKPSKPKKPSKPKKPKKPDS 924
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 77-260 7.34e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.15  E-value: 7.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399   77 PPKPNFLKNTVNTARSAPDMPDPPKPKAFGNRFENMSENKGNKVPVKPKPPDSSLDPEPS-------KVPFPKVPLQKPP 149
Cdd:PRK10263  402 QPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTyqteqtyQQPAAQEPLYQQP 481

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399  150 SSIFANDTkdTSPKPLVSTTKPS-----WIKDIPKAEVNGPTTPKMPSAPKPKSTmamlrQQPEENSNTESTVRSSPVSN 224
Cdd:PRK10263  482 QPVEQQPV--VEPEPVVEETKPArpplyYFEEVEEKRAREREQLAAWYQPIPEPV-----KEPEPIKSSLKAPSVAAVPP 554

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 688605399  225 VKPSSfraknSFTKLEEGVKDGAKASSTNESVSKPV 260
Cdd:PRK10263  555 VEAAA-----AVSPLASGVKKATLATGAAATVAAPV 585
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 119-344 9.63e-04

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 42.61  E-value: 9.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399 119 KVPVK-PKPPDSSLDPEPSKVPfPKVPLQKPPSSIFAND---TKDTSPKPLVSTTKPSWIKDiPKAEVNGPTTPKMPSAP 194
Cdd:PLN03209 322 KIPSQrVPPKESDAADGPKPVP-TKPVTPEAPSPPIEEEppqPKAVVPRPLSPYTAYEDLKP-PTSPIPTPPSSSPASSK 399

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399 195 KPKSTMAMLRQQPEENSNTESTVRSSPVSNVKPSSFRAKNSFTKLEEgVKDGAKASSTNESVSKPVAPIKPNFPKKAHGP 274
Cdd:PLN03209 400 SVDAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRPLSPYARYED-LKPPTSPSPTAPTGVSPSVSSTSSVPAVPDTA 478

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399 275 PAQTVNDDPSAPKKKTLPNTYALGSAPSKPNRPPKvnlEKFKKGPEVPTESPGPKNVTPPPPPAAHPSNQ 344
Cdd:PLN03209 479 PATAATDAAAPPPANMRPLSPYAVYDDLKPPTSPS---PAAPVGKVAPSSTNEVVKVGNSAPPTALADEQ 545
PHA03247 PHA03247
large tegument protein UL36; Provisional
 13-366 1.21e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399   13 SEDNKSDVKAIMARFQAGGASvDGAPNVRLKPPVQPTLSSGPVVPSKKPVLETSLSGGATSTSTPPKPNFLKNT----VN 88
Cdd:PHA03247 2584 SRARRPDAPPQSARPRAPVDD-RGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPapgrVS 2662

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399   89 TARSAPDMPDPPKPKAFGNRFENmsenKGNKVPVKP-----KPPDSSLDPEPSKVPF-PKVPLQKPPSSIFANdtkdTSP 162
Cdd:PHA03247 2663 RPRRARRLGRAAQASSPPQRPRR----RAARPTVGSltslaDPPPPPPTPEPAPHALvSATPLPPGPAAARQA----SPA 2734

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399  163 KPLVSTTKPSWIKDIPKAEVNGPTTPKMPSAPkPKSTMAMLRQQPEENSNTESTVRSSPVSNVKPSSFRAKNSFTKLEEG 242
Cdd:PHA03247 2735 LPAAPAPPAVPAGPATPGGPARPARPPTTAGP-PAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLA 2813

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688605399  243 VKDGAKASSTNESVSKPVAPIKPNFPKKAHGPPAQTVNDD----PSAPKKKTLPNtyalGSAPSKPNRPPKVNLEKFKK- 317
Cdd:PHA03247 2814 PAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGgsvaPGGDVRRRPPS----RSPAAKPAAPARPPVRRLARp 2889

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 688605399  318 GPEVPTES-PGPKNVTPPPPPAAHPSNQVPPALPSQPLPPSLPPRHPGPP 366
Cdd:PHA03247 2890 AVSRSTESfALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRP 2939
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 447-492 3.58e-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: 3.58e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 688605399  447 KAKSD-CKGGKNDLSIKKGESIDIIRitDNPEGKWLGRNQDGLFGYV 492
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 ...
 441-500 4.42e-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: 35.99  E-value: 4.42e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688605399 441 QVMHQVKAKSdckgGKNDLSIKKGEsidIIRITD-NPEGKWL-GRNQDGLFGYVKTEMVQIN 500
Cdd:cd11898    3 RVLYDFAAEP----GNNELTVKEGE---IITVTNpNVGGGWIeAKNSQGERGLVPTDYVEIV 57
SH3_SH3TC cd11885
Src Homology 3 domain of SH3 domain and tetratricopeptide repeat-containing (SH3TC) proteins ...
 445-497 4.44e-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: 4.44e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 688605399 445 QVKAKSDCKG-GKNDLSIKKGESIDIIRITdNPEGKWL-GRN-QDGLFGYVKTEMV 497
Cdd:cd11885    1 SCTAKMDFEGvEPGELSFRQGDSIEIIGDL-IPGLQWFvGRSkSSGRVGFVPTNHF 55
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 680-712 4.61e-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: 4.61e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 688605399 680 DLAVQAGETVDVISKSDPDKFICRNKEGKFGYV 712
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 ...
 680-712 5.35e-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: 5.35e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 688605399 680 DLAVQAGETVDVISK--SDPDKFICRNKEGKFGYV 712
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 ...
 458-499 5.57e-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: 5.57e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 688605399 458 DLSIKKGESIDIIRITDNPEGKWLGRNQDGLFGYVKTEMVQI 499
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.
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