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Conserved domains on  [gi|392887538|ref|NP_001252089|]
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DOCKER domain-containing protein [Caenorhabditis elegans]

Protein Classification

DHR2_DOCK domain-containing protein( domain architecture ID 10184840)

DHR2_DOCK domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DHR2_DOCK cd11684
Dock Homology Region 2, a GEF domain, of Dedicator of Cytokinesis proteins; DOCK proteins ...
799-1230 1.55e-92

Dock Homology Region 2, a GEF domain, of Dedicator of Cytokinesis proteins; DOCK proteins comprise a family of atypical guanine nucleotide exchange factors (GEFs) that lack the conventional Dbl homology (DH) domain. As GEFs, they activate the small GTPases Rac and Cdc42 by exchanging bound GDP for free GTP. They are also called the CZH (CED-5, Dock180, and MBC-zizimin homology) family, after the first family members identified. Dock180 was first isolated as a binding partner for the adaptor protein Crk. The Caenorhabditis elegans protein, Ced-5, is essential for cell migration and phagocytosis, while the Drosophila ortholog, Myoblast city (MBC), is necessary for myoblast fusion and dorsal closure. DOCKs are divided into four classes (A-D) based on sequence similarity and domain architecture: class A includes Dock1 (or Dock180), 2 and 5; class B includes Dock3 and 4; class C includes Dock6, 7, and 8; and class D includes Dock9, 10 and 11. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1, and DHR-2 (also called CZH2 or Docker). This alignment model represents the DHR-2 domain of DOCK proteins, which contains the catalytic GEF activity for Rac and/or Cdc42.


:

Pssm-ID: 212566 [Multi-domain]  Cd Length: 392  Bit Score: 303.45  E-value: 1.55e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  799 LRSAWFDTLAEIYEQDRWFAEASVCHAHSVAIIAreleerkelevdwrvfdWINNRIAETEQSqggdaGSVQPAGFTTDN 878
Cdd:cd11684     2 LYIRYLHKLADLHEERGNYVEAALCLLLHADLYA-----------------WDLKALVPALAE-----SLSFPEQTSFER 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  879 LGAKIDKTAAALMLAERFEAVGPLYRLIVPVLEKNMNFTSLVSVYAELQQTYSRAAEVrssgKRHLGAYFRVRFNGERHF 958
Cdd:cd11684    60 KEALYKKAIDLFDKGKAWEFAIALYKELIPQYENNFDYAKLSEVHRKIAKLYEKIAEK----DRLFPTYFRVGFYGKGFP 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  959 GSEHNTDWIYREAGLTSLAAFALEIKEKCQrqvghDRVQIEANEQLDLSKIDPTVAYVQITHVEPSIP--AAAGIADQHR 1036
Cdd:cd11684   136 ESLRGKEFIYRGPEFERLGDFCERLKSLYP-----GAEIIQSSEEPDDEILDSEGQYIQITSVEPYFDdeDLVSRAAPGV 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1037 NDFLVHTNLSEFSYECATIENERKvsKEPAIHEQCLKRTVLRVSPSpvsedsraatgFPATRRRLPVISVHFEQFSPLEF 1116
Cdd:cd11684   211 RQFYRNNNINTFVYERPFTKGGKK--SQNEITDQWKERTILTTEES-----------FPTILRRSEVVSIEEIELSPIEN 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1117 ACQKLNTKAEQIRKTLNAASNGRQLDVKGLQLLLQGAVLPTVNAGPLAYAEVFTKEEQRERYGDDGLV-KLRESFRNLMN 1195
Cdd:cd11684   278 AIEDIEKKTEELRSLINKYRSGDSPNVNPLQMLLQGTVDAAVNGGPVAYAEAFLSEEYLSNYPEAEKVkKLKEAFEEFLE 357
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 392887538 1196 SCQLAIEANASAIGSDQQTYHEVLVSSFDAMHERL 1230
Cdd:cd11684   358 ILKRGLALHAKLCPPEMAPLHEELEEGFEKLFKEL 392
 
Name Accession Description Interval E-value
DHR2_DOCK cd11684
Dock Homology Region 2, a GEF domain, of Dedicator of Cytokinesis proteins; DOCK proteins ...
799-1230 1.55e-92

Dock Homology Region 2, a GEF domain, of Dedicator of Cytokinesis proteins; DOCK proteins comprise a family of atypical guanine nucleotide exchange factors (GEFs) that lack the conventional Dbl homology (DH) domain. As GEFs, they activate the small GTPases Rac and Cdc42 by exchanging bound GDP for free GTP. They are also called the CZH (CED-5, Dock180, and MBC-zizimin homology) family, after the first family members identified. Dock180 was first isolated as a binding partner for the adaptor protein Crk. The Caenorhabditis elegans protein, Ced-5, is essential for cell migration and phagocytosis, while the Drosophila ortholog, Myoblast city (MBC), is necessary for myoblast fusion and dorsal closure. DOCKs are divided into four classes (A-D) based on sequence similarity and domain architecture: class A includes Dock1 (or Dock180), 2 and 5; class B includes Dock3 and 4; class C includes Dock6, 7, and 8; and class D includes Dock9, 10 and 11. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1, and DHR-2 (also called CZH2 or Docker). This alignment model represents the DHR-2 domain of DOCK proteins, which contains the catalytic GEF activity for Rac and/or Cdc42.


Pssm-ID: 212566 [Multi-domain]  Cd Length: 392  Bit Score: 303.45  E-value: 1.55e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  799 LRSAWFDTLAEIYEQDRWFAEASVCHAHSVAIIAreleerkelevdwrvfdWINNRIAETEQSqggdaGSVQPAGFTTDN 878
Cdd:cd11684     2 LYIRYLHKLADLHEERGNYVEAALCLLLHADLYA-----------------WDLKALVPALAE-----SLSFPEQTSFER 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  879 LGAKIDKTAAALMLAERFEAVGPLYRLIVPVLEKNMNFTSLVSVYAELQQTYSRAAEVrssgKRHLGAYFRVRFNGERHF 958
Cdd:cd11684    60 KEALYKKAIDLFDKGKAWEFAIALYKELIPQYENNFDYAKLSEVHRKIAKLYEKIAEK----DRLFPTYFRVGFYGKGFP 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  959 GSEHNTDWIYREAGLTSLAAFALEIKEKCQrqvghDRVQIEANEQLDLSKIDPTVAYVQITHVEPSIP--AAAGIADQHR 1036
Cdd:cd11684   136 ESLRGKEFIYRGPEFERLGDFCERLKSLYP-----GAEIIQSSEEPDDEILDSEGQYIQITSVEPYFDdeDLVSRAAPGV 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1037 NDFLVHTNLSEFSYECATIENERKvsKEPAIHEQCLKRTVLRVSPSpvsedsraatgFPATRRRLPVISVHFEQFSPLEF 1116
Cdd:cd11684   211 RQFYRNNNINTFVYERPFTKGGKK--SQNEITDQWKERTILTTEES-----------FPTILRRSEVVSIEEIELSPIEN 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1117 ACQKLNTKAEQIRKTLNAASNGRQLDVKGLQLLLQGAVLPTVNAGPLAYAEVFTKEEQRERYGDDGLV-KLRESFRNLMN 1195
Cdd:cd11684   278 AIEDIEKKTEELRSLINKYRSGDSPNVNPLQMLLQGTVDAAVNGGPVAYAEAFLSEEYLSNYPEAEKVkKLKEAFEEFLE 357
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 392887538 1196 SCQLAIEANASAIGSDQQTYHEVLVSSFDAMHERL 1230
Cdd:cd11684   358 ILKRGLALHAKLCPPEMAPLHEELEEGFEKLFKEL 392
DHR-2_Lobe_C pfam20421
DHR-2, Lobe C; DOCK (dedicator of cytokinesis) proteins are guanine nucleotide exchange ...
1132-1233 6.86e-27

DHR-2, Lobe C; DOCK (dedicator of cytokinesis) proteins are guanine nucleotide exchange factors (GEFs) that activate some small GTPases, such as Rac or Cdc42, by exchanging bound GDP for free GTP to control cell migration, morphogenesis, and phagocytosis. These proteins share a DOCK-type C2 domain (also termed the DOCK-homology region (DHR)-1) at the N-terminal, and the DHR-2 domain (also termed the DOCKER domain) at the C-terminal. DHR-2 is the GEF catalytic domain organized into three lobes A, B and C, with the Rho-family binding site and catalytic centre generated entirely from lobes B and C. This entry represents Lobe C which form an antiparallel four alpha-helical bundle and contains a loop known as the nucleotide sensor characterized by a conserved valine residue essential for catalytic activity.


Pssm-ID: 466570 [Multi-domain]  Cd Length: 103  Bit Score: 105.75  E-value: 6.86e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  1132 LNAASNGRQLDVKGLQLLLQGAVLPTVNAGPLAYAEVFTKEEQRERYGDDGLVKLRESFRNLMNSCQLAIEANASAIGSD 1211
Cdd:pfam20421    2 LEAAINAPPPNIKTLQMVLQGSVDVQVNAGPLEYAEAFLSEKNVDNYPAEKVEKLKEEFRDFLKVCGEALRLNKKLISED 81
                           90       100
                   ....*....|....*....|..
gi 392887538  1212 QQTYHEVLVSSFDAMHERLQTF 1233
Cdd:pfam20421   82 QREYQEELEEGFEKLKEKLEPY 103
 
Name Accession Description Interval E-value
DHR2_DOCK cd11684
Dock Homology Region 2, a GEF domain, of Dedicator of Cytokinesis proteins; DOCK proteins ...
799-1230 1.55e-92

Dock Homology Region 2, a GEF domain, of Dedicator of Cytokinesis proteins; DOCK proteins comprise a family of atypical guanine nucleotide exchange factors (GEFs) that lack the conventional Dbl homology (DH) domain. As GEFs, they activate the small GTPases Rac and Cdc42 by exchanging bound GDP for free GTP. They are also called the CZH (CED-5, Dock180, and MBC-zizimin homology) family, after the first family members identified. Dock180 was first isolated as a binding partner for the adaptor protein Crk. The Caenorhabditis elegans protein, Ced-5, is essential for cell migration and phagocytosis, while the Drosophila ortholog, Myoblast city (MBC), is necessary for myoblast fusion and dorsal closure. DOCKs are divided into four classes (A-D) based on sequence similarity and domain architecture: class A includes Dock1 (or Dock180), 2 and 5; class B includes Dock3 and 4; class C includes Dock6, 7, and 8; and class D includes Dock9, 10 and 11. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1, and DHR-2 (also called CZH2 or Docker). This alignment model represents the DHR-2 domain of DOCK proteins, which contains the catalytic GEF activity for Rac and/or Cdc42.


Pssm-ID: 212566 [Multi-domain]  Cd Length: 392  Bit Score: 303.45  E-value: 1.55e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  799 LRSAWFDTLAEIYEQDRWFAEASVCHAHSVAIIAreleerkelevdwrvfdWINNRIAETEQSqggdaGSVQPAGFTTDN 878
Cdd:cd11684     2 LYIRYLHKLADLHEERGNYVEAALCLLLHADLYA-----------------WDLKALVPALAE-----SLSFPEQTSFER 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  879 LGAKIDKTAAALMLAERFEAVGPLYRLIVPVLEKNMNFTSLVSVYAELQQTYSRAAEVrssgKRHLGAYFRVRFNGERHF 958
Cdd:cd11684    60 KEALYKKAIDLFDKGKAWEFAIALYKELIPQYENNFDYAKLSEVHRKIAKLYEKIAEK----DRLFPTYFRVGFYGKGFP 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  959 GSEHNTDWIYREAGLTSLAAFALEIKEKCQrqvghDRVQIEANEQLDLSKIDPTVAYVQITHVEPSIP--AAAGIADQHR 1036
Cdd:cd11684   136 ESLRGKEFIYRGPEFERLGDFCERLKSLYP-----GAEIIQSSEEPDDEILDSEGQYIQITSVEPYFDdeDLVSRAAPGV 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1037 NDFLVHTNLSEFSYECATIENERKvsKEPAIHEQCLKRTVLRVSPSpvsedsraatgFPATRRRLPVISVHFEQFSPLEF 1116
Cdd:cd11684   211 RQFYRNNNINTFVYERPFTKGGKK--SQNEITDQWKERTILTTEES-----------FPTILRRSEVVSIEEIELSPIEN 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1117 ACQKLNTKAEQIRKTLNAASNGRQLDVKGLQLLLQGAVLPTVNAGPLAYAEVFTKEEQRERYGDDGLV-KLRESFRNLMN 1195
Cdd:cd11684   278 AIEDIEKKTEELRSLINKYRSGDSPNVNPLQMLLQGTVDAAVNGGPVAYAEAFLSEEYLSNYPEAEKVkKLKEAFEEFLE 357
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 392887538 1196 SCQLAIEANASAIGSDQQTYHEVLVSSFDAMHERL 1230
Cdd:cd11684   358 ILKRGLALHAKLCPPEMAPLHEELEEGFEKLFKEL 392
DHR2_DOCK_D cd11694
Dock Homology Region 2, a GEF domain, of Class D Dedicator of Cytokinesis proteins; DOCK ...
799-1230 1.24e-76

Dock Homology Region 2, a GEF domain, of Class D Dedicator of Cytokinesis proteins; DOCK proteins are atypical guanine nucleotide exchange factors (GEFs) that lack the conventional Dbl homology (DH) domain. As GEFs, they activate small GTPases by exchanging bound GDP for free GTP. They are divided into four classes (A-D) based on sequence similarity and domain architecture; class D, also called the Zizimin subfamily, includes Dock9, 10 and 11. Class D Docks are specific GEFs for Cdc42. Dock9 plays important roles in spine formation and dendritic growth. Dock10 and Dock11 are preferentially expressed in lymphocytes. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of class D DOCKs, which contains the catalytic GEF activity for Cdc42. Class D DOCKs also contain a Pleckstrin homology (PH) domain at the N-terminus.


Pssm-ID: 212567  Cd Length: 376  Bit Score: 258.42  E-value: 1.24e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  799 LRSAWFDTLAEIYEQDRWFAEASVCHAHSVAIIARELEERkelevdwrvfdwinnriaeteqsqggdagsvqpagfttDN 878
Cdd:cd11694     2 LRKTWLESMARIHEKNGNFSEAAMCYIHIAALVAEYLKRK--------------------------------------DL 43
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  879 LGAKIDKTAAALMLAERFEAVGPLYRLIVPVLEKNMNFTSLVSVYAELQQTYSRAAEVRSSGKRHLGAYFRVRFNGERHF 958
Cdd:cd11694    44 LLELLEACVEGLWKAERYELLGELYKLIIPIYEKRRDFEQLADCYRTLHRAYEKVVEVMESGKRLLGTYYRVAFYGQAFF 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  959 GSEHNTDWIYREAGLTSLAafalEIKEKCQRQ----VGHDRVQ-IEANEQLDLSKIDPTVAYVQITHVEPSIPAAAgiAD 1033
Cdd:cd11694   124 EEEDGKEYIYKEPKVTSLS----EISERLLKLygdkFGSENVKlIQDSGKVNPKDLDPKYAYIQVTHVTPYFDEKE--LE 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1034 QHRNDFLVHTNLSEFSYECATIENERKVSkepAIHEQCLKRTVLRVSPSpvsedsraatgFPATRRRLPVISVHFEQFSP 1113
Cdd:cd11694   198 DRKTEFERNHNIRRFVFETPFTLSGKARG---AVEEQWKRRTILTTSHS-----------FPYVKKRIPVVQREIIELSP 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1114 LEFACQKLNTKAEQIRKTLNAAsngrQLDVKGLQLLLQGAVLPTVNAGPLAYAEVFTKEEQRERYGDDGLVKLRESFRNL 1193
Cdd:cd11694   264 IEVAIDEMQSKVKELEELISTE----PVDMKKLQLRLQGSVSVQVNAGPLAYARAFLEPTTVKNYPDDQVEDLKDVFRDF 339
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 392887538 1194 MNSCQLAIEANASAIGSDQQTYHEVLVSSFDAMHERL 1230
Cdd:cd11694   340 IKACGQALELNERLIKEDQREYHEVLKENYRKMVKEL 376
DHR2_DOCK11 cd11700
Dock Homology Region 2, a GEF domain, of Class D Dedicator of Cytokinesis 11; Dock11, also ...
799-1230 5.21e-67

Dock Homology Region 2, a GEF domain, of Class D Dedicator of Cytokinesis 11; Dock11, also called Zizimin2 or activated Cdc42-associated GEF (ACG), is an atypical guanine nucleotide exchange factor (GEF) that lacks the conventional Dbl homology (DH) domain. As a GEF, it activates the small GTPase Cdc42 by exchanging bound GDP for free GTP. Dock11 is predominantly expressed in lymphocytes and is found in high levels in germinal center B lymphocytes after T cell dependent antigen immunization. DOCK proteins are divided into four classes (A-D) based on sequence similarity and domain architecture; class D includes Dock9, 10 and 11. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of Dock11, which contains the catalytic GEF activity for Cdc42. Class D DOCKs also contain a Pleckstrin homology (PH) domain at the N-terminus.


Pssm-ID: 212573  Cd Length: 413  Bit Score: 232.58  E-value: 5.21e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  799 LRSAWFDTLAEIYEQDRWFAEASVCHAHSVAIIARELEERKELEVDWRVFDWINNRIAEtEQSQGGDAGsVQPAGFTTDN 878
Cdd:cd11700     3 LRKTWLDSMAKIHVKNGDFSEAAMCYVHVAALVAEFLHRKKLFPSGCAAFKKITPNIDE-EGAMKEDIG-MMDVHYSEEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  879 LGAKIDKTAAALMLAERFEAVGPLYRLIVPVLEKNMNFTSLVSVYAELQQTYSRAAEVRSSGKRHLGAYFRVRFNGERHF 958
Cdd:cd11700    81 LVELLEQCVDGLWKAERYELISEISKLIIPIYEKRREFEKLTQLYRTLHGAYAKILEVMHTGKRLLGTFFRVAFYGQGFF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  959 GSEHNTDWIYREAGLTSLAAFALEIKEKCQRQVGHDRVQ-IEANEQLDLSKIDPTVAYVQITHVEPSIPAAAgiADQHRN 1037
Cdd:cd11700   161 EEEDGKEYIYKEPKLTGLSEISHRLLKLYGEKFGSENVKiIQDSNKVNQKDLDPKYAHIQVTYVKPYFDDKE--MAERKT 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1038 DFLVHTNLSEFSYECA-TIENErkvsKEPAIHEQCLKRTVLRVSPSpvsedsraatgFPATRRRLPVISVHFEQFSPLEF 1116
Cdd:cd11700   239 EFERNHNIQRFVFETPyTLSGK----KQGGVEEQCKRRTILTTANS-----------FPYVKKRIPVNGEKQTNLKPIDV 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1117 ACQKLNTKAEQIRKTLNAAsngrQLDVKGLQLLLQGAVLPTVNAGPLAYAEVFTKEEQRERYGDDGLVKLRESFRNLMNS 1196
Cdd:cd11700   304 ATDEIKDKTAELQKLCSNQ----DVDMIQLQLKLQGCVSVQVNAGPLAYARAFLDDSQASKYPNKKVKELKEMFRKFIQA 379
                         410       420       430
                  ....*....|....*....|....*....|....
gi 392887538 1197 CQLAIEANASAIGSDQQTYHEVLVSSFDAMHERL 1230
Cdd:cd11700   380 CSIALELNERLIKEDQVEYHEGLKSNFRDMVKEL 413
DHR2_DOCK9 cd11698
Dock Homology Region 2, a GEF domain, of Class D Dedicator of Cytokinesis 9; Dock9, also ...
799-1230 1.19e-65

Dock Homology Region 2, a GEF domain, of Class D Dedicator of Cytokinesis 9; Dock9, also called Zizimin1, is an atypical guanine nucleotide exchange factor (GEF) that lacks the conventional Dbl homology (DH) domain. As a GEF, it activates the small GTPase Cdc42 by exchanging bound GDP for free GTP. It plays important roles in spine formation and dendritic growth. DOCK proteins are divided into four classes (A-D) based on sequence similarity and domain architecture; class D includes Dock9, 10 and 11. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of Dock9, which contains the catalytic GEF activity for Cdc42. Class D DOCKs also contain a Pleckstrin homology (PH) domain at the N-terminus.


Pssm-ID: 212571  Cd Length: 415  Bit Score: 228.76  E-value: 1.19e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  799 LRSAWFDTLAEIYEQDRWFAEASVCHAHSVAIIARELEERKELEVDWRVFDWINNRIAEtEQSQGGDAGsVQPAGFTTDN 878
Cdd:cd11698     2 LRKTWLDSMARIHVKNGDLSEAAMCYVHVAALVAEYLTRKGMFRQGCTAFRVITPNIDE-EASMMEDVG-MQDVHFNEDV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  879 LGAKIDKTAAALMLAERFEAVGPLYRLIVPVLEKNMNFTSLVSVYAELQQTYSRAAEVRSSGKRHLGAYFRVRFNGERHF 958
Cdd:cd11698    80 LMELLEQCADGLWKAERYELIADIYKLIIPIYEKRRDFERLAHLYDTLHRAYSKVTEVMHSGKRLLGTYFRVAFFGQGFF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  959 GSEHNTDWIYREAGLTSLAAFALEIKEKCQRQVGHDRVQ-IEANEQLDLSKIDPTVAYVQITHVEPSIPAAAgiADQHRN 1037
Cdd:cd11698   160 EDEDGKEYIYKEPKLTPLSEISQRLLKLYSDKFGSENVKmIQDSGKVNPKDLDSKYAYIQVTHVTPYFDEKE--LQERKT 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1038 DFLVHTNLSEFSYECATIENERkvsKEPAIHEQCLKRTVLRVSPSpvsedsraatgFPATRRRLPVISVHFEQFSPLEFA 1117
Cdd:cd11698   238 DFERSHNIRRFMFEMPFTQSGK---RQGGVEEQCKRRTILTAIHC-----------FPYVKKRIPVMYQHHTDLNPIEVA 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1118 CQKLNTKAEQIRKTLNAAsngrQLDVKGLQLLLQGAVLPTVNAGPLAYAEVFTKEEQRERYGDDGLVKLRESFRNLMNSC 1197
Cdd:cd11698   304 IDEMSKKVAELRQLCSSA----EVDMIKLQLKLQGSVSVQVNAGPLAYARAFLDDTNTKRYPDNKVKLLKEVFRQFVEAC 379
                         410       420       430
                  ....*....|....*....|....*....|...
gi 392887538 1198 QLAIEANASAIGSDQQTYHEVLVSSFDAMHERL 1230
Cdd:cd11698   380 GQALAVNERLIKEDQLEYQEEMKANYREMAKEL 412
DHR2_DOCK_C cd11695
Dock Homology Region 2, a GEF domain, of Class C Dedicator of Cytokinesis proteins; DOCK ...
796-1230 2.12e-57

Dock Homology Region 2, a GEF domain, of Class C Dedicator of Cytokinesis proteins; DOCK proteins are atypical guanine nucleotide exchange factors (GEFs) that lack the conventional Dbl homology (DH) domain. As GEFs, they activate small GTPases by exchanging bound GDP for free GTP. They are divided into four classes (A-D) based on sequence similarity and domain architecture; class C, also called the Zizimin-related (Zir) subfamily, includes Dock6, 7 and 8. Class C DOCKs have been shown to have GEF activity for both Rac and Cdc42. Dock6 regulates neurite outgrowth. Dock7 plays a critical roles in the early stages of axon formation, neuronal polarity, and myelination. Dock8 regulates T and B cell numbers and functions, and plays essential roles in humoral immune responses and the proper formation of B cell immunological synapses. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of Class C Docks, which contains the catalytic GEF activity for Rac and Cdc42.


Pssm-ID: 212568  Cd Length: 368  Bit Score: 203.30  E-value: 2.12e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  796 SAALRSAWFDTLAEIYEQDRWFAEASVCHAHSVAIiareleerkelevdwrvfdwinnriaeteqsqggdagsvqpagft 875
Cdd:cd11695     1 SPDLRLTWLQNMAEKHYERKNFAEAAQCLVHAAAL--------------------------------------------- 35
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  876 tdNLGAKIDKTAAALMLAERFEAVGPLYRLIVPVLEKNMNFTSLVSVYAELQQTYSRAAEVrSSGKRHLGAYFRVRFNGE 955
Cdd:cd11695    36 --GLVGLLEQAAESFSKAGMYEAVNEVYKLLIPILEANRDYKKLAEIHGKLQDAFTKIEKQ-QGGKRMFGTYFRVGFYGS 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  956 RhFGSEHNTDWIYREAGLTSLAAFALEIKEKCQRQVGHDRVQI--EANEqLDLSKIDPTVAYVQITHVEPSIpaaagiaD 1033
Cdd:cd11695   113 K-FGDLDGKEFIYKEPAITKLPEISHRLETFYGERFGEERVEVikDSNP-VDTSKLDPDKAYIQITYVEPYF-------D 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1034 QHR-----NDFLVHTNLSEFSYeCATIENERKVSKEpaIHEQCLKRTVLRVSPSpvsedsraatgFPATRRRLPVISVHF 1108
Cdd:cd11695   184 EYElkertTYFERNYNLRRFMY-ATPFTPDGKAHGE--LAEQYKRKTILTTENS-----------FPYVKTRLQVVNREE 249
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1109 EQFSPLEFACQKLNTKAEQirktLNAASNGRQLDVKGLQLLLQGAVLPTVNAGPLAYAEVF-TKEEQRERYGDDGLVKLR 1187
Cdd:cd11695   250 IVLTPIEVAIEDVQKKTRE----LAAATTQEPPDPKMLQMVLQGSIGTTVNQGPLEVANVFlSDIPLDPKELDRHQNKLR 325
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 392887538 1188 ESFRNLMNSCQLAIEANASAIGSDQQTYHEVLVSSFDAMHERL 1230
Cdd:cd11695   326 LCFKEFSKKCYDALEKNKELIGPDQKEYQKELERNYENFKEKL 368
DHR2_DOCK10 cd11699
Dock Homology Region 2, a GEF domain, of Class D Dedicator of Cytokinesis 10; Dock10, also ...
799-1230 7.90e-57

Dock Homology Region 2, a GEF domain, of Class D Dedicator of Cytokinesis 10; Dock10, also called Zizimin3, is an atypical guanine nucleotide exchange factor (GEF) that lacks the conventional Dbl homology (DH) domain. As a GEF, it activates the small GTPase Cdc42 by exchanging bound GDP for free GTP. Dock10 is preferentially expressed in lymphocytes and may play a role in interleukin-4 induced activation of B cells. It may also play a role in the invasion of tumor cells. DOCK proteins are divided into four classes (A-D) based on sequence similarity and domain architecture; class D includes Dock9, 10 and 11. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of Dock10, which contains the catalytic GEF activity for Cdc42. Class D DOCKs also contain a Pleckstrin homology (PH) domain at the N-terminus.


Pssm-ID: 212572  Cd Length: 446  Bit Score: 204.12  E-value: 7.90e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  799 LRSAWFDTLAEIYEQDRWFAEASVCHAHSVAIIARELEERKELEVD---------------------------------W 845
Cdd:cd11699     3 LRRTWLESMAKIHARNGDLSEAAMCYIHIAALIAEYLKRKGYWKMEkictssmlpedsqvydsnlllttstggsmfsmgW 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  846 RVFDWINNRIAEtEQSQGGDAGsVQPAGFTTDNLGAKIDKTAAALMLAERFEAVGPLYRLIVPVLEKNMNFTSLVSVYAE 925
Cdd:cd11699    83 PAFLSITPNIKE-EGAMKEDSG-MQDTPYNENTLVEQLELCVDYLWKSERYELIADVNKPVIAVFEKQRDFKRLSELYYD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  926 LQQTYSRAAEVRSSGKRHLGAYFRVRFNGERHFGSEHNTDWIYREAGLTSLAAFALEIKEKCQRQVGHDRVQ-IEANEQL 1004
Cdd:cd11699   161 IHRSYLKVAEVVNSEKRLFGRYYRVAFYGQGFFEEEEGKEYIYKEPKLTGLSEISQRLLKLYADKFGADNVKiIQDSNKV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1005 DLSKIDPTVAYVQITHVEPSIPAAAgiADQHRNDFLVHTNLSEFSYECA-TIENErkvsKEPAIHEQCLKRTVLRVSPSp 1083
Cdd:cd11699   241 NPKELDPKFAYIQVTYVTPYFDEKE--QEDRKTDFEMHHNINRFVFETPfTLSGK----KHGGVEEQCKRRTILTTSHS- 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1084 vsedsraatgFPATRRRLPVISVHFEQFSPLEFACQKLNTKAEQirktLNAASNGRQLDVKGLQLLLQGAVLPTVNAGPL 1163
Cdd:cd11699   314 ----------FPYVKKRIQVVSQTSTELNPIEVAIDEMSKKVSE----LNQLCTMEEVDMIRLQLKLQGSVSVKVNAGPM 379
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392887538 1164 AYAEVFTKEEQRERYGDDGLVKLRESFRNLMNSCQLAIEANASAIGSDQQTYHEVLVSSFDAMHERL 1230
Cdd:cd11699   380 AYARAFLEETNAKKYPDNQVKLLKEIFRQFAEACGQALDVNERLIKEDQLEYQEEMRSHYRDMLSEL 446
DHR2_DOCK7 cd11703
Dock Homology Region 2, a GEF domain, of Class C Dedicator of Cytokinesis 7; Dock7, also ...
757-1231 1.70e-50

Dock Homology Region 2, a GEF domain, of Class C Dedicator of Cytokinesis 7; Dock7, also called Zizimin-related 2 (Zir2), is an atypical guanine nucleotide exchange factor (GEF) that lacks the conventional Dbl homology (DH) domain. As a GEF, it activates the small GTPases Rac1 and Cdc42 by exchanging bound GDP for free GTP. It plays a critical role in the initial specification of axon formation in hippocampal neurons. It affects neuronal polarity by regulating microtubule dynamics. Dock7 also plays a role in controlling myelination by Schwann cells. It may also play important roles in the function and distribution of dermal and follicular melanocytes. DOCK proteins are divided into four classes (A-D) based on sequence similarity and domain architecture; class C includes Dock6, 7 and 8. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of Dock7, which contains the catalytic GEF activity for Rac and/or Cdc42.


Pssm-ID: 212576  Cd Length: 473  Bit Score: 186.44  E-value: 1.70e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  757 DLLRQLRGVMTATVALKDAANDPIRLADLHLQLADSYRGSAALRSAWFDTLAEIYEQDRWFAEASVCHAHSVAIIARELE 836
Cdd:cd11703     1 DLVFNLHMILSDTVKMKEHQEDPEMLIDLMYRIAKGYQTSPDLRLTWLQNMAGKHSERSNHAEAAQCLVHSAALVAEYLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  837 ERKELE---VDWRVFDWINNRIAEtEQSQGGDAGSVQPAG------FTTDNLGAKIDKTAAALMLAERFEAVGPLYRLIV 907
Cdd:cd11703    81 MLEDRKylpVGCVTFQNISSNVLE-ESAVSDDVVSPDEEGicsgkyFTEAGLVGLLEQAAASFSMAGMYEAVNEVYKVLI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  908 PVLEKNMNFTSLVSVYAELQQTYSRAaeVRSSGKRHLGAYFRVRFNGERhFGSEHNTDWIYREAGLTSLAAFALEIKEKC 987
Cdd:cd11703   160 PIHEANRDAKKLATIHGKLQEAFSKI--VHQDGKRMFGTYFRVGFYGTK-FGDLDEQEFVYKEPAITKLAEISHRLEGFY 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  988 QRQVGHDRVQ-IEANEQLDLSKIDPTVAYVQITHVEPSIPAAAgiADQHRNDFLVHTNLSEFSYeCATIENERKVSKEpa 1066
Cdd:cd11703   237 GERFGEDVVEvIKDSNPVDKCKLDPNKAFIQITYVEPYFDTYE--MKDRITYFDKNYNLRRFMY-CTPFTLDGRAHGE-- 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1067 IHEQCLKRTVLRVSPSpvsedsraatgFPATRRRLPVISVHFEQFSPLEFACQKLNTKAEQirktLNAASNGRQLDVKGL 1146
Cdd:cd11703   312 LHEQFKRKTILTTSHA-----------FPYIKTRINVIHKEEIILTPIEVAIEDMQKKTQE----LAFATHQDPADPKML 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1147 QLLLQGAVLPTVNAGPLAYAEVFTKEEQRERYGDDGLVKLRESFRNLMNSCQLAIEANASAIGSDQQTYHEVLVSSFDAM 1226
Cdd:cd11703   377 QMVLQGSVGTTVNQGPLEVAQVFLSEIPSDPKLFRHHNKLRLCFKDFTKRCEDALRKNKSLIGPDQKEYQRELERNYHRL 456

                  ....*
gi 392887538 1227 HERLQ 1231
Cdd:cd11703   457 KEALQ 461
DHR2_DOCK6 cd11702
Dock Homology Region 2, a GEF domain, of Class C Dedicator of Cytokinesis 6; Dock6, also ...
796-1230 8.92e-48

Dock Homology Region 2, a GEF domain, of Class C Dedicator of Cytokinesis 6; Dock6, also called Zizimin-related 1 (Zir1), is an atypical guanine nucleotide exchange factor (GEF) that lacks the conventional Dbl homology (DH) domain. As a GEF, it activates the small GTPases Rac and Cdc42 by exchanging bound GDP for free GTP. It is widely expressed and shows highest expression in the dorsal root ganglion and the brain. It regulates neurite outgrowth. DOCK proteins are divided into four classes (A-D) based on sequence similarity and domain architecture; class C includes Dock6, 7 and 8. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of Dock6, which contains the catalytic GEF activity for Rac and/or Cdc42.


Pssm-ID: 212575  Cd Length: 423  Bit Score: 177.12  E-value: 8.92e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  796 SAALRSAWFDTLAEIYEQDRWFAEASVCHAHSVAIIARELEERKELE---VDWRVFDWINNRIAEtEQSQGGDAGSVQPA 872
Cdd:cd11702     1 SPDLRLTWLQNMAGKHSERGNHAEAAHCLVHSAALVAEYLSMLEDCRhlpVGCVSFQNISSNVLE-ESAVSDDILSPDEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  873 G------FTTDNLGAKIDKTAAALMLAERFEAVGPLYRLIVPVLEKNMNFTSLVSVYAELQQTYSRAAEVRSSGKRHLGA 946
Cdd:cd11702    80 GicsgkyFTELGLVGLLEQAAASFNMGGLYEAVNEVYKILIPIHEANRDYKKLAVVHGKLQEAFNKITNQSSGWERMFGT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  947 YFRVRFNGErHFGSEHNTDWIYREAGLTSLAAFALEIKEKCQRQVGHDRVQ-IEANEQLDLSKIDPTVAYVQITHVEPSI 1025
Cdd:cd11702   160 YFRVGFYGC-KFGDLDEQEFVYKEPSITKLAEISHRLEEFYTERFGDEVVEiIKDSNPVDKSKLDPNKAYIQITYVEPFF 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1026 PAAAgiADQHRNDFLVHTNLSEFSYeCATIENERKVSKEpaIHEQCLKRTVLRVSPSpvsedsraatgFPATRRRLPVIs 1105
Cdd:cd11702   239 DTYE--LKDRVTYFDKNYNLRTFLF-CTPFTLDGRAHGE--LHEQYKRKTILTTSHA-----------FPYIKTRINVL- 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1106 vHFEQ--FSPLEFACQKLNTKAEQirktLNAASNGRQLDVKGLQLLLQGAVLPTVNAGPLAYAEVFTKE--EQRERYGDD 1181
Cdd:cd11702   302 -HREEivLIPVEVAIEDMQKKTQE----LAFATHQDPADAKMLQMVLQGCVGTTVNQGPLEVAQVFLSEipEDPKLFRHH 376
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 392887538 1182 GlvKLRESFRNLMNSCQLAIEANASAIGSDQQTYHEVLVSSFDAMHERL 1230
Cdd:cd11702   377 N--KLRLCFKDFTKRCEDALRKNKALIGPDQKEYHRELERNYQRLREAL 423
DHR2_DOCK8 cd11701
Dock Homology Region 2, a GEF domain, of Class C Dedicator of Cytokinesis 8; Dock8, also ...
796-1230 1.06e-45

Dock Homology Region 2, a GEF domain, of Class C Dedicator of Cytokinesis 8; Dock8, also called Zizimin-related 3 (Zir3), is an atypical guanine nucleotide exchange factor (GEF) that lacks the conventional Dbl homology (DH) domain. As a GEF, it activates the small GTPases Rac1 and Cdc42 by exchanging bound GDP for free GTP. Dock8 is highly expressed in the immune system and it regulates T and B cell numbers and functions. It plays essential roles in humoral immune responses and the proper formation of B cell immunological synapses. Dock8 deficiency is a primary immune deficiency that results in extreme susceptibility to cutaneous viral infections, elevated IgE levels, and eosinophilia. It was originally described as an autosomal recessive form of hyper IgE syndrome (AR-HIES). DOCK proteins are divided into four classes (A-D) based on sequence similarity and domain architecture; class C includes Dock6, 7 and 8. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of Dock8, which contains the catalytic GEF activity for Rac and/or Cdc42.


Pssm-ID: 212574  Cd Length: 422  Bit Score: 170.99  E-value: 1.06e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  796 SAALRSAWFDTLAEIYEQDRWFAEASVCHAHSVAIIARELEERKELE---VDWRVFDWINNRIAEtEQSQGGDAGSVQPA 872
Cdd:cd11701     2 SPDLRLTWLQNMAEKHTKRKCFTEAAMCLVHAAALVAEYLSMLEDHSylpVGSVSFQNISSNVLE-ESAVSDDILSPDED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  873 G------FTTDNLGAKIDKTAAALMLAERFEAVGPLYRLIVPVLEKNMNFTSLVSVYAELQQTYSRAAEvrSSGKRHLGA 946
Cdd:cd11701    81 GvcsgryFTENGLVGLLEQAAELFSTGGLYETVNEVYKIVIPILEAHRDFRKLASTHDKLQKAFDNIIN--KGHKRMFGT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  947 YFRVRFNGERhFGSEHNTDWIYREAGLTSLAAFALEIKEKCQRQVGHDRVQ-IEANEQLDLSKIDPTVAYVQITHVEPSI 1025
Cdd:cd11701   159 YFRVGFYGSK-FGDLDEQEFIYKEPAITKLPEISHRLEGFYGQCFGDDVVEvIKDSTPVDKSKLDPNKAYIQITFVEPYF 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1026 PaaagiaDQHRNDFLVH----TNLSEFSYECATIENERKVSKepaIHEQCLKRTVLRvspspvsedsrAATGFPATRRRL 1101
Cdd:cd11701   238 D------DYEMKDRVTYfeknFNLRRFMYTTPFTLDGRPRGE---LSEQYKRKTILT-----------TMHAFPYIKTRI 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1102 PVISVHFEQFSPLEFACQKLNTKAEQirktLNAASNGRQLDVKGLQLLLQGAVLPTVNAGPLAYAEVFTKE----EQRER 1177
Cdd:cd11701   298 NVIQKEEFDLTPIEVAIEDMQKKTRE----LAEATHQEPPDAKMLQMVLQGSVGATVNQGPLEVAQVFLAEipadPKLYR 373
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 392887538 1178 YGDdglvKLRESFRNLMNSCQLAIEANASAIGSDQQTYHEVLVSSFDAMHERL 1230
Cdd:cd11701   374 HHN----KLRLCFKEFIMRCGEAVEKNKRLITADQREYQQELKKNYNKLRENL 422
DHR-2_Lobe_C pfam20421
DHR-2, Lobe C; DOCK (dedicator of cytokinesis) proteins are guanine nucleotide exchange ...
1132-1233 6.86e-27

DHR-2, Lobe C; DOCK (dedicator of cytokinesis) proteins are guanine nucleotide exchange factors (GEFs) that activate some small GTPases, such as Rac or Cdc42, by exchanging bound GDP for free GTP to control cell migration, morphogenesis, and phagocytosis. These proteins share a DOCK-type C2 domain (also termed the DOCK-homology region (DHR)-1) at the N-terminal, and the DHR-2 domain (also termed the DOCKER domain) at the C-terminal. DHR-2 is the GEF catalytic domain organized into three lobes A, B and C, with the Rho-family binding site and catalytic centre generated entirely from lobes B and C. This entry represents Lobe C which form an antiparallel four alpha-helical bundle and contains a loop known as the nucleotide sensor characterized by a conserved valine residue essential for catalytic activity.


Pssm-ID: 466570 [Multi-domain]  Cd Length: 103  Bit Score: 105.75  E-value: 6.86e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  1132 LNAASNGRQLDVKGLQLLLQGAVLPTVNAGPLAYAEVFTKEEQRERYGDDGLVKLRESFRNLMNSCQLAIEANASAIGSD 1211
Cdd:pfam20421    2 LEAAINAPPPNIKTLQMVLQGSVDVQVNAGPLEYAEAFLSEKNVDNYPAEKVEKLKEEFRDFLKVCGEALRLNKKLISED 81
                           90       100
                   ....*....|....*....|..
gi 392887538  1212 QQTYHEVLVSSFDAMHERLQTF 1233
Cdd:pfam20421   82 QREYQEELEEGFEKLKEKLEPY 103
DHR-2_Lobe_A pfam06920
DHR-2, Lobe A; This entry represents a conserved region within a number of eukaryotic ...
784-935 1.28e-21

DHR-2, Lobe A; This entry represents a conserved region within a number of eukaryotic dedicator of cytokinesis proteins (DOCK), which are guanine nucleotide exchange factors (GEFs), that activate some small GTPases by exchanging bound GDP for free GTP such as Rac. These proteins have a DOCK-homology region 1 (DHR-1, also known as DOCK-type C2 domain) at the N-terminus and a DHR-2 (also known as DOCKER domain) at the C-terminal. The DHR-2 is a GEF catalytic domain organized into three lobes, A, B and C, with the Rho-family binding site and catalytic centre generated entirely from lobes B and C. This entry represents Lobe A, formed from an antiparallel array of alpha helices that adopts a tetratricopeptide repeat-like fold, which through extensive contacts with lobe B, stabilizes DHR-2 domain.


Pssm-ID: 462040 [Multi-domain]  Cd Length: 154  Bit Score: 92.74  E-value: 1.28e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538   784 DLHLQLADSYRGSAALRSAWFDTLAEIYEQDRWFAEASVCHAHSVAIIARELEERKELEVDWRV--FDWINNRIAETEQS 861
Cdd:pfam06920    1 DLQYSLANSYKSSPDLRLTWLENLAEKHLENGNFSEAAQCLIHIAALIAEYLKLKGKIPNPLGAsaFEKISPNILREESA 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392887538   862 QGGDAGSVQPAGFTTDNLGAKIDKTAAALMLAERFEAVGPLYRLIVPVLEKNMNFTSLVSVYAELQQTYSRAAE 935
Cdd:pfam06920   81 LKDDSGVCDSPHFTEDGLVGLLEEAIDYLDKAERYELAIELYKLLLPIYESRRDYKKLSECHGKLAEAYEKIVE 154
DHR2_DOCK_A cd11697
Dock Homology Region 2, a GEF domain, of Class A Dedicator of Cytokinesis proteins; DOCK ...
942-1229 7.28e-11

Dock Homology Region 2, a GEF domain, of Class A Dedicator of Cytokinesis proteins; DOCK proteins are atypical guanine nucleotide exchange factors (GEFs) that lack the conventional Dbl homology (DH) domain. As GEFs, they activate small GTPases by exchanging bound GDP for free GTP. They are divided into four classes (A-D) based on sequence similarity and domain architecture; class A includes Dock1, 2 and 5. Class A DOCKs are specific GEFs for Rac. Dock1 interacts with the scaffold protein Elmo and the resulting complex functions upstream of Rac in many biological events including phagocytosis of apoptotic cells, cell migration and invasion. Dock2 plays an important role in lymphocyte migration and activation, T-cell differentiation, neutrophil chemotaxis, and type I interferon induction. Dock5 functions upstream of Rac1 to regulate osteoclast function. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of class A DOCKs, which contains the catalytic GEF activity for Rac and/or Cdc42. Class A DOCKs also contain an SH3 domain at the N-terminal region and a PxxP motif at the C-terminus.


Pssm-ID: 212570  Cd Length: 400  Bit Score: 65.81  E-value: 7.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  942 RHLGAYFRVRFNGERHFGSEHNTDWIYREAGLTSLAAFALEI------KEKCQRQVGHDRVQIEANEQldlskidptvaY 1015
Cdd:cd11697   120 RPEPEYFRVGYYGQGFPSFLRNKVFIYRGKEYERLSDFSARLlnqfpnAELMNTLTPPGDEIKESPGQ-----------Y 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1016 VQITHVEP---------SIPAAAGIADQHRNDflvhtNLSEFSYECATIENERKVSKEPAihEQCLKRTVLRVspspvse 1086
Cdd:cd11697   189 LQINKVDPvmderprfkGKPVSDQILNYYKVN-----EVQRFTFSRPFRRGTKDPDNEFA--NMWLERTTLTT------- 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1087 dsraATGFPATRRRLPVISVHFEQFSPLEFACQKLNTKAEQIRKTLNAASNGRQLDVKGLQLLLQGAVLPTVNAGPLAYA 1166
Cdd:cd11697   255 ----AYKLPGILRWFEVVSTSTVEISPLENAIETMEDTNKKIRDLILQHQSDPTLPINPLSMLLNGIVDAAVMGGIANYE 330
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392887538 1167 EVFTKEEQRERYGDDG--LVKLRESFRNLMNSCQLAIEANASAIGSDQQTYHEVLVSSFDAMHER 1229
Cdd:cd11697   331 KAFFTEEYLDEHPEDQelIERLKDLIAEQIPLLEAGLKIHKQKAPESLRPLHERMEECFAKMKEH 395
DHR-2_Lobe_B pfam20422
DHR-2, Lobe B; DOCK (dedicator of cytokinesis) proteins are guanine nucleotide exchange ...
1005-1080 2.38e-08

DHR-2, Lobe B; DOCK (dedicator of cytokinesis) proteins are guanine nucleotide exchange factors (GEFs) that activate some small GTPases, such as Rac or Cdc42, by exchanging bound GDP for free GTP to control cell migration, morphogenesis, and phagocytosis. These proteins share a DOCK-type C2 domain (also termed the DOCK-homology region (DHR)-1) at the N-terminal, and the DHR-2 domain (also termed the DOCKER domain) at the C-terminal. DHR-2 is the GEF catalytic domain organized into three lobes A, B and C, with the Rho-family binding site and catalytic centre generated entirely from lobes B and C. This entry represents Lobe B which adopts an unusual architecture of two antiparallel beta sheets disposed in a loosely packed orthogonal arrangement. This lobe changes its position relative to lobe C and the bound GTPase, which suggests that lobe B distinguishes between the switch 1 conformations of Rac1 and Cdc42.


Pssm-ID: 466571 [Multi-domain]  Cd Length: 77  Bit Score: 52.23  E-value: 2.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  1005 DLSKIDPTVAYVQITHVEP-----SIPaaagiadQHRNDFLVHTNLSEFSYECATIENERKVSkepAIHEQCLKRTVLRV 1079
Cdd:pfam20422    5 DESILDPDKAYIQITSVEPyfddsELN-------DRVTYFERNNNVNRFVFETPFTKSGKAQG---EFEEQWKRRTILTT 74

                   .
gi 392887538  1080 S 1080
Cdd:pfam20422   75 E 75
DHR2_DOCK_B cd11696
Dock Homology Region 2, a GEF domain, of Class B Dedicator of Cytokinesis proteins; DOCK ...
947-1230 1.41e-05

Dock Homology Region 2, a GEF domain, of Class B Dedicator of Cytokinesis proteins; DOCK proteins are atypical guanine nucleotide exchange factors (GEFs) that lack the conventional Dbl homology (DH) domain. As GEFs, they activate small GTPases by exchanging bound GDP for free GTP. They are divided into four classes (A-D) based on sequence similarity and domain architecture; class B includes Dock3 and 4. Dock3 is a specific GEF for Rac and it regulates N-cadherin dependent cell-cell adhesion, cell polarity, and neuronal morphology. It promotes axonal growth by stimulating actin polymerization and microtubule assembly. Dock4 activates the Ras family GTPase Rap1, probably indirectly through interaction with Rap regulatory proteins. It plays a role in regulating dendritic growth and branching in hippocampal neurons, where it is highly expressed. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of class B DOCKs, which contains the catalytic GEF activity for Rac and/or Cdc42. Class B DOCKs also contain an SH3 domain at the N-terminal region and a PxxP motif at the C-terminus.


Pssm-ID: 212569  Cd Length: 391  Bit Score: 48.98  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538  947 YFRVRFNGERHFGSEHNTDWIYREAGLTSLAAFaleiKEKCQRQVGHDRVqIEANEQLDLSKIDPTVAYVQITHVEP--- 1023
Cdd:cd11696   120 YFRVGFYGKGFPLFLRNKQFVYRGLDYERIGAF----TQRLQSEFPQAHI-LTKNTPPDDAILQADGQYIQICNVKPvpe 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1024 --SIPAAAGIADQHRNDFLVHtNLSEFSYEcatieneRKVSKEPAIHEQCLK-----RTVLRVSPSpvsedsraatgFPA 1096
Cdd:cd11696   195 rrPVLQMVGVPDKVRSFYRVN-DVRKFQYD-------RPIHKGPIDKDNEFKslwieRTTLVTEHS-----------LPG 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1097 TRRRLPVISVHFEQFSPLEFACQKLNTKAEQIRKTLNAASNGRQLDVKGLQLLLQGAVLPTVNAGPLAYAEVFTKEEQRE 1176
Cdd:cd11696   256 ILRWFEVVSREVEEIPPVENACETVENKNQELRSLISQYQADPTRNINPFSMRLQGVIDAAVNGGIAKYQEAFFTPEFIL 335
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392887538 1177 RYGDDG--LVKLRESFRNLMNSCQLAIEANASAIGSDQQTYHEVLVSSFDAMHERL 1230
Cdd:cd11696   336 SHPEDAehIARLRELILEQVQILEAGLALHGKLAPPEVRPLHKRLVERFTQMKQSL 391
DHR2_DOCK2 cd11706
Dock Homology Region 2, a GEF domain, of Class A Dedicator of Cytokinesis 2; Dock2 is a ...
1094-1236 5.33e-05

Dock Homology Region 2, a GEF domain, of Class A Dedicator of Cytokinesis 2; Dock2 is a hematopoietic cell-specific, class A DOCK and is an atypical guanine nucleotide exchange factor (GEF) that lacks the conventional Dbl homology (DH) domain. As a GEF, it activates small GTPases by exchanging bound GDP for free GTP. It plays an important role in lymphocyte migration and activation, T-cell differentiation, neutrophil chemotaxis, and type I interferon induction. DOCK proteins are divided into four classes (A-D) based on sequence similarity and domain architecture; class A includes Dock1, 2 and 5. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of Dock2, which contains the catalytic GEF activity for Rac and/or Cdc42. Class A DOCKs, like Dock2, are specific GEFs for Rac and they contain an SH3 domain at the N-terminal region and a PxxP motif at the C-terminus.


Pssm-ID: 212579  Cd Length: 421  Bit Score: 47.29  E-value: 5.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1094 FPATRRRLPVISVHFEQFSPLEFACQKLNTKAEQIRKTLNAASNGRQLDVKGLQLLLQGAVLPTVNAGPLAYAEVFTKEE 1173
Cdd:cd11706   276 LPGILRWFEVTHMSQTTISPLENAIETMSTTNEKILMMINQYQSDESLPINPLSMLLNGIVDPAVMGGFAKYEKAFFTEE 355
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392887538 1174 QRERYGDD--GLVKLRESFRNLMNSCQLAIEANASAIGSDQQTYHEVLVSSFDAMHERLQTFFGA 1236
Cdd:cd11706   356 YVRDHPEDqdKLTRLKDLIAWQIPLLGAGIKIHGKRVTDDLRPFHERMEECFKQLKMKVEKEYGV 420
DHR2_DOCK5 cd11708
Dock Homology Region 2, a GEF domain, of Class A Dedicator of Cytokinesis 5; Dock5 is an ...
1091-1234 4.06e-04

Dock Homology Region 2, a GEF domain, of Class A Dedicator of Cytokinesis 5; Dock5 is an atypical guanine nucleotide exchange factor (GEF) that lacks the conventional Dbl homology (DH) domain. As a GEF, it activates small GTPases by exchanging bound GDP for free GTP. It functions upstream of Rac1 to regulate osteoclast function. DOCK proteins are divided into four classes (A-D) based on sequence similarity and domain architecture; class A includes Dock1, 2 and 5. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of Dock5, which contains the catalytic GEF activity for Rac and/or Cdc42. Class A DOCKs, like Dock5, are specific GEFs for Rac and they contain an SH3 domain at the N-terminal region and a PxxP motif at the C-terminus.


Pssm-ID: 212581  Cd Length: 400  Bit Score: 44.17  E-value: 4.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887538 1091 ATGFPATRRRLPVISVHFEQFSPLEFACQKLNTKAEQIRKTLNAASNGRQLDVKGLQLLLQGAVLPTVNAGPLAYAEVFT 1170
Cdd:cd11708   255 AYRFPGILKWFEVKQISTEEISPLENAIETMELTNEKISNLVQQHAWDRSLPVHPLSMLLNGIVDPAVMGGFSNYEKAFF 334
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392887538 1171 KEEQRERYGDDgLVKLrESFRNLMnSCQLAIEANASAIGSDQQT-----YHEVLVSSFDAMHERLQTFF 1234
Cdd:cd11708   335 TEKYLQEHPED-QEKI-ELLKQLI-ALQMPLLAEGIRIHGEKLTeqlkpLHERLVSCFKDLRAKVEKLY 400
 
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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