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Conserved domains on  [gi|61676215|ref|NP_082820|]
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ras-interacting protein 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Myo5p-like_CBD_Rasip1 cd15472
cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 ...
 545-911 0e+00

cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 (Rasip1 or RAIN) is an effector of the small G protein Rap1 and plays an important role in endothelial junction stabilization. Rasip1, like afadin, is a multi domain protein, that contains beside a myosin5-like CBD, a Ras-associated domain and a PDZ domain.


:

Pssm-ID: 271256  Cd Length: 366  Bit Score: 568.83  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 545 EEEALLGEIVRAAASGaGDLPPLGPATLLALCVQHSARELELGHLPRLLGRLARLIKEAVWEKIKEIGDRQPEnHPEGVP 624
Cdd:cd15472   2 HEDALLRRILTLIEPG-GDDHKLTPAFLLCLCIQHSATHFEPGHFGKLLLKIAKRIQEIVWEKTKELAEKQPE-HQDPAS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 625 EVPLTPEAVSVELRPLILWMANTTELLSFVQEKVLEMEKEADQEG--LSSDPQLCNDLELCDEALALLDEVIMCTFQQSV 702
Cdd:cd15472  80 LSLLSIAELAPDLQPLLFWMSNSIELLYFIQQKVPLYEQSMEEELdvGSKESLLSSTLTASEEAMTVLEEVIMYTFQQCV 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 703 YYLTKTLYSTLPALLDSNPFTAgaELPGPGAELEAMPPGLRPTLGVFQAALELTSQCELHPDLVSQTFGYLFFFSNASLL 782
Cdd:cd15472 160 YYLTKTLYVALPALLDSNPFTA--EERESWSGGSRLPEGVRRVLEIYQATLDLLRQYQVHPEIASQMFAYLFFFSNASLF 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 783 NSLMERGQGRPFYQWSRAVQIRTNLDLVLDWLQGAGLGDIATEFFRKLSIAVNLLCVPRTSLLKASWSSLRTDYPTLTPA 862
Cdd:cd15472 238 NQLMEKGSGGGFFQWSRGVQIRANLDLLLDWLQGAGLGDLAEEFFRKLSSTVNLLATPKEQLLQMSWSSLRAEFPALNPA 317

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 61676215 863 QLHHLLSHYQLGPGRGPPPAWDPPPAERDAVDTGDIFESFSSHPPLILP 911
Cdd:cd15472 318 QLHHLLRQYQLGSGRGPPWAQPSPEDAPAAVRTEDILESFDNHPPLVLP 366
FHA_RAIN cd22734
forkhead associated (FHA) domain found in Ras-interacting protein 1 (Rain); Rain, also called ...
 372-484 3.35e-58

forkhead associated (FHA) domain found in Ras-interacting protein 1 (Rain); Rain, also called Rasip1, is an endothelial-specific Ras-interacting protein required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. It acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Rain interacts with Ras in a GTP-dependent manner and may serve as an effector for endomembrane-associated Ras. It contains an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


:

Pssm-ID: 438786  Cd Length: 119  Bit Score: 194.99  E-value: 3.35e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 372 SNRPYFLLLQGYQDAQDFVVYVMTREQHVFGRGGPSSSRGGSPAPYVDTFLNAPDILPRHCTVRA------GPEPPAMVR 445
Cdd:cd22734   1 ADRPYFLLLQGYNDRQDFVLYVMSGKTHIFGRGPKSSSRPGPKAPKVDTFLSAPDILPRHCAVRRadavgeQPHGPALVR 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 61676215 446 PSRGAPVTHNGCLLLREAELHPGDLLGLGEHFLFMYKDP 484
Cdd:cd22734  81 PFRGALVTHNGAPLLREAELQPGDLLGLGEHFLFMYKDP 119
Ubl1_cv_Nsp3_N-like super family cl28922
first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV ...
 131-250 1.59e-46

first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV non-structural protein 3 (Nsp3) and related proteins; This ubiquitin-like (Ubl) domain (Ubl1) is found at the N-terminus of coronavirus Nsp3, a large multi-functional multi-domain protein which is an essential component of the replication/transcription complex (RTC). The functions of Ubl1 in CoVs are related to single-stranded RNA (ssRNA) binding and to interacting with the nucleocapsid (N) protein. SARS-CoV Ubl1 has been shown to bind ssRNA having AUA patterns, and since the 5'-UTR of the SARS-CoV genome has a number of AUA repeats, it may bind there. In mouse hepatitis virus (MHV), this Ubl1 domain binds the cognate N protein. Adjacent to Ubl1 is a Glu-rich acidic region (also referred to as hypervariable region, HVR); Ubl1 together with HVR has been called Nsp3a. Currently, the function of HVR in CoVs is unknown. This model corresponds to one of two Ubl domains in Nsp3; the other is located N-terminal to the papain-like protease (PLpro) and is not represented by this model.


The actual alignment was detected with superfamily member cd17116:

Pssm-ID: 475130  Cd Length: 121  Bit Score: 162.11  E-value: 1.59e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 131 EPPLPTRAAvPPGVLKIFASGLASGANYKSVLATERSTARELVAEALERYGLtggrgagDSGCVDAYALCDALGRPA--- 207
Cdd:cd17116   3 PAELSTQAS-APGVLKIFGDSICPGANYKSVLATPRSSAQELVKEALERYGL-------ARSEAKQYVLCDVIGRFTgae 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 61676215 208 ----VGVGGGEWRAEHLRVLADAERPLLVQDLWRARPGWARRFELRG 250
Cdd:cd17116  75 kdqsRSSSSERWRTECLRVIGDNEKPLLLQSLWKPKEGFSRRFELRR 121
 
Name Accession Description Interval E-value
Myo5p-like_CBD_Rasip1 cd15472
cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 ...
 545-911 0e+00

cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 (Rasip1 or RAIN) is an effector of the small G protein Rap1 and plays an important role in endothelial junction stabilization. Rasip1, like afadin, is a multi domain protein, that contains beside a myosin5-like CBD, a Ras-associated domain and a PDZ domain.


Pssm-ID: 271256  Cd Length: 366  Bit Score: 568.83  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 545 EEEALLGEIVRAAASGaGDLPPLGPATLLALCVQHSARELELGHLPRLLGRLARLIKEAVWEKIKEIGDRQPEnHPEGVP 624
Cdd:cd15472   2 HEDALLRRILTLIEPG-GDDHKLTPAFLLCLCIQHSATHFEPGHFGKLLLKIAKRIQEIVWEKTKELAEKQPE-HQDPAS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 625 EVPLTPEAVSVELRPLILWMANTTELLSFVQEKVLEMEKEADQEG--LSSDPQLCNDLELCDEALALLDEVIMCTFQQSV 702
Cdd:cd15472  80 LSLLSIAELAPDLQPLLFWMSNSIELLYFIQQKVPLYEQSMEEELdvGSKESLLSSTLTASEEAMTVLEEVIMYTFQQCV 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 703 YYLTKTLYSTLPALLDSNPFTAgaELPGPGAELEAMPPGLRPTLGVFQAALELTSQCELHPDLVSQTFGYLFFFSNASLL 782
Cdd:cd15472 160 YYLTKTLYVALPALLDSNPFTA--EERESWSGGSRLPEGVRRVLEIYQATLDLLRQYQVHPEIASQMFAYLFFFSNASLF 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 783 NSLMERGQGRPFYQWSRAVQIRTNLDLVLDWLQGAGLGDIATEFFRKLSIAVNLLCVPRTSLLKASWSSLRTDYPTLTPA 862
Cdd:cd15472 238 NQLMEKGSGGGFFQWSRGVQIRANLDLLLDWLQGAGLGDLAEEFFRKLSSTVNLLATPKEQLLQMSWSSLRAEFPALNPA 317

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 61676215 863 QLHHLLSHYQLGPGRGPPPAWDPPPAERDAVDTGDIFESFSSHPPLILP 911
Cdd:cd15472 318 QLHHLLRQYQLGSGRGPPWAQPSPEDAPAAVRTEDILESFDNHPPLVLP 366
FHA_RAIN cd22734
forkhead associated (FHA) domain found in Ras-interacting protein 1 (Rain); Rain, also called ...
 372-484 3.35e-58

forkhead associated (FHA) domain found in Ras-interacting protein 1 (Rain); Rain, also called Rasip1, is an endothelial-specific Ras-interacting protein required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. It acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Rain interacts with Ras in a GTP-dependent manner and may serve as an effector for endomembrane-associated Ras. It contains an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438786  Cd Length: 119  Bit Score: 194.99  E-value: 3.35e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 372 SNRPYFLLLQGYQDAQDFVVYVMTREQHVFGRGGPSSSRGGSPAPYVDTFLNAPDILPRHCTVRA------GPEPPAMVR 445
Cdd:cd22734   1 ADRPYFLLLQGYNDRQDFVLYVMSGKTHIFGRGPKSSSRPGPKAPKVDTFLSAPDILPRHCAVRRadavgeQPHGPALVR 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 61676215 446 PSRGAPVTHNGCLLLREAELHPGDLLGLGEHFLFMYKDP 484
Cdd:cd22734  81 PFRGALVTHNGAPLLREAELQPGDLLGLGEHFLFMYKDP 119
RA_Radil_like cd17116
Ras-associating (RA) domain found in ras-associating and dilute domain-containing protein ...
 131-250 1.59e-46

Ras-associating (RA) domain found in ras-associating and dilute domain-containing protein (Radil) and similar proteins; Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility through linking Rap1 to beta2-integrin activation.This family also includes Ras-interacting protein 1 (Rain, also termed Rasip1), which is a novel Ras-interacting protein with a unique subcellular localization. It interacts with Ras in a GTP-dependent manner, and may serve as an effector for endomembrane-associated Ras. Radil contains RA, DIL, and PDZ domains. In contrast, Rain contains a myosin5-like cargo binding domain, a RA domain and a PDZ domain. RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes.


Pssm-ID: 340636  Cd Length: 121  Bit Score: 162.11  E-value: 1.59e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 131 EPPLPTRAAvPPGVLKIFASGLASGANYKSVLATERSTARELVAEALERYGLtggrgagDSGCVDAYALCDALGRPA--- 207
Cdd:cd17116   3 PAELSTQAS-APGVLKIFGDSICPGANYKSVLATPRSSAQELVKEALERYGL-------ARSEAKQYVLCDVIGRFTgae 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 61676215 208 ----VGVGGGEWRAEHLRVLADAERPLLVQDLWRARPGWARRFELRG 250
Cdd:cd17116  75 kdqsRSSSSERWRTECLRVIGDNEKPLLLQSLWKPKEGFSRRFELRR 121
DIL pfam01843
DIL domain; The DIL domain has no known function.
 768-875 2.95e-31

DIL domain; The DIL domain has no known function.


Pssm-ID: 460359 [Multi-domain]  Cd Length: 103  Bit Score: 118.08  E-value: 2.95e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215   768 QTFGYLFFFSNASLLNSLMERgqgRPFYQWSRAVQIRTNLDLVLDWLQGAGLGDIATEFFRKLSIAVNLLCVPRTSLLka 847
Cdd:pfam01843   1 QLFSQLFYFINAELFNRLLLR---KKYCSWSKGMQIRYNLSRLEEWARSNGLESEARDHLAPLIQAAQLLQLRKSTLE-- 75

                          90       100
                  ....*....|....*....|....*...
gi 61676215   848 SWSSLRTDYPTLTPAQLHHLLSHYQLGP 875
Cdd:pfam01843  76 DLDSILQVCPALNPLQLHRLLTLYQPDD 103
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 141-252 5.58e-16

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 73.91  E-value: 5.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215   141 PPGVLKIFASGLASGANYKSVLATERSTARELVAEALERYGLTggrgagdsGCVDAYALCDALGRpavgvGGGEwraehl 220
Cdd:pfam00788   1 DDGVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLEKFGLE--------DDPRDYVLVEVLER-----GGGE------ 61

                          90       100       110
                  ....*....|....*....|....*....|..
gi 61676215   221 RVLADAERPLLVQDLWRaRPGWARRFELRGRE 252
Cdd:pfam00788  62 RRLPDDECPLQIQLQWP-RDASDSRFLLRKRD 92
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 142-252 6.94e-08

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 50.76  E-value: 6.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215    142 PGVLKIFASGLASGAnYKSVLATERSTARELVAEALERYGLTGGrgagdsgcVDAYALCDALGRPAvgvgggewraehLR 221
Cdd:smart00314   2 TFVLRVYVDDLPGGT-YKTLRVSSRTTARDVIQQLLEKFHLTDD--------PEEYVLVEVLPDGK------------ER 60

                           90       100       110
                   ....*....|....*....|....*....|.
gi 61676215    222 VLADAERPLLVQDLWRaRPGWARRFELRGRE 252
Cdd:smart00314  61 VLPDDENPLQLQKLWP-RRGPNLRFVLRKRD 90
 
Name Accession Description Interval E-value
Myo5p-like_CBD_Rasip1 cd15472
cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 ...
 545-911 0e+00

cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 (Rasip1 or RAIN) is an effector of the small G protein Rap1 and plays an important role in endothelial junction stabilization. Rasip1, like afadin, is a multi domain protein, that contains beside a myosin5-like CBD, a Ras-associated domain and a PDZ domain.


Pssm-ID: 271256  Cd Length: 366  Bit Score: 568.83  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 545 EEEALLGEIVRAAASGaGDLPPLGPATLLALCVQHSARELELGHLPRLLGRLARLIKEAVWEKIKEIGDRQPEnHPEGVP 624
Cdd:cd15472   2 HEDALLRRILTLIEPG-GDDHKLTPAFLLCLCIQHSATHFEPGHFGKLLLKIAKRIQEIVWEKTKELAEKQPE-HQDPAS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 625 EVPLTPEAVSVELRPLILWMANTTELLSFVQEKVLEMEKEADQEG--LSSDPQLCNDLELCDEALALLDEVIMCTFQQSV 702
Cdd:cd15472  80 LSLLSIAELAPDLQPLLFWMSNSIELLYFIQQKVPLYEQSMEEELdvGSKESLLSSTLTASEEAMTVLEEVIMYTFQQCV 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 703 YYLTKTLYSTLPALLDSNPFTAgaELPGPGAELEAMPPGLRPTLGVFQAALELTSQCELHPDLVSQTFGYLFFFSNASLL 782
Cdd:cd15472 160 YYLTKTLYVALPALLDSNPFTA--EERESWSGGSRLPEGVRRVLEIYQATLDLLRQYQVHPEIASQMFAYLFFFSNASLF 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 783 NSLMERGQGRPFYQWSRAVQIRTNLDLVLDWLQGAGLGDIATEFFRKLSIAVNLLCVPRTSLLKASWSSLRTDYPTLTPA 862
Cdd:cd15472 238 NQLMEKGSGGGFFQWSRGVQIRANLDLLLDWLQGAGLGDLAEEFFRKLSSTVNLLATPKEQLLQMSWSSLRAEFPALNPA 317

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 61676215 863 QLHHLLSHYQLGPGRGPPPAWDPPPAERDAVDTGDIFESFSSHPPLILP 911
Cdd:cd15472 318 QLHHLLRQYQLGSGRGPPWAQPSPEDAPAAVRTEDILESFDNHPPLVLP 366
FHA_RAIN cd22734
forkhead associated (FHA) domain found in Ras-interacting protein 1 (Rain); Rain, also called ...
 372-484 3.35e-58

forkhead associated (FHA) domain found in Ras-interacting protein 1 (Rain); Rain, also called Rasip1, is an endothelial-specific Ras-interacting protein required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. It acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Rain interacts with Ras in a GTP-dependent manner and may serve as an effector for endomembrane-associated Ras. It contains an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438786  Cd Length: 119  Bit Score: 194.99  E-value: 3.35e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 372 SNRPYFLLLQGYQDAQDFVVYVMTREQHVFGRGGPSSSRGGSPAPYVDTFLNAPDILPRHCTVRA------GPEPPAMVR 445
Cdd:cd22734   1 ADRPYFLLLQGYNDRQDFVLYVMSGKTHIFGRGPKSSSRPGPKAPKVDTFLSAPDILPRHCAVRRadavgeQPHGPALVR 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 61676215 446 PSRGAPVTHNGCLLLREAELHPGDLLGLGEHFLFMYKDP 484
Cdd:cd22734  81 PFRGALVTHNGAPLLREAELQPGDLLGLGEHFLFMYKDP 119
RA_Radil_like cd17116
Ras-associating (RA) domain found in ras-associating and dilute domain-containing protein ...
 131-250 1.59e-46

Ras-associating (RA) domain found in ras-associating and dilute domain-containing protein (Radil) and similar proteins; Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility through linking Rap1 to beta2-integrin activation.This family also includes Ras-interacting protein 1 (Rain, also termed Rasip1), which is a novel Ras-interacting protein with a unique subcellular localization. It interacts with Ras in a GTP-dependent manner, and may serve as an effector for endomembrane-associated Ras. Radil contains RA, DIL, and PDZ domains. In contrast, Rain contains a myosin5-like cargo binding domain, a RA domain and a PDZ domain. RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes.


Pssm-ID: 340636  Cd Length: 121  Bit Score: 162.11  E-value: 1.59e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 131 EPPLPTRAAvPPGVLKIFASGLASGANYKSVLATERSTARELVAEALERYGLtggrgagDSGCVDAYALCDALGRPA--- 207
Cdd:cd17116   3 PAELSTQAS-APGVLKIFGDSICPGANYKSVLATPRSSAQELVKEALERYGL-------ARSEAKQYVLCDVIGRFTgae 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 61676215 208 ----VGVGGGEWRAEHLRVLADAERPLLVQDLWRARPGWARRFELRG 250
Cdd:cd17116  75 kdqsRSSSSERWRTECLRVIGDNEKPLLLQSLWKPKEGFSRRFELRR 121
Myo5-like_CBD cd14945
Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied ...
 544-875 4.84e-46

Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5 a,b,c) in vertebrates and two (myo2 and myo4) in fungi and related to plant class XI myosins. Their C-terminal cargo binding domains is important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. MyoV-CBDs interact with several adaptor proteins that in turn interact with the cargo.


Pssm-ID: 271253 [Multi-domain]  Cd Length: 288  Bit Score: 167.19  E-value: 4.84e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 544 REEEALLGEIVRAAASGAGDLPpLGPATLLALCVQHSARELELGHLPRLLGRLARLIKEAVWEKikeigdrqpenhpegV 623
Cdd:cd14945   1 SEEDSLLRGIVTDFEPSSGDHK-LTPAYILYLCIRHAASNGLTGQSTSLLNKVLKTIQQVVQQH---------------N 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 624 PEVPLtpeavsvelrpLILWMANTTELLSFVQEKV-LEMEKEADQEGLSSDPQLCNDLELCDEalaLLDEVIMCTFQQSV 702
Cdd:cd14945  65 DDMQL-----------LAFWLSNASELLYFLKQDSkLYGAAGEAPQKEEEQKLTVSDLNELKQ---DLEAVSIKIYQQAL 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 703 YYLTKTLYSTLPALLDsnpftagaelpgpgaeleamppglrptlgVFQAALELTSQCELHPDLVSQTFGYLFFFSNASLL 782
Cdd:cd14945 131 KYLNKNLQPKIRDIVK-----------------------------FLNSFLDLLKSFHVHPEIRSQVFTQLFSFINARLF 181

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 783 NSLMERgqgRPFYQWSRAVQIRTNLDLVLDWLQGAGLGDIATEFFRKLSIAVNLLCVPRTSllKASWSSLRTDYPTLTPA 862
Cdd:cd14945 182 NQLITK---KDALSWSRGMQIRANISRLEEWCEGRGLEHLAVDFLSKLIQAVQLLQLKKYT--QEDIEILCELCPSLNPA 256

                       330
                ....*....|...
gi 61676215 863 QLHHLLSHYQLGP 875
Cdd:cd14945 257 QLQAILTQYQPAN 269
FHA_RADIL-like cd22712
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ...
 372-484 2.71e-42

forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing protein (Radil)-like family; The Radil-like family includes Radil and Ras-interacting protein 1 (Rain). Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility by linking Rap1 to beta2-integrin activation. Rain, also called Rasip1, is an endothelial-specific Ras-interacting protein required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. It acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Rain interacts with Ras in a GTP-dependent manner and may serve as an effector for endomembrane-associated Ras. Both Radil and Rain contain an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438764 [Multi-domain]  Cd Length: 120  Bit Score: 150.15  E-value: 2.71e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 372 SNRPYFLLLQGYQDAQDFVVYVMTREQHVFGRGGPSssrggspAPYVDTFLNAPDILPRHCTVRAGPEP----------- 440
Cdd:cd22712   1 SDYPYLLTLRGFSPKQDLLVYPLLEQVILVGSRTEG-------ARKVDISLRAPDILPQHCWIRRKPEPlsddedsdkes 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 61676215 441 ---PAMVRPSRGAPVTHNGCLLLREAELHPGDLLGLGEHFLFMYKDP 484
Cdd:cd22712  74 adyRVVLSPLRGAHVTVNGVPVLSETELHPGDLLGIGEHYLFLFKDP 120
DIL pfam01843
DIL domain; The DIL domain has no known function.
 768-875 2.95e-31

DIL domain; The DIL domain has no known function.


Pssm-ID: 460359 [Multi-domain]  Cd Length: 103  Bit Score: 118.08  E-value: 2.95e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215   768 QTFGYLFFFSNASLLNSLMERgqgRPFYQWSRAVQIRTNLDLVLDWLQGAGLGDIATEFFRKLSIAVNLLCVPRTSLLka 847
Cdd:pfam01843   1 QLFSQLFYFINAELFNRLLLR---KKYCSWSKGMQIRYNLSRLEEWARSNGLESEARDHLAPLIQAAQLLQLRKSTLE-- 75

                          90       100
                  ....*....|....*....|....*...
gi 61676215   848 SWSSLRTDYPTLTPAQLHHLLSHYQLGP 875
Cdd:pfam01843  76 DLDSILQVCPALNPLQLHRLLTLYQPDD 103
FHA_RADIL cd22733
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ...
 375-484 3.28e-18

forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein (Radil); Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility through linking Rap1 to beta2-integrin activation. It contains an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438785  Cd Length: 113  Bit Score: 81.00  E-value: 3.28e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 375 PYFLLLQGYQDAQDFVVYVMTREQHVfgrggpSSSRGGSPAPYVDtfLNAPDILPRHCTVRAGPEPPA------MVRPSR 448
Cdd:cd22733   6 PHLLLLQGYNQQHDCLVYLLNREQHT------VGQETPSSKPNIS--LSAPDILPLHCTIRRVRLPKHrseeklVLEPIP 77

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 61676215 449 GAPVTHNGCLLLREAELHPGDLLGLGEHFLFMYKDP 484
Cdd:cd22733  78 GAHVSVNFSEVERTTLLRHGDLLSFGAYYLFLFKDP 113
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 144-249 1.98e-16

Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in various functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. RA-containing proteins include RalGDS, AF6, RIN, RASSF1, SNX27, CYR1, STE50, and phospholipase C epsilon.


Pssm-ID: 340563  Cd Length: 87  Bit Score: 75.05  E-value: 1.98e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 144 VLKIFASGLASGANYKSVLATERSTARELVAEALERYGLTggrgagdsGCVDAYALCDALGrpavgvgggewRAEHLRVL 223
Cdd:cd17043   1 VLKVYDDDLAPGSAYKSILVSSTTTAREVVQLLLEKYGLE--------EDPEDYSLYEVSE-----------KQETERVL 61

                        90       100
                ....*....|....*....|....*.
gi 61676215 224 ADAERPLLVQDLWRaRPGWARRFELR 249
Cdd:cd17043  62 HDDECPLLIQLEWG-PQGTEFRFVLK 86
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 141-252 5.58e-16

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 73.91  E-value: 5.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215   141 PPGVLKIFASGLASGANYKSVLATERSTARELVAEALERYGLTggrgagdsGCVDAYALCDALGRpavgvGGGEwraehl 220
Cdd:pfam00788   1 DDGVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLEKFGLE--------DDPRDYVLVEVLER-----GGGE------ 61

                          90       100       110
                  ....*....|....*....|....*....|..
gi 61676215   221 RVLADAERPLLVQDLWRaRPGWARRFELRGRE 252
Cdd:pfam00788  62 RRLPDDECPLQIQLQWP-RDASDSRFLLRKRD 92
Myo5p-like_CBD_afadin cd15471
cargo binding domain of myosin 5-like of afadin; Afadin is an actin filament (F-actin) and ...
 640-876 9.91e-13

cargo binding domain of myosin 5-like of afadin; Afadin is an actin filament (F-actin) and Rap1 small G protein-binding protein, found in cadherin-based adherens junctions in epithelial cells, endothelial cells, and fibroblasts. It interacts with cell adhesion molecules and signaling molecules and plays a role in the formation of cell junctions, cell polarization, migration, survival, proliferation, and differentiation. Afadin is a multi domain protein, that contains beside a myosin5-like CBD, two Ras-associated domains, a forkhead-associated domain, a PDZ domain, three proline-rich domains, and an F-actin-binding domain.


Pssm-ID: 271255  Cd Length: 322  Bit Score: 70.42  E-value: 9.91e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 640 LILWMANTTELLSFVQekvlemekeadqeglsSDPQLCNDLELCDEALAlldEVIMCTFQQSVYYLTKTLYSTLPALLDS 719
Cdd:cd15471  79 LAFWMANASELLNFLK----------------QDRDLSAFSVQAQDVLA---EAVQSAFSYLVRCLQEELERSLPAFLDS 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 720 NPFTAGaelpgpgaeleamPPGLRPTLGVFQAALELTSQCELHPDLVSQTFGYLFFFSNASLLNSLMERGQGRPFYQ-WS 798
Cdd:cd15471 140 LVSLDD-------------EPAIGDVLHTLSSAMRLLRRCRVNAALTIQLFSQLFHFINAWLFNSLVSNPDSGLCTRyWG 206

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 799 RAVQIRtnLDLVLDWLQGAGLGDIATEFFRKLSIAVNLLCVPRTS--LLKASWSSLRtdypTLTPAQLHHLLSHYQLGPG 876
Cdd:cd15471 207 KRLRQR--LAHVEAWAERQGLELAADCHLDRIVQAANLLTAPKYSaeDVANLSSTCF----KLNSLQLRALLSHYQPPPG 280
Myo5_CBD cd15470
Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, ...
 640-871 3.61e-12

Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. The MyoV-CBDs directly interact with several adaptor proteins, in case of Myo5a, melanophilin (MLPH), Rab interacting lysosomal protein-like 2 (RILPL2), and granuphilin, and in case of Myo5b, Rab11-family interacting protein 2.


Pssm-ID: 271254 [Multi-domain]  Cd Length: 332  Bit Score: 68.78  E-value: 3.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 640 LILWMANTTELLS----FVQEKVLEMEKEADQEGLssdpQLCN-DLelcDEALALLDEVIMCTFQQSVYYLTKTLYSTLP 714
Cdd:cd15470  72 LSFWLVNTCRLLNclkqYSGEEEFMKHNTPKQNEH----CLKNfDL---SEYRQVLSDLAIQIYQQLIKRAEEILQPTLD 144

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 715 ALLDsnpftagaelpgpgaeleamppglrpTLGVFQAAleLTSQCeLHPDLVSQTFGYLFFFSNASLLNSLMERGQgrpF 794
Cdd:cd15470 145 SLLQ--------------------------QLNSFHTT--LTQHG-LDPELIKQVFRQLFYLICASTLNNLLLRKD---L 192

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 61676215 795 YQWSRAVQIRTNLDLVLDWLQGAGLGDI-ATEFFRKLSIAVNLLCVPRTSLLKAswSSLRTDYPTLTPAQLHHLLSHY 871
Cdd:cd15470 193 CSWSKGMQIRYNVSQLEEWLRDKGLQDSgARETLEPLIQAAQLLQVKKTTEEDA--QSICEMCTKLTTAQIVKILNLY 268
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 142-252 6.94e-08

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 50.76  E-value: 6.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215    142 PGVLKIFASGLASGAnYKSVLATERSTARELVAEALERYGLTGGrgagdsgcVDAYALCDALGRPAvgvgggewraehLR 221
Cdd:smart00314   2 TFVLRVYVDDLPGGT-YKTLRVSSRTTARDVIQQLLEKFHLTDD--------PEEYVLVEVLPDGK------------ER 60

                           90       100       110
                   ....*....|....*....|....*....|.
gi 61676215    222 VLADAERPLLVQDLWRaRPGWARRFELRGRE 252
Cdd:smart00314  61 VLPDDENPLQLQKLWP-RRGPNLRFVLRKRD 90
Myo5p-like_CBD_fungal cd15474
cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin ...
 636-872 8.95e-08

cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin cables, actin filaments that are bundled by fimbrin, in the presence of tropomyosin. This is in contrast to the other vertebrate class V myosins. Like other class V myosins, fungal myosin 2 and 4 contain a C-terminal cargo binding domain. In case of Myo4 it has been shown to bind to the adapter protein She3p (Swi5p-dependent HO expression 3), which in turn anchors myosin 4 to its cargos, zip-coded mRNP (messenger ribonucleoprotein particles) and tER (tubular endoplasmic reticulum). Myo 2 binds to Vac17, vacuole-specific cargo adaptor, and Mmr1, mitochondria-specific cargo adaptor. Both adaptors bind competitivly at the same site.


Pssm-ID: 271258  Cd Length: 352  Bit Score: 55.12  E-value: 8.95e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 636 ELRPLIL-WMANTTELLSFVQEKVLEMEKEADQEGLSSDPQLCNDLElcDEALALLDEVimctfqqsvyyltktlYSTLP 714
Cdd:cd15474  78 ETIPDGAfWLANLHELRSFVVYLLSLIEHSSSDEFSKESEEYWNTLF--DKTLKHLSNI----------------YSTWI 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 715 ALLD--SNPFTAGAEL-----PGPGAELEAMPPGLRPT----------LGVFQAALELTS-QCELHPDLVSQTFGYLfff 776
Cdd:cd15474 140 DKLNkhLSPKIEGAVLvlltsLDLSELIDLNKEFFNKPkkkmadlitfLNEVYDLLQSFSvQPELLNAIVSSTLQYI--- 216

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 777 sNASLLNSLMergQGRPFYQWSRAVQIRTNLDLVLDWLQGAGLGDiATEFFRKLSIAVNLLCVPRTSL--LKAswssLRT 854
Cdd:cd15474 217 -NVEAFNSLI---TKRSALSWKRGSQISYNVSRLKEWCHQHGLSD-ANLQLEPLIQASKLLQLRKDDEndFKI----ILS 287

                       250
                ....*....|....*...
gi 61676215 855 DYPTLTPAQLHHLLSHYQ 872
Cdd:cd15474 288 VCYALNPAQIQKLLDKYQ 305
Myo5p-like_CBD_DIL_ANK cd15473
cargo binding domain of myosin 5-like of dil and ankyrin domain containing protein; DIL and ...
 640-871 1.57e-06

cargo binding domain of myosin 5-like of dil and ankyrin domain containing protein; DIL and ankyrin domain-containing protein are a group of fungal proteins that contain a domain homologous to the cargo binding domain of class V myosins and ankyrin repeats. Their function is unknown.


Pssm-ID: 271257 [Multi-domain]  Cd Length: 316  Bit Score: 51.02  E-value: 1.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 640 LILWMANTTELLSFvqekvlemekeadqegLSSDPQLCndlELCDEALALLDEVImctfqQSVY-YLTKTLYSTLPALLD 718
Cdd:cd15473  78 LAFWLSNVTLLLHY----------------LKKDAGLV---EATPEFQQELAELI-----NEIFvLIIRDAERRIDKLLD 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 719 SNP------FTAgaelpgpgaeleamppglrpTLGVfqaaLELTsqcELHPDLVSQTFGYLFFFSNASLLNSLMERgqgR 792
Cdd:cd15473 134 ASPrnitslLSS--------------------TLYV----LELY---DVHPAIIIQALSQLFYWLGCELFNRILTN---K 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 793 PFYQWSRAVQIRTNLDLVLDWLQGAGLGDIATEFFRKlsIAVNLLCvPRTSLLKasW----SSLrTDYPTL--------- 859
Cdd:cd15473 184 KYLCRSKAMQIRMNLSALEDWARSNNLQPEKGESPPR--IARSHLA-PVIQLLQ--WlqclSSL-DDFESLiatiqqlda 257

                       250
                ....*....|...
gi 61676215 860 -TPAQLHHLLSHY 871
Cdd:cd15473 258 lNPLQLLRAVKDY 270
FHA_AFDN cd22711
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ...
 422-484 7.68e-06

forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ALL1-fused gene from chromosome 6 protein, protein AF-6, Afadin adherens junction formation factor, or MLLT4, is a nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. It is essential for the organization of adherens junctions. It may play a key role in the organization of epithelial structures of the embryonic ectoderm. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438763 [Multi-domain]  Cd Length: 106  Bit Score: 45.78  E-value: 7.68e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 61676215 422 LNAPDILPRHCTVrAGPEPPAMVRPSRGAPVTH-NGCLLLREAELHPGDLLGLGEHFLFMYKDP 484
Cdd:cd22711  44 LFGPDILPRHCVI-THMEGVVTVTPASQDAETYvNGQRIYETTMLQHGMVVQFGRSHTFRFCDP 106
RA2_DAGK-theta cd01783
Ras-associating (RA) domain 2 found in diacylgylcerol kinase theta (DAGK-theta) and similar ...
 143-182 1.86e-05

Ras-associating (RA) domain 2 found in diacylgylcerol kinase theta (DAGK-theta) and similar proteins; DAGK phosphorylates the second messenger diacylglycerol to phosphatidic acid as part of a protein kinase C pathway. DAGK-theta is characterized as a type V DAGK that has three cysteine-rich domains (all other isoforms have two), a proline/glycine-rich domain at its N-terminal, and a proposed Ras-associating (RA) domain. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has a beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. There are ten mammalian isoforms of DAGK have been identified to date, these are organized into five categories based on the domain architecture. DAGK-theta also contains a pleckstrin homology (PH) domain. The subcellular localization and the activity of DAGK-theta are regulated in a complex (stimulation- and cell type-dependent) manner. This family corresponds to the second RA domain of DAGK-theta.


Pssm-ID: 340481  Cd Length: 95  Bit Score: 44.14  E-value: 1.86e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 61676215 143 GVLKIFASGLASGANYKSVLATERSTARELVAEALERYGL 182
Cdd:cd01783   1 GYIRVYPGWLKVGVAYKSIPVTKETTVEEVIKEALPKFGL 40
RA2_Afadin cd01781
Ras-associating (RA) domain 2 found in Afadin; Afadin, also termed ALL1-fused gene from ...
 143-251 5.01e-05

Ras-associating (RA) domain 2 found in Afadin; Afadin, also termed ALL1-fused gene from chromosome 6 protein (AF-6), or canoe, is involved in many fundamental signaling cascades in cells. In addition, it is involved in oncogenesis and metastasis. Afadin has multiple domains: from the N-terminus to the C-terminus it has two Ras-associated (RA) domains, a forkhead-associated domain, a dilute domain, a PDZ domain, three proline-rich domains, and an F-actin binding domain. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has a beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. Afadin is abundant at cadherin-based adherens junctions in epithelial cells, endothelial cells, and fibroblasts. This family corresponds to the second RA domain of afadin.


Pssm-ID: 340479  Cd Length: 102  Bit Score: 43.03  E-value: 5.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 143 GVLKIFASGLASGANYKSVLATERSTARELVAEALERYGLtggrgagDSGCVDAYALCDALGRPAVG-VGGGEWRAEhlR 221
Cdd:cd01781   2 GTLKIYGDSLKPEVPYKTLLLSTNDTADFVVREALEKYGL-------EKENPKDYCLVQVVLPPGGSpRLDGGGGKE--R 72

                        90       100       110
                ....*....|....*....|....*....|
gi 61676215 222 VLADAERPLLVQDLWrARPGWARRFELRGR 251
Cdd:cd01781  73 ILDDDECPLAILMRW-PPSKGTLVFQLRRR 101
Myo5b_CBD cd15477
Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, ...
 761-819 1.01e-03

Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. They interact with several adaptor proteins, in case of Myo5b-CBD, Rab11-family interacting protein 2.


Pssm-ID: 271261  Cd Length: 372  Bit Score: 42.54  E-value: 1.01e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 61676215 761 LHPDLVSQTFGYLFFFSNASLLNSLMERgqgRPFYQWSRAVQIRTNLDLVLDWLQGAGL 819
Cdd:cd15477 200 LDPEIIQQVFKQLFYMINAVTLNNLLLR---KDVCSWSTGMQLRYNISQLEEWLRGRNL 255
Myo5c_CBD cd15476
Cargo binding domain of myosin 5C; Class V myosins are well studied unconventional myosins, ...
 738-843 1.19e-03

Cargo binding domain of myosin 5C; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. The MyoV-CBDs directly interact with several adaptor proteins.MyoVb and myoVc areprimarily expressed in epithelial cells, and have been implicated as motors involved in recycling endosomes.


Pssm-ID: 271260 [Multi-domain]  Cd Length: 332  Bit Score: 42.08  E-value: 1.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 738 MPPGLRPT-------LGVFQAALeltSQCELHPDLVSQTFGYLFFFSNASLLNSLMERgqgRPFYQWSRAVQIRTNLDLV 810
Cdd:cd15476 136 MENNLQPTissilqqLSYFYSTM---CQHGMDPELIKQAVKQLFFLIGAVTLNSIFLR---KDMCSCRKGMQIRCNISYL 209

                        90       100       110
                ....*....|....*....|....*....|....
gi 61676215 811 LDWLQGAGL-GDIATEFFRKLSIAVNLLCVPRTS 843
Cdd:cd15476 210 EEWLKEKNLqNSNAKETLEPLSQAAWLLQVNKTT 243
RA_Myosin-IX cd01779
Ras-associating (RA) domain found in Myosin-IX; Myosins IX (Myo9) is a class of unique motor ...
 144-251 3.33e-03

Ras-associating (RA) domain found in Myosin-IX; Myosins IX (Myo9) is a class of unique motor proteins with a common structure of an N-terminal extension preceding a myosin head homologous to the Ras-association (RA) domain, a head (motor) domain, a neck with IQ motifs that bind light chains and a C-terminal tail containing a Rho-GTPase activating protein (RhoGAP) domain. The RA domain is located at its head domain and has the beta-grasp ubiquitin-like fold with unknown function. There are two genes for myosins IX in humans, IXa and IXb, that are different in their expression and localization. IXa is expressed abundantly in brain and testis and IXb is expressed abundantly in tissues of the immune system.


Pssm-ID: 340477  Cd Length: 97  Bit Score: 37.69  E-value: 3.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676215 144 VLKIFASGLASGANYKSVLATERSTARELVAEALERYGLTGgrgagdsgcVDAYALCDALGRPavGVGGGEWRaehlrvL 223
Cdd:cd01779   1 MVRVYPGALSPETEFLSVEATKQTTASEVIECLVAKLRLDK---------AECYELAEVCGSG--GQGCKERR------L 63

                        90       100       110
                ....*....|....*....|....*....|....
gi 61676215 224 ADAERPLLVQDLWRARPGWAR------RFELRGR 251
Cdd:cd01779  64 GPSENPVQVQLLWPKMAGDSDnqvtsyRFFLREK 97
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
 427-479 4.03e-03

forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438782 [Multi-domain]  Cd Length: 99  Bit Score: 37.59  E-value: 4.03e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 61676215 427 ILPRHCTVRAGPEPPAMVRPSRGAPVTHNGCLLLREAELHPGDLLGLGEHFLF 479
Cdd:cd22730  42 ILPEHCIIDITPEGQVMLTPQKNTRTFVNGSAVTSPIQLHHGDRILWGNNHFF 94
 
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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