NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|512854841|ref|XP_004916311|]
View 

ras-interacting protein 1 isoform X2 [Xenopus tropicalis]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
520-884 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: 611.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 520 QEEDSVLKEIIEKTGNPGSDFKLAPAYLFSLCLEHSTKALDPGHFPKLVMKIASFIKEVVWEKIKEIGDKQPENQqDRGL 599
Cdd:cd15472    1 AHEDALLRRILTLIEPGGDDHKLTPAFLLCLCIQHSATHFEPGHFGKLLLKIAKRIQEIVWEKTKELAEKQPEHQ-DPAS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 600 PCALGIEEVATDLRPLMLWMSNSMELLNFVQRKILDLEKEWESEGS--SQDTLLSSDIEACEESMALLDEVIMYTFQQCV 677
Cdd:cd15472   80 LSLLSIAELAPDLQPLLFWMSNSIELLYFIQQKVPLYEQSMEEELDvgSKESLLSSTLTASEEAMTVLEEVIMYTFQQCV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 678 YYLTKTLYAALPALLESNPFTDPaSLSDVGELSNMPEGTRGTLAIYQATLDLTRECELHPDLVSQTFGYLFFFSNASLFN 757
Cdd:cd15472  160 YYLTKTLYVALPALLDSNPFTAE-ERESWSGGSRLPEGVRRVLEIYQATLDLLRQYQVHPEIASQMFAYLFFFSNASLFN 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 758 TLMEKGNGEPFYQWSKAVQIRTNLDLVLDWLQGIGLGDIAAEFFRKLSATVNLLCIPKTSLMKVSWSTLRNDYPALSSAQ 837
Cdd:cd15472  239 QLMEKGSGGGFFQWSRGVQIRANLDLLLDWLQGAGLGDLAEEFFRKLSSTVNLLATPKEQLLQMSWSSLRAEFPALNPAQ 318
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 512854841 838 LNHLLRNYHLGVGRSHPAAWEPPEEEKEEI-TNNIFESFTEHPPLILP 884
Cdd:cd15472  319 LHHLLRQYQLGSGRGPPWAQPSPEDAPAAVrTEDILESFDNHPPLVLP 366
FHA_RAIN cd22734
forkhead associated (FHA) domain found in Ras-interacting protein 1 (Rain); Rain, also called ...
352-465 3.64e-70

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: 227.74  E-value: 3.64e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 352 AEHPYFLLLQGYNKDQDFVIYVMTRKKHLFGRAEKSL---RDKGPYVDTFLSAPDILPRHCSVWRLDSSGQ--KYIVRVR 426
Cdd:cd22734    1 ADRPYFLLLQGYNDRQDFVLYVMSGKTHIFGRGPKSSsrpGPKAPKVDTFLSAPDILPRHCAVRRADAVGEqpHGPALVR 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 512854841 427 PYRGALVTHNGRVLQRETELHTGDLLGLGEHFLFMYKDP 465
Cdd:cd22734   81 PFRGALVTHNGAPLLREAELQPGDLLGLGEHFLFMYKDP 119
RA_Radil_like cd17116
Ras-associating (RA) domain found in ras-associating and dilute domain-containing protein ...
112-223 1.36e-64

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: 212.57  E-value: 1.36e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 112 EDLVELSSQKNLPGILKIFGDDISSGTNYKSVLATPRSSAEELVKEALERYAVADSETEVFVLCDVVGRFVGLE------ 185
Cdd:cd17116    1 DDPAELSTQASAPGVLKIFGDSICPGANYKSVLATPRSSAQELVKEALERYGLARSEAKQYVLCDVIGRFTGAEkdqsrs 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 512854841 186 ---GEWKMEYLRVVGDNERPLVLQEMWKPKTGFSRRFEIRR 223
Cdd:cd17116   81 sssERWRTECLRVIGDNEKPLLLQSLWKPKEGFSRRFELRR 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 ...
520-884 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: 611.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 520 QEEDSVLKEIIEKTGNPGSDFKLAPAYLFSLCLEHSTKALDPGHFPKLVMKIASFIKEVVWEKIKEIGDKQPENQqDRGL 599
Cdd:cd15472    1 AHEDALLRRILTLIEPGGDDHKLTPAFLLCLCIQHSATHFEPGHFGKLLLKIAKRIQEIVWEKTKELAEKQPEHQ-DPAS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 600 PCALGIEEVATDLRPLMLWMSNSMELLNFVQRKILDLEKEWESEGS--SQDTLLSSDIEACEESMALLDEVIMYTFQQCV 677
Cdd:cd15472   80 LSLLSIAELAPDLQPLLFWMSNSIELLYFIQQKVPLYEQSMEEELDvgSKESLLSSTLTASEEAMTVLEEVIMYTFQQCV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 678 YYLTKTLYAALPALLESNPFTDPaSLSDVGELSNMPEGTRGTLAIYQATLDLTRECELHPDLVSQTFGYLFFFSNASLFN 757
Cdd:cd15472  160 YYLTKTLYVALPALLDSNPFTAE-ERESWSGGSRLPEGVRRVLEIYQATLDLLRQYQVHPEIASQMFAYLFFFSNASLFN 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 758 TLMEKGNGEPFYQWSKAVQIRTNLDLVLDWLQGIGLGDIAAEFFRKLSATVNLLCIPKTSLMKVSWSTLRNDYPALSSAQ 837
Cdd:cd15472  239 QLMEKGSGGGFFQWSRGVQIRANLDLLLDWLQGAGLGDLAEEFFRKLSSTVNLLATPKEQLLQMSWSSLRAEFPALNPAQ 318
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 512854841 838 LNHLLRNYHLGVGRSHPAAWEPPEEEKEEI-TNNIFESFTEHPPLILP 884
Cdd:cd15472  319 LHHLLRQYQLGSGRGPPWAQPSPEDAPAAVrTEDILESFDNHPPLVLP 366
FHA_RAIN cd22734
forkhead associated (FHA) domain found in Ras-interacting protein 1 (Rain); Rain, also called ...
352-465 3.64e-70

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: 227.74  E-value: 3.64e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 352 AEHPYFLLLQGYNKDQDFVIYVMTRKKHLFGRAEKSL---RDKGPYVDTFLSAPDILPRHCSVWRLDSSGQ--KYIVRVR 426
Cdd:cd22734    1 ADRPYFLLLQGYNDRQDFVLYVMSGKTHIFGRGPKSSsrpGPKAPKVDTFLSAPDILPRHCAVRRADAVGEqpHGPALVR 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 512854841 427 PYRGALVTHNGRVLQRETELHTGDLLGLGEHFLFMYKDP 465
Cdd:cd22734   81 PFRGALVTHNGAPLLREAELQPGDLLGLGEHFLFMYKDP 119
RA_Radil_like cd17116
Ras-associating (RA) domain found in ras-associating and dilute domain-containing protein ...
112-223 1.36e-64

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: 212.57  E-value: 1.36e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 112 EDLVELSSQKNLPGILKIFGDDISSGTNYKSVLATPRSSAEELVKEALERYAVADSETEVFVLCDVVGRFVGLE------ 185
Cdd:cd17116    1 DDPAELSTQASAPGVLKIFGDSICPGANYKSVLATPRSSAQELVKEALERYGLARSEAKQYVLCDVIGRFTGAEkdqsrs 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 512854841 186 ---GEWKMEYLRVVGDNERPLVLQEMWKPKTGFSRRFEIRR 223
Cdd:cd17116   81 sssERWRTECLRVIGDNEKPLLLQSLWKPKEGFSRRFELRR 121
DIL pfam01843
DIL domain; The DIL domain has no known function.
742-849 2.67e-29

DIL domain; The DIL domain has no known function.


Pssm-ID: 460359 [Multi-domain]  Cd Length: 103  Bit Score: 112.30  E-value: 2.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841  742 QTFGYLFFFSNASLFNTLMEKGNgepFYQWSKAVQIRTNLDLVLDWLQGIGLGDIAAEFFRKLSATVNLLCIPKTSLmkV 821
Cdd:pfam01843   1 QLFSQLFYFINAELFNRLLLRKK---YCSWSKGMQIRYNLSRLEEWARSNGLESEARDHLAPLIQAAQLLQLRKSTL--E 75
                          90       100
                  ....*....|....*....|....*...
gi 512854841  822 SWSTLRNDYPALSSAQLNHLLRNYHLGV 849
Cdd:pfam01843  76 DLDSILQVCPALNPLQLHRLLTLYQPDD 103
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
124-225 1.17e-17

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: 78.91  E-value: 1.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841  124 PGILKIFGDDISSGTNYKSVLATPRSSAEELVKEALERYAVADSETEvFVLCDVVGRfvgLEGEWKMEylrvvgDNERPL 203
Cdd:pfam00788   2 DGVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLEKFGLEDDPRD-YVLVEVLER---GGGERRLP------DDECPL 71
                          90       100
                  ....*....|....*....|..
gi 512854841  204 VLQEMWKPKTGfSRRFEIRRKQ 225
Cdd:pfam00788  72 QIQLQWPRDAS-DSRFLLRKRD 92
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
124-224 1.80e-10

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: 58.08  E-value: 1.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841   124 PGILKIFGDDISSGTnYKSVLATPRSSAEELVKEALERYAVaDSETEVFVLCDVVGRfvGLEgewkmeylRVVGDNERPL 203
Cdd:smart00314   2 TFVLRVYVDDLPGGT-YKTLRVSSRTTARDVIQQLLEKFHL-TDDPEEYVLVEVLPD--GKE--------RVLPDDENPL 69
                           90       100
                   ....*....|....*....|.
gi 512854841   204 VLQEMWKPKTGfSRRFEIRRK 224
Cdd:smart00314  70 QLQKLWPRRGP-NLRFVLRKR 89
 
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 ...
520-884 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: 611.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 520 QEEDSVLKEIIEKTGNPGSDFKLAPAYLFSLCLEHSTKALDPGHFPKLVMKIASFIKEVVWEKIKEIGDKQPENQqDRGL 599
Cdd:cd15472    1 AHEDALLRRILTLIEPGGDDHKLTPAFLLCLCIQHSATHFEPGHFGKLLLKIAKRIQEIVWEKTKELAEKQPEHQ-DPAS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 600 PCALGIEEVATDLRPLMLWMSNSMELLNFVQRKILDLEKEWESEGS--SQDTLLSSDIEACEESMALLDEVIMYTFQQCV 677
Cdd:cd15472   80 LSLLSIAELAPDLQPLLFWMSNSIELLYFIQQKVPLYEQSMEEELDvgSKESLLSSTLTASEEAMTVLEEVIMYTFQQCV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 678 YYLTKTLYAALPALLESNPFTDPaSLSDVGELSNMPEGTRGTLAIYQATLDLTRECELHPDLVSQTFGYLFFFSNASLFN 757
Cdd:cd15472  160 YYLTKTLYVALPALLDSNPFTAE-ERESWSGGSRLPEGVRRVLEIYQATLDLLRQYQVHPEIASQMFAYLFFFSNASLFN 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 758 TLMEKGNGEPFYQWSKAVQIRTNLDLVLDWLQGIGLGDIAAEFFRKLSATVNLLCIPKTSLMKVSWSTLRNDYPALSSAQ 837
Cdd:cd15472  239 QLMEKGSGGGFFQWSRGVQIRANLDLLLDWLQGAGLGDLAEEFFRKLSSTVNLLATPKEQLLQMSWSSLRAEFPALNPAQ 318
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 512854841 838 LNHLLRNYHLGVGRSHPAAWEPPEEEKEEI-TNNIFESFTEHPPLILP 884
Cdd:cd15472  319 LHHLLRQYQLGSGRGPPWAQPSPEDAPAAVrTEDILESFDNHPPLVLP 366
FHA_RAIN cd22734
forkhead associated (FHA) domain found in Ras-interacting protein 1 (Rain); Rain, also called ...
352-465 3.64e-70

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: 227.74  E-value: 3.64e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 352 AEHPYFLLLQGYNKDQDFVIYVMTRKKHLFGRAEKSL---RDKGPYVDTFLSAPDILPRHCSVWRLDSSGQ--KYIVRVR 426
Cdd:cd22734    1 ADRPYFLLLQGYNDRQDFVLYVMSGKTHIFGRGPKSSsrpGPKAPKVDTFLSAPDILPRHCAVRRADAVGEqpHGPALVR 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 512854841 427 PYRGALVTHNGRVLQRETELHTGDLLGLGEHFLFMYKDP 465
Cdd:cd22734   81 PFRGALVTHNGAPLLREAELQPGDLLGLGEHFLFMYKDP 119
RA_Radil_like cd17116
Ras-associating (RA) domain found in ras-associating and dilute domain-containing protein ...
112-223 1.36e-64

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: 212.57  E-value: 1.36e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 112 EDLVELSSQKNLPGILKIFGDDISSGTNYKSVLATPRSSAEELVKEALERYAVADSETEVFVLCDVVGRFVGLE------ 185
Cdd:cd17116    1 DDPAELSTQASAPGVLKIFGDSICPGANYKSVLATPRSSAQELVKEALERYGLARSEAKQYVLCDVIGRFTGAEkdqsrs 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 512854841 186 ---GEWKMEYLRVVGDNERPLVLQEMWKPKTGFSRRFEIRR 223
Cdd:cd17116   81 sssERWRTECLRVIGDNEKPLLLQSLWKPKEGFSRRFELRR 121
Myo5-like_CBD cd14945
Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied ...
521-847 1.12e-55

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: 194.54  E-value: 1.12e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 521 EEDSVLKEIIEKTGNPGSDFKLAPAYLFSLCLEHSTKALDPGHFPKLVMKIASFIKEVVWEKikeigdkqpenqQDrglp 600
Cdd:cd14945    2 EEDSLLRGIVTDFEPSSGDHKLTPAYILYLCIRHAASNGLTGQSTSLLNKVLKTIQQVVQQH------------ND---- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 601 calgieevatDLRPLMLWMSNSMELLNFVQRKILDLEKEWESEgsSQDTLLSSDIEACEESMALLDEVIMYTFQQCVYYL 680
Cdd:cd14945   66 ----------DMQLLAFWLSNASELLYFLKQDSKLYGAAGEAP--QKEEEQKLTVSDLNELKQDLEAVSIKIYQQALKYL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 681 TKTLYAALpallesnpftdpaslsdvgelsnmpegtRGTLAIYQATLDLTRECELHPDLVSQTFGYLFFFSNASLFNTLM 760
Cdd:cd14945  134 NKNLQPKI----------------------------RDIVKFLNSFLDLLKSFHVHPEIRSQVFTQLFSFINARLFNQLI 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 761 EKGngePFYQWSKAVQIRTNLDLVLDWLQGIGLGDIAAEFFRKLSATVNLLCIPKTSLMkvSWSTLRNDYPALSSAQLNH 840
Cdd:cd14945  186 TKK---DALSWSRGMQIRANISRLEEWCEGRGLEHLAVDFLSKLIQAVQLLQLKKYTQE--DIEILCELCPSLNPAQLQA 260

                 ....*..
gi 512854841 841 LLRNYHL 847
Cdd:cd14945  261 ILTQYQP 267
FHA_RADIL-like cd22712
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ...
355-465 1.59e-39

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: 142.06  E-value: 1.59e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 355 PYFLLLQGYNKDQDFVIYVMTRKKHLFGRAEkslrDKGPYVDTFLSAPDILPRHCSVWR----------LDSSGQKYIVR 424
Cdd:cd22712    4 PYLLTLRGFSPKQDLLVYPLLEQVILVGSRT----EGARKVDISLRAPDILPQHCWIRRkpeplsddedSDKESADYRVV 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 512854841 425 VRPYRGALVTHNGRVLQRETELHTGDLLGLGEHFLFMYKDP 465
Cdd:cd22712   80 LSPLRGAHVTVNGVPVLSETELHPGDLLGIGEHYLFLFKDP 120
DIL pfam01843
DIL domain; The DIL domain has no known function.
742-849 2.67e-29

DIL domain; The DIL domain has no known function.


Pssm-ID: 460359 [Multi-domain]  Cd Length: 103  Bit Score: 112.30  E-value: 2.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841  742 QTFGYLFFFSNASLFNTLMEKGNgepFYQWSKAVQIRTNLDLVLDWLQGIGLGDIAAEFFRKLSATVNLLCIPKTSLmkV 821
Cdd:pfam01843   1 QLFSQLFYFINAELFNRLLLRKK---YCSWSKGMQIRYNLSRLEEWARSNGLESEARDHLAPLIQAAQLLQLRKSTL--E 75
                          90       100
                  ....*....|....*....|....*...
gi 512854841  822 SWSTLRNDYPALSSAQLNHLLRNYHLGV 849
Cdd:pfam01843  76 DLDSILQVCPALNPLQLHRLLTLYQPDD 103
Myo5p-like_CBD_afadin cd15471
cargo binding domain of myosin 5-like of afadin; Afadin is an actin filament (F-actin) and ...
522-853 5.43e-24

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: 103.93  E-value: 5.43e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 522 EDSVLKEIIEKTGNPGSDFKLAPAYLFSLCLEHSTKALDPGHF------PKLVM---KIASFIKEVvwekikeigdkqpe 592
Cdd:cd15471    3 EEPFLSAVITYTNSSTPHFKLSPAYTLYLAARYRLSTHYRPELtpteraHKLTAflnKIASLIQQV-------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 593 nqqdrglpcalgIEEVATDLRPLMLWMSNSMELLNFVQrkildlekewesegssQDTLLSsdiEACEESMALLDEVIMYT 672
Cdd:cd15471   69 ------------IQEQRNIAGALAFWMANASELLNFLK----------------QDRDLS---AFSVQAQDVLAEAVQSA 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 673 FQQCVYYLTKTLYAALPALLESnpftdpaslsdvGELSNMPEGTRGTLAIYQATLDLTRECELHPDLVSQTFGYLFFFSN 752
Cdd:cd15471  118 FSYLVRCLQEELERSLPAFLDS------------LVSLDDEPAIGDVLHTLSSAMRLLRRCRVNAALTIQLFSQLFHFIN 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 753 ASLFNTLM-EKGNGEPFYQWSKAVQIRtnLDLVLDWL--QGIGLgdiAAE--FFRKLSATvNLLCIPKTS---LMKVSwS 824
Cdd:cd15471  186 AWLFNSLVsNPDSGLCTRYWGKRLRQR--LAHVEAWAerQGLEL---AADchLDRIVQAA-NLLTAPKYSaedVANLS-S 258
                        330       340
                 ....*....|....*....|....*....
gi 512854841 825 TLRNdypaLSSAQLNHLLRNYHLGVGRSH 853
Cdd:cd15471  259 TCFK----LNSLQLRALLSHYQPPPGEPP 283
FHA_RADIL cd22733
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ...
355-465 1.84e-23

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: 96.02  E-value: 1.84e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 355 PYFLLLQGYNKDQDFVIYVMTRKKHLFGRAEKSLRdkgPYVDtfLSAPDILPRHCSVWRL---DSSGQKYIVrVRPYRGA 431
Cdd:cd22733    6 PHLLLLQGYNQQHDCLVYLLNREQHTVGQETPSSK---PNIS--LSAPDILPLHCTIRRVrlpKHRSEEKLV-LEPIPGA 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 512854841 432 LVTHNGRVLQRETELHTGDLLGLGEHFLFMYKDP 465
Cdd:cd22733   80 HVSVNFSEVERTTLLRHGDLLSFGAYYLFLFKDP 113
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
124-225 1.17e-17

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: 78.91  E-value: 1.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841  124 PGILKIFGDDISSGTNYKSVLATPRSSAEELVKEALERYAVADSETEvFVLCDVVGRfvgLEGEWKMEylrvvgDNERPL 203
Cdd:pfam00788   2 DGVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLEKFGLEDDPRD-YVLVEVLER---GGGERRLP------DDECPL 71
                          90       100
                  ....*....|....*....|..
gi 512854841  204 VLQEMWKPKTGfSRRFEIRRKQ 225
Cdd:pfam00788  72 QIQLQWPRDAS-DSRFLLRKRD 92
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
126-223 6.44e-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: 73.51  E-value: 6.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 126 ILKIFGDDISSGTNYKSVLATPRSSAEELVKEALERYAVADSeTEVFVLCDVVGrfvglegewKMEYLRVVGDNERPLVL 205
Cdd:cd17043    1 VLKVYDDDLAPGSAYKSILVSSTTTAREVVQLLLEKYGLEED-PEDYSLYEVSE---------KQETERVLHDDECPLLI 70
                         90
                 ....*....|....*...
gi 512854841 206 QEMWKPKTGfSRRFEIRR 223
Cdd:cd17043   71 QLEWGPQGT-EFRFVLKR 87
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
124-224 1.80e-10

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: 58.08  E-value: 1.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841   124 PGILKIFGDDISSGTnYKSVLATPRSSAEELVKEALERYAVaDSETEVFVLCDVVGRfvGLEgewkmeylRVVGDNERPL 203
Cdd:smart00314   2 TFVLRVYVDDLPGGT-YKTLRVSSRTTARDVIQQLLEKFHL-TDDPEEYVLVEVLPD--GKE--------RVLPDDENPL 69
                           90       100
                   ....*....|....*....|.
gi 512854841   204 VLQEMWKPKTGfSRRFEIRRK 224
Cdd:smart00314  70 QLQKLWPRRGP-NLRFVLRKR 89
RA2_Afadin cd01781
Ras-associating (RA) domain 2 found in Afadin; Afadin, also termed ALL1-fused gene from ...
125-224 2.24e-10

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: 58.44  E-value: 2.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 125 GILKIFGDDISSGTNYKSVLATPRSSAEELVKEALERYAVADSETEVFVLCDVV---GRFVGLEGEWKMEYlrVVGDNER 201
Cdd:cd01781    2 GTLKIYGDSLKPEVPYKTLLLSTNDTADFVVREALEKYGLEKENPKDYCLVQVVlppGGSPRLDGGGGKER--ILDDDEC 79
                         90       100
                 ....*....|....*....|...
gi 512854841 202 PLVLQEMWKPKTGfSRRFEIRRK 224
Cdd:cd01781   80 PLAILMRWPPSKG-TLVFQLRRR 101
Myo5_CBD cd15470
Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, ...
541-845 1.19e-07

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: 54.52  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 541 KLAPAYLFSLCLEHsTKALDPGHfpklvmKIASFIKEVVwEKIKEIGDKQPEnqqdrglpcalgieevatDLRPLMLWMS 620
Cdd:cd15470   24 PGLPAYILFMCIRH-ADYVNDEA------KVRSLLTATI-NAIKKVLKKHSE------------------DFEMLSFWLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 621 NSMELLNFVqRKILDLEKEWESEGSSQD--TLLSSDIEaceESMALLDEVIMYTFQQCVYYLTKTLYAALPALLesnpft 698
Cdd:cd15470   78 NTCRLLNCL-KQYSGEEEFMKHNTPKQNehCLKNFDLS---EYRQVLSDLAIQIYQQLIKRAEEILQPTLDSLL------ 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 699 dpaslsdvGELSNmpegtrgtlaIYQAtldLTRECeLHPDLVSQTFGYLFFFSNASLFNTLMEKGNgepFYQWSKAVQIR 778
Cdd:cd15470  148 --------QQLNS----------FHTT---LTQHG-LDPELIKQVFRQLFYLICASTLNNLLLRKD---LCSWSKGMQIR 202
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512854841 779 TNLDLVLDWLQGIGLGDIAA-EFFRKLSATVNLLCIPKTSLMKVswSTLRNDYPALSSAQLNHLLRNY 845
Cdd:cd15470  203 YNVSQLEEWLRDKGLQDSGArETLEPLIQAAQLLQVKKTTEEDA--QSICEMCTKLTTAQIVKILNLY 268
FHA_AFDN cd22711
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ...
385-465 1.14e-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: 48.09  E-value: 1.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 385 EKSLRDKGPYVDtfLSAPDILPRHCSVWRLDSsgqkyIVRVRPYRG-ALVTHNGRVLQRETELHTGDLLGLGEHFLFMYK 463
Cdd:cd22711   32 ERSPANSGQFIQ--LFGPDILPRHCVITHMEG-----VVTVTPASQdAETYVNGQRIYETTMLQHGMVVQFGRSHTFRFC 104

                 ..
gi 512854841 464 DP 465
Cdd:cd22711  105 DP 106
Myo5p-like_CBD_fungal cd15474
cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin ...
611-853 1.22e-05

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: 48.57  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 611 DLRPLML-WMSNSMELLNFVQRKILDLEKEWESEGSSQDTLLSSDIEacEESMALLDEVIMYTFQQCVYYLTKTLYAALP 689
Cdd:cd15474   78 ETIPDGAfWLANLHELRSFVVYLLSLIEHSSSDEFSKESEEYWNTLF--DKTLKHLSNIYSTWIDKLNKHLSPKIEGAVL 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 690 ALLESNPFTDPASLSDvgelsNMPEGTRGTLAIYQATLDLTREC----ELHPDLVSQTFGYLFFFSNASLFNTLMekgNG 765
Cdd:cd15474  156 VLLTSLDLSELIDLNK-----EFFNKPKKKMADLITFLNEVYDLlqsfSVQPELLNAIVSSTLQYINVEAFNSLI---TK 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 766 EPFYQWSKAVQIRTNLDLVLDWLQGIGLGDiAAEFFRKLSATVNLLCIPKTSL--MKVswstLRNDYPALSSAQLNHLLR 843
Cdd:cd15474  228 RSALSWKRGSQISYNVSRLKEWCHQHGLSD-ANLQLEPLIQASKLLQLRKDDEndFKI----ILSVCYALNPAQIQKLLD 302
                        250
                 ....*....|
gi 512854841 844 NYHLGVGRSH 853
Cdd:cd15474  303 KYQPANYEAP 312
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
360-460 1.31e-05

forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.


Pssm-ID: 438714 [Multi-domain]  Cd Length: 92  Bit Score: 44.57  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 360 LQGYNKDQDFVIYVMTRKKHLFGRAEKSlrdkgpyvDTFLSAPDILPRHCSVWRLDSSgqkyiVRVRPYRGALVTH-NGR 438
Cdd:cd00060    2 LIVLDGDGGGREFPLTKGVVTIGRSPDC--------DIVLDDPSVSRRHARIEVDGGG-----VYLEDLGSTNGTFvNGK 68
                         90       100
                 ....*....|....*....|...
gi 512854841 439 VLQRETELHTGDLLGLGEH-FLF 460
Cdd:cd00060   69 RITPPVPLQDGDVIRLGDTtFRF 91
RA2_DAGK-theta cd01783
Ras-associating (RA) domain 2 found in diacylgylcerol kinase theta (DAGK-theta) and similar ...
125-205 1.50e-04

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: 41.44  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 125 GILKIFGDDISSGTNYKSVLATPRSSAEELVKEALERYAVADSETEVFVLCDVV-GRFVglegewkMEylRVVGDNERPL 203
Cdd:cd01783    1 GYIRVYPGWLKVGVAYKSIPVTKETTVEEVIKEALPKFGLQDEDPEDFRLVEVLmDKGV-------VE--RVMLRDECPW 71

                 ..
gi 512854841 204 VL 205
Cdd:cd01783   72 LI 73
FHA_KIF16 cd22708
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ...
396-465 3.16e-04

forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 family includes StARD9/KIF16A and KIF16B. StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. 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: 438760 [Multi-domain]  Cd Length: 109  Bit Score: 41.10  E-value: 3.16e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 396 DTFLSAPDILPRHCsvwRLDSSGQKyiVRVRPYRGALVTHNGRVLQRETELHTGDLLGLGEHFLFMYKDP 465
Cdd:cd22708   45 DIVLDGEDIEAEHC---IIENVGGV--VTLHPLPGALCAVNGQVITQPTRLTQGDVILLGKTNMFRFNHP 109
Myo5p-like_CBD_DIL_ANK cd15473
cargo binding domain of myosin 5-like of dil and ankyrin domain containing protein; DIL and ...
734-845 5.50e-04

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: 42.93  E-value: 5.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 734 ELHPDLVSQTFGYLFFFSNASLFNTLMEKgngEPFYQWSKAVQIRTNLDLVLDWLQGIGLGDIAAEFF-----RKLSATV 808
Cdd:cd15473  154 DVHPAIIIQALSQLFYWLGCELFNRILTN---KKYLCRSKAMQIRMNLSALEDWARSNNLQPEKGESPpriarSHLAPVI 230
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 512854841 809 NLL----CIpkTSLMKVS--WSTLRNdYPALSSAQLNHLLRNY 845
Cdd:cd15473  231 QLLqwlqCL--SSLDDFEslIATIQQ-LDALNPLQLLRAVKDY 270
FHA_KIF1 cd22705
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ...
390-460 6.03e-04

forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 family includes KIF1A, KIF1B, and KIF1C. KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. 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: 438757 [Multi-domain]  Cd Length: 101  Bit Score: 39.91  E-value: 6.03e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512854841 390 DKGPYVDTFLSAPDILPRHCsvwRLDSSGQkyIVRVRPYRGALVTHNGRVLQRETELHTGDLLGLGEHFLF 460
Cdd:cd22705   32 DADVPQDIQLSGTHILEEHC---TFENEDG--VVTLEPCEGALTYVNGKRVTEPTRLKTGSRVILGKNHVF 97
FHA_KIF28P cd22709
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ...
355-465 9.48e-04

forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; KIF28P, also called kinesin-like protein 6 (KLP6), is a microtubule-dependent motor protein required for mitochondrion morphology and transport of mitochondria in neuronal cells. 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: 438761 [Multi-domain]  Cd Length: 102  Bit Score: 39.51  E-value: 9.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 355 PYFLLLqgyNKDQdfviyVMTRK-KHLF-------GRAekslrDKGPYVDTFLSAPDILPRHCSVWRLDSSgqkyiVRVR 426
Cdd:cd22709    1 PHLLNL---NEDP-----QLSGViVHFLqegettiGRA-----DAEPEPDIVLSGLSIQKQHAVITNTDGK-----VTIE 62
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 512854841 427 PYR-GALVTHNGRVLQRETELHTGDLLGLGEHFLFMYKDP 465
Cdd:cd22709   63 PVSpGAKVIVNGVPVTGETELHHLDRVILGSNHLYVFVGP 102
FHA_KIF14 cd22707
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ...
399-465 2.10e-03

forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; KIF14 is a microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity. It plays a role in many processes like cell division, cytokinesis and in cell proliferation and apoptosis. KIF14 is a potential oncogene and is involved in the metastasis of various cancers. Mutations of KIF14 cause primary microcephaly by impairing cytokinesis. 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: 438759 [Multi-domain]  Cd Length: 108  Bit Score: 38.79  E-value: 2.10e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512854841 399 LSAPDILPRHCSVWRLDSsgqkyIVRVRPYRGALVTHNGRVLQRETELHTGDLLGLGEHFLFMYKDP 465
Cdd:cd22707   47 LSGALIADDHCTIENNGG-----KVTIIPVGDAETYVNGELISEPTVLHHGDRVILGGDHYFRFNHP 108
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
374-460 3.47e-03

forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438725 [Multi-domain]  Cd Length: 95  Bit Score: 37.58  E-value: 3.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512854841 374 MTRKKHLFGRAEKS-LRDKGPYVDtflsapdilPRHCSVwRLDSSGQKYIVRVRPYRGALVthNGRVLQRETELHTGDLL 452
Cdd:cd22673   18 LTKKSCTFGRDLSCdIRIQLPGVS---------REHCRI-EVDENGKAYLENLSTTNPTLV--NGKAIEKSAELKDGDVI 85

                 ....*....
gi 512854841 453 GLGEH-FLF 460
Cdd:cd22673   86 TIGGRsFRF 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH