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Conserved domains on  [gi|251823858|ref|NP_001156506|]
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regulatory-associated protein of mTOR isoform 2 [Homo sapiens]

Protein Classification

raptor family protein( domain architecture ID 13861730)

raptor (regulatory-associated protein of mTOR) family protein similar to Schizosaccharomyces pombe target of rapamycin complex 1 subunit mip1, a component of TORC1, which regulates multiple cellular processes to control cell growth in response to environmental signals

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Raptor_N pfam14538
Raptor N-terminal CASPase like domain; This domain is found at the N-terminus of the Raptor ...
55-206 7.63e-97

Raptor N-terminal CASPase like domain; This domain is found at the N-terminus of the Raptor protein. It has been identified to have a CASPase like structure. It conserves the characteriztic cys/his dyad of the caspases suggesting it may have a peptidase activity.


:

Pssm-ID: 464202  Cd Length: 152  Bit Score: 304.58  E-value: 7.63e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858    55 MKTVSVALVLCLNVGVDPPDVVKTTPCARLECWIDPLSMGPQKALETIGANLQKQYENWQPRARYKQSLDPTVDEVKKLC 134
Cdd:pfam14538    1 LKTVSVALVLCLNIGVDPPDVVKTKPCARLECWIDPSSMSPQKALEEIGKNLQDQYESWQPRARYKQSLDPSVEDVKKLC 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 251823858   135 TSLRRNAKEERVLFHYNGHGVPRPTVNGEVWVFNKNYTQYIPLSIYDLQTWMGSPSIFVYDCSNAGLIVKSF 206
Cdd:pfam14538   81 SKLRRNAKDERVLFHYNGHGVPRPTSNGEIWVFNKDYTQYIPLSIYDLFSWLGSPSIFIFDCSNAGNLLNAF 152
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
869-1164 7.90e-24

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 103.18  E-value: 7.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858  869 SVVKFHPFTPCIAVADKDSICF-WDWEKGEKLDYF--HNGNPRYTRVTAmeylngqDCSLLLTATDDGAIRVWknfaDLE 945
Cdd:cd00200    13 TCVAFSPDGKLLATGSGDGTIKvWDLETGELLRTLkgHTGPVRDVAASA-------DGTYLASGSSDKTIRLW----DLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858  946 KNpEMVTAWQGLSDMLpttrgagMVVDWEQETGLLMSSGDVRIVRIWDTDREMKVQDIpTGADSCVTSLSCDSHRSLIVA 1025
Cdd:cd00200    82 TG-ECVRTLTGHTSYV-------SSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTL-RGHTDWVNSVAFSPDGTFVAS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858 1026 GLGDGSIRVYDrrMALSECrVMTYREHTAWVvkASLQKRPDG-HIVSVSVNGDVRIFDPRMPESVNVLQI-VKGLTALDI 1103
Cdd:cd00200   153 SSQDGTIKLWD--LRTGKC-VATLTGHTGEV--NSVAFSPDGeKLLSSSSDGTIKLWDLSTGKCLGTLRGhENGVNSVAF 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251823858 1104 HPQADLIACGSVNqftaiynssgeliNNIKYYDGFMGQRV-------GAISCLAFHPHWPHLAVGSND 1164
Cdd:cd00200   228 SPDGYLLASGSED-------------GTIRVWDLRTGECVqtlsghtNSVTSLAWSPDGKRLASGSAD 282
 
Name Accession Description Interval E-value
Raptor_N pfam14538
Raptor N-terminal CASPase like domain; This domain is found at the N-terminus of the Raptor ...
55-206 7.63e-97

Raptor N-terminal CASPase like domain; This domain is found at the N-terminus of the Raptor protein. It has been identified to have a CASPase like structure. It conserves the characteriztic cys/his dyad of the caspases suggesting it may have a peptidase activity.


Pssm-ID: 464202  Cd Length: 152  Bit Score: 304.58  E-value: 7.63e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858    55 MKTVSVALVLCLNVGVDPPDVVKTTPCARLECWIDPLSMGPQKALETIGANLQKQYENWQPRARYKQSLDPTVDEVKKLC 134
Cdd:pfam14538    1 LKTVSVALVLCLNIGVDPPDVVKTKPCARLECWIDPSSMSPQKALEEIGKNLQDQYESWQPRARYKQSLDPSVEDVKKLC 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 251823858   135 TSLRRNAKEERVLFHYNGHGVPRPTVNGEVWVFNKNYTQYIPLSIYDLQTWMGSPSIFVYDCSNAGLIVKSF 206
Cdd:pfam14538   81 SKLRRNAKDERVLFHYNGHGVPRPTSNGEIWVFNKDYTQYIPLSIYDLFSWLGSPSIFIFDCSNAGNLLNAF 152
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
869-1164 7.90e-24

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 103.18  E-value: 7.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858  869 SVVKFHPFTPCIAVADKDSICF-WDWEKGEKLDYF--HNGNPRYTRVTAmeylngqDCSLLLTATDDGAIRVWknfaDLE 945
Cdd:cd00200    13 TCVAFSPDGKLLATGSGDGTIKvWDLETGELLRTLkgHTGPVRDVAASA-------DGTYLASGSSDKTIRLW----DLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858  946 KNpEMVTAWQGLSDMLpttrgagMVVDWEQETGLLMSSGDVRIVRIWDTDREMKVQDIpTGADSCVTSLSCDSHRSLIVA 1025
Cdd:cd00200    82 TG-ECVRTLTGHTSYV-------SSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTL-RGHTDWVNSVAFSPDGTFVAS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858 1026 GLGDGSIRVYDrrMALSECrVMTYREHTAWVvkASLQKRPDG-HIVSVSVNGDVRIFDPRMPESVNVLQI-VKGLTALDI 1103
Cdd:cd00200   153 SSQDGTIKLWD--LRTGKC-VATLTGHTGEV--NSVAFSPDGeKLLSSSSDGTIKLWDLSTGKCLGTLRGhENGVNSVAF 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251823858 1104 HPQADLIACGSVNqftaiynssgeliNNIKYYDGFMGQRV-------GAISCLAFHPHWPHLAVGSND 1164
Cdd:cd00200   228 SPDGYLLASGSED-------------GTIRVWDLRTGECVqtlsghtNSVTSLAWSPDGKRLASGSAD 282
WD40 COG2319
WD40 repeat [General function prediction only];
880-1173 4.45e-18

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 88.04  E-value: 4.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858  880 IAVADKD-SICFWDWEKGEKLDYF--HNGnprytRVTAMEYL-NGQdcsLLLTATDDGAIRVWknfaDLEKNPEMVTawq 955
Cdd:COG2319   135 LASGSADgTVRLWDLATGKLLRTLtgHSG-----AVTSVAFSpDGK---LLASGSDDGTVRLW----DLATGKLLRT--- 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858  956 glsdmLPTTRGAGMVVDWEQETGLLMSSGDVRIVRIWDTDREmKVQDIPTGADSCVTSLSCDSHRSLIVAGLGDGSIRVY 1035
Cdd:COG2319   200 -----LTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG-KLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLW 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858 1036 DRRmalSECRVMTYREHTAWVVKASLqkRPDG-HIVSVSVNGDVRIFDPRMPESVNVLQI-VKGLTALDIHPQADLIACG 1113
Cdd:COG2319   274 DLA---TGELLRTLTGHSGGVNSVAF--SPDGkLLASGSDDGTVRLWDLATGKLLRTLTGhTGAVRSVAFSPDGKTLASG 348
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 251823858 1114 SVNQFTAIYN-SSGELINNIKyydgfmgQRVGAISCLAFHPHWPHLAVGSNDYYISVYSVE 1173
Cdd:COG2319   349 SDDGTVRLWDlATGELLRTLT-------GHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
 
Name Accession Description Interval E-value
Raptor_N pfam14538
Raptor N-terminal CASPase like domain; This domain is found at the N-terminus of the Raptor ...
55-206 7.63e-97

Raptor N-terminal CASPase like domain; This domain is found at the N-terminus of the Raptor protein. It has been identified to have a CASPase like structure. It conserves the characteriztic cys/his dyad of the caspases suggesting it may have a peptidase activity.


Pssm-ID: 464202  Cd Length: 152  Bit Score: 304.58  E-value: 7.63e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858    55 MKTVSVALVLCLNVGVDPPDVVKTTPCARLECWIDPLSMGPQKALETIGANLQKQYENWQPRARYKQSLDPTVDEVKKLC 134
Cdd:pfam14538    1 LKTVSVALVLCLNIGVDPPDVVKTKPCARLECWIDPSSMSPQKALEEIGKNLQDQYESWQPRARYKQSLDPSVEDVKKLC 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 251823858   135 TSLRRNAKEERVLFHYNGHGVPRPTVNGEVWVFNKNYTQYIPLSIYDLQTWMGSPSIFVYDCSNAGLIVKSF 206
Cdd:pfam14538   81 SKLRRNAKDERVLFHYNGHGVPRPTSNGEIWVFNKDYTQYIPLSIYDLFSWLGSPSIFIFDCSNAGNLLNAF 152
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
869-1164 7.90e-24

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 103.18  E-value: 7.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858  869 SVVKFHPFTPCIAVADKDSICF-WDWEKGEKLDYF--HNGNPRYTRVTAmeylngqDCSLLLTATDDGAIRVWknfaDLE 945
Cdd:cd00200    13 TCVAFSPDGKLLATGSGDGTIKvWDLETGELLRTLkgHTGPVRDVAASA-------DGTYLASGSSDKTIRLW----DLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858  946 KNpEMVTAWQGLSDMLpttrgagMVVDWEQETGLLMSSGDVRIVRIWDTDREMKVQDIpTGADSCVTSLSCDSHRSLIVA 1025
Cdd:cd00200    82 TG-ECVRTLTGHTSYV-------SSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTL-RGHTDWVNSVAFSPDGTFVAS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858 1026 GLGDGSIRVYDrrMALSECrVMTYREHTAWVvkASLQKRPDG-HIVSVSVNGDVRIFDPRMPESVNVLQI-VKGLTALDI 1103
Cdd:cd00200   153 SSQDGTIKLWD--LRTGKC-VATLTGHTGEV--NSVAFSPDGeKLLSSSSDGTIKLWDLSTGKCLGTLRGhENGVNSVAF 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251823858 1104 HPQADLIACGSVNqftaiynssgeliNNIKYYDGFMGQRV-------GAISCLAFHPHWPHLAVGSND 1164
Cdd:cd00200   228 SPDGYLLASGSED-------------GTIRVWDLRTGECVqtlsghtNSVTSLAWSPDGKRLASGSAD 282
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
911-1176 4.49e-20

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 92.01  E-value: 4.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858  911 RVTAMEYLNGQDcsLLLTATDDGAIRVWknfaDLEKNpEMVTAWQGLSdmlpttrGAGMVVDWEQETGLLMSSGDVRIVR 990
Cdd:cd00200    11 GVTCVAFSPDGK--LLATGSGDGTIKVW----DLETG-ELLRTLKGHT-------GPVRDVAASADGTYLASGSSDKTIR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858  991 IWDTDREMKVQDIpTGADSCVTSLSCDSHRSLIVAGLGDGSIRVYDrrMALSECrVMTYREHTAWVVkaSLQKRPDGHIV 1070
Cdd:cd00200    77 LWDLETGECVRTL-TGHTSYVSSVAFSPDGRILSSSSRDKTIKVWD--VETGKC-LTTLRGHTDWVN--SVAFSPDGTFV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858 1071 -SVSVNGDVRIFDPRMPESVNVLQI-VKGLTALDIHPQADLIACGSVNQFTAIYN-SSGELINNIKYYDGFmgqrvgaIS 1147
Cdd:cd00200   151 aSSSQDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDlSTGKCLGTLRGHENG-------VN 223
                         250       260
                  ....*....|....*....|....*....
gi 251823858 1148 CLAFHPHWPHLAVGSNDYYISVYSVEKRV 1176
Cdd:cd00200   224 SVAFSPDGYLLASGSEDGTIRVWDLRTGE 252
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
965-1172 3.68e-19

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 89.32  E-value: 3.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858  965 RGAGMVVDWEQETGLLMSSGDVRIVRIWDTDReMKVQDIPTGADSCVTSLSCDSHRSLIVAGLGDGSIRVYDRRmalSEC 1044
Cdd:cd00200     9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDLET-GELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE---TGE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858 1045 RVMTYREHTAWVvkASLQKRPDGHIVSVS-VNGDVRIFDPRMPESVNVLQ-IVKGLTALDIHPQADLIACGSVNQFTAIY 1122
Cdd:cd00200    85 CVRTLTGHTSYV--SSVAFSPDGRILSSSsRDKTIKVWDVETGKCLTTLRgHTDWVNSVAFSPDGTFVASSSQDGTIKLW 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 251823858 1123 N-SSGELINNIKYYDGFmgqrvgaISCLAFHPHWPHLAVGSNDYYISVYSV 1172
Cdd:cd00200   163 DlRTGKCVATLTGHTGE-------VNSVAFSPDGEKLLSSSSDGTIKLWDL 206
WD40 COG2319
WD40 repeat [General function prediction only];
880-1173 4.45e-18

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 88.04  E-value: 4.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858  880 IAVADKD-SICFWDWEKGEKLDYF--HNGnprytRVTAMEYL-NGQdcsLLLTATDDGAIRVWknfaDLEKNPEMVTawq 955
Cdd:COG2319   135 LASGSADgTVRLWDLATGKLLRTLtgHSG-----AVTSVAFSpDGK---LLASGSDDGTVRLW----DLATGKLLRT--- 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858  956 glsdmLPTTRGAGMVVDWEQETGLLMSSGDVRIVRIWDTDREmKVQDIPTGADSCVTSLSCDSHRSLIVAGLGDGSIRVY 1035
Cdd:COG2319   200 -----LTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG-KLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLW 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858 1036 DRRmalSECRVMTYREHTAWVVKASLqkRPDG-HIVSVSVNGDVRIFDPRMPESVNVLQI-VKGLTALDIHPQADLIACG 1113
Cdd:COG2319   274 DLA---TGELLRTLTGHSGGVNSVAF--SPDGkLLASGSDDGTVRLWDLATGKLLRTLTGhTGAVRSVAFSPDGKTLASG 348
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 251823858 1114 SVNQFTAIYN-SSGELINNIKyydgfmgQRVGAISCLAFHPHWPHLAVGSNDYYISVYSVE 1173
Cdd:COG2319   349 SDDGTVRLWDlATGELLRTLT-------GHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
871-1082 3.39e-15

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 77.38  E-value: 3.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858  871 VKFHPFTPCIAVADKDSICF-WDWEKGEKLDYF--HNGNprytrVTAMEYLngQDCSLLLTATDDGAIRVWknfaDLEKN 947
Cdd:cd00200    57 VAASADGTYLASGSSDKTIRlWDLETGECVRTLtgHTSY-----VSSVAFS--PDGRILSSSSRDKTIKVW----DVETG 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858  948 pEMVTAWQGLSDmlpttrgAGMVVDWEQETGLLMSSGDVRIVRIWDT--------------------------------- 994
Cdd:cd00200   126 -KCLTTLRGHTD-------WVNSVAFSPDGTFVASSSQDGTIKLWDLrtgkcvatltghtgevnsvafspdgekllssss 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858  995 DREMKVQDIPTGADSC--------VTSLSCDSHRSLIVAGLGDGSIRVYDRRMAlsECrVMTYREHTAWVVKASLQkrPD 1066
Cdd:cd00200   198 DGTIKLWDLSTGKCLGtlrghengVNSVAFSPDGYLLASGSEDGTIRVWDLRTG--EC-VQTLSGHTNSVTSLAWS--PD 272
                         250
                  ....*....|....*..
gi 251823858 1067 GH-IVSVSVNGDVRIFD 1082
Cdd:cd00200   273 GKrLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
952-1173 1.48e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 68.01  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858  952 TAWQGLSDMLPTTRGAGMVVDWEQETGLLMSSGDVRIVRIWDTDREmKVQDIPTGADSCVTSLSCDSHRSLIVAGLGDGS 1031
Cdd:COG2319    23 AALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAG-ALLATLLGHTAAVLSVAFSPDGRLLASASADGT 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858 1032 IRVYDrrmALSECRVMTYREHTAWVVKASLqkRPDGH-IVSVSVNGDVRIFDPRMPESVNVLQIVKG-LTALDIHPQADL 1109
Cdd:COG2319   102 VRLWD---LATGLLLRTLTGHTGAVRSVAF--SPDGKtLASGSADGTVRLWDLATGKLLRTLTGHSGaVTSVAFSPDGKL 176
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 251823858 1110 IACGSVNQFTAIYN-SSGELINNIKYYDgfmgqrvGAISCLAFHPHWPHLAVGSNDYYISVYSVE 1173
Cdd:COG2319   177 LASGSDDGTVRLWDlATGKLLRTLTGHT-------GAVRSVAFSPDGKLLASGSADGTVRLWDLA 234
WDR74 cd22857
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ...
880-1175 2.00e-08

WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and plants is an essential factor for ribosome assembly. In cooperation with the assembly factor NVL2, WDR74 participates in an early cleavage of the pre-rRNA processing pathway. NVL2 is a type II double ring, AAA-ATPase, that may mediate the release of WDR74 from nucleolar pre-60S particles. WDR74 has been implicated in tumorigenesis. In lung cancer, it regulates cell proliferation, cell cycle progression, chemoresistance and cell aggressiveness, by inducing nuclear beta-catenin accumulation and driving downstream Wnt-responsive genes expression. In melanoma, it promotes apoptosis resistance and aggressive behavior by regulating the RPL5-MDM2-p53 pathway. WDR74 contains an N-terminal seven-bladed beta-propeller WD40 domain that associates with the D1-AAA domain of the AAA-ATPase NVL2, and a flexible lysine-rich C-terminus that extends outward from the WD40 domain, and is required for nucleolar localization.


Pssm-ID: 439303 [Multi-domain]  Cd Length: 325  Bit Score: 57.62  E-value: 2.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858  880 IAVADKD-SICFWDWEKGEKLDYFHNGNPRYT-----RVTAMEYLNGQdcslLLTATDDGAIRVWKNFADLEKNPEmVTA 953
Cdd:cd22857    47 LAVARKNgTVEVLDPENGDLLASFSDSEPATKlseedHFVGLHLFSGT----LLTCTSKGSLRSTKLPDDSTASSS-PTA 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858  954 WQGLSDMLPTTRGagmvvdwEQETGLLMSSGDVRIVRIWDTdrEMKVQDI---------------PTgadsCVTS---LS 1015
Cdd:cd22857   122 WVCLGGNLLCMRV-------DPNENYFAFGGKEVELNVWDL--EEKPGKIwraknvpndslglrvPV----WVTDltfLS 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858 1016 CDSHRSlIVAGLGDGSIRVYD----RRmalsecRVM--TYREHTAWVVKASlqkrPDGHIVSVSVN-GDVRIFDPRMpes 1088
Cdd:cd22857   189 KDDHRK-IVTGTGYHQVRLYDtraqRR------PVVsvDFGETPIKAVAED----PDGHTVYVGDTsGDLASIDLRT--- 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823858 1089 vnvlqivkgltaldihpqadliacgsvnqftaiynssGELINNikyYDGFMGqrvGAISCLAFHPHWPHLAVGSNDYYIS 1168
Cdd:cd22857   255 -------------------------------------GKLLGC---FKGKCG---GSIRSIARHPELPLIASCGLDRYLR 291

                  ....*..
gi 251823858 1169 VYSVEKR 1175
Cdd:cd22857   292 IWDTETR 298
 
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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