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Conserved domains on  [gi|2038185774|ref|XP_041506597|]
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GATOR complex protein WDR59 isoform X4 [Microtus oregoni]

Protein Classification

RWD and mRING-H2-C3H3C2_WDR59 domain-containing protein( domain architecture ID 13237405)

protein containing domains WD40, RWD, and mRING-H2-C3H3C2_WDR59

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
mRING-H2-C3H3C2_WDR59 cd16692
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 59 ...
 848-894 7.94e-32

Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 59 (WDR59) and similar proteins; WDR59 is a component of the GATOR2 complex, which also includes another four subunits, Seh1, Sec13, Sea2/WDR24, and Mio/Sea4. GATOR2 and GATOR1, which is composed of three subunits, DEPDC5, Nprl2, and Nprl3, form the Rag-interacting complex GATOR (GAP Activity Towards Rags). Inhibition of GATOR1 subunits makes mTORC1 signaling resistant to amino acid deprivation. In contrast, inhibition of GATOR2 subunits suppresses mTORC1 signaling and GATOR2 negatively regulates DEPDC5. WDR59 contains an N-terminal WD40 domain followed by a RWD domain, and a C-terminal RING-H2 finger with an unusual arrangement of zinc-coordinating residues. The cysteines and histidines in the RING-H2 finger are arranged as a modified C3H3C2-type, rather than the canonical C3H2C3-type. Sea3 is the yeast counterpart of WDR59. It is not included in this subfamily.


:

Pssm-ID: 438353  Cd Length: 47  Bit Score: 117.49  E-value: 7.94e-32
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2038185774 848 FQCAICHVAVRGSSNFCLTCGHGGHTSHMMEWFRTQEVCPTGCGCHC 894
Cdd:cd16692     1 LQCAICHVAVRGSSNFCLACGHGGHTSHMMEWFRTQDVCPTGCGCHC 47
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 60-243 1.80e-17

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: 83.92  E-value: 1.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774  60 NANYLATSH-DGDIRIWDKRKPSTAVEYlAAHLSKIHGLDWHPDSeHILATSSQDNSVKFWDYRQPRKYLNILPCQVPVW 138
Cdd:cd00200    62 DGTYLASGSsDKTIRLWDLETGECVRTL-TGHTSYVSSVAFSPDG-RILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVN 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774 139 KARYTPFSNGLVTVMvpqlrRENSLLLWNVfDLNTPVHTFVGHDDVVLEFQWrrqkegSKD-YQLVTWSRDQTLRMWrvD 217
Cdd:cd00200   140 SVAFSPDGTFVASSS-----QDGTIKLWDL-RTGKCVATLTGHTGEVNSVAF------SPDgEKLLSSSSDGTIKLW--D 205

                         170       180
                  ....*....|....*....|....*.
gi 2038185774 218 YQMQRLCAndILDGVDEFIESISLLP 243
Cdd:cd00200   206 LSTGKCLG--TLRGHENGVNSVAFSP 229
RWD smart00591
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily ...
 301-401 1.68e-11

domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily related to the UBCc domain;


:

Pssm-ID: 214735  Cd Length: 107  Bit Score: 61.60  E-value: 1.68e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774  301 EFSLINVQIRNVNVEMDAADRSCTVSVHCSNHR---------VKMLVTFPAQYPnNAAPSFQFINPTTITSAVKAKLLKI 371
Cdd:smart00591   1 ELEALESIYPEDFEVIDEDARIPEITIKLSPSSdegedqyvsLTLQVKLPENYP-DEAPPISLLNSEGLSDEQLAELLKK 79

                           90       100       110
                   ....*....|....*....|....*....|
gi 2038185774  372 LKDTSLQkvKRNQSCLEPCLRQLVSCLESF 401
Cdd:smart00591  80 LEEIAEE--NLGEVMIFELVEKLQEFLSEF 107
 
Name Accession Description Interval E-value
mRING-H2-C3H3C2_WDR59 cd16692
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 59 ...
 848-894 7.94e-32

Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 59 (WDR59) and similar proteins; WDR59 is a component of the GATOR2 complex, which also includes another four subunits, Seh1, Sec13, Sea2/WDR24, and Mio/Sea4. GATOR2 and GATOR1, which is composed of three subunits, DEPDC5, Nprl2, and Nprl3, form the Rag-interacting complex GATOR (GAP Activity Towards Rags). Inhibition of GATOR1 subunits makes mTORC1 signaling resistant to amino acid deprivation. In contrast, inhibition of GATOR2 subunits suppresses mTORC1 signaling and GATOR2 negatively regulates DEPDC5. WDR59 contains an N-terminal WD40 domain followed by a RWD domain, and a C-terminal RING-H2 finger with an unusual arrangement of zinc-coordinating residues. The cysteines and histidines in the RING-H2 finger are arranged as a modified C3H3C2-type, rather than the canonical C3H2C3-type. Sea3 is the yeast counterpart of WDR59. It is not included in this subfamily.


Pssm-ID: 438353  Cd Length: 47  Bit Score: 117.49  E-value: 7.94e-32
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2038185774 848 FQCAICHVAVRGSSNFCLTCGHGGHTSHMMEWFRTQEVCPTGCGCHC 894
Cdd:cd16692     1 LQCAICHVAVRGSSNFCLACGHGGHTSHMMEWFRTQDVCPTGCGCHC 47
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 60-243 1.80e-17

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: 83.92  E-value: 1.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774  60 NANYLATSH-DGDIRIWDKRKPSTAVEYlAAHLSKIHGLDWHPDSeHILATSSQDNSVKFWDYRQPRKYLNILPCQVPVW 138
Cdd:cd00200    62 DGTYLASGSsDKTIRLWDLETGECVRTL-TGHTSYVSSVAFSPDG-RILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVN 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774 139 KARYTPFSNGLVTVMvpqlrRENSLLLWNVfDLNTPVHTFVGHDDVVLEFQWrrqkegSKD-YQLVTWSRDQTLRMWrvD 217
Cdd:cd00200   140 SVAFSPDGTFVASSS-----QDGTIKLWDL-RTGKCVATLTGHTGEVNSVAF------SPDgEKLLSSSSDGTIKLW--D 205

                         170       180
                  ....*....|....*....|....*.
gi 2038185774 218 YQMQRLCAndILDGVDEFIESISLLP 243
Cdd:cd00200   206 LSTGKCLG--TLRGHENGVNSVAFSP 229
WD40 COG2319
WD40 repeat [General function prediction only];
60-217 1.77e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 79.57  E-value: 1.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774  60 NANYLAT-SHDGDIRIWDKRKPsTAVEYLAAHLSKIHGLDWHPDSeHILATSSQDNSVKFWDYRQPRKYLNILPCQVPVW 138
Cdd:COG2319   131 DGKTLASgSADGTVRLWDLATG-KLLRTLTGHSGAVTSVAFSPDG-KLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVR 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774 139 KARYTPFSNGLVTVmvpqlRRENSLLLWNVfDLNTPVHTFVGHDDVVLEFQWrrqkegSKDYQ-LVTWSRDQTLRMWRVD 217
Cdd:COG2319   209 SVAFSPDGKLLASG-----SADGTVRLWDL-ATGKLLRTLTGHSGSVRSVAF------SPDGRlLASGSADGTVRLWDLA 276
RWD smart00591
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily ...
 301-401 1.68e-11

domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily related to the UBCc domain;


Pssm-ID: 214735  Cd Length: 107  Bit Score: 61.60  E-value: 1.68e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774  301 EFSLINVQIRNVNVEMDAADRSCTVSVHCSNHR---------VKMLVTFPAQYPnNAAPSFQFINPTTITSAVKAKLLKI 371
Cdd:smart00591   1 ELEALESIYPEDFEVIDEDARIPEITIKLSPSSdegedqyvsLTLQVKLPENYP-DEAPPISLLNSEGLSDEQLAELLKK 79

                           90       100       110
                   ....*....|....*....|....*....|
gi 2038185774  372 LKDTSLQkvKRNQSCLEPCLRQLVSCLESF 401
Cdd:smart00591  80 LEEIAEE--NLGEVMIFELVEKLQEFLSEF 107
zf-RING_16 pfam17120
RING/Ubox like zinc-binding domain;
850-898 1.91e-11

RING/Ubox like zinc-binding domain;


Pssm-ID: 375001  Cd Length: 57  Bit Score: 59.72  E-value: 1.91e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2038185774 850 CAICHVAVRGSSNFCLTCGHGGHTSHMMEWFRTQE-VCPTGCGCHCLLES 898
Cdd:pfam17120   7 CNYCCLRVRGRVFLCGVCQHVLHASCAREWWENDDgECPSGCGCNCLEHH 56
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 31-214 9.25e-09

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 59.33  E-value: 9.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774  31 IISQRRDTRKPTVALSAVAGASQVKWNKKNANYLATSH-DGDIRIWDKRKPSTAVEyLAAHLSKIHGLDWHPDSEHILAT 109
Cdd:PLN00181  515 IIKDGRDIHYPVVELASRSKLSGICWNSYIKSQVASSNfEGVVQVWDVARSQLVTE-MKEHEKRVWSIDYSSADPTLLAS 593

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774 110 SSQDNSVKFWDYRQP------RKYLNILPCQVPVWKARYTPFSNGlvtvmvpqlrrENSLLLWNVFDLNTPVHTFVGHDD 183
Cdd:PLN00181  594 GSDDGSVKLWSINQGvsigtiKTKANICCVQFPSESGRSLAFGSA-----------DHKVYYYDLRNPKLPLCTMIGHSK 662

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2038185774 184 VVlefQWRRQKEGSkdyQLVTWSRDQTLRMW 214
Cdd:PLN00181  663 TV---SYVRFVDSS---TLVSSSTDNTLKLW 687
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 87-120 1.05e-05

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 43.07  E-value: 1.05e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2038185774   87 LAAHLSKIHGLDWHPDSeHILATSSQDNSVKFWD 120
Cdd:smart00320   8 LKGHTGPVTSVAFSPDG-KYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
87-120 1.30e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.02  E-value: 1.30e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2038185774  87 LAAHLSKIHGLDWHPDSEHiLATSSQDNSVKFWD 120
Cdd:pfam00400   7 LEGHTGSVTSLAFSPDGKL-LASGSDDGTVKVWD 39
RWD_GCN2 cd23823
RWD domain of eIF-2-alpha kinase GCN2 and related proteins; GCN2 (EC 2.7.11.1), also called ...
 327-404 1.64e-04

RWD domain of eIF-2-alpha kinase GCN2 and related proteins; GCN2 (EC 2.7.11.1), also called eukaryotic translation initiation factor 2-alpha kinase 4 (EIF2AK4), acts as a metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to low amino acid availability. It also plays a role in modulating the adaptive immune response to yellow fever virus infection and promotes dendritic cells to initiate autophagy and antigene presentation to both CD4(+) and CD8(+) T-cells under amino acid starvation.


Pssm-ID: 467659  Cd Length: 117  Bit Score: 41.82  E-value: 1.64e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038185774 327 VHCSnhrVKMLVTFPAQYPNnAAPSFQFINPTTITSAVKAKLLKILKDTSLQKVKrnqsclEPCLRQLVSCLESFVNQ 404
Cdd:cd23823    48 NHVS---VDLHVKFPPTYPD-VPPEIELENVKGLSDEQLEELLKELEELAKELLG------EEMIFELAEAVQEFLEE 115
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
 320-401 3.32e-03

RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. The function of this domain is unknown. GCN2 is the alpha-subunit of the only translation initiation factor (eIF2 alpha) kinase that appears in all eukaryotes. Its function requires an interaction with GCN1 via the domain at its N-terminus, which is termed the RWD domain after three major RWD-containing proteins: RING finger-containing proteins, WD-repeat-containing proteins, and yeast DEAD (DEXD)-like helicases. The structure forms an alpha + beta sandwich fold consisting of two layers: a four-stranded antiparallel beta-sheet, and three side-by-side alpha-helices.


Pssm-ID: 399058  Cd Length: 111  Bit Score: 38.07  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774 320 DRSCTVSVHCSNHRVKMLVTFPAQYPnNAAPSFQFINPTTITSAVKAKLLKILKdtslQKVKRNQSclEPCLRQLVSCLE 399
Cdd:pfam05773  36 SLDSDESDSSHLPPLVLKFTLPEDYP-DEPPKISLSSPWNLSDEQVLSLLEELE----ELAEENLG--EVMIFELIEWLQ 108


                  ..
gi 2038185774 400 SF 401
Cdd:pfam05773 109 EN 110
 
Name Accession Description Interval E-value
mRING-H2-C3H3C2_WDR59 cd16692
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 59 ...
 848-894 7.94e-32

Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 59 (WDR59) and similar proteins; WDR59 is a component of the GATOR2 complex, which also includes another four subunits, Seh1, Sec13, Sea2/WDR24, and Mio/Sea4. GATOR2 and GATOR1, which is composed of three subunits, DEPDC5, Nprl2, and Nprl3, form the Rag-interacting complex GATOR (GAP Activity Towards Rags). Inhibition of GATOR1 subunits makes mTORC1 signaling resistant to amino acid deprivation. In contrast, inhibition of GATOR2 subunits suppresses mTORC1 signaling and GATOR2 negatively regulates DEPDC5. WDR59 contains an N-terminal WD40 domain followed by a RWD domain, and a C-terminal RING-H2 finger with an unusual arrangement of zinc-coordinating residues. The cysteines and histidines in the RING-H2 finger are arranged as a modified C3H3C2-type, rather than the canonical C3H2C3-type. Sea3 is the yeast counterpart of WDR59. It is not included in this subfamily.


Pssm-ID: 438353  Cd Length: 47  Bit Score: 117.49  E-value: 7.94e-32
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2038185774 848 FQCAICHVAVRGSSNFCLTCGHGGHTSHMMEWFRTQEVCPTGCGCHC 894
Cdd:cd16692     1 LQCAICHVAVRGSSNFCLACGHGGHTSHMMEWFRTQDVCPTGCGCHC 47
mRING-H2-C3H3C2_Mio-like cd16488
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein mio and ...
 849-892 4.40e-21

Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein mio and its homologs; This subfamily contains Mio, WDR24, WDR59, and their counterparts Sea4, Sea2, and Sea3 from yeast, respectively. Mio/Sea4, Sea2/WDR24, and Sea3/WDR59 are components of the GATOR2 complex, which also includes another two subunits, Seh1and Sec13. GATOR2 and GATOR1, which is composed of three subunits, DEPDC5, Nprl2, and Nprl3, form the Rag-interacting complex GATOR (GAP Activity Towards Rags). Inhibition of GATOR1 subunits makes mTORC1 signaling resistant to amino acid deprivation. In contrast, inhibition of GATOR2 subunits suppresses mTORC1 signaling and GATOR2 negatively regulates DEPDC5. All subfamily members contain an N-terminal WD40 domain and a C-terminal RING-H2 finger with an unusual arrangement of zinc-coordinating residues. The cysteines and histidines in the RING-H2 finger are arranged as a modified C3H3C2-type, rather than the canonical C3H2C3-type.


Pssm-ID: 438151 [Multi-domain]  Cd Length: 44  Bit Score: 87.00  E-value: 4.40e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2038185774 849 QCAICHVAVRGSSNFCLTCGHGGHTSHMMEWFRTQEVCPTGCGC 892
Cdd:cd16488     1 SCAICHLPVKGLSSFCLNCGHGGHAECIREWFEDHTECPTGCGC 44
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 60-243 1.80e-17

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: 83.92  E-value: 1.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774  60 NANYLATSH-DGDIRIWDKRKPSTAVEYlAAHLSKIHGLDWHPDSeHILATSSQDNSVKFWDYRQPRKYLNILPCQVPVW 138
Cdd:cd00200    62 DGTYLASGSsDKTIRLWDLETGECVRTL-TGHTSYVSSVAFSPDG-RILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVN 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774 139 KARYTPFSNGLVTVMvpqlrRENSLLLWNVfDLNTPVHTFVGHDDVVLEFQWrrqkegSKD-YQLVTWSRDQTLRMWrvD 217
Cdd:cd00200   140 SVAFSPDGTFVASSS-----QDGTIKLWDL-RTGKCVATLTGHTGEVNSVAF------SPDgEKLLSSSSDGTIKLW--D 205

                         170       180
                  ....*....|....*....|....*.
gi 2038185774 218 YQMQRLCAndILDGVDEFIESISLLP 243
Cdd:cd00200   206 LSTGKCLG--TLRGHENGVNSVAFSP 229
mRING-H2-C3H3C2_WDR24 cd16693
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 24 ...
 850-894 3.22e-17

Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 24 (WDR24) and similar proteins; WDR24 is a component of the GATOR2 complex, which also includes another four subunits, Seh1, Sec13, Sea3/WDR59, and Mio/Sea4. GATOR2 and GATOR1, which is composed of three subunits, DEPDC5, Nprl2, and Nprl3, form the Rag-interacting complex GATOR (GAP Activity Towards Rags). Inhibition of GATOR1 subunits makes mTORC1 signaling resistant to amino acid deprivation. In contrast, inhibition of GATOR2 subunits suppresses mTORC1 signaling and GATOR2 negatively regulates DEPDC5. WDR24 contains an N-terminal WD40 domain and a C-terminal RING-H2 finger with an unusual arrangement of zinc-coordinating residues. The cysteines and histidines in the RING-H2 finger are arranged as a modified C3H3C2-type, rather than the canonical C3H2C3-type. Sea2 is the yeast counterpart of WDR24. It is not included in this subfamily.


Pssm-ID: 438354  Cd Length: 46  Bit Score: 75.78  E-value: 3.22e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2038185774 850 CAICHVAVRGSSNFCLTCGHGGHTSHMMEWFRTQEVCPTGCGCHC 894
Cdd:cd16693     2 CSVCHLPVKGLYVWCQGCGHGGHLEHMKEWFSTNSHCPAGCGHLC 46
WD40 COG2319
WD40 repeat [General function prediction only];
60-217 1.77e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 79.57  E-value: 1.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774  60 NANYLAT-SHDGDIRIWDKRKPsTAVEYLAAHLSKIHGLDWHPDSeHILATSSQDNSVKFWDYRQPRKYLNILPCQVPVW 138
Cdd:COG2319   131 DGKTLASgSADGTVRLWDLATG-KLLRTLTGHSGAVTSVAFSPDG-KLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVR 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774 139 KARYTPFSNGLVTVmvpqlRRENSLLLWNVfDLNTPVHTFVGHDDVVLEFQWrrqkegSKDYQ-LVTWSRDQTLRMWRVD 217
Cdd:COG2319   209 SVAFSPDGKLLASG-----SADGTVRLWDL-ATGKLLRTLTGHSGSVRSVAF------SPDGRlLASGSADGTVRLWDLA 276
WD40 COG2319
WD40 repeat [General function prediction only];
62-243 2.52e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 79.18  E-value: 2.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774  62 NYLAT-SHDGDIRIWDkRKPSTAVEYLAAHLSKIHGLDWHPDSEHiLATSSQDNSVKFWDyRQPRKYLNILP-CQVPVWK 139
Cdd:COG2319   217 KLLASgSADGTVRLWD-LATGKLLRTLTGHSGSVRSVAFSPDGRL-LASGSADGTVRLWD-LATGELLRTLTgHSGGVNS 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774 140 ARYTPFSNGLVTVmvpqlRRENSLLLWNVfDLNTPVHTFVGHDDVVLEFQWRRQKEgskdyQLVTWSRDQTLRMWRVDYQ 219
Cdd:COG2319   294 VAFSPDGKLLASG-----SDDGTVRLWDL-ATGKLLRTLTGHTGAVRSVAFSPDGK-----TLASGSDDGTVRLWDLATG 362

                         170       180
                  ....*....|....*....|....
gi 2038185774 220 MQRLcandILDGVDEFIESISLLP 243
Cdd:COG2319   363 ELLR----TLTGHTGAVTSVAFSP 382
WD40 COG2319
WD40 repeat [General function prediction only];
63-217 9.25e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 74.18  E-value: 9.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774  63 YLAT-SHDGDIRIWDKRKPsTAVEYLAAHLSKIHGLDWHPDSeHILATSSQDNSVKFWDYRQPRKYLNILPCQVPVWKAR 141
Cdd:COG2319   176 LLASgSDDGTVRLWDLATG-KLLRTLTGHTGAVRSVAFSPDG-KLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVA 253

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038185774 142 YTPfsNG--LVTVmvpqlRRENSLLLWNVfDLNTPVHTFVGHDDVVLEFQWrrqkegSKD-YQLVTWSRDQTLRMWRVD 217
Cdd:COG2319   254 FSP--DGrlLASG-----SADGTVRLWDL-ATGELLRTLTGHSGGVNSVAF------SPDgKLLASGSDDGTVRLWDLA 318
WD40 COG2319
WD40 repeat [General function prediction only];
63-217 1.34e-13

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 73.79  E-value: 1.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774  63 YLAT-SHDGDIRIWDkRKPSTAVEYLAAHLSKIHGLDWHPDSEHiLATSSQDNSVKFWDYRQPRKYLNILPCQVPVWKAR 141
Cdd:COG2319   260 LLASgSADGTVRLWD-LATGELLRTLTGHSGGVNSVAFSPDGKL-LASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVA 337

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038185774 142 YTPFSNGLVTVmvpqlRRENSLLLWNVfDLNTPVHTFVGHDDVVLEFQWrrqkegSKDYQ-LVTWSRDQTLRMWRVD 217
Cdd:COG2319   338 FSPDGKTLASG-----SDDGTVRLWDL-ATGELLRTLTGHTGAVTSVAF------SPDGRtLASGSADGTVRLWDLA 402
mRING-H2-C3H3C2_Mio cd16691
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein mio and ...
 863-894 6.14e-13

Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein mio and simialr proteins; This family contains Mio,its counterpart Sea4 from yeast, and other homologs. Mio/Sea4 is a component of the GATOR2 complex, which also includes another four subunits, Seh1, Sec13, Sea2/WDR24, and Sea3/WDR59. GATOR2 and GATOR1, which is composed of three subunits, DEPDC5, Nprl2, and Nprl3, form the Rag-interacting complex GATOR (GAP Activity Towards Rags). Inhibition of GATOR1 subunits makes mTORC1 signaling resistant to amino acid deprivation. In contrast, inhibition of GATOR2 subunits suppresses mTORC1 signaling and GATOR2 negatively regulates DEPDC5. Mio interacts with endogenous RagA and RagC, and plays an essential role in the activation of mTOR Complex 1 (mTORC1) by amino acids. In GATOR2, Mio and Seh1 localize to lysosomes and autolysosomes, and form a heterodimer that is required to oppose the TORC1 inhibitory activity of the Iml1/GATOR1 complex to prevent the constitutive down-regulation of TORC1 activity in later stages of oogenesis. A tissue-specific requirement is necessary for Mio to be involved in cell growth in the female germ line. Mio contains an N-terminal WD40 domain and a C-terminal RING-H2 finger with an unusual arrangement of zinc-coordinating residues. The cysteines and histidines in the RING-H2 finger are arranged as a modified C3H3C2-type, rather than the canonical C3H2C3-type.


Pssm-ID: 438352  Cd Length: 75  Bit Score: 64.78  E-value: 6.14e-13
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2038185774 863 FCLTCGHGGHTSHMMEWFRTQEVCP-TGCGCHC 894
Cdd:cd16691    43 WCQTCRHGGHAGHLQEWFRDHSECPvSGCDCKC 75
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 87-232 4.88e-12

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: 67.75  E-value: 4.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774  87 LAAHLSKIHGLDWHPDSEHiLATSSQDNSVKFWDYRQPRKYLNILPCQVPVWKARYTPFSNGLVTVmvpqlRRENSLLLW 166
Cdd:cd00200     5 LKGHTGGVTCVAFSPDGKL-LATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASG-----SSDKTIRLW 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038185774 167 NVfDLNTPVHTFVGHDDVVLEFQWrrqkegSKDYQLVTWS-RDQTLRMWRVDYQMQRLCANDILDGV 232
Cdd:cd00200    79 DL-ETGECVRTLTGHTSYVSSVAF------SPDGRILSSSsRDKTIKVWDVETGKCLTTLRGHTDWV 138
RWD smart00591
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily ...
 301-401 1.68e-11

domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily related to the UBCc domain;


Pssm-ID: 214735  Cd Length: 107  Bit Score: 61.60  E-value: 1.68e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774  301 EFSLINVQIRNVNVEMDAADRSCTVSVHCSNHR---------VKMLVTFPAQYPnNAAPSFQFINPTTITSAVKAKLLKI 371
Cdd:smart00591   1 ELEALESIYPEDFEVIDEDARIPEITIKLSPSSdegedqyvsLTLQVKLPENYP-DEAPPISLLNSEGLSDEQLAELLKK 79

                           90       100       110
                   ....*....|....*....|....*....|
gi 2038185774  372 LKDTSLQkvKRNQSCLEPCLRQLVSCLESF 401
Cdd:smart00591  80 LEEIAEE--NLGEVMIFELVEKLQEFLSEF 107
zf-RING_16 pfam17120
RING/Ubox like zinc-binding domain;
850-898 1.91e-11

RING/Ubox like zinc-binding domain;


Pssm-ID: 375001  Cd Length: 57  Bit Score: 59.72  E-value: 1.91e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2038185774 850 CAICHVAVRGSSNFCLTCGHGGHTSHMMEWFRTQE-VCPTGCGCHCLLES 898
Cdd:pfam17120   7 CNYCCLRVRGRVFLCGVCQHVLHASCAREWWENDDgECPSGCGCNCLEHH 56
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 54-151 6.39e-10

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: 61.20  E-value: 6.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774  54 VKWNKKNANYLATSHDGDIRIWDKRKPSTaVEYLAAHLSKIHGLDWHPDSeHILATSSQDNSVKFWDYRqPRKYLNILPC 133
Cdd:cd00200   183 VAFSPDGEKLLSSSSDGTIKLWDLSTGKC-LGTLRGHENGVNSVAFSPDG-YLLASGSEDGTIRVWDLR-TGECVQTLSG 259

                          90
                  ....*....|....*....
gi 2038185774 134 -QVPVWKARYTPFSNGLVT 151
Cdd:cd00200   260 hTNSVTSLAWSPDGKRLAS 278
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 31-214 9.25e-09

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 59.33  E-value: 9.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774  31 IISQRRDTRKPTVALSAVAGASQVKWNKKNANYLATSH-DGDIRIWDKRKPSTAVEyLAAHLSKIHGLDWHPDSEHILAT 109
Cdd:PLN00181  515 IIKDGRDIHYPVVELASRSKLSGICWNSYIKSQVASSNfEGVVQVWDVARSQLVTE-MKEHEKRVWSIDYSSADPTLLAS 593

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774 110 SSQDNSVKFWDYRQP------RKYLNILPCQVPVWKARYTPFSNGlvtvmvpqlrrENSLLLWNVFDLNTPVHTFVGHDD 183
Cdd:PLN00181  594 GSDDGSVKLWSINQGvsigtiKTKANICCVQFPSESGRSLAFGSA-----------DHKVYYYDLRNPKLPLCTMIGHSK 662

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2038185774 184 VVlefQWRRQKEGSkdyQLVTWSRDQTLRMW 214
Cdd:PLN00181  663 TV---SYVRFVDSS---TLVSSSTDNTLKLW 687
zinc_ribbon_16 pfam17034
Zinc-ribbon like family; This family is found at the C-terminus of WD40 repeat structures in ...
 862-894 5.92e-08

Zinc-ribbon like family; This family is found at the C-terminus of WD40 repeat structures in eukaryotes.


Pssm-ID: 374955  Cd Length: 125  Bit Score: 51.97  E-value: 5.92e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2038185774 862 NFCLTCGHGGHTSHMMEWFRTQEVCPTG-CGCHC 894
Cdd:pfam17034  89 SFCLSCGHGSHADHATEWFSTHSICPVAdCNCLC 122
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 54-120 1.12e-07

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: 54.26  E-value: 1.12e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038185774  54 VKWNKKNANYLATSHDGDIRIWDKRKPSTaVEYLAAHLSKIHGLDWHPDSeHILATSSQDNSVKFWD 120
Cdd:cd00200   225 VAFSPDGYLLASGSEDGTIRVWDLRTGEC-VQTLSGHTNSVTSLAWSPDG-KRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
27-217 2.40e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 54.15  E-value: 2.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774  27 TASHIISQRRDTRKPTVALSAVAGASQVKWNKKNANYLATSHDGDIRIWDkRKPSTAVEYLAAHLSKIHGLDWHPDSeHI 106
Cdd:COG2319    15 DLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLD-AAAGALLATLLGHTAAVLSVAFSPDG-RL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774 107 LATSSQDNSVKFWDYRQPRKYLNILPCQVPVWKARYTPfsNG--LVTVmvpqlRRENSLLLWNVFDlNTPVHTFVGHDDV 184
Cdd:COG2319    93 LASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSP--DGktLASG-----SADGTVRLWDLAT-GKLLRTLTGHSGA 164

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2038185774 185 VLEFQWrrqkegSKD-YQLVTWSRDQTLRMWRVD 217
Cdd:COG2319   165 VTSVAF------SPDgKLLASGSDDGTVRLWDLA 192
WD40 COG2319
WD40 repeat [General function prediction only];
62-120 3.29e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 53.76  E-value: 3.29e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774  62 NYLAT-SHDGDIRIWDkRKPSTAVEYLAAHLSKIHGLDWHPDSeHILATSSQDNSVKFWD 120
Cdd:COG2319   343 KTLASgSDDGTVRLWD-LATGELLRTLTGHTGAVTSVAFSPDG-RTLASGSADGTVRLWD 400
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 87-120 1.05e-05

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 43.07  E-value: 1.05e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2038185774   87 LAAHLSKIHGLDWHPDSeHILATSSQDNSVKFWD 120
Cdd:smart00320   8 LKGHTGPVTSVAFSPDG-KYLASGSDDGTIKLWD 40
RING-H2 cd16448
H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type ...
 850-888 1.18e-04

H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). This family corresponds to the H2 subclass of RING (RING-H2) finger proteins that are characterized by containing C3H2C3-type canonical RING-H2 fingers or noncanonical RING-H2 finger variants, including C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type modified RING-H2 fingers. The canonical RING-H2 finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-H-X2-C-X(4-48)-C-X2-C, X is any amino acid and the number of X residues varies in different fingers. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-H2 finger can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serves as a scaffold for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 438112 [Multi-domain]  Cd Length: 43  Bit Score: 40.08  E-value: 1.18e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2038185774 850 CAICHVAVRGSSNF-CLTCGHGGHTSHMMEWFRTQE-VCPT 888
Cdd:cd16448     1 CVICLEEFEEGDVVrLLPCGHVFHLACILRWLESGNnTCPL 41
WD40 pfam00400
WD domain, G-beta repeat;
87-120 1.30e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.02  E-value: 1.30e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2038185774  87 LAAHLSKIHGLDWHPDSEHiLATSSQDNSVKFWD 120
Cdd:pfam00400   7 LEGHTGSVTSLAFSPDGKL-LASGSDDGTVKVWD 39
RWD_GCN2 cd23823
RWD domain of eIF-2-alpha kinase GCN2 and related proteins; GCN2 (EC 2.7.11.1), also called ...
 327-404 1.64e-04

RWD domain of eIF-2-alpha kinase GCN2 and related proteins; GCN2 (EC 2.7.11.1), also called eukaryotic translation initiation factor 2-alpha kinase 4 (EIF2AK4), acts as a metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to low amino acid availability. It also plays a role in modulating the adaptive immune response to yellow fever virus infection and promotes dendritic cells to initiate autophagy and antigene presentation to both CD4(+) and CD8(+) T-cells under amino acid starvation.


Pssm-ID: 467659  Cd Length: 117  Bit Score: 41.82  E-value: 1.64e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038185774 327 VHCSnhrVKMLVTFPAQYPNnAAPSFQFINPTTITSAVKAKLLKILKDTSLQKVKrnqsclEPCLRQLVSCLESFVNQ 404
Cdd:cd23823    48 NHVS---VDLHVKFPPTYPD-VPPEIELENVKGLSDEQLEELLKELEELAKELLG------EEMIFELAEAVQEFLEE 115
PTZ00420 PTZ00420
coronin; Provisional
 1-130 4.07e-04

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 44.17  E-value: 4.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774   1 MPLLKVTAKSPA-RANGTLELCS------GILMTASHI--------------ISQRRDTRKPTVAL--SAVAGASQVKWN 57
Cdd:PTZ00420    4 VPLIKNLYPDPSnNLFDDLRICSrvidscGIACSSGFVavpwevegggligaIRLENQMRKPPVIKlkGHTSSILDLQFN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774  58 KKNANYLAT-SHDGDIRIWDKRKPSTAVE-------YLAAHLSKIHGLDWHPDSEHILATSSQDNSVKFWDYRQPRKYLN 129
Cdd:PTZ00420   84 PCFSEILASgSEDLTIRVWEIPHNDESVKeikdpqcILKGHKKKISIIDWNPMNYYIMCSSGFDSFVNIWDIENEKRAFQ 163


                  .
gi 2038185774 130 I 130
Cdd:PTZ00420  164 I 164
RING-H2_TTC3 cd16481
RING finger, H2 subclass, found in Tetratricopeptide repeat protein 3 (TTC3) and similar ...
 849-888 1.60e-03

RING finger, H2 subclass, found in Tetratricopeptide repeat protein 3 (TTC3) and similar proteins; TTC3, also known as protein DCRR1, TPR repeat protein D, TPR repeat protein 3, or RING finger protein 105 (RNF105), is an E3 ubiquitin-protein ligase encoded by a gene within the Down syndrome (DS) critical region on chromosome 21. It affects differentiation and Golgi compactness in neurons through specific actin-regulating pathways. It inhibits the neuronal-like differentiation of pheocromocytoma cells by activating RhoA and by binding to Citron proteins. TTC3 is an Akt-specific E3 ligase that binds to phosphorylated Akt and facilitates its ubiquitination and degradation within the nucleus. It contains four N-terminal TPR motifs, a potential coiled-coil region and a Citron binding region in the central part, and a C-terminal C3H2C2-type RING-H2 finger.


Pssm-ID: 438144 [Multi-domain]  Cd Length: 45  Bit Score: 36.94  E-value: 1.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2038185774 849 QCAICHVAVRGSSNFCLTCGHGGHTSHMMEWFRTQEVCPT 888
Cdd:cd16481     1 PCIICHDDLKPDQLAKLECGHIFHKECIKQWLKEQSTCPT 40
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
 320-401 3.32e-03

RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. The function of this domain is unknown. GCN2 is the alpha-subunit of the only translation initiation factor (eIF2 alpha) kinase that appears in all eukaryotes. Its function requires an interaction with GCN1 via the domain at its N-terminus, which is termed the RWD domain after three major RWD-containing proteins: RING finger-containing proteins, WD-repeat-containing proteins, and yeast DEAD (DEXD)-like helicases. The structure forms an alpha + beta sandwich fold consisting of two layers: a four-stranded antiparallel beta-sheet, and three side-by-side alpha-helices.


Pssm-ID: 399058  Cd Length: 111  Bit Score: 38.07  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774 320 DRSCTVSVHCSNHRVKMLVTFPAQYPnNAAPSFQFINPTTITSAVKAKLLKILKdtslQKVKRNQSclEPCLRQLVSCLE 399
Cdd:pfam05773  36 SLDSDESDSSHLPPLVLKFTLPEDYP-DEPPKISLSSPWNLSDEQVLSLLEELE----ELAEENLG--EVMIFELIEWLQ 108


                  ..
gi 2038185774 400 SF 401
Cdd:pfam05773 109 EN 110
eIF2A pfam08662
Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation ...
 70-121 6.77e-03

Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation initiation factors.


Pssm-ID: 462552 [Multi-domain]  Cd Length: 194  Bit Score: 38.79  E-value: 6.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038185774  70 GDIRIWD---KRKPSTAVEYLAAHLskihglDWHPDSEHIL-ATSSQ----DNSVKFWDY 121
Cdd:pfam08662 125 GDIEFWDvvnKKKIATAEASNATLC------EWSPDGRYFLtATTAPrlrvDNGFKIWHY 178
 
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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