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Conserved domains on  [gi|58331266|ref|NP_085058|]
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GATOR2 complex protein WDR59 isoform 1 [Homo sapiens]

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 ...
 922-968 8.84e-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: 8.84e-32
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 58331266 922 FQCAICHVAVRGSSNFCLTCGHGGHTSHMMEWFRTQEVCPTGCGCHC 968
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 ...
 100-343 5.43e-25

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: 106.27  E-value: 5.43e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266 100 TLQGHTRVISDLDWAVfEPDLLVTSSVDTYIYIWDIKDT---RKPTVALSAVAGASQVKWNKKnanCLATSHDGDVRIWD 176
Cdd:cd00200   4 TLKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGellRTLKGHTGPVRDVAASADGTY---LASGSSDKTIRLWD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266 177 KRKPSTAVEYlAAHLSKIHGLDWHPDSeHILATSSQDNSVKFWDYRQPRKYLNILPCQVPVWKARYTPFSNGLVTVMvpq 256
Cdd:cd00200  80 LETGECVRTL-TGHTSYVSSVAFSPDG-RILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSS--- 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266 257 lrRENSLLLWNVfDLNTPVHTFVGHDDVVLEFQWRKQKEgskdyQLVTWSRDQTLRMWrvDSQMQRLCAndILDGVDEFI 336
Cdd:cd00200 155 --QDGTIKLWDL-RTGKCVATLTGHTGEVNSVAFSPDGE-----KLLSSSSDGTIKLW--DLSTGKCLG--TLRGHENGV 222


                ....*..
gi 58331266 337 ESISLLP 343
Cdd:cd00200 223 NSVAFSP 229
RWD smart00591
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily ...
 394-494 3.13e-13

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: 66.61  E-value: 3.13e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266    394 EFSLINVQIRNVNVEMDAADRSCTVSVHCSNHR---------VKMLVKFPAQYPnNAAPSFQFINPTTITSTMKAKLLKI 464
Cdd:smart00591   1 ELEALESIYPEDFEVIDEDARIPEITIKLSPSSdegedqyvsLTLQVKLPENYP-DEAPPISLLNSEGLSDEQLAELLKK 79

                           90       100       110
                   ....*....|....*....|....*....|
gi 58331266    465 LKDTALQkvKRGQSCLEPCLRQLVSCLESF 494
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 ...
 922-968 8.84e-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: 8.84e-32
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 58331266 922 FQCAICHVAVRGSSNFCLTCGHGGHTSHMMEWFRTQEVCPTGCGCHC 968
Cdd:cd16692   1 LQCAICHVAVRGSSNFCLACGHGGHTSHMMEWFRTQDVCPTGCGCHC 47
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 100-343 5.43e-25

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: 106.27  E-value: 5.43e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266 100 TLQGHTRVISDLDWAVfEPDLLVTSSVDTYIYIWDIKDT---RKPTVALSAVAGASQVKWNKKnanCLATSHDGDVRIWD 176
Cdd:cd00200   4 TLKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGellRTLKGHTGPVRDVAASADGTY---LASGSSDKTIRLWD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266 177 KRKPSTAVEYlAAHLSKIHGLDWHPDSeHILATSSQDNSVKFWDYRQPRKYLNILPCQVPVWKARYTPFSNGLVTVMvpq 256
Cdd:cd00200  80 LETGECVRTL-TGHTSYVSSVAFSPDG-RILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSS--- 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266 257 lrRENSLLLWNVfDLNTPVHTFVGHDDVVLEFQWRKQKEgskdyQLVTWSRDQTLRMWrvDSQMQRLCAndILDGVDEFI 336
Cdd:cd00200 155 --QDGTIKLWDL-RTGKCVATLTGHTGEVNSVAFSPDGE-----KLLSSSSDGTIKLW--DLSTGKCLG--TLRGHENGV 222


                ....*..
gi 58331266 337 ESISLLP 343
Cdd:cd00200 223 NSVAFSP 229
WD40 COG2319
WD40 repeat [General function prediction only];
78-343 1.22e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 104.61  E-value: 1.22e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266  78 AASSNQRVDLykWKDGSGEVGTTLQGHTRVISDLDWAvfePD--LLVTSSVDTYIYIWDIKDTRKPTVALSAVAGASQVK 155
Cdd:COG2319 137 SGSADGTVRL--WDLATGKLLRTLTGHSGAVTSVAFS---PDgkLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVA 211

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266 156 WNKkNANCLAT-SHDGDVRIWDkRKPSTAVEYLAAHLSKIHGLDWHPDSEHiLATSSQDNSVKFWDyRQPRKYLNILP-C 233
Cdd:COG2319 212 FSP-DGKLLASgSADGTVRLWD-LATGKLLRTLTGHSGSVRSVAFSPDGRL-LASGSADGTVRLWD-LATGELLRTLTgH 287

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266 234 QVPVWKARYTPFSNGLVTVmvpqlRRENSLLLWNVfDLNTPVHTFVGHDDVVLEFQWrkqkegSKD-YQLVTWSRDQTLR 312
Cdd:COG2319 288 SGGVNSVAFSPDGKLLASG-----SDDGTVRLWDL-ATGKLLRTLTGHTGAVRSVAF------SPDgKTLASGSDDGTVR 355

                       250       260       270
                ....*....|....*....|....*....|.
gi 58331266 313 MWRVDSQMQRLcandILDGVDEFIESISLLP 343
Cdd:COG2319 356 LWDLATGELLR----TLTGHTGAVTSVAFSP 382
RWD smart00591
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily ...
 394-494 3.13e-13

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: 66.61  E-value: 3.13e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266    394 EFSLINVQIRNVNVEMDAADRSCTVSVHCSNHR---------VKMLVKFPAQYPnNAAPSFQFINPTTITSTMKAKLLKI 464
Cdd:smart00591   1 ELEALESIYPEDFEVIDEDARIPEITIKLSPSSdegedqyvsLTLQVKLPENYP-DEAPPISLLNSEGLSDEQLAELLKK 79

                           90       100       110
                   ....*....|....*....|....*....|
gi 58331266    465 LKDTALQkvKRGQSCLEPCLRQLVSCLESF 494
Cdd:smart00591  80 LEEIAEE--NLGEVMIFELVEKLQEFLSEF 107
zf-RING_16 pfam17120
RING/Ubox like zinc-binding domain;
924-972 1.95e-11

RING/Ubox like zinc-binding domain;


Pssm-ID: 375001  Cd Length: 57  Bit Score: 60.11  E-value: 1.95e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 58331266   924 CAICHVAVRGSSNFCLTCGHGGHTSHMMEWFRTQE-VCPTGCGCHCLLES 972
Cdd:pfam17120   7 CNYCCLRVRGRVFLCGVCQHVLHASCAREWWENDDgECPSGCGCNCLEHH 56
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 117-314 1.48e-08

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 58.94  E-value: 1.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266  117 EPDLLVTSSVDTYIYIWD----IKDTRK---PTVALSAVAGASQVKWNKKNANCLATSH-DGDVRIWDKRKPSTAVEyLA 188
Cdd:PLN00181 494 DGEFFATAGVNKKIKIFEcesiIKDGRDihyPVVELASRSKLSGICWNSYIKSQVASSNfEGVVQVWDVARSQLVTE-MK 572

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266  189 AHLSKIHGLDWHPDSEHILATSSQDNSVKFWDYRQP------RKYLNILPCQVPVWKARYTPFSNGlvtvmvpqlrrENS 262
Cdd:PLN00181 573 EHEKRVWSIDYSSADPTLLASGSDDGSVKLWSINQGvsigtiKTKANICCVQFPSESGRSLAFGSA-----------DHK 641

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 58331266  263 LLLWNVFDLNTPVHTFVGHDDVVlefQWRKQKEGSkdyQLVTWSRDQTLRMW 314
Cdd:PLN00181 642 VYYYDLRNPKLPLCTMIGHSKTV---SYVRFVDSS---TLVSSSTDNTLKLW 687
RWD_GCN2 cd23823
RWD domain of eIF-2-alpha kinase GCN2 and related proteins; GCN2 (EC 2.7.11.1), also called ...
 420-497 1.02e-05

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: 45.67  E-value: 1.02e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58331266 420 VHCSnhrVKMLVKFPAQYPNnAAPSFQFINPTTITSTMKAKLLKILKDTALQKVKrgqsclEPCLRQLVSCLESFVNQ 497
Cdd:cd23823  48 NHVS---VDLHVKFPPTYPD-VPPEIELENVKGLSDEQLEELLKELEELAKELLG------EEMIFELAEAVQEFLEE 115
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 187-220 2.09e-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: 42.30  E-value: 2.09e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 58331266    187 LAAHLSKIHGLDWHPDSeHILATSSQDNSVKFWD 220
Cdd:smart00320   8 LKGHTGPVTSVAFSPDG-KYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
187-220 2.45e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.25  E-value: 2.45e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 58331266   187 LAAHLSKIHGLDWHPDSEHiLATSSQDNSVKFWD 220
Cdd:pfam00400   7 LEGHTGSVTSLAFSPDGKL-LASGSDDGTVKVWD 39
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
 413-494 4.38e-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: 4.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266   413 DRSCTVSVHCSNHRVKMLVKFPAQYPnNAAPSFQFINPTTITSTMKAKLLKILKDTAlqkvkrgQSCL-EPCLRQLVSCL 491
Cdd:pfam05773  36 SLDSDESDSSHLPPLVLKFTLPEDYP-DEPPKISLSSPWNLSDEQVLSLLEELEELA-------EENLgEVMIFELIEWL 107


                  ...
gi 58331266   492 ESF 494
Cdd:pfam05773 108 QEN 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 ...
 922-968 8.84e-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: 8.84e-32
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 58331266 922 FQCAICHVAVRGSSNFCLTCGHGGHTSHMMEWFRTQEVCPTGCGCHC 968
Cdd:cd16692   1 LQCAICHVAVRGSSNFCLACGHGGHTSHMMEWFRTQDVCPTGCGCHC 47
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 100-343 5.43e-25

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: 106.27  E-value: 5.43e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266 100 TLQGHTRVISDLDWAVfEPDLLVTSSVDTYIYIWDIKDT---RKPTVALSAVAGASQVKWNKKnanCLATSHDGDVRIWD 176
Cdd:cd00200   4 TLKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGellRTLKGHTGPVRDVAASADGTY---LASGSSDKTIRLWD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266 177 KRKPSTAVEYlAAHLSKIHGLDWHPDSeHILATSSQDNSVKFWDYRQPRKYLNILPCQVPVWKARYTPFSNGLVTVMvpq 256
Cdd:cd00200  80 LETGECVRTL-TGHTSYVSSVAFSPDG-RILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSS--- 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266 257 lrRENSLLLWNVfDLNTPVHTFVGHDDVVLEFQWRKQKEgskdyQLVTWSRDQTLRMWrvDSQMQRLCAndILDGVDEFI 336
Cdd:cd00200 155 --QDGTIKLWDL-RTGKCVATLTGHTGEVNSVAFSPDGE-----KLLSSSSDGTIKLW--DLSTGKCLG--TLRGHENGV 222


                ....*..
gi 58331266 337 ESISLLP 343
Cdd:cd00200 223 NSVAFSP 229
WD40 COG2319
WD40 repeat [General function prediction only];
78-343 1.22e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 104.61  E-value: 1.22e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266  78 AASSNQRVDLykWKDGSGEVGTTLQGHTRVISDLDWAvfePD--LLVTSSVDTYIYIWDIKDTRKPTVALSAVAGASQVK 155
Cdd:COG2319 137 SGSADGTVRL--WDLATGKLLRTLTGHSGAVTSVAFS---PDgkLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVA 211

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266 156 WNKkNANCLAT-SHDGDVRIWDkRKPSTAVEYLAAHLSKIHGLDWHPDSEHiLATSSQDNSVKFWDyRQPRKYLNILP-C 233
Cdd:COG2319 212 FSP-DGKLLASgSADGTVRLWD-LATGKLLRTLTGHSGSVRSVAFSPDGRL-LASGSADGTVRLWD-LATGELLRTLTgH 287

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266 234 QVPVWKARYTPFSNGLVTVmvpqlRRENSLLLWNVfDLNTPVHTFVGHDDVVLEFQWrkqkegSKD-YQLVTWSRDQTLR 312
Cdd:COG2319 288 SGGVNSVAFSPDGKLLASG-----SDDGTVRLWDL-ATGKLLRTLTGHTGAVRSVAF------SPDgKTLASGSDDGTVR 355

                       250       260       270
                ....*....|....*....|....*....|.
gi 58331266 313 MWRVDSQMQRLcandILDGVDEFIESISLLP 343
Cdd:COG2319 356 LWDLATGELLR----TLTGHTGAVTSVAFSP 382
WD40 COG2319
WD40 repeat [General function prediction only];
46-318 3.19e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 103.45  E-value: 3.19e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266  46 APFEGHRkisrqskWDIGAVQWNPhDSfaHYFA-ASSNQRVDLykWKDGSGEVGTTLQGHTRVISDLDWAvfePD--LLV 122
Cdd:COG2319 156 RTLTGHS-------GAVTSVAFSP-DG--KLLAsGSDDGTVRL--WDLATGKLLRTLTGHTGAVRSVAFS---PDgkLLA 220

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266 123 TSSVDTYIYIWDIKDTRKPTVALSAVAGASQVKWNKKNANCLATSHDGDVRIWDkRKPSTAVEYLAAHLSKIHGLDWHPD 202
Cdd:COG2319 221 SGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWD-LATGELLRTLTGHSGGVNSVAFSPD 299

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266 203 SEHiLATSSQDNSVKFWDYRQPRKYLNILPCQVPVWKARYTPFSNGLVTVmvpqlRRENSLLLWNVfDLNTPVHTFVGHD 282
Cdd:COG2319 300 GKL-LASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASG-----SDDGTVRLWDL-ATGELLRTLTGHT 372

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 58331266 283 DVVLEFQWrkqkegSKDYQ-LVTWSRDQTLRMWRVDS 318
Cdd:COG2319 373 GAVTSVAF------SPDGRtLASGSADGTVRLWDLAT 403
mRING-H2-C3H3C2_Mio-like cd16488
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein mio and ...
 923-966 4.81e-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: 4.81e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 58331266 923 QCAICHVAVRGSSNFCLTCGHGGHTSHMMEWFRTQEVCPTGCGC 966
Cdd:cd16488   1 SCAICHLPVKGLSSFCLNCGHGGHAECIREWFEDHTECPTGCGC 44
WD40 COG2319
WD40 repeat [General function prediction only];
17-318 5.59e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 96.52  E-value: 5.59e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266  17 SQATAMSVDCLGQHAVLSGRRFLYIVNLDAPFEGHRKISRQSKWDIGAVQWNPHDsfAHYFAASSNQRVDLykWKDGSGE 96
Cdd:COG2319  36 AAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDG--RLLASASADGTVRL--WDLATGL 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266  97 VGTTLQGHTRVISDLdwaVFEPD--LLVTSSVDTYIYIWDIKDTRK------PTVALSAVAGASQVKWnkknancLAT-S 167
Cdd:COG2319 112 LLRTLTGHTGAVRSV---AFSPDgkTLASGSADGTVRLWDLATGKLlrtltgHSGAVTSVAFSPDGKL-------LASgS 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266 168 HDGDVRIWDKRKPsTAVEYLAAHLSKIHGLDWHPDSeHILATSSQDNSVKFWDYRQPRKYLNILPCQVPVWKARYTPfsN 247
Cdd:COG2319 182 DDGTVRLWDLATG-KLLRTLTGHTGAVRSVAFSPDG-KLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSP--D 257

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58331266 248 G--LVTVmvpqlRRENSLLLWNVfDLNTPVHTFVGHDDVVLEFQWrkqkegSKD-YQLVTWSRDQTLRMWRVDS 318
Cdd:COG2319 258 GrlLASG-----SADGTVRLWDL-ATGELLRTLTGHSGGVNSVAF------SPDgKLLASGSDDGTVRLWDLAT 319
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 48-251 3.33e-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: 3.33e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266  48 FEGHRKisrqskwDIGAVQWNPHDsfaHYFAASSNQ---RVdlykWKDGSGEVGTTLQGHTRVISDLDWAVFePDLLVTS 124
Cdd:cd00200  89 LTGHTS-------YVSSVAFSPDG---RILSSSSRDktiKV----WDVETGKCLTTLRGHTDWVNSVAFSPD-GTFVASS 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266 125 SVDTYIYIWDIKDTRKPTVALSAVAGASQVKWNKKNANCLATSHDGDVRIWDKRKPSTaVEYLAAHLSKIHGLDWHPDSe 204
Cdd:cd00200 154 SQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKC-LGTLRGHENGVNSVAFSPDG- 231

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 58331266 205 HILATSSQDNSVKFWDYRqPRKYLNILPC-QVPVWKARYTPFSNGLVT 251
Cdd:cd00200 232 YLLASGSEDGTIRVWDLR-TGECVQTLSGhTNSVTSLAWSPDGKRLAS 278
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 48-315 3.59e-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: 3.59e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266  48 FEGHRKisrqskwDIGAVQWNPHDSFahYFAASSNQRVDLYKWKDGsgEVGTTLQGHTRVISDLDWAVFEpDLLVTSSVD 127
Cdd:cd00200   5 LKGHTG-------GVTCVAFSPDGKL--LATGSGDGTIKVWDLETG--ELLRTLKGHTGPVRDVAASADG-TYLASGSSD 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266 128 TYIYIWDIKDTRKP-----------TVALSA----VAGASQ---VK-WNKKNANCLAT---------------------- 166
Cdd:cd00200  73 KTIRLWDLETGECVrtltghtsyvsSVAFSPdgriLSSSSRdktIKvWDVETGKCLTTlrghtdwvnsvafspdgtfvas 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266 167 -SHDGDVRIWDKRKPSTaVEYLAAHLSKIHGLDWHPDSEHILATSSqDNSVKFWDYRQPRkylnilpcqvpvWKARYTPF 245
Cdd:cd00200 153 sSQDGTIKLWDLRTGKC-VATLTGHTGEVNSVAFSPDGEKLLSSSS-DGTIKLWDLSTGK------------CLGTLRGH 218

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58331266 246 SNGLVTVMVPQLRR-------ENSLLLWNVfDLNTPVHTFVGHDDVVLEFQWrkqkegSKDYQ-LVTWSRDQTLRMWR 315
Cdd:cd00200 219 ENGVNSVAFSPDGYllasgseDGTIRVWDL-RTGECVQTLSGHTNSVTSLAW------SPDGKrLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
78-343 1.14e-19

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 92.67  E-value: 1.14e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266  78 AASSNQRVDLYKWKDGSGEVGTTLQGHTRVISDLDWAVfEPDLLVTSSVDTYIYIWDIKDTRKPTVALSAVAGASQVKWN 157
Cdd:COG2319  51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSP-DGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFS 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266 158 KkNANCLAT-SHDGDVRIWDKRKPsTAVEYLAAHLSKIHGLDWHPDSeHILATSSQDNSVKFWDYRQPRKYLNILPCQVP 236
Cdd:COG2319 130 P-DGKTLASgSADGTVRLWDLATG-KLLRTLTGHSGAVTSVAFSPDG-KLLASGSDDGTVRLWDLATGKLLRTLTGHTGA 206

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266 237 VWKARYTPFSNGLVTVmvpqlRRENSLLLWNVfDLNTPVHTFVGHDDVVLEFQWrkqkegSKDYQ-LVTWSRDQTLRMWR 315
Cdd:COG2319 207 VRSVAFSPDGKLLASG-----SADGTVRLWDL-ATGKLLRTLTGHSGSVRSVAF------SPDGRlLASGSADGTVRLWD 274

                       250       260
                ....*....|....*....|....*...
gi 58331266 316 VDSQMQRlcanDILDGVDEFIESISLLP 343
Cdd:COG2319 275 LATGELL----RTLTGHSGGVNSVAFSP 298
mRING-H2-C3H3C2_WDR24 cd16693
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 24 ...
 924-968 4.85e-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: 75.39  E-value: 4.85e-17
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 58331266 924 CAICHVAVRGSSNFCLTCGHGGHTSHMMEWFRTQEVCPTGCGCHC 968
Cdd:cd16693   2 CSVCHLPVKGLYVWCQGCGHGGHLEHMKEWFSTNSHCPAGCGHLC 46
WD40 COG2319
WD40 repeat [General function prediction only];
78-343 3.98e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 78.80  E-value: 3.98e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266  78 AASSNQRVDLYKWKDGSGEVGTTLQGHTRVISDLDWAVFEPDLLVTSSVDTYIyIWDIKDTRKPTVALSAVAGASQVKWN 157
Cdd:COG2319   9 LAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLL-LLDAAAGALLATLLGHTAAVLSVAFS 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266 158 KKNANCLATSHDGDVRIWDkRKPSTAVEYLAAHLSKIHGLDWHPDSeHILATSSQDNSVKFWDyRQPRKYLNILPC-QVP 236
Cdd:COG2319  88 PDGRLLASASADGTVRLWD-LATGLLLRTLTGHTGAVRSVAFSPDG-KTLASGSADGTVRLWD-LATGKLLRTLTGhSGA 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266 237 VWKARYTPfsNG--LVTVmvpqlRRENSLLLWNVFDlNTPVHTFVGHDDVVLEFQWrkqkegSKD-YQLVTWSRDQTLRM 313
Cdd:COG2319 165 VTSVAFSP--DGklLASG-----SDDGTVRLWDLAT-GKLLRTLTGHTGAVRSVAF------SPDgKLLASGSADGTVRL 230

                       250       260       270
                ....*....|....*....|....*....|
gi 58331266 314 WRVDSQMQRLcandILDGVDEFIESISLLP 343
Cdd:COG2319 231 WDLATGKLLR----TLTGHSGSVRSVAFSP 256
RWD smart00591
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily ...
 394-494 3.13e-13

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: 66.61  E-value: 3.13e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266    394 EFSLINVQIRNVNVEMDAADRSCTVSVHCSNHR---------VKMLVKFPAQYPnNAAPSFQFINPTTITSTMKAKLLKI 464
Cdd:smart00591   1 ELEALESIYPEDFEVIDEDARIPEITIKLSPSSdegedqyvsLTLQVKLPENYP-DEAPPISLLNSEGLSDEQLAELLKK 79

                           90       100       110
                   ....*....|....*....|....*....|
gi 58331266    465 LKDTALQkvKRGQSCLEPCLRQLVSCLESF 494
Cdd:smart00591  80 LEEIAEE--NLGEVMIFELVEKLQEFLSEF 107
mRING-H2-C3H3C2_Mio cd16691
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein mio and ...
 937-968 5.59e-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: 5.59e-13
                        10        20        30
                ....*....|....*....|....*....|...
gi 58331266 937 FCLTCGHGGHTSHMMEWFRTQEVCP-TGCGCHC 968
Cdd:cd16691  43 WCQTCRHGGHAGHLQEWFRDHSECPvSGCDCKC 75
zf-RING_16 pfam17120
RING/Ubox like zinc-binding domain;
924-972 1.95e-11

RING/Ubox like zinc-binding domain;


Pssm-ID: 375001  Cd Length: 57  Bit Score: 60.11  E-value: 1.95e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 58331266   924 CAICHVAVRGSSNFCLTCGHGGHTSHMMEWFRTQE-VCPTGCGCHCLLES 972
Cdd:pfam17120   7 CNYCCLRVRGRVFLCGVCQHVLHASCAREWWENDDgECPSGCGCNCLEHH 56
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 117-314 1.48e-08

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 58.94  E-value: 1.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266  117 EPDLLVTSSVDTYIYIWD----IKDTRK---PTVALSAVAGASQVKWNKKNANCLATSH-DGDVRIWDKRKPSTAVEyLA 188
Cdd:PLN00181 494 DGEFFATAGVNKKIKIFEcesiIKDGRDihyPVVELASRSKLSGICWNSYIKSQVASSNfEGVVQVWDVARSQLVTE-MK 572

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266  189 AHLSKIHGLDWHPDSEHILATSSQDNSVKFWDYRQP------RKYLNILPCQVPVWKARYTPFSNGlvtvmvpqlrrENS 262
Cdd:PLN00181 573 EHEKRVWSIDYSSADPTLLASGSDDGSVKLWSINQGvsigtiKTKANICCVQFPSESGRSLAFGSA-----------DHK 641

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 58331266  263 LLLWNVFDLNTPVHTFVGHDDVVlefQWRKQKEGSkdyQLVTWSRDQTLRMW 314
Cdd:PLN00181 642 VYYYDLRNPKLPLCTMIGHSKTV---SYVRFVDSS---TLVSSSTDNTLKLW 687
zinc_ribbon_16 pfam17034
Zinc-ribbon like family; This family is found at the C-terminus of WD40 repeat structures in ...
 936-968 4.46e-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: 52.74  E-value: 4.46e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 58331266   936 NFCLTCGHGGHTSHMMEWFRTQEVCPTG-CGCHC 968
Cdd:pfam17034  89 SFCLSCGHGSHADHATEWFSTHSICPVAdCNCLC 122
RWD_GCN2 cd23823
RWD domain of eIF-2-alpha kinase GCN2 and related proteins; GCN2 (EC 2.7.11.1), also called ...
 420-497 1.02e-05

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: 45.67  E-value: 1.02e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58331266 420 VHCSnhrVKMLVKFPAQYPNnAAPSFQFINPTTITSTMKAKLLKILKDTALQKVKrgqsclEPCLRQLVSCLESFVNQ 497
Cdd:cd23823  48 NHVS---VDLHVKFPPTYPD-VPPEIELENVKGLSDEQLEELLKELEELAKELLG------EEMIFELAEAVQEFLEE 115
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 187-220 2.09e-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: 42.30  E-value: 2.09e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 58331266    187 LAAHLSKIHGLDWHPDSeHILATSSQDNSVKFWD 220
Cdd:smart00320   8 LKGHTGPVTSVAFSPDG-KYLASGSDDGTIKLWD 40
PTZ00420 PTZ00420
coronin; Provisional
 101-222 2.99e-05

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 48.02  E-value: 2.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266  101 LQGHTRVISDLDWAVFEPDLLVTSSVDTYIYIWDIKDTRKpTVALSAVAGASQVKWNKKNANCLATSHDGDVRIWDKRKP 180
Cdd:PTZ00420 121 LKGHKKKISIIDWNPMNYYIMCSSGFDSFVNIWDIENEKR-AFQINMPKKLSSLKWNIKGNLLSGTCVGKHMHIIDPRKQ 199

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 58331266  181 STAVEYLAAHLSK------IHGLDwhPDSEHILATSSQDNS---VKFWDYR 222
Cdd:PTZ00420 200 EIASSFHIHDGGKntkniwIDGLG--GDDNYILSTGFSKNNmreMKLWDLK 248
RING-H2 cd16448
H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type ...
 924-962 1.17e-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: 40.46  E-value: 1.17e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 58331266 924 CAICHVAVRGSSNF-CLTCGHGGHTSHMMEWFRTQE-VCPT 962
Cdd:cd16448   1 CVICLEEFEEGDVVrLLPCGHVFHLACILRWLESGNnTCPL 41
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 58-232 2.38e-04

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 45.08  E-value: 2.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266   58 SKWDIGAVQWNphdSFAHYFAASSNQRVDLYKWKDGSGEVGTTLQGHTRVISDLDWAVFEPDLLVTSSVDTYIYIWDIKD 137
Cdd:PLN00181 531 SRSKLSGICWN---SYIKSQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPTLLASGSDDGSVKLWSINQ 607

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266  138 trkpTVALSAV---AGASQVKWNKKNANCLA-TSHDGDVRIWDKRKPSTAVEYLAAHLSKIHGLDWHPDSehILATSSQD 213
Cdd:PLN00181 608 ----GVSIGTIktkANICCVQFPSESGRSLAfGSADHKVYYYDLRNPKLPLCTMIGHSKTVSYVRFVDSS--TLVSSSTD 681

                        170
                 ....*....|....*....
gi 58331266  214 NSVKFWDYRQPRKYLNILP 232
Cdd:PLN00181 682 NTLKLWDLSMSISGINETP 700
WD40 pfam00400
WD domain, G-beta repeat;
187-220 2.45e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.25  E-value: 2.45e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 58331266   187 LAAHLSKIHGLDWHPDSEHiLATSSQDNSVKFWD 220
Cdd:pfam00400   7 LEGHTGSVTSLAFSPDGKL-LASGSDDGTVKVWD 39
PTZ00420 PTZ00420
coronin; Provisional
 167-230 6.05e-04

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 43.79  E-value: 6.05e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58331266  167 SHDGDVRIWDKRKPSTAVE-------YLAAHLSKIHGLDWHPDSEHILATSSQDNSVKFWDYRQPRKYLNI 230
Cdd:PTZ00420  94 SEDLTIRVWEIPHNDESVKeikdpqcILKGHKKKISIIDWNPMNYYIMCSSGFDSFVNIWDIENEKRAFQI 164
PTZ00421 PTZ00421
coronin; Provisional
 61-223 7.51e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 43.34  E-value: 7.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266   61 DIGAVQWNPHDSfAHYFAASSNQRVdlYKWkdGSGEVGTT---------LQGHTRVISDLDWAVFEPDLLVTSSVDTYIY 131
Cdd:PTZ00421  77 PIIDVAFNPFDP-QKLFTASEDGTI--MGW--GIPEEGLTqnisdpivhLQGHTKKVGIVSFHPSAMNVLASAGADMVVN 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266  132 IWDIKDTRKPTVALSAVAGASQVKWNKKNANCLATSHDGDVRIWDKRKpSTAVEYLAAHLS-KIHGLDWHPDSEHILA-- 208
Cdd:PTZ00421 152 VWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRD-GTIVSSVEAHASaKSQRCLWAKRKDLIITlg 230

                        170
                 ....*....|....*.
gi 58331266  209 -TSSQDNSVKFWDYRQ 223
Cdd:PTZ00421 231 cSKSQQRQIMLWDTRK 246
RING-H2_TTC3 cd16481
RING finger, H2 subclass, found in Tetratricopeptide repeat protein 3 (TTC3) and similar ...
 923-962 1.73e-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: 1.73e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 58331266 923 QCAICHVAVRGSSNFCLTCGHGGHTSHMMEWFRTQEVCPT 962
Cdd:cd16481   1 PCIICHDDLKPDQLAKLECGHIFHKECIKQWLKEQSTCPT 40
WD40 pfam00400
WD domain, G-beta repeat;
95-134 1.97e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 1.97e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 58331266    95 GEVGTTLQGHTRVISDLDWAvFEPDLLVTSSVDTYIYIWD 134
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFS-PDGKLLASGSDDGTVKVWD 39
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
 413-494 4.38e-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: 4.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266   413 DRSCTVSVHCSNHRVKMLVKFPAQYPnNAAPSFQFINPTTITSTMKAKLLKILKDTAlqkvkrgQSCL-EPCLRQLVSCL 491
Cdd:pfam05773  36 SLDSDESDSSHLPPLVLKFTLPEDYP-DEPPKISLSSPWNLSDEQVLSLLEELEELA-------EENLgEVMIFELIEWL 107


                  ...
gi 58331266   492 ESF 494
Cdd:pfam05773 108 QEN 110
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 94-134 4.81e-03

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: 35.75  E-value: 4.81e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 58331266     94 SGEVGTTLQGHTRVISDLDWAvfePD--LLVTSSVDTYIYIWD 134
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFS---PDgkYLASGSDDGTIKLWD 40
RWD_DRWD_ELF-like cd11605
RWD, DRWD, and ELF domain family; The family includes the RWD, double-RWD (DRWD), and ELF ...
 406-480 6.36e-03

RWD, DRWD, and ELF domain family; The family includes the RWD, double-RWD (DRWD), and ELF domains. They belong to the ubiquitin-conjugating (UBC) superfamily that represents a structural domain with an alpha-beta(4)-alpha(3) core fold. The RWD domain (named after three major RWD-containing proteins: RING finger, WD-repeat-containing proteins and DEXD-like helicases) mediates protein-protein interactions in a variety of pathways in eukaryotes. The DRWD domain is responsible for substrate binding. It is involved in interactions with other kinetochore proteins. The ELF (N-terminal E2-like fold) domain is found in all Fanconi anemia group L protein (FANCL) homologs. It is required to promote efficient DNA damage-induced FANCD2 (Fanconi anemia group D2 protein) monoubiquitination in vertebrate cells.


Pssm-ID: 467641  Cd Length: 94  Bit Score: 37.16  E-value: 6.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331266 406 NVEMDAADRSCTVSVHCSNH------RVKMLVKFPAQYPNNAAPSFQFINPTTITSTMKAKLLKILKDTALQkvKRGQSC 479
Cdd:cd11605   9 ELEVLSDDSPLRFSIRLSPEeeeddpPLELEFTLPPGYPPEEPPLITLRSPKLSSAERLSLLKLELEEAAEE--NLGEPM 86


                .
gi 58331266 480 L 480
Cdd:cd11605  87 L 87
 
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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