NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1958748330|ref|XP_038954184|]
View 

GATOR2 complex protein WDR59 isoform X10 [Rattus norvegicus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 925-971 4.81e-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: 118.26  E-value: 4.81e-32
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1958748330 925 FQCAICHVAVRGSSNFCLTCGHGGHTSHMMEWFRTQEVCPTGCGCHC 971
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 7.15e-24

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


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 102.80  E-value: 7.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 100 TLQGHTRVISDLDWAVfEPDLLVTSSVDTYIYIWDIKDTRKPA---VALSAVAGASQVKWNKKnanYLATSHDGDVRIWD 176
Cdd:cd00200     4 TLKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGELLRtlkGHTGPVRDVAASADGTY---LASGSSDKTIRLWD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 177 KRKPSTAVEYlAAHLSKIHGLDWHPDSeHIFATSSQDNSVKFWDYRQPRKYLNILPCQVPVWKARYTPFSNGLVTVMvpq 256
Cdd:cd00200    80 LETGECVRTL-TGHTSYVSSVAFSPDG-RILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSS--- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 257 lrRENSLLLWNVfDLNTPVHTFVGHDDVVLEFQWrrqkegSKD-YQLVTWSRDQTLRMWrvDYQMQRLCAndILDGVDEF 335
Cdd:cd00200   155 --QDGTIKLWDL-RTGKCVATLTGHTGEVNSVAF------SPDgEKLLSSSSDGTIKLW--DLSTGKCLG--TLRGHENG 221


                  ....*...
gi 1958748330 336 IESISLLP 343
Cdd:cd00200   222 VNSVAFSP 229
RWD smart00591
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily ...
 394-494 1.83e-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: 1.83e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330  394 EFSLINVQIRNVNVEMDAADRSCTVSVHCSNHR---------VKMLVTFPAQYPnNAAPSFQFINPTTITSAVKAKLLKI 464
Cdd:smart00591   1 ELEALESIYPEDFEVIDEDARIPEITIKLSPSSdegedqyvsLTLQVKLPENYP-DEAPPISLLNSEGLSDEQLAELLKK 79

                           90       100       110
                   ....*....|....*....|....*....|
gi 1958748330  465 LKDTSLQkvKRNQSCLEPCLRQLVSCLESF 494
Cdd:smart00591  80 LEEIAEE--NLGEVMIFELVEKLQEFLSEF 107
WD40 super family cl43672
WD40 repeat [General function prediction only];
46-137 6.50e-05

WD40 repeat [General function prediction only];


The actual alignment was detected with superfamily member COG2319:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 46.44  E-value: 6.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330  46 APFEGHRkisrqskWDIGAVQWNPHDSFAhyFAASSNQRVDLykWKDGSGEVGTTLQGHTRVISDLDWAvfePD--LLVT 123
Cdd:COG2319   324 RTLTGHT-------GAVRSVAFSPDGKTL--ASGSDDGTVRL--WDLATGELLRTLTGHTGAVTSVAFS---PDgrTLAS 389

                          90
                  ....*....|....
gi 1958748330 124 SSVDTYIYIWDIKD 137
Cdd:COG2319   390 GSADGTVRLWDLAT 403
 
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 ...
 925-971 4.81e-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: 118.26  E-value: 4.81e-32
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1958748330 925 FQCAICHVAVRGSSNFCLTCGHGGHTSHMMEWFRTQEVCPTGCGCHC 971
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 7.15e-24

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 102.80  E-value: 7.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 100 TLQGHTRVISDLDWAVfEPDLLVTSSVDTYIYIWDIKDTRKPA---VALSAVAGASQVKWNKKnanYLATSHDGDVRIWD 176
Cdd:cd00200     4 TLKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGELLRtlkGHTGPVRDVAASADGTY---LASGSSDKTIRLWD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 177 KRKPSTAVEYlAAHLSKIHGLDWHPDSeHIFATSSQDNSVKFWDYRQPRKYLNILPCQVPVWKARYTPFSNGLVTVMvpq 256
Cdd:cd00200    80 LETGECVRTL-TGHTSYVSSVAFSPDG-RILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSS--- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 257 lrRENSLLLWNVfDLNTPVHTFVGHDDVVLEFQWrrqkegSKD-YQLVTWSRDQTLRMWrvDYQMQRLCAndILDGVDEF 335
Cdd:cd00200   155 --QDGTIKLWDL-RTGKCVATLTGHTGEVNSVAF------SPDgEKLLSSSSDGTIKLW--DLSTGKCLG--TLRGHENG 221


                  ....*...
gi 1958748330 336 IESISLLP 343
Cdd:cd00200   222 VNSVAFSP 229
WD40 COG2319
WD40 repeat [General function prediction only];
46-317 2.89e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 103.45  E-value: 2.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330  46 APFEGHRkisrqskWDIGAVQWNPhDSfaHYFA-ASSNQRVDLykWKDGSGEVGTTLQGHTRVISDLDWAvfePD--LLV 122
Cdd:COG2319   156 RTLTGHS-------GAVTSVAFSP-DG--KLLAsGSDDGTVRL--WDLATGKLLRTLTGHTGAVRSVAFS---PDgkLLA 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 123 TSSVDTYIYIWDIKDTRKPAVALSAVAGASQVKWNKkNANYLAT-SHDGDVRIWDkRKPSTAVEYLAAHLSKIHGLDWHP 201
Cdd:COG2319   221 SGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSP-DGRLLASgSADGTVRLWD-LATGELLRTLTGHSGGVNSVAFSP 298

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 202 DSEHIfATSSQDNSVKFWDYRQPRKYLNILPCQVPVWKARYTPFSNGLVTVmvpqlRRENSLLLWNVfDLNTPVHTFVGH 281
Cdd:COG2319   299 DGKLL-ASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASG-----SDDGTVRLWDL-ATGELLRTLTGH 371

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958748330 282 DDVVLEFQWrrqkegSKDYQ-LVTWSRDQTLRMWRVD 317
Cdd:COG2319   372 TGAVTSVAF------SPDGRtLASGSADGTVRLWDLA 402
zf-RING_16 pfam17120
RING/Ubox like zinc-binding domain;
927-975 1.58e-11

RING/Ubox like zinc-binding domain;


Pssm-ID: 375001  Cd Length: 57  Bit Score: 60.11  E-value: 1.58e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958748330 927 CAICHVAVRGSSNFCLTCGHGGHTSHMMEWFRTQE-VCPTGCGCHCLLES 975
Cdd:pfam17120   7 CNYCCLRVRGRVFLCGVCQHVLHASCAREWWENDDgECPSGCGCNCLEHH 56
RWD smart00591
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily ...
 394-494 1.83e-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: 1.83e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330  394 EFSLINVQIRNVNVEMDAADRSCTVSVHCSNHR---------VKMLVTFPAQYPnNAAPSFQFINPTTITSAVKAKLLKI 464
Cdd:smart00591   1 ELEALESIYPEDFEVIDEDARIPEITIKLSPSSdegedqyvsLTLQVKLPENYP-DEAPPISLLNSEGLSDEQLAELLKK 79

                           90       100       110
                   ....*....|....*....|....*....|
gi 1958748330  465 LKDTSLQkvKRNQSCLEPCLRQLVSCLESF 494
Cdd:smart00591  80 LEEIAEE--NLGEVMIFELVEKLQEFLSEF 107
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 117-314 2.57e-08

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 58.17  E-value: 2.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 117 EPDLLVTSSVDTYIYIWD----IKDTRK---PAVALSAVAGASQVKWNKKNANYLATSH-DGDVRIWDKRKPSTAVEyLA 188
Cdd:PLN00181  494 DGEFFATAGVNKKIKIFEcesiIKDGRDihyPVVELASRSKLSGICWNSYIKSQVASSNfEGVVQVWDVARSQLVTE-MK 572

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 189 AHLSKIHGLDWHPDSEHIFATSSQDNSVKFWDYRQP------RKYLNILPCQVPVWKARYTPFSNGlvtvmvpqlrrENS 262
Cdd:PLN00181  573 EHEKRVWSIDYSSADPTLLASGSDDGSVKLWSINQGvsigtiKTKANICCVQFPSESGRSLAFGSA-----------DHK 641

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958748330 263 LLLWNVFDLNTPVHTFVGHDDVVlefQWRRQKEGSkdyQLVTWSRDQTLRMW 314
Cdd:PLN00181  642 VYYYDLRNPKLPLCTMIGHSKTV---SYVRFVDSS---TLVSSSTDNTLKLW 687
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 187-220 3.46e-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: 41.91  E-value: 3.46e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958748330  187 LAAHLSKIHGLDWHPDSeHIFATSSQDNSVKFWD 220
Cdd:smart00320   8 LKGHTGPVTSVAFSPDG-KYLASGSDDGTIKLWD 40
WD40 COG2319
WD40 repeat [General function prediction only];
46-137 6.50e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 46.44  E-value: 6.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330  46 APFEGHRkisrqskWDIGAVQWNPHDSFAhyFAASSNQRVDLykWKDGSGEVGTTLQGHTRVISDLDWAvfePD--LLVT 123
Cdd:COG2319   324 RTLTGHT-------GAVRSVAFSPDGKTL--ASGSDDGTVRL--WDLATGELLRTLTGHTGAVTSVAFS---PDgrTLAS 389

                          90
                  ....*....|....
gi 1958748330 124 SSVDTYIYIWDIKD 137
Cdd:COG2319   390 GSADGTVRLWDLAT 403
RWD_GCN2 cd23823
RWD domain of eIF-2-alpha kinase GCN2 and related proteins; GCN2 (EC 2.7.11.1), also called ...
 420-497 1.79e-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: 1.79e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958748330 420 VHCSnhrVKMLVTFPAQYPNnAAPSFQFINPTTITSAVKAKLLKILKDTSLQKVKrnqsclEPCLRQLVSCLESFVNQ 497
Cdd:cd23823    48 NHVS---VDLHVKFPPTYPD-VPPEIELENVKGLSDEQLEELLKELEELAKELLG------EEMIFELAEAVQEFLEE 115
WD40 pfam00400
WD domain, G-beta repeat;
187-220 3.26e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.87  E-value: 3.26e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1958748330 187 LAAHLSKIHGLDWHPDSEHIfATSSQDNSVKFWD 220
Cdd:pfam00400   7 LEGHTGSVTSLAFSPDGKLL-ASGSDDGTVKVWD 39
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
 413-494 3.62e-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: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 413 DRSCTVSVHCSNHRVKMLVTFPAQYPnNAAPSFQFINPTTITSAVKAKLLKILKdtslQKVKRNQSclEPCLRQLVSCLE 492
Cdd:pfam05773  36 SLDSDESDSSHLPPLVLKFTLPEDYP-DEPPKISLSSPWNLSDEQVLSLLEELE----ELAEENLG--EVMIFELIEWLQ 108


                  ..
gi 1958748330 493 SF 494
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 ...
 925-971 4.81e-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: 118.26  E-value: 4.81e-32
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1958748330 925 FQCAICHVAVRGSSNFCLTCGHGGHTSHMMEWFRTQEVCPTGCGCHC 971
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 7.15e-24

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 102.80  E-value: 7.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 100 TLQGHTRVISDLDWAVfEPDLLVTSSVDTYIYIWDIKDTRKPA---VALSAVAGASQVKWNKKnanYLATSHDGDVRIWD 176
Cdd:cd00200     4 TLKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGELLRtlkGHTGPVRDVAASADGTY---LASGSSDKTIRLWD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 177 KRKPSTAVEYlAAHLSKIHGLDWHPDSeHIFATSSQDNSVKFWDYRQPRKYLNILPCQVPVWKARYTPFSNGLVTVMvpq 256
Cdd:cd00200    80 LETGECVRTL-TGHTSYVSSVAFSPDG-RILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSS--- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 257 lrRENSLLLWNVfDLNTPVHTFVGHDDVVLEFQWrrqkegSKD-YQLVTWSRDQTLRMWrvDYQMQRLCAndILDGVDEF 335
Cdd:cd00200   155 --QDGTIKLWDL-RTGKCVATLTGHTGEVNSVAF------SPDgEKLLSSSSDGTIKLW--DLSTGKCLG--TLRGHENG 221


                  ....*...
gi 1958748330 336 IESISLLP 343
Cdd:cd00200   222 VNSVAFSP 229
WD40 COG2319
WD40 repeat [General function prediction only];
46-317 2.89e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 103.45  E-value: 2.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330  46 APFEGHRkisrqskWDIGAVQWNPhDSfaHYFA-ASSNQRVDLykWKDGSGEVGTTLQGHTRVISDLDWAvfePD--LLV 122
Cdd:COG2319   156 RTLTGHS-------GAVTSVAFSP-DG--KLLAsGSDDGTVRL--WDLATGKLLRTLTGHTGAVRSVAFS---PDgkLLA 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 123 TSSVDTYIYIWDIKDTRKPAVALSAVAGASQVKWNKkNANYLAT-SHDGDVRIWDkRKPSTAVEYLAAHLSKIHGLDWHP 201
Cdd:COG2319   221 SGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSP-DGRLLASgSADGTVRLWD-LATGELLRTLTGHSGGVNSVAFSP 298

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 202 DSEHIfATSSQDNSVKFWDYRQPRKYLNILPCQVPVWKARYTPFSNGLVTVmvpqlRRENSLLLWNVfDLNTPVHTFVGH 281
Cdd:COG2319   299 DGKLL-ASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASG-----SDDGTVRLWDL-ATGELLRTLTGH 371

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958748330 282 DDVVLEFQWrrqkegSKDYQ-LVTWSRDQTLRMWRVD 317
Cdd:COG2319   372 TGAVTSVAF------SPDGRtLASGSADGTVRLWDLA 402
mRING-H2-C3H3C2_Mio-like cd16488
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein mio and ...
 926-969 3.46e-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: 87.38  E-value: 3.46e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1958748330 926 QCAICHVAVRGSSNFCLTCGHGGHTSHMMEWFRTQEVCPTGCGC 969
Cdd:cd16488     1 SCAICHLPVKGLSSFCLNCGHGGHAECIREWFEDHTECPTGCGC 44
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 48-251 2.64e-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: 92.40  E-value: 2.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330  48 FEGHRKisrqskwDIGAVQWNPHDsfaHYFAASSNQ---RVdlykWKDGSGEVGTTLQGHTRVISDLDWAVFePDLLVTS 124
Cdd:cd00200    89 LTGHTS-------YVSSVAFSPDG---RILSSSSRDktiKV----WDVETGKCLTTLRGHTDWVNSVAFSPD-GTFVASS 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 125 SVDTYIYIWDIKDTRKPAVALSAVAGASQVKWNKKNANYLATSHDGDVRIWDKRKPSTaVEYLAAHLSKIHGLDWHPDSe 204
Cdd:cd00200   154 SQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKC-LGTLRGHENGVNSVAFSPDG- 231

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958748330 205 HIFATSSQDNSVKFWDYRqPRKYLNILPC-QVPVWKARYTPFSNGLVT 251
Cdd:cd00200   232 YLLASGSEDGTIRVWDLR-TGECVQTLSGhTNSVTSLAWSPDGKRLAS 278
WD40 COG2319
WD40 repeat [General function prediction only];
78-317 1.54e-19

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 92.28  E-value: 1.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330  78 AASSNQRVDLYKWKDGSGEVGTTLQGHTRVISDLDWAVfEPDLLVTSSVDTYIYIWDIKDTRKPAVALSAVAGASQVKWN 157
Cdd:COG2319    51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSP-DGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFS 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 158 KkNANYLAT-SHDGDVRIWDKRKPsTAVEYLAAHLSKIHGLDWHPDSEHIfATSSQDNSVKFWDYRQPRKYLNILPCQVP 236
Cdd:COG2319   130 P-DGKTLASgSADGTVRLWDLATG-KLLRTLTGHSGAVTSVAFSPDGKLL-ASGSDDGTVRLWDLATGKLLRTLTGHTGA 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 237 VWKARYTPFSNGLVTVmvpqlRRENSLLLWNVfDLNTPVHTFVGHDDVVLEFQWrrqkegSKDYQ-LVTWSRDQTLRMWR 315
Cdd:COG2319   207 VRSVAFSPDGKLLASG-----SADGTVRLWDL-ATGKLLRTLTGHSGSVRSVAF------SPDGRlLASGSADGTVRLWD 274


                  ..
gi 1958748330 316 VD 317
Cdd:COG2319   275 LA 276
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 48-344 3.24e-19

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 89.32  E-value: 3.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330  48 FEGHRKisrqskwDIGAVQWNPHDSFahYFAASSNQRVDLYKWKDGsgEVGTTLQGHTRVISDLDWAVFEpDLLVTSSVD 127
Cdd:cd00200     5 LKGHTG-------GVTCVAFSPDGKL--LATGSGDGTIKVWDLETG--ELLRTLKGHTGPVRDVAASADG-TYLASGSSD 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 128 TYIYIWDIKdTRKPAVALSAVAGA-SQVKWNKKNaNYLATSH-DGDVRIWD--KRKPSTAveyLAAHLSKIHGLDWHPDS 203
Cdd:cd00200    73 KTIRLWDLE-TGECVRTLTGHTSYvSSVAFSPDG-RILSSSSrDKTIKVWDveTGKCLTT---LRGHTDWVNSVAFSPDG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 204 EHIfATSSQDNSVKFWDYRQPRKYLNILPCQVPVWKARYTPFSNGLVTVmvpqlRRENSLLLWnvfDLNT--PVHTFVGH 281
Cdd:cd00200   148 TFV-ASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSS-----SSDGTIKLW---DLSTgkCLGTLRGH 218

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958748330 282 DDVVLEFQWrrqkeGSKDYQLVTWSRDQTLRMWrvDYQMQRLCAndILDGVDEFIESISLLPE 344
Cdd:cd00200   219 ENGVNSVAF-----SPDGYLLASGSEDGTIRVW--DLRTGECVQ--TLSGHTNSVTSLAWSPD 272
mRING-H2-C3H3C2_WDR24 cd16693
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 24 ...
 927-971 3.49e-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: 3.49e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1958748330 927 CAICHVAVRGSSNFCLTCGHGGHTSHMMEWFRTQEVCPTGCGCHC 971
Cdd:cd16693     2 CSVCHLPVKGLYVWCQGCGHGGHLEHMKEWFSTNSHCPAGCGHLC 46
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 48-220 7.09e-15

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 76.22  E-value: 7.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330  48 FEGHRKisrqskwDIGAVQWNPHDSFAhyFAASSNQRVDLykWKDGSGEVGTTLQGHTRVISDLDWAvfePDL--LVTSS 125
Cdd:cd00200   131 LRGHTD-------WVNSVAFSPDGTFV--ASSSQDGTIKL--WDLRTGKCVATLTGHTGEVNSVAFS---PDGekLLSSS 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 126 VDTYIYIWDIKDTRKPAVALSAVAGASQVKWNKKNANYLATSHDGDVRIWDKRKPSTaVEYLAAHLSKIHGLDWHPDSeH 205
Cdd:cd00200   197 SDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGEC-VQTLSGHTNSVTSLAWSPDG-K 274

                         170
                  ....*....|....*
gi 1958748330 206 IFATSSQDNSVKFWD 220
Cdd:cd00200   275 RLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
78-317 1.78e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 76.49  E-value: 1.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330  78 AASSNQRVDLYKWKDGSGEVGTTLQGHTRVISDLDWAVFEPDLLVTSSVDTYIyIWDIKDTRKPAVALSAVAGASQVKWN 157
Cdd:COG2319     9 LAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLL-LLDAAAGALLATLLGHTAAVLSVAFS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 158 KKNANYLATSHDGDVRIWDkRKPSTAVEYLAAHLSKIHGLDWHPDSEHIfATSSQDNSVKFWDyRQPRKYLNILPC-QVP 236
Cdd:COG2319    88 PDGRLLASASADGTVRLWD-LATGLLLRTLTGHTGAVRSVAFSPDGKTL-ASGSADGTVRLWD-LATGKLLRTLTGhSGA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 237 VWKARYTPfsNG--LVTVmvpqlRRENSLLLWNVFDlNTPVHTFVGHDDVVLEFQWRRQkeGSkdyQLVTWSRDQTLRMW 314
Cdd:COG2319   165 VTSVAFSP--DGklLASG-----SDDGTVRLWDLAT-GKLLRTLTGHTGAVRSVAFSPD--GK---LLASGSADGTVRLW 231


                  ...
gi 1958748330 315 RVD 317
Cdd:COG2319   232 DLA 234
mRING-H2-C3H3C2_Mio cd16691
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein mio and ...
 940-971 4.57e-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: 65.16  E-value: 4.57e-13
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958748330 940 FCLTCGHGGHTSHMMEWFRTQEVCP-TGCGCHC 971
Cdd:cd16691    43 WCQTCRHGGHAGHLQEWFRDHSECPvSGCDCKC 75
zf-RING_16 pfam17120
RING/Ubox like zinc-binding domain;
927-975 1.58e-11

RING/Ubox like zinc-binding domain;


Pssm-ID: 375001  Cd Length: 57  Bit Score: 60.11  E-value: 1.58e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958748330 927 CAICHVAVRGSSNFCLTCGHGGHTSHMMEWFRTQE-VCPTGCGCHCLLES 975
Cdd:pfam17120   7 CNYCCLRVRGRVFLCGVCQHVLHASCAREWWENDDgECPSGCGCNCLEHH 56
RWD smart00591
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily ...
 394-494 1.83e-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: 1.83e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330  394 EFSLINVQIRNVNVEMDAADRSCTVSVHCSNHR---------VKMLVTFPAQYPnNAAPSFQFINPTTITSAVKAKLLKI 464
Cdd:smart00591   1 ELEALESIYPEDFEVIDEDARIPEITIKLSPSSdegedqyvsLTLQVKLPENYP-DEAPPISLLNSEGLSDEQLAELLKK 79

                           90       100       110
                   ....*....|....*....|....*....|
gi 1958748330  465 LKDTSLQkvKRNQSCLEPCLRQLVSCLESF 494
Cdd:smart00591  80 LEEIAEE--NLGEVMIFELVEKLQEFLSEF 107
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 117-314 2.57e-08

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 58.17  E-value: 2.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 117 EPDLLVTSSVDTYIYIWD----IKDTRK---PAVALSAVAGASQVKWNKKNANYLATSH-DGDVRIWDKRKPSTAVEyLA 188
Cdd:PLN00181  494 DGEFFATAGVNKKIKIFEcesiIKDGRDihyPVVELASRSKLSGICWNSYIKSQVASSNfEGVVQVWDVARSQLVTE-MK 572

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 189 AHLSKIHGLDWHPDSEHIFATSSQDNSVKFWDYRQP------RKYLNILPCQVPVWKARYTPFSNGlvtvmvpqlrrENS 262
Cdd:PLN00181  573 EHEKRVWSIDYSSADPTLLASGSDDGSVKLWSINQGvsigtiKTKANICCVQFPSESGRSLAFGSA-----------DHK 641

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958748330 263 LLLWNVFDLNTPVHTFVGHDDVVlefQWRRQKEGSkdyQLVTWSRDQTLRMW 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 ...
 939-971 4.14e-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: 4.14e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1958748330 939 NFCLTCGHGGHTSHMMEWFRTQEVCPTG-CGCHC 971
Cdd:pfam17034  89 SFCLSCGHGSHADHATEWFSTHSICPVAdCNCLC 122
PTZ00420 PTZ00420
coronin; Provisional
 101-222 2.40e-05

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 48.02  E-value: 2.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 101 LQGHTRVISDLDWAVFEPDLLVTSSVDTYIYIWDIKDTRKpAVALSAVAGASQVKWNKKNANYLATSHDGDVRIWDKRKP 180
Cdd:PTZ00420  121 LKGHKKKISIIDWNPMNYYIMCSSGFDSFVNIWDIENEKR-AFQINMPKKLSSLKWNIKGNLLSGTCVGKHMHIIDPRKQ 199

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958748330 181 STAVEYLAAHLSK------IHGLDwhPDSEHIFATSSQDNS---VKFWDYR 222
Cdd:PTZ00420  200 EIASSFHIHDGGKntkniwIDGLG--GDDNYILSTGFSKNNmreMKLWDLK 248
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 187-220 3.46e-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: 41.91  E-value: 3.46e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958748330  187 LAAHLSKIHGLDWHPDSeHIFATSSQDNSVKFWD 220
Cdd:smart00320   8 LKGHTGPVTSVAFSPDG-KYLASGSDDGTIKLWD 40
WD40 COG2319
WD40 repeat [General function prediction only];
46-137 6.50e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 46.44  E-value: 6.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330  46 APFEGHRkisrqskWDIGAVQWNPHDSFAhyFAASSNQRVDLykWKDGSGEVGTTLQGHTRVISDLDWAvfePD--LLVT 123
Cdd:COG2319   324 RTLTGHT-------GAVRSVAFSPDGKTL--ASGSDDGTVRL--WDLATGELLRTLTGHTGAVTSVAFS---PDgrTLAS 389

                          90
                  ....*....|....
gi 1958748330 124 SSVDTYIYIWDIKD 137
Cdd:COG2319   390 GSADGTVRLWDLAT 403
RING-H2 cd16448
H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type ...
 927-965 9.12e-05

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: 40.85  E-value: 9.12e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958748330 927 CAICHVAVRGSSNF-CLTCGHGGHTSHMMEWFRTQE-VCPT 965
Cdd:cd16448     1 CVICLEEFEEGDVVrLLPCGHVFHLACILRWLESGNnTCPL 41
PTZ00421 PTZ00421
coronin; Provisional
 108-277 1.14e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 46.04  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 108 ISDLDWAVFEPDLLVTSSVDTYIYIWDI------KDTRKPAVALSavaGASQ----VKWNKKNANYLATSH-DGDVRIWD 176
Cdd:PTZ00421   78 IIDVAFNPFDPQKLFTASEDGTIMGWGIpeegltQNISDPIVHLQ---GHTKkvgiVSFHPSAMNVLASAGaDMVVNVWD 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 177 KRKpSTAVEYLAAHLSKIHGLDWHPDSEhIFATSSQDNSVKFWDYRQPRKYLNI-----LPCQVPVWKARytpfSNGLVT 251
Cdd:PTZ00421  155 VER-GKAVEVIKCHSDQITSLEWNLDGS-LLCTTSKDKKLNIIDPRDGTIVSSVeahasAKSQRCLWAKR----KDLIIT 228

                         170       180
                  ....*....|....*....|....*.
gi 1958748330 252 VMVPQLrRENSLLLWNVFDLNTPVHT 277
Cdd:PTZ00421  229 LGCSKS-QQRQIMLWDTRKMASPYST 253
RWD_GCN2 cd23823
RWD domain of eIF-2-alpha kinase GCN2 and related proteins; GCN2 (EC 2.7.11.1), also called ...
 420-497 1.79e-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: 1.79e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958748330 420 VHCSnhrVKMLVTFPAQYPNnAAPSFQFINPTTITSAVKAKLLKILKDTSLQKVKrnqsclEPCLRQLVSCLESFVNQ 497
Cdd:cd23823    48 NHVS---VDLHVKFPPTYPD-VPPEIELENVKGLSDEQLEELLKELEELAKELLG------EEMIFELAEAVQEFLEE 115
WD40 pfam00400
WD domain, G-beta repeat;
187-220 3.26e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.87  E-value: 3.26e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1958748330 187 LAAHLSKIHGLDWHPDSEHIfATSSQDNSVKFWD 220
Cdd:pfam00400   7 LEGHTGSVTSLAFSPDGKLL-ASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 58-232 5.80e-04

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 43.92  E-value: 5.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330  58 SKWDIGAVQWNphdSFAHYFAASSNQRVDLYKWKDGSGEVGTTLQGHTRVISDLDWAVFEPDLLVTSSVDTYIYIWDIKD 137
Cdd:PLN00181  531 SRSKLSGICWN---SYIKSQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPTLLASGSDDGSVKLWSINQ 607

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 138 trkpAVALSAV---AGASQVKWNKKNANYLA-TSHDGDVRIWDKRKPSTAVEYLAAHLSKIHGLDWHPDSehIFATSSQD 213
Cdd:PLN00181  608 ----GVSIGTIktkANICCVQFPSESGRSLAfGSADHKVYYYDLRNPKLPLCTMIGHSKTVSYVRFVDSS--TLVSSSTD 681

                         170
                  ....*....|....*....
gi 1958748330 214 NSVKFWDYRQPRKYLNILP 232
Cdd:PLN00181  682 NTLKLWDLSMSISGINETP 700
RING-H2_TTC3 cd16481
RING finger, H2 subclass, found in Tetratricopeptide repeat protein 3 (TTC3) and similar ...
 926-970 1.37e-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: 37.33  E-value: 1.37e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1958748330 926 QCAICHVAVRGSSNFCLTCGHGGHTSHMMEWFRTQEVCPTgcgCH 970
Cdd:cd16481     1 PCIICHDDLKPDQLAKLECGHIFHKECIKQWLKEQSTCPT---CR 42
PTZ00420 PTZ00420
coronin; Provisional
 167-230 1.62e-03

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 42.24  E-value: 1.62e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958748330 167 SHDGDVRIWDKRKPSTAVE-------YLAAHLSKIHGLDWHPDSEHIFATSSQDNSVKFWDYRQPRKYLNI 230
Cdd:PTZ00420   94 SEDLTIRVWEIPHNDESVKeikdpqcILKGHKKKISIIDWNPMNYYIMCSSGFDSFVNIWDIENEKRAFQI 164
WD40 pfam00400
WD domain, G-beta repeat;
95-134 2.29e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.55  E-value: 2.29e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1958748330  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 3.62e-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: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748330 413 DRSCTVSVHCSNHRVKMLVTFPAQYPnNAAPSFQFINPTTITSAVKAKLLKILKdtslQKVKRNQSclEPCLRQLVSCLE 492
Cdd:pfam05773  36 SLDSDESDSSHLPPLVLKFTLPEDYP-DEPPKISLSSPWNLSDEQVLSLLEELE----ELAEENLG--EVMIFELIEWLQ 108


                  ..
gi 1958748330 493 SF 494
Cdd:pfam05773 109 EN 110
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 94-134 5.60e-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: 35.37  E-value: 5.60e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958748330   94 SGEVGTTLQGHTRVISDLDWAvfePD--LLVTSSVDTYIYIWD 134
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFS---PDgkYLASGSDDGTIKLWD 40
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH