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Conserved domains on  [gi|1624731610|ref|NP_001357007|]
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GATOR2 complex protein MIOS isoform 2 [Homo sapiens]

Protein Classification

GATOR complex protein MIOS( domain architecture ID 11455578)

GATOR complex protein MIOS acts as a component of the GATOR subcomplex GATOR2, and functions within the amino acid-sensing branch of the TORC1 signaling pathway

CATH:  3.30.40.10|2.130.10.10
Gene Ontology:  GO:0008270|GO:0061700|GO:0032006|GO:0005515
PubMed:  10322433|8804826|8317827|10653689|30069656|29026209
SCOP:  3000160|4002744

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
mRING-H2-C3H3C2_Mio cd16691
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein mio and ...
 678-754 2.06e-38

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: 136.81  E-value: 2.06e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1624731610 678 LPRCALCLINMGTPVSSCPGGTKSDekVDLSKDKKLAQFNNWFTWCHNCRHGGHAGHMLSWFRDHAECPVSACTCKC 754
Cdd:cd16691     1 LPRCSLCLIPMGTPSSSLPGATASD--VDLSSDKKLAPFSSWFTWCQTCRHGGHAGHLQEWFRDHSECPVSGCDCKC 75
WD40 COG2319
WD40 repeat [General function prediction only];
84-327 8.69e-09

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 58.38  E-value: 8.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624731610  84 NGRVVLTSlGQDHNSKFKDLIGKEFV---PKHARQCNTLAWNPlDSNWLAAGLDkhraDFSVLIWDicskytpdivpmek 160
Cdd:COG2319   131 DGKTLASG-SADGTVRLWDLATGKLLrtlTGHSGAVTSVAFSP-DGKLLASGSD----DGTVRLWD-------------- 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624731610 161 vkLSAGETETTLLvtkplyelGQNDACLSLCWLPRDQKLLLAGMHRNLAIFDLRNTSQKMFVN--TKAVQGVTVDPyfhD 238
Cdd:COG2319   191 --LATGKLLRTLT--------GHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTghSGSVRSVAFSP---D 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624731610 239 --RVAS-FYEGQVAIWDLRKfEKPVLTLTEQPKPLTKVAWCPTRTgLLATLTRDsNIIRLYDMQhTPTPIGDETEPTIIE 315
Cdd:COG2319   258 grLLASgSADGTVRLWDLAT-GELLRTLTGHSGGVNSVAFSPDGK-LLASGSDD-GTVRLWDLA-TGKLLRTLTGHTGAV 333

                         250
                  ....*....|....
gi 1624731610 316 RSVQ--PCDNYIAS 327
Cdd:COG2319   334 RSVAfsPDGKTLAS 347
 
Name Accession Description Interval E-value
mRING-H2-C3H3C2_Mio cd16691
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein mio and ...
 678-754 2.06e-38

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: 136.81  E-value: 2.06e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1624731610 678 LPRCALCLINMGTPVSSCPGGTKSDekVDLSKDKKLAQFNNWFTWCHNCRHGGHAGHMLSWFRDHAECPVSACTCKC 754
Cdd:cd16691     1 LPRCSLCLIPMGTPSSSLPGATASD--VDLSSDKKLAPFSSWFTWCQTCRHGGHAGHLQEWFRDHSECPVSGCDCKC 75
zinc_ribbon_16 pfam17034
Zinc-ribbon like family; This family is found at the C-terminus of WD40 repeat structures in ...
 633-754 1.15e-23

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: 97.04  E-value: 1.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624731610 633 CNFCGKSIsYSCSAVPH---QGRGFSQYGVSGSPTKSKVTSCPGCRKPLPRCALCLINMGTpvSSCPGGTKSDEKVDLSK 709
Cdd:pfam17034   1 CNFCNKSI-TPFSSKHHtniQQSNVPSTGGRKFVNISKSTLCPACSQPLPRCAVCGLSLGT--SNLTNKDSRRKSVVKDP 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1624731610 710 DKKLAQFNNWFTWCHNCRHGGHAGHMLSWFRDHAECPVSACTCKC 754
Cdd:pfam17034  78 QDFEKLFEKWFSFCLSCGHGSHADHATEWFSTHSICPVADCNCLC 122
WD40 COG2319
WD40 repeat [General function prediction only];
84-327 8.69e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 58.38  E-value: 8.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624731610  84 NGRVVLTSlGQDHNSKFKDLIGKEFV---PKHARQCNTLAWNPlDSNWLAAGLDkhraDFSVLIWDicskytpdivpmek 160
Cdd:COG2319   131 DGKTLASG-SADGTVRLWDLATGKLLrtlTGHSGAVTSVAFSP-DGKLLASGSD----DGTVRLWD-------------- 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624731610 161 vkLSAGETETTLLvtkplyelGQNDACLSLCWLPRDQKLLLAGMHRNLAIFDLRNTSQKMFVN--TKAVQGVTVDPyfhD 238
Cdd:COG2319   191 --LATGKLLRTLT--------GHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTghSGSVRSVAFSP---D 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624731610 239 --RVAS-FYEGQVAIWDLRKfEKPVLTLTEQPKPLTKVAWCPTRTgLLATLTRDsNIIRLYDMQhTPTPIGDETEPTIIE 315
Cdd:COG2319   258 grLLASgSADGTVRLWDLAT-GELLRTLTGHSGGVNSVAFSPDGK-LLASGSDD-GTVRLWDLA-TGKLLRTLTGHTGAV 333

                         250
                  ....*....|....
gi 1624731610 316 RSVQ--PCDNYIAS 327
Cdd:COG2319   334 RSVAfsPDGKTLAS 347
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 112-299 2.02e-07

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 53.49  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624731610 112 HARQCNTLAWNPlDSNWLAAGLdkhrADFSVLIWDICS-----KYTPDIVPMEKVKLSAGeteTTLLVT----------- 175
Cdd:cd00200     8 HTGGVTCVAFSP-DGKLLATGS----GDGTIKVWDLETgellrTLKGHTGPVRDVAASAD---GTYLASgssdktirlwd 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624731610 176 ----KPLYEL-GQNDACLSLCWLPRDQKLLLAGMHRNLAIFDLRNTSQKMFVN--TKAVQGVTVDPyFHDRVASF-YEGQ 247
Cdd:cd00200    80 letgECVRTLtGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRghTDWVNSVAFSP-DGTFVASSsQDGT 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1624731610 248 VAIWDLRKFeKPVLTLTEQPKPLTKVAWCPTRTGLLATlTRDSNiIRLYDMQ 299
Cdd:cd00200   159 IKLWDLRTG-KCVATLTGHTGEVNSVAFSPDGEKLLSS-SSDGT-IKLWDLS 207
 
Name Accession Description Interval E-value
mRING-H2-C3H3C2_Mio cd16691
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein mio and ...
 678-754 2.06e-38

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: 136.81  E-value: 2.06e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1624731610 678 LPRCALCLINMGTPVSSCPGGTKSDekVDLSKDKKLAQFNNWFTWCHNCRHGGHAGHMLSWFRDHAECPVSACTCKC 754
Cdd:cd16691     1 LPRCSLCLIPMGTPSSSLPGATASD--VDLSSDKKLAPFSSWFTWCQTCRHGGHAGHLQEWFRDHSECPVSGCDCKC 75
zinc_ribbon_16 pfam17034
Zinc-ribbon like family; This family is found at the C-terminus of WD40 repeat structures in ...
 633-754 1.15e-23

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: 97.04  E-value: 1.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624731610 633 CNFCGKSIsYSCSAVPH---QGRGFSQYGVSGSPTKSKVTSCPGCRKPLPRCALCLINMGTpvSSCPGGTKSDEKVDLSK 709
Cdd:pfam17034   1 CNFCNKSI-TPFSSKHHtniQQSNVPSTGGRKFVNISKSTLCPACSQPLPRCAVCGLSLGT--SNLTNKDSRRKSVVKDP 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1624731610 710 DKKLAQFNNWFTWCHNCRHGGHAGHMLSWFRDHAECPVSACTCKC 754
Cdd:pfam17034  78 QDFEKLFEKWFSFCLSCGHGSHADHATEWFSTHSICPVADCNCLC 122
mRING-H2-C3H3C2_Mio-like cd16488
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein mio and ...
 720-752 1.80e-11

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: 59.26  E-value: 1.80e-11
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1624731610 720 FTWCHNCRHGGHAGHMLSWFRDHAECPVSaCTC 752
Cdd:cd16488    13 SSFCLNCGHGGHAECIREWFEDHTECPTG-CGC 44
mRING-H2-C3H3C2_WDR59 cd16692
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 59 ...
 721-754 1.55e-09

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: 53.93  E-value: 1.55e-09
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1624731610 721 TWCHNCRHGGHAGHMLSWFRDHAECPvSACTCKC 754
Cdd:cd16692    15 NFCLACGHGGHTSHMMEWFRTQDVCP-TGCGCHC 47
WD40 COG2319
WD40 repeat [General function prediction only];
84-327 8.69e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 58.38  E-value: 8.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624731610  84 NGRVVLTSlGQDHNSKFKDLIGKEFV---PKHARQCNTLAWNPlDSNWLAAGLDkhraDFSVLIWDicskytpdivpmek 160
Cdd:COG2319   131 DGKTLASG-SADGTVRLWDLATGKLLrtlTGHSGAVTSVAFSP-DGKLLASGSD----DGTVRLWD-------------- 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624731610 161 vkLSAGETETTLLvtkplyelGQNDACLSLCWLPRDQKLLLAGMHRNLAIFDLRNTSQKMFVN--TKAVQGVTVDPyfhD 238
Cdd:COG2319   191 --LATGKLLRTLT--------GHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTghSGSVRSVAFSP---D 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624731610 239 --RVAS-FYEGQVAIWDLRKfEKPVLTLTEQPKPLTKVAWCPTRTgLLATLTRDsNIIRLYDMQhTPTPIGDETEPTIIE 315
Cdd:COG2319   258 grLLASgSADGTVRLWDLAT-GELLRTLTGHSGGVNSVAFSPDGK-LLASGSDD-GTVRLWDLA-TGKLLRTLTGHTGAV 333

                         250
                  ....*....|....
gi 1624731610 316 RSVQ--PCDNYIAS 327
Cdd:COG2319   334 RSVAfsPDGKTLAS 347
mRING-H2-C3H3C2_WDR24 cd16693
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 24 ...
 720-754 1.40e-08

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: 51.13  E-value: 1.40e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1624731610 720 FTWCHNCRHGGHAGHMLSWFRDHAECPvSACTCKC 754
Cdd:cd16693    13 YVWCQGCGHGGHLEHMKEWFSTNSHCP-AGCGHLC 46
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 112-299 2.02e-07

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 53.49  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624731610 112 HARQCNTLAWNPlDSNWLAAGLdkhrADFSVLIWDICS-----KYTPDIVPMEKVKLSAGeteTTLLVT----------- 175
Cdd:cd00200     8 HTGGVTCVAFSP-DGKLLATGS----GDGTIKVWDLETgellrTLKGHTGPVRDVAASAD---GTYLASgssdktirlwd 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624731610 176 ----KPLYEL-GQNDACLSLCWLPRDQKLLLAGMHRNLAIFDLRNTSQKMFVN--TKAVQGVTVDPyFHDRVASF-YEGQ 247
Cdd:cd00200    80 letgECVRTLtGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRghTDWVNSVAFSP-DGTFVASSsQDGT 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1624731610 248 VAIWDLRKFeKPVLTLTEQPKPLTKVAWCPTRTGLLATlTRDSNiIRLYDMQ 299
Cdd:cd00200   159 IKLWDLRTG-KCVATLTGHTGEVNSVAFSPDGEKLLSS-SSDGT-IKLWDLS 207
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 84-297 6.94e-07

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 51.57  E-value: 6.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624731610  84 NGRVVLTSlGQDHNSKFKDLIGKEFV---PKHARQCNTLAWNPlDSNWLAAGLDkhraDFSVLIWDicskytpdivpmek 160
Cdd:cd00200   104 DGRILSSS-SRDKTIKVWDVETGKCLttlRGHTDWVNSVAFSP-DGTFVASSSQ----DGTIKLWD-------------- 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624731610 161 vkLSAGETETTLLvtkplyelGQNDACLSLCWLPRDQKLLLAGMHRNLAIFDLRNTSQK--MFVNTKAVQGVTVDPYFHD 238
Cdd:cd00200   164 --LRTGKCVATLT--------GHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLgtLRGHENGVNSVAFSPDGYL 233

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1624731610 239 RVASFYEGQVAIWDLRKFEkPVLTLTEQPKPLTKVAWCPTrTGLLATLTRDsNIIRLYD 297
Cdd:cd00200   234 LASGSEDGTIRVWDLRTGE-CVQTLSGHTNSVTSLAWSPD-GKRLASGSAD-GTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
84-299 3.18e-06

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 50.29  E-value: 3.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624731610  84 NGRVVLTSlGQDHNSKFKDLIGKEFV---PKHARQCNTLAWNPlDSNWLAAGldkhRADFSVLIWDicskytpdivpmek 160
Cdd:COG2319   215 DGKLLASG-SADGTVRLWDLATGKLLrtlTGHSGSVRSVAFSP-DGRLLASG----SADGTVRLWD-------------- 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624731610 161 vkLSAGETETTLLvtkplyelGQNDACLSLCWLPRDQKLLLAGMHRNLAIFDLrNTSQKMFV---NTKAVQGVTVDPyFH 237
Cdd:COG2319   275 --LATGELLRTLT--------GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL-ATGKLLRTltgHTGAVRSVAFSP-DG 342

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1624731610 238 DRVAS-FYEGQVAIWDLRKfEKPVLTLTEQPKPLTKVAWCPTRTgLLATLTRDsNIIRLYDMQ 299
Cdd:COG2319   343 KTLASgSDDGTVRLWDLAT-GELLRTLTGHTGAVTSVAFSPDGR-TLASGSAD-GTVRLWDLA 402
zf-RING_16 pfam17120
RING/Ubox like zinc-binding domain;
720-755 1.25e-03

RING/Ubox like zinc-binding domain;


Pssm-ID: 375001  Cd Length: 57  Bit Score: 37.77  E-value: 1.25e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1624731610 720 FTWCHNCRHGGHAGHMLSWF-RDHAECPvSACTCKCM 755
Cdd:pfam17120  18 VFLCGVCQHVLHASCAREWWeNDDGECP-SGCGCNCL 53
 
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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