|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
647-994 |
6.40e-29 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 121.17 E-value: 6.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 647 QPPGGPLRATLTGCHKGITAIAWSLEEKLLVVGTQDGAMVVWDVEEQQVVHVLMGHTAEVKCVRVFAQGTLAISASKDHT 726
Cdd:COG2319 106 DLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGT 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 727 LRLWSLLSGQEkVTILDGgsqnptepqswdlHVDERNNVVYSTSGARInmwnletsklvfcITGdvsdpwvcvallaaqg 806
Cdd:COG2319 186 VRLWDLATGKL-LRTLTG-------------HTGAVRSVAFSPDGKLL-------------ASG---------------- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 807 lllalSKGGQVSLWSSAMGKLQekHQLSSIKEETPTCAVSIQSRaRLVAGFSSGSIALVSAGEDRLLEKLP---EAVGFL 883
Cdd:COG2319 223 -----SADGTVRLWDLATGKLL--RTLTGHSGSVRSVAFSPDGR-LLASGSADGTVRLWDLATGELLRTLTghsGGVNSV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 884 VVSEDDSLLV-AGFGRFVRIF-LADSQGFHRFMAsdleHEDMVETAVLGPENNLIITGSRDALIQVWSLsEQGTLLNVLE 961
Cdd:COG2319 295 AFSPDGKLLAsGSDDGTVRLWdLATGKLLRTLTG----HTGAVRSVAFSPDGKTLASGSDDGTVRLWDL-ATGELLRTLT 369
|
330 340 350
....*....|....*....|....*....|....*
gi 1720427671 962 GVGAPVSLLV--RGGTLVVSASRkSSSFKVWDLKS 994
Cdd:COG2319 370 GHTGAVTSVAfsPDGRTLASGSA-DGTVRLWDLAT 403
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
653-949 |
1.80e-27 |
|
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: 113.97 E-value: 1.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 653 LRATLTGCHKGITAIAWSLEEKLLVVGTQDGAMVVWDVEEQQVVHVLMGHTAEVKCVRVFAQGTLAISASKDHTLRLWSl 732
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 733 LSGQEKVTILDGGSQNPTepqSWDLHVDERnnVVYSTSGAR-INMWNLETSKLVFCITGdVSDPWVCVALLAAQGLLLAL 811
Cdd:cd00200 80 LETGECVRTLTGHTSYVS---SVAFSPDGR--ILSSSSRDKtIKVWDVETGKCLTTLRG-HTDWVNSVAFSPDGTFVASS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 812 SKGGQVSLWSSAMGKLqeKHQLSSIKEETPTCAVSiQSRARLVAGFSSGSIALVSAGEDRLLEKLP---EAVGFLVVSED 888
Cdd:cd00200 154 SQDGTIKLWDLRTGKC--VATLTGHTGEVNSVAFS-PDGEKLLSSSSDGTIKLWDLSTGKCLGTLRgheNGVNSVAFSPD 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720427671 889 DSLLVAG-FGRFVRIFlaDSQGFhRFMASDLEHEDMVETAVLGPENNLIITGSRDALIQVWS 949
Cdd:cd00200 231 GYLLASGsEDGTIRVW--DLRTG-ECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
844-1211 |
2.00e-26 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 113.47 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 844 AVSIQSRARLVAGFSSGSIALVSAGEDRLLEKLPE---AVGFLVVSEDDSLLV-AGFGRFVRIFLADSQGFHRFMAsdlE 919
Cdd:COG2319 42 LAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGhtaAVLSVAFSPDGRLLAsASADGTVRLWDLATGLLLRTLT---G 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 920 HEDMVETAVLGPENNLIITGSRDALIQVWSLsEQGTLLNVLEGVGAPVSLLV--RGGTLVVSASRkSSSFKVWDLKSTKK 997
Cdd:COG2319 119 HTGAVRSVAFSPDGKTLASGSADGTVRLWDL-ATGKLLRTLTGHSGAVTSVAfsPDGKLLASGSD-DGTVRLWDLATGKL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 998 LQSPTPFLDRTGLAAVSHHGSFVYFpkVGDKNKVTIWDLAEGEEQDCLDT-SNEVRCLEVAEQAKLLFTGLVSGIVLVFP 1076
Cdd:COG2319 197 LRTLTGHTGAVRSVAFSPDGKLLAS--GSADGTVRLWDLATGKLLRTLTGhSGSVRSVAFSPDGRLLASGSADGTVRLWD 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 1077 LNSRQDVLCIPPPEARkaVNCMSLSKSENRLAIA-YDNIVLVLDISPGDPCPAIEGPTytfytqlpETIVSVAVLAD-YR 1154
Cdd:COG2319 275 LATGELLRTLTGHSGG--VNSVAFSPDGKLLASGsDDGTVRLWDLATGKLLRTLTGHT--------GAVRSVAFSPDgKT 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720427671 1155 VVYGMSDGSLFLYDCACSK-VFPLEAHGSRVSCVEVSHSEQLAVSGAEDALLCLWDLQ 1211
Cdd:COG2319 345 LASGSDDGTVRLWDLATGElLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
931-1254 |
3.91e-17 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 83.54 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 931 PENNLIITGSRDALIQVWSLsEQGTLLNVLEGVGAPVS--LLVRGGTLVVSASrksssfkvwdlkstkklqsptpfLDRT 1008
Cdd:cd00200 19 PDGKLLATGSGDGTIKVWDL-ETGELLRTLKGHTGPVRdvAASADGTYLASGS-----------------------SDKT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 1009 glaavshhgsfvyfpkvgdknkVTIWDLAEGEeqdCLDT----SNEVRCLEVAEQAKLLFTGLVSGIVLVFPLNSRQDVL 1084
Cdd:cd00200 75 ----------------------IRLWDLETGE---CVRTltghTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLT 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 1085 CIPPPEArkAVNCMSLSKSENRLAIA-YDNIVLVLDISPGDPCPAIEGPTytfytqlpETIVSVAVLAD-YRVVYGMSDG 1162
Cdd:cd00200 130 TLRGHTD--WVNSVAFSPDGTFVASSsQDGTIKLWDLRTGKCVATLTGHT--------GEVNSVAFSPDgEKLLSSSSDG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 1163 SLFLYDCACSKVF-PLEAHGSRVSCVEVSHSEQLAVSGAEDALLCLWDLQACRGMFEMS-YENSccrgVRCACFSRDDKH 1240
Cdd:cd00200 200 TIKLWDLSTGKCLgTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSgHTNS----VTSLAWSPDGKR 275
|
330
....*....|....
gi 1720427671 1241 VFAGMEDRSVTAWS 1254
Cdd:cd00200 276 LASGSADGTIRIWD 289
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
694-731 |
1.27e-06 |
|
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: 46.15 E-value: 1.27e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1720427671 694 QVVHVLMGHTAEVKCVRVFAQGTLAISASKDHTLRLWS 731
Cdd:smart00320 3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
694-731 |
1.32e-05 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 43.49 E-value: 1.32e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1720427671 694 QVVHVLMGHTAEVKCVRVFAQGTLAISASKDHTLRLWS 731
Cdd:pfam00400 2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
108-214 |
1.40e-04 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 45.16 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 108 GHQELLAQLRQQLRQDESrthtPLVLFGPPGIGKTSLMCKLAQQVPEllghkTVVVLRLLGTsklSLDARSLLRslsfQV 187
Cdd:COG3267 27 SHREALARLEYALAQGGG----FVVLTGEVGTGKTTLLRRLLERLPD-----DVKVAYIPNP---QLSPAELLR----AI 90
|
90 100
....*....|....*....|....*..
gi 1720427671 188 CLAYGLPLPPAQVLEAHSRVGHFFHTL 214
Cdd:COG3267 91 ADELGLEPKGASKADLLRQLQEFLLEL 117
|
|
| FxSxx_TPR |
NF040586 |
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ... |
106-144 |
5.14e-04 |
|
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.
Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 44.52 E-value: 5.14e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1720427671 106 FCGHQELLAQLRQQLRQdESRTHTPLVLFGPPGIGKTSL 144
Cdd:NF040586 8 FTGREELLERLRDQLRS-GGAAVVPQALHGLGGVGKTQL 45
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
108-154 |
6.11e-04 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 41.75 E-value: 6.11e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1720427671 108 GHQELLAQLRQQLRQDESRthtPLVLFGPPGIGKTSLMCKLAQQVPE 154
Cdd:cd00009 2 GQEEAIEALREALELPPPK---NLLLYGPPGTGKTTLARAIANELFR 45
|
|
| NACHT |
pfam05729 |
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ... |
130-297 |
1.69e-03 |
|
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription activation. This family is closely related to pfam00931.
Pssm-ID: 428606 [Multi-domain] Cd Length: 166 Bit Score: 40.75 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 130 PLVLFGPPGIGKTSLMCKLAQ--QVPELLGHKTVVVLRLLGTSKLSLDARSlLRSLSFQVCLAYGLPLPP--AQVLEAHS 205
Cdd:pfam05729 2 TVILQGEAGSGKTTLLQKLALlwAQGKLPQGFDFVFFLPCRELSRSGNARS-LADLLFSQWPEPAAPVSEvwAVILELPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 206 RVGHFFHTLLHTVSQRNFESLVLLLDSVDDldsichsprvSWLPLKCPPRVHLILSTCSGQqvLHNLQQTLKDPsTYWEV 285
Cdd:pfam05729 81 RLLLILDGLDELVSDLGQLDGPCPVLTLLS----------SLLRKKLLPGASLLLTVRPDA--LRDLRRGLEEP-RYLEV 147
|
170
....*....|..
gi 1720427671 286 KALSGSQGQEFI 297
Cdd:pfam05729 148 RGFSESDRKQYV 159
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1172-1209 |
2.22e-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: 36.91 E-value: 2.22e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1720427671 1172 SKVFPLEAHGSRVSCVEVSHSEQLAVSGAEDALLCLWD 1209
Cdd:smart00320 3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1177-1209 |
2.64e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 36.94 E-value: 2.64e-03
10 20 30
....*....|....*....|....*....|...
gi 1720427671 1177 LEAHGSRVSCVEVSHSEQLAVSGAEDALLCLWD 1209
Cdd:pfam00400 7 LEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| ruvB |
TIGR00635 |
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ... |
106-144 |
5.45e-03 |
|
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129721 [Multi-domain] Cd Length: 305 Bit Score: 40.36 E-value: 5.45e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1720427671 106 FCGHQELLAQLRQQLRQDESRTHTP--LVLFGPPGIGKTSL 144
Cdd:TIGR00635 6 FIGQEKVKEQLQLFIEAAKMRQEALdhLLLYGPPGLGKTTL 46
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
647-994 |
6.40e-29 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 121.17 E-value: 6.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 647 QPPGGPLRATLTGCHKGITAIAWSLEEKLLVVGTQDGAMVVWDVEEQQVVHVLMGHTAEVKCVRVFAQGTLAISASKDHT 726
Cdd:COG2319 106 DLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGT 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 727 LRLWSLLSGQEkVTILDGgsqnptepqswdlHVDERNNVVYSTSGARInmwnletsklvfcITGdvsdpwvcvallaaqg 806
Cdd:COG2319 186 VRLWDLATGKL-LRTLTG-------------HTGAVRSVAFSPDGKLL-------------ASG---------------- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 807 lllalSKGGQVSLWSSAMGKLQekHQLSSIKEETPTCAVSIQSRaRLVAGFSSGSIALVSAGEDRLLEKLP---EAVGFL 883
Cdd:COG2319 223 -----SADGTVRLWDLATGKLL--RTLTGHSGSVRSVAFSPDGR-LLASGSADGTVRLWDLATGELLRTLTghsGGVNSV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 884 VVSEDDSLLV-AGFGRFVRIF-LADSQGFHRFMAsdleHEDMVETAVLGPENNLIITGSRDALIQVWSLsEQGTLLNVLE 961
Cdd:COG2319 295 AFSPDGKLLAsGSDDGTVRLWdLATGKLLRTLTG----HTGAVRSVAFSPDGKTLASGSDDGTVRLWDL-ATGELLRTLT 369
|
330 340 350
....*....|....*....|....*....|....*
gi 1720427671 962 GVGAPVSLLV--RGGTLVVSASRkSSSFKVWDLKS 994
Cdd:COG2319 370 GHTGAVTSVAfsPDGRTLASGSA-DGTVRLWDLAT 403
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
653-949 |
1.80e-27 |
|
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: 113.97 E-value: 1.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 653 LRATLTGCHKGITAIAWSLEEKLLVVGTQDGAMVVWDVEEQQVVHVLMGHTAEVKCVRVFAQGTLAISASKDHTLRLWSl 732
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 733 LSGQEKVTILDGGSQNPTepqSWDLHVDERnnVVYSTSGAR-INMWNLETSKLVFCITGdVSDPWVCVALLAAQGLLLAL 811
Cdd:cd00200 80 LETGECVRTLTGHTSYVS---SVAFSPDGR--ILSSSSRDKtIKVWDVETGKCLTTLRG-HTDWVNSVAFSPDGTFVASS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 812 SKGGQVSLWSSAMGKLqeKHQLSSIKEETPTCAVSiQSRARLVAGFSSGSIALVSAGEDRLLEKLP---EAVGFLVVSED 888
Cdd:cd00200 154 SQDGTIKLWDLRTGKC--VATLTGHTGEVNSVAFS-PDGEKLLSSSSDGTIKLWDLSTGKCLGTLRgheNGVNSVAFSPD 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720427671 889 DSLLVAG-FGRFVRIFlaDSQGFhRFMASDLEHEDMVETAVLGPENNLIITGSRDALIQVWS 949
Cdd:cd00200 231 GYLLASGsEDGTIRVW--DLRTG-ECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
650-1037 |
1.91e-26 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 113.47 E-value: 1.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 650 GGPLRATLTGCHKGITAIAWSLEEKLLVVGTQDGAMVVWDVEEQQVVHVLMGHTAEVKCVRVFAQGTLAISASKDHTLRL 729
Cdd:COG2319 67 AGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 730 WSLLSGQEkVTILDGgsqnptepqswdlHVDERNNVVYSTSGARInmwnletsklvfcITGdvsdpwvcvallaaqglll 809
Cdd:COG2319 147 WDLATGKL-LRTLTG-------------HSGAVTSVAFSPDGKLL-------------ASG------------------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 810 alSKGGQVSLWSSAMGKLQekHQLSSIKEETPTCAVSIQSRaRLVAGFSSGSIALVSAGEDRLLEKLP---EAVGFLVVS 886
Cdd:COG2319 181 --SDDGTVRLWDLATGKLL--RTLTGHTGAVRSVAFSPDGK-LLASGSADGTVRLWDLATGKLLRTLTghsGSVRSVAFS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 887 EDDSLLV-AGFGRFVRIFLADSQGFHRFMASdleHEDMVETAVLGPENNLIITGSRDALIQVWSLSEqGTLLNVLEGVGA 965
Cdd:COG2319 256 PDGRLLAsGSADGTVRLWDLATGELLRTLTG---HSGGVNSVAFSPDGKLLASGSDDGTVRLWDLAT-GKLLRTLTGHTG 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720427671 966 PVSLLV--RGGTLVVSASRkSSSFKVWDLKSTKKLQSPTPFLDRTGLAAVSHHGSFVYFpkVGDKNKVTIWDLA 1037
Cdd:COG2319 332 AVRSVAfsPDGKTLASGSD-DGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS--GSADGTVRLWDLA 402
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
844-1211 |
2.00e-26 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 113.47 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 844 AVSIQSRARLVAGFSSGSIALVSAGEDRLLEKLPE---AVGFLVVSEDDSLLV-AGFGRFVRIFLADSQGFHRFMAsdlE 919
Cdd:COG2319 42 LAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGhtaAVLSVAFSPDGRLLAsASADGTVRLWDLATGLLLRTLT---G 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 920 HEDMVETAVLGPENNLIITGSRDALIQVWSLsEQGTLLNVLEGVGAPVSLLV--RGGTLVVSASRkSSSFKVWDLKSTKK 997
Cdd:COG2319 119 HTGAVRSVAFSPDGKTLASGSADGTVRLWDL-ATGKLLRTLTGHSGAVTSVAfsPDGKLLASGSD-DGTVRLWDLATGKL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 998 LQSPTPFLDRTGLAAVSHHGSFVYFpkVGDKNKVTIWDLAEGEEQDCLDT-SNEVRCLEVAEQAKLLFTGLVSGIVLVFP 1076
Cdd:COG2319 197 LRTLTGHTGAVRSVAFSPDGKLLAS--GSADGTVRLWDLATGKLLRTLTGhSGSVRSVAFSPDGRLLASGSADGTVRLWD 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 1077 LNSRQDVLCIPPPEARkaVNCMSLSKSENRLAIA-YDNIVLVLDISPGDPCPAIEGPTytfytqlpETIVSVAVLAD-YR 1154
Cdd:COG2319 275 LATGELLRTLTGHSGG--VNSVAFSPDGKLLASGsDDGTVRLWDLATGKLLRTLTGHT--------GAVRSVAFSPDgKT 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720427671 1155 VVYGMSDGSLFLYDCACSK-VFPLEAHGSRVSCVEVSHSEQLAVSGAEDALLCLWDLQ 1211
Cdd:COG2319 345 LASGSDDGTVRLWDLATGElLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
844-1255 |
2.79e-26 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 113.08 E-value: 2.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 844 AVSIQSRARLVAGFSSGSIALVSAGEDRLLEKLPEAVGFLVVSEDDSLLVAGFGRFVRIFLADSQGFHRfmASDLEHEDM 923
Cdd:COG2319 3 SADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALL--ATLLGHTAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 924 VETAVLGPENNLIITGSRDALIQVWSLSeQGTLLNVLEGVGAPVSLLV--RGGTLVVSASRkSSSFKVWDLKSTKKLQSP 1001
Cdd:COG2319 81 VLSVAFSPDGRLLASASADGTVRLWDLA-TGLLLRTLTGHTGAVRSVAfsPDGKTLASGSA-DGTVRLWDLATGKLLRTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 1002 TPFLDRTGLAAVSHHGSFVYFpkVGDKNKVTIWDLAEGEEQDCLD-TSNEVRCLEVAEQAKLLFTGLVSGIVLVFPLNSR 1080
Cdd:COG2319 159 TGHSGAVTSVAFSPDGKLLAS--GSDDGTVRLWDLATGKLLRTLTgHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 1081 QDVLCIPPPEARkaVNCMSLSKSENRLAIA-YDNIVLVLDISPGDPCPAIEGPTytfytqlpETIVSVAVLAD-YRVVYG 1158
Cdd:COG2319 237 KLLRTLTGHSGS--VRSVAFSPDGRLLASGsADGTVRLWDLATGELLRTLTGHS--------GGVNSVAFSPDgKLLASG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 1159 MSDGSLFLYDCACSK-VFPLEAHGSRVSCVEVSHSEQLAVSGAEDALLCLWDLQACRGMFEMSYENSccrGVRCACFSRD 1237
Cdd:COG2319 307 SDDGTVRLWDLATGKlLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTG---AVTSVAFSPD 383
|
410
....*....|....*...
gi 1720427671 1238 DKHVFAGMEDRSVTAWST 1255
Cdd:COG2319 384 GRTLASGSADGTVRLWDL 401
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
650-1066 |
9.12e-26 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 111.54 E-value: 9.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 650 GGPLRATLTGCHKGITAIAWSLEEKLLVVGTQDGAMVVWDVEEQQVVHVLMGHTAEVKCVRVFAQGTLAISASKDHTLRL 729
Cdd:COG2319 25 LGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 730 WSLLSGQEKVTILDggsqnptepqswdlHVDERNNVVYSTSGARInmwnletsklvfcITGdvsdpwvcvallaaqglll 809
Cdd:COG2319 105 WDLATGLLLRTLTG--------------HTGAVRSVAFSPDGKTL-------------ASG------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 810 alSKGGQVSLWSSAMGKLQekHQLSSIKEETPTCAVSIQSRaRLVAGFSSGSIALVSAGEDRLLEKLP---EAVGFLVVS 886
Cdd:COG2319 139 --SADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGK-LLASGSDDGTVRLWDLATGKLLRTLTghtGAVRSVAFS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 887 EDDSLLV-AGFGRFVRIFLADSQGFHRFMASdleHEDMVETAVLGPENNLIITGSRDALIQVWSLSEqGTLLNVLEGVGA 965
Cdd:COG2319 214 PDGKLLAsGSADGTVRLWDLATGKLLRTLTG---HSGSVRSVAFSPDGRLLASGSADGTVRLWDLAT-GELLRTLTGHSG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 966 PVSLLV--RGGTLVVSASRkSSSFKVWDLKSTKKLQSPTPFLDRTGLAAVSHHGSFVYFpkVGDKNKVTIWDLAEGEEQD 1043
Cdd:COG2319 290 GVNSVAfsPDGKLLASGSD-DGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLAS--GSDDGTVRLWDLATGELLR 366
|
410 420
....*....|....*....|....
gi 1720427671 1044 CLDT-SNEVRCLEVAEQAKLLFTG 1066
Cdd:COG2319 367 TLTGhTGAVTSVAFSPDGRTLASG 390
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
884-1267 |
2.52e-23 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 104.22 E-value: 2.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 884 VVSEDDSLLVAGFGRFVRIFLADSQGFHRfmASDLEHEDMVETAVLGPENNLIITGSRDALIQVWSLSEQGTLLNVLEGV 963
Cdd:COG2319 1 ALSADGAALAAASADLALALLAAALGALL--LLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 964 GAPVSLLVRGGTLVVSASRKSSSFKVWDLKSTKKLQSPTPFLDRTGLAAVSHHGSFVYFpkVGDKNKVTIWDLAEGEEQD 1043
Cdd:COG2319 79 AAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLAS--GSADGTVRLWDLATGKLLR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 1044 CLDT-SNEVRCLEVAEQAKLLFTGLVSGIVLVFPLNSRQDVLCIPPPEARkaVNCMSLSKSENRLAIA-YDNIVLVLDIS 1121
Cdd:COG2319 157 TLTGhSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGA--VRSVAFSPDGKLLASGsADGTVRLWDLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 1122 PGDPCPAIEGPTytfytqlpETIVSVAVLAD-YRVVYGMSDGSLFLYDCACSK-VFPLEAHGSRVSCVEVSHSEQLAVSG 1199
Cdd:COG2319 235 TGKLLRTLTGHS--------GSVRSVAFSPDgRLLASGSADGTVRLWDLATGElLRTLTGHSGGVNSVAFSPDGKLLASG 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720427671 1200 AEDALLCLWDLQACRGMFEMSYENSccrGVRCACFSRDDKHVFAGMEDRSVTAWSTVDGTLLAVQFVH 1267
Cdd:COG2319 307 SDDGTVRLWDLATGKLLRTLTGHTG---AVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGH 371
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
651-790 |
1.20e-17 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 85.08 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 651 GPLRATLTGCHKGITAIAWSLEEKLLVVGTQDGAMVVWDVEEQQVVHVLMGHTAEVKCVRVFAQGTLAISASKDHTLRLW 730
Cdd:cd00200 125 GKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLW 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720427671 731 SLLSGQEKVTIldGGSQNPtepqSWDLHVDERNNVVYSTSGAR-INMWNLETSKLVFCITG 790
Cdd:cd00200 205 DLSTGKCLGTL--RGHENG----VNSVAFSPDGYLLASGSEDGtIRVWDLRTGECVQTLSG 259
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
931-1254 |
3.91e-17 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 83.54 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 931 PENNLIITGSRDALIQVWSLsEQGTLLNVLEGVGAPVS--LLVRGGTLVVSASrksssfkvwdlkstkklqsptpfLDRT 1008
Cdd:cd00200 19 PDGKLLATGSGDGTIKVWDL-ETGELLRTLKGHTGPVRdvAASADGTYLASGS-----------------------SDKT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 1009 glaavshhgsfvyfpkvgdknkVTIWDLAEGEeqdCLDT----SNEVRCLEVAEQAKLLFTGLVSGIVLVFPLNSRQDVL 1084
Cdd:cd00200 75 ----------------------IRLWDLETGE---CVRTltghTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLT 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 1085 CIPPPEArkAVNCMSLSKSENRLAIA-YDNIVLVLDISPGDPCPAIEGPTytfytqlpETIVSVAVLAD-YRVVYGMSDG 1162
Cdd:cd00200 130 TLRGHTD--WVNSVAFSPDGTFVASSsQDGTIKLWDLRTGKCVATLTGHT--------GEVNSVAFSPDgEKLLSSSSDG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 1163 SLFLYDCACSKVF-PLEAHGSRVSCVEVSHSEQLAVSGAEDALLCLWDLQACRGMFEMS-YENSccrgVRCACFSRDDKH 1240
Cdd:cd00200 200 TIKLWDLSTGKCLgTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSgHTNS----VTSLAWSPDGKR 275
|
330
....*....|....
gi 1720427671 1241 VFAGMEDRSVTAWS 1254
Cdd:cd00200 276 LASGSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
648-731 |
2.76e-14 |
|
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: 75.06 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 648 PPGGPLRATLTGCHKGITAIAWSLEEKLLVVGTQDGAMVVWDVEEQQVVHVLMGHTAEVKCVRVFAQGTLAISASKDHTL 727
Cdd:cd00200 206 LSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTI 285
|
....
gi 1720427671 728 RLWS 731
Cdd:cd00200 286 RIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1048-1267 |
2.00e-13 |
|
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: 72.37 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 1048 SNEVRCLEVAEQAKLLFTGLVSGIVLVFPLNSRQDVLCIPppEARKAVNCMSLSKSENRLAIA-YDNIVLVLDISPGDPC 1126
Cdd:cd00200 9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLK--GHTGPVRDVAASADGTYLASGsSDKTIRLWDLETGECV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 1127 PAIEGPTytfytqlpETIVSVAVLADYRVVYG-MSDGSLFLYDCACSK-VFPLEAHGSRVSCVEVSHSEQLAVSGAEDAL 1204
Cdd:cd00200 87 RTLTGHT--------SYVSSVAFSPDGRILSSsSRDKTIKVWDVETGKcLTTLRGHTDWVNSVAFSPDGTFVASSSQDGT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720427671 1205 LCLWDLQA--CRGMFEMSYENsccrgVRCACFSRDDKHVFAGMEDRSVTAWSTVDGTLLAVQFVH 1267
Cdd:cd00200 159 IKLWDLRTgkCVATLTGHTGE-----VNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH 218
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
694-731 |
1.27e-06 |
|
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: 46.15 E-value: 1.27e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1720427671 694 QVVHVLMGHTAEVKCVRVFAQGTLAISASKDHTLRLWS 731
Cdd:smart00320 3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
694-731 |
1.32e-05 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 43.49 E-value: 1.32e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1720427671 694 QVVHVLMGHTAEVKCVRVFAQGTLAISASKDHTLRLWS 731
Cdd:pfam00400 2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
108-214 |
1.40e-04 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 45.16 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 108 GHQELLAQLRQQLRQDESrthtPLVLFGPPGIGKTSLMCKLAQQVPEllghkTVVVLRLLGTsklSLDARSLLRslsfQV 187
Cdd:COG3267 27 SHREALARLEYALAQGGG----FVVLTGEVGTGKTTLLRRLLERLPD-----DVKVAYIPNP---QLSPAELLR----AI 90
|
90 100
....*....|....*....|....*..
gi 1720427671 188 CLAYGLPLPPAQVLEAHSRVGHFFHTL 214
Cdd:COG3267 91 ADELGLEPKGASKADLLRQLQEFLLEL 117
|
|
| WDR74 |
cd22857 |
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ... |
1089-1211 |
1.93e-04 |
|
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and plants is an essential factor for ribosome assembly. In cooperation with the assembly factor NVL2, WDR74 participates in an early cleavage of the pre-rRNA processing pathway. NVL2 is a type II double ring, AAA-ATPase, that may mediate the release of WDR74 from nucleolar pre-60S particles. WDR74 has been implicated in tumorigenesis. In lung cancer, it regulates cell proliferation, cell cycle progression, chemoresistance and cell aggressiveness, by inducing nuclear beta-catenin accumulation and driving downstream Wnt-responsive genes expression. In melanoma, it promotes apoptosis resistance and aggressive behavior by regulating the RPL5-MDM2-p53 pathway. WDR74 contains an N-terminal seven-bladed beta-propeller WD40 domain that associates with the D1-AAA domain of the AAA-ATPase NVL2, and a flexible lysine-rich C-terminus that extends outward from the WD40 domain, and is required for nucleolar localization.
Pssm-ID: 439303 [Multi-domain] Cd Length: 325 Bit Score: 45.30 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 1089 PEARKAVNCMSLS--KSENRLAIAY-DNIVLVLDISPGDPCPAIEGPTYTFYTQLPETIVSVAVLAdyRVVYGMSD-GSL 1164
Cdd:cd22857 27 PDKSKAVQALSIAdrESEPLLAVARkNGTVEVLDPENGDLLASFSDSEPATKLSEEDHFVGLHLFS--GTLLTCTSkGSL 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1720427671 1165 FLY-----DCACSKVFPLEAHGSRVSCVEVSHSEQLAVSGAEDALLCLWDLQ 1211
Cdd:cd22857 105 RSTklpddSTASSSPTAWVCLGGNLLCMRVDPNENYFAFGGKEVELNVWDLE 156
|
|
| ANAPC4_WD40 |
pfam12894 |
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ... |
664-709 |
2.92e-04 |
|
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,
Pssm-ID: 403945 [Multi-domain] Cd Length: 91 Bit Score: 41.11 E-value: 2.92e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1720427671 664 ITAIAWSLEEKLLVVGTQDGAMVVWDVEEQQVVHVLMGHTAEVKCV 709
Cdd:pfam12894 41 VTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGSDLITCL 86
|
|
| FxSxx_TPR |
NF040586 |
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ... |
106-144 |
5.14e-04 |
|
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.
Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 44.52 E-value: 5.14e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1720427671 106 FCGHQELLAQLRQQLRQdESRTHTPLVLFGPPGIGKTSL 144
Cdd:NF040586 8 FTGREELLERLRDQLRS-GGAAVVPQALHGLGGVGKTQL 45
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
108-154 |
6.11e-04 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 41.75 E-value: 6.11e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1720427671 108 GHQELLAQLRQQLRQDESRthtPLVLFGPPGIGKTSLMCKLAQQVPE 154
Cdd:cd00009 2 GQEEAIEALREALELPPPK---NLLLYGPPGTGKTTLARAIANELFR 45
|
|
| NACHT |
pfam05729 |
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ... |
130-297 |
1.69e-03 |
|
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription activation. This family is closely related to pfam00931.
Pssm-ID: 428606 [Multi-domain] Cd Length: 166 Bit Score: 40.75 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 130 PLVLFGPPGIGKTSLMCKLAQ--QVPELLGHKTVVVLRLLGTSKLSLDARSlLRSLSFQVCLAYGLPLPP--AQVLEAHS 205
Cdd:pfam05729 2 TVILQGEAGSGKTTLLQKLALlwAQGKLPQGFDFVFFLPCRELSRSGNARS-LADLLFSQWPEPAAPVSEvwAVILELPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427671 206 RVGHFFHTLLHTVSQRNFESLVLLLDSVDDldsichsprvSWLPLKCPPRVHLILSTCSGQqvLHNLQQTLKDPsTYWEV 285
Cdd:pfam05729 81 RLLLILDGLDELVSDLGQLDGPCPVLTLLS----------SLLRKKLLPGASLLLTVRPDA--LRDLRRGLEEP-RYLEV 147
|
170
....*....|..
gi 1720427671 286 KALSGSQGQEFI 297
Cdd:pfam05729 148 RGFSESDRKQYV 159
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1172-1209 |
2.22e-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: 36.91 E-value: 2.22e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1720427671 1172 SKVFPLEAHGSRVSCVEVSHSEQLAVSGAEDALLCLWD 1209
Cdd:smart00320 3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1177-1209 |
2.64e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 36.94 E-value: 2.64e-03
10 20 30
....*....|....*....|....*....|...
gi 1720427671 1177 LEAHGSRVSCVEVSHSEQLAVSGAEDALLCLWD 1209
Cdd:pfam00400 7 LEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
651-689 |
3.15e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 36.55 E-value: 3.15e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1720427671 651 GPLRATLTGCHKGITAIAWSLEEKLLVVGTQDGAMVVWD 689
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
651-689 |
5.18e-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: 36.14 E-value: 5.18e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1720427671 651 GPLRATLTGCHKGITAIAWSLEEKLLVVGTQDGAMVVWD 689
Cdd:smart00320 2 GELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| ruvB |
TIGR00635 |
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ... |
106-144 |
5.45e-03 |
|
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129721 [Multi-domain] Cd Length: 305 Bit Score: 40.36 E-value: 5.45e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1720427671 106 FCGHQELLAQLRQQLRQDESRTHTP--LVLFGPPGIGKTSL 144
Cdd:TIGR00635 6 FIGQEKVKEQLQLFIEAAKMRQEALdhLLLYGPPGLGKTTL 46
|
|
| HolB |
COG0470 |
DNA polymerase III, delta prime subunit [Replication, recombination and repair]; |
109-159 |
6.06e-03 |
|
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
Pssm-ID: 440238 [Multi-domain] Cd Length: 289 Bit Score: 40.34 E-value: 6.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1720427671 109 HQELLAQLRQQLRQDesRTHTPLVLFGPPGIGKTSLMCKLAQqvpELLGHK 159
Cdd:COG0470 1 QEEAWEQLLAAAESG--RLPHALLLHGPPGIGKTTLALALAR---DLLCEN 46
|
|
| |
