|
Name |
Accession |
Description |
Interval |
E-value |
| YvrE |
COG3386 |
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ... |
34-299 |
2.82e-85 |
|
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 442613 [Multi-domain] Cd Length: 266 Bit Score: 257.13 E-value: 2.82e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 34 GCRWAEGPVYVPAGRyLVWSDIPNDRLLRWDETTGAVGVFRSPAGFPNGNTLDGQGRLVTCEQGnRRVTRTEH-DGSVTV 112
Cdd:COG3386 6 GFRLGEGPVWDPDGR-LYWVDIPGGRIHRYDPDGGAVEVFAEPSGRPNGLAFDPDGRLLVADHG-RGLVRFDPaDGEVTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 113 IAERFeGKRLNSPNDAVVRSDGSVWFSDPefgiaTDYEGHRGeseigarnVYRVDPaDGRVRLVADGFEGPNGLVFSPDE 192
Cdd:COG3386 84 LADEY-GKPLNRPNDGVVDPDGRLYFTDM-----GEYLPTGA--------LYRVDP-DGSLRVLADGLTFPNGIAFSPDG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 193 SRLYVSDSLANHIRVFDVRDDGTLGGGEVFAECAN--GNFDNIRFDDAGRLWAAAL-HGGVHCYDPDGTLLGRVLVPGT- 268
Cdd:COG3386 149 RTLYVADTGAGRIYRFDLDADGTLGNRRVFADLPDgpGGPDGLAVDADGNLWVALWgGGGVVRFDPDGELLGRIELPERr 228
|
250 260 270
....*....|....*....|....*....|....*..
gi 1907443934 269 VANVRFGGARRNRMFIAADTT------LYSLMMSVTG 299
Cdd:COG3386 229 PTNVAFGGPDLRTLYVTTARSlplagaLFRVRVDVPG 265
|
|
| SGL |
pfam08450 |
SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in ... |
37-284 |
2.60e-56 |
|
SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in proteins expressed by a variety of eukaryotic and prokaryotic species. These proteins include various enzymes, such as senescence marker protein 30 (SMP-30), gluconolactonase and luciferin-regenerating enzyme (LRE). SMP-30 is known to hydrolyse diisopropyl phosphorofluoridate in the liver, and has been noted as having sequence similarity, in the region described in this family, with PON1 and LRE.
Pssm-ID: 462480 [Multi-domain] Cd Length: 246 Bit Score: 182.08 E-value: 2.60e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 37 WAEGPVYVPAGRYLVWSDIPNDRLLRWDETTGAVGVFRSPAgfPNGNT-LDGQGRLVTCEQGNRRVTRTEhDGSVTVIAE 115
Cdd:pfam08450 1 LGEGPVWDEEEGALYWVDILGGRIHRLDPATGKETVWDTPG--PVGAIaPRDDGGLIVALKDGVALLDLA-TGELTPLAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 116 RFEG-KRLNSPNDAVVRSDGSVWFSDPEFGIATDYEGhrgeseiGArnVYRVDPaDGRVRLVADGFEGPNGLVFSPDESR 194
Cdd:pfam08450 78 PEDDdWPLNRFNDGKVDPDGRFWFGTMGDDEAPGGDP-------GA--LYRLDP-DGKLTRVLDGLTISNGLAWSPDGRT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 195 LYVSDSLANHIRVFDV-RDDGTLGGGEVFAECA--NGNFDNIRFDDAGRLWAAALHGG-VHCYDPDGTLLGRVLVPGT-V 269
Cdd:pfam08450 148 LYFADSPARKIWAYDYdLDGGLISNRRVFADFKpgLGRPDGMAVDAEGNVWVARWGGGkVVRFDPDGKLLREIELPAKrP 227
|
250
....*....|....*
gi 1907443934 270 ANVRFGGARRNRMFI 284
Cdd:pfam08450 228 TSCAFGGPDLRTLYV 242
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
51-259 |
5.78e-16 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 76.21 E-value: 5.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 51 VW-SDIPNDRLLRWDETTGAVGVFRSPAG--FPNGNTLDGQGRLVTCEQGNRRVTR-TEHDGSVTVIAERFEGKRlnsPN 126
Cdd:COG4257 72 LWfTDNGNNRIGRIDPKTGEITTFALPGGgsNPHGIAFDPDGNLWFTDQGGNRIGRlDPATGEVTEFPLPTGGAG---PY 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 127 DAVVRSDGSVWFSDPefgiatdyeghrgeseiGARNVYRVDPADGRVRLVA--DGFEGPNGLVFSPDEsRLYVSDSLANH 204
Cdd:COG4257 149 GIAVDPDGNLWVTDF-----------------GANAIGRIDPDTGTLTEYAlpTPGAGPRGLAVDPDG-NLWVADTGSGR 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907443934 205 IRVFDVRDdgtlGGGEVFAECANGNF-DNIRFDDAGRLWAAALHGG-VHCYDPDGTL 259
Cdd:COG4257 211 IGRFDPKT----GTVTEYPLPGGGARpYGVAVDGDGRVWFAESGANrIVRFDPDTEL 263
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
76-291 |
3.95e-13 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 68.12 E-value: 3.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 76 PAGFPNGNTLDGQGRLVTCEQGNRRVTR-TEHDGSVTviaeRFEGKRLNSPNDAVVRSDGSVWFsdpefgiaTDYEGHRg 154
Cdd:COG4257 15 PGSGPRDVAVDPDGAVWFTDQGGGRIGRlDPATGEFT----EYPLGGGSGPHGIAVDPDGNLWF--------TDNGNNR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 155 eseigarnVYRVDPADGRVRLVA--DGFEGPNGLVFSPDEsRLYVSDSLANHIRVFDVRDDGTLgggEVFAECANGNFDN 232
Cdd:COG4257 82 --------IGRIDPKTGEITTFAlpGGGSNPHGIAFDPDG-NLWFTDQGGNRIGRLDPATGEVT---EFPLPTGGAGPYG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 233 IRFDDAGRLWAAALHGG-VHCYDPDGTLLGRVLVPGTvanvrfgGARRNRMFIAADTTLY 291
Cdd:COG4257 150 IAVDPDGNLWVTDFGANaIGRIDPDTGTLTEYALPTP-------GAGPRGLAVDPDGNLW 202
|
|
| NHL |
cd05819 |
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ... |
45-244 |
3.05e-11 |
|
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.
Pssm-ID: 271320 [Multi-domain] Cd Length: 269 Bit Score: 62.72 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 45 PAGRYLVwSDIPNDRLLRWDETTGAVGVFRSPAGF------PNGNTLDGQGRLVTCEQGNRRVTRTEHDGS-VTVIAERF 117
Cdd:cd05819 64 SDGNLYV-ADTGNHRIQKFDPDGNFLASFGGSGDGdgefngPRGIAVDSSGNIYVADTGNHRIQKFDPDGEfLTTFGSGG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 118 EGK-RLNSPNDAVVRSDGSVWFSDpefgiatdYEGHRgeseigarnVYRVDPADGRVRLVADG------FEGPNGLVFSP 190
Cdd:cd05819 143 SGPgQFNGPTGVAVDSDGNIYVAD--------TGNHR---------IQVFDPDGNFLTTFGSTgtgpgqFNYPTGIAVDS 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907443934 191 DEsRLYVSDSLANHIRVFDvrDDGTLGGGEVFAECANGNFDN---IRFDDAGRLWAA 244
Cdd:cd05819 206 DG-NIYVADSGNNRVQVFD--PDGAGFGGNGNFLGSDGQFNRpsgLAVDSDGNLYVA 259
|
|
| NHL |
cd05819 |
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ... |
38-244 |
1.00e-09 |
|
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.
Pssm-ID: 271320 [Multi-domain] Cd Length: 269 Bit Score: 58.10 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 38 AEGPVYVpagrylvwSDIPNDRLLRWDETTGAVGVFRSPAG------FPNGNTLDGQGRLVTCEQGNRRVTRTEHDGSV- 110
Cdd:cd05819 17 SSGNIYV--------ADTGNNRIQVFDPDGNFITSFGSFGSgdgqfnEPAGVAVDSDGNLYVADTGNHRIQKFDPDGNFl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 111 -TVIAERFEGKRLNSPNDAVVRSDGSVWfsdpefgIAtDYEGHRgeseigarnVYRVDPADGRVRLV------ADGFEGP 183
Cdd:cd05819 89 aSFGGSGDGDGEFNGPRGIAVDSSGNIY-------VA-DTGNHR---------IQKFDPDGEFLTTFgsggsgPGQFNGP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907443934 184 NGLVFSPDEsRLYVSDSLANHIRVFDVRDDGTLGGGEVFAEcaNGNFDN---IRFDDAGRLWAA 244
Cdd:cd05819 152 TGVAVDSDG-NIYVADTGNHRIQVFDPDGNFLTTFGSTGTG--PGQFNYptgIAVDSDGNIYVA 212
|
|
| Pgl |
COG2706 |
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism]; |
45-217 |
1.02e-09 |
|
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];
Pssm-ID: 442025 [Multi-domain] Cd Length: 352 Bit Score: 58.76 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 45 PAGRYLVWSDIPNDRLL--RWDETTG---AVGVFRSPAGF--------PNGNTLdgqgrLVTCEQGNRrVT---RTEHDG 108
Cdd:COG2706 159 PDGRFLYVPDLGTDRIYvyRLDPATGklpEPPEVSLPPGSgprhlafhPNGRFA-----YVINELDST-VSvyaYDAATG 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 109 SVTVI------AERFEGKrlNSPNDAVVRSDGS-VWFSDpefgiatdyeghRGESEIGarnVYRVDPADGRVRLVAD--- 178
Cdd:COG2706 233 TLTLIqtvstlPEDFTGE--NWAADIHISPDGRfLYVSN------------RGHNSIA---VFAIDADGGKLTLVGHvpt 295
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907443934 179 GFEGPNGLVFSPDESRLYVSDSLANHIRVFDV-RDDGTLG 217
Cdd:COG2706 296 GGKWPRDFAIDPDGRFLLVANQKSDNITVFRIdADTGKLT 335
|
|
| Lactonase |
pfam10282 |
Lactonase, 7-bladed beta-propeller; This entry contains bacterial 6-phosphogluconolactonases ... |
45-217 |
6.62e-08 |
|
Lactonase, 7-bladed beta-propeller; This entry contains bacterial 6-phosphogluconolactonases (6PGL)YbhE-type (EC:3.1.1.31) which hydrolyse 6-phosphogluconolactone to 6-phosphogluconate. The entry also contains the fungal muconate lactonising enzyme carboxy-cis,cis-muconate cyclase (EC:5.5.1.5) and muconate cycloisomerase (EC:5.5.1.1), which convert cis,cis-muconates to muconolactones and vice versa as part of the microbial beta-ketoadipate pathway. Structures of proteins in this family have revealed a 7-bladed beta-propeller fold.
Pssm-ID: 431196 [Multi-domain] Cd Length: 340 Bit Score: 52.99 E-value: 6.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 45 PAGRYLVWSDIPNDRLLRW--DETTG---AVGVFRSPAGF--------PNGNTLdgqgrLVTCEQGNRrVTRTEHDGS-- 109
Cdd:pfam10282 152 PDGKFLVVPDLGTDRVRVYklDAGGGkltPPASVQTPPGSgprhlafhPNGKYA-----YVVNELSST-VTVFEYDPAtg 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 110 -------VTVIAERFEGKrlNSPNDAVVRSDGSvwfsdpefgiaTDYEGHRGESEIGarnVYRVDPADGRVRLVAD---G 179
Cdd:pfam10282 226 tfeelqtVSTLPEGFTGT--NGAAAIRVSPDGK-----------FLYVSNRGHDSIA---VFAVDEAGGTLTLVERvstE 289
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907443934 180 FEGPNGLVFSPDESRLYVSDSLANHIRVFDV-RDDGTLG 217
Cdd:pfam10282 290 GDFPRDFNIDPDGKFLVVANQDSDNVTVFRRdPETGKLT 328
|
|
| NHL_like_6 |
cd14962 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
80-273 |
8.71e-08 |
|
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.
Pssm-ID: 271332 [Multi-domain] Cd Length: 271 Bit Score: 52.20 E-value: 8.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 80 PNGNTLDGQGRLVTCEQGNRRVTR-TEHDGSVTVIAERfEGKRLNSPNDAVVRSDGSVWFSDpefgiatdyeghrgeseI 158
Cdd:cd14962 14 PYGVAADGRGRIYVADTGRGAVFVfDLPNGKVFVIGNA-GPNRFVSPIGVAIDANGNLYVSD-----------------A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 159 GARNVYRVDPADGRVRLVADGFEG--PNGLVFSPDESRLYVSDSLANHIRVFD-----VRDDGTLGGGEvfaecanGNFD 231
Cdd:cd14962 76 ELGKVFVFDRDGKFLRAIGAGALFkrPTGIAVDPAGKRLYVVDTLAHKVKVFDldgrlLFDIGKRGSGP-------GEFN 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907443934 232 ---NIRFDDAGRLWAA-ALHGGVHCYDPDGTLL---GRV-LVPGTVANVR 273
Cdd:cd14962 149 lptDLAVDRDGNLYVTdTMNFRVQIFDADGKFLrsfGERgDGPGSFARPK 198
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
156-285 |
1.83e-07 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 51.23 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 156 SEIGARNVYRVDPADGRVRLVADGFEGPNGLVFSPDESRLYVSDSLANHIRVFDVRDdgtlggGEVFAECANGNF-DNIR 234
Cdd:COG3391 85 ANSGSGRVSVIDLATGKVVATIPVGGGPRGLAVDPDGGRLYVADSGNGRVSVIDTAT------GKVVATIPVGAGpHGIA 158
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907443934 235 FDDAG-RLWAAALHGG-----VHCYDP-DGTLLGRVLVPGTVANVRFGGARRnRMFIA 285
Cdd:COG3391 159 VDPDGkRLYVANSGSNtvsviVSVIDTaTGKVVATIPVGGGPVGVAVSPDGR-RLYVA 215
|
|
| NHL_like_3 |
cd14956 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
62-293 |
3.31e-07 |
|
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.
Pssm-ID: 271326 [Multi-domain] Cd Length: 274 Bit Score: 50.74 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 62 RWDETTGAVGVFRSPAGFPNGNTLDGQGRLVTCEQGNRRVTRTEHDGS-VTVIAERFEGK-RLNSPNDAVVRSDGSVWfs 139
Cdd:cd14956 44 TFLRRFGTTGDGPGQFGRPRGLAVDKDGWLYVADYWGDRIQVFTLTGElQTIGGSSGSGPgQFNAPRGVAVDADGNLY-- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 140 dpefgiATDYEGHRgeseigarnVYRVDPADGRVRLV------ADGFEGPNGLVFSPDeSRLYVSDSLANHIRVFDVRDD 213
Cdd:cd14956 122 ------VADFGNQR---------IQKFDPDGSFLRQWggtgiePGSFNYPRGVAVDPD-GTLYVADTYNDRIQVFDNDGA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 214 GTLGGGEVFAEcaNGNFD---NIRFDDAGRLWAAALHGG-VHCYDPDGTLLGRVLVPGTvANVRFGGARrnRMFIAADTT 289
Cdd:cd14956 186 FLRKWGGRGTG--PGQFNypyGIAIDPDGNVFVADFGNNrIQKFTADGTFLTSWGSPGT-GPGQFKNPW--GVVVDADGT 260
|
....
gi 1907443934 290 LYSL 293
Cdd:cd14956 261 VYVA 264
|
|
| Arylesterase |
pfam01731 |
Arylesterase; This family consists of arylesterases (Also known as serum paraoxonase) EC:3.1.1. ... |
162-213 |
4.66e-07 |
|
Arylesterase; This family consists of arylesterases (Also known as serum paraoxonase) EC:3.1.1.2. These enzymes hydrolyse organophosphorus esters such as paraoxon and are found in the liver and blood. They confer resistance to organophosphate toxicity. Human arylesterase (PON1) is associated with HDL and may protect against LDL oxidation.
Pssm-ID: 334656 Cd Length: 86 Bit Score: 47.07 E-value: 4.66e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1907443934 162 NVYRVDPadGRVRLVADGFEGPNGLVFSPDESRLYVSDSLANHIRVFDVRDD 213
Cdd:pfam01731 37 GVVYYSP--SEVKVVASGFSFANGINYSPDKKYIYVASSLRHSIHVMKKHAN 86
|
|
| NHL |
cd05819 |
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ... |
69-263 |
7.08e-06 |
|
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.
Pssm-ID: 271320 [Multi-domain] Cd Length: 269 Bit Score: 46.54 E-value: 7.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 69 AVGVFRSPAGFpngnTLDGQGRLVTCEQGNRRVTRTEHDG-SVTVIAER-FEGKRLNSPNDAVVRSDGSVWfsdpefgiA 146
Cdd:cd05819 3 GPGELNNPQGI----AVDSSGNIYVADTGNNRIQVFDPDGnFITSFGSFgSGDGQFNEPAGVAVDSDGNLY--------V 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 147 TDYEGHRgeseigarnVYRVDPaDGRVRLV-------ADGFEGPNGLVFSPDeSRLYVSDSLANHIRVFD-----VRDDG 214
Cdd:cd05819 71 ADTGNHR---------IQKFDP-DGNFLASfggsgdgDGEFNGPRGIAVDSS-GNIYVADTGNHRIQKFDpdgefLTTFG 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907443934 215 TLGGGevfaecaNGNFDN---IRFDDAGRLWAA-ALHGGVHCYDPDGTLLGRV 263
Cdd:cd05819 140 SGGSG-------PGQFNGptgVAVDSDGNIYVAdTGNHRIQVFDPDGNFLTTF 185
|
|
| Pgl |
COG2706 |
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism]; |
61-260 |
1.02e-05 |
|
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];
Pssm-ID: 442025 [Multi-domain] Cd Length: 352 Bit Score: 46.44 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 61 LRWDETTGA---VGVFRSPAGFPNGNTLDGQGRLVtceqgnrrVTRTEHDGSVTVIAERFEGkRLNSPNDAVVRSDGSVW 137
Cdd:COG2706 73 FRIDPADGTltlLNTVSSGGASPCHLSVDPDGRFL--------FVANYGGGSVSVFPIDADG-SLGEPVQVIQHEGSGPN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 138 FSDPEF----GIATDYEGHR------GESEIgarNVYRVDPADGRVRLVAD-----GFeGPNGLVFSPDESRLYVSDSLA 202
Cdd:COG2706 144 PERQEGphahSVVFDPDGRFlyvpdlGTDRI---YVYRLDPATGKLPEPPEvslppGS-GPRHLAFHPNGRFAYVINELD 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907443934 203 NHIRVFDV-RDDGTLGGGEVfaecangnFDNIRFDDAGRLWAAALHggVHcydPDGTLL 260
Cdd:COG2706 220 STVSVYAYdAATGTLTLIQT--------VSTLPEDFTGENWAADIH--IS---PDGRFL 265
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
40-210 |
1.23e-05 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 45.84 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 40 GPVYVPAGRYLVWSDIPNDRLLRWDETTGAVGVFRSPAGFPNGNTLDGQGR--LVTCEqGNRRVTRTehDGSVTVIAERF 117
Cdd:COG3391 72 GADAGADGRRLYVANSGSGRVSVIDLATGKVVATIPVGGGPRGLAVDPDGGrlYVADS-GNGRVSVI--DTATGKVVATI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 118 EGKrlNSPNDAVVRSDGSvwfsdpeFGIATDYEGHRGeSEIgarnVYRVDPADGRVRLVADGFEGPNGLVFSPDESRLYV 197
Cdd:COG3391 149 PVG--AGPHGIAVDPDGK-------RLYVANSGSNTV-SVI----VSVIDTATGKVVATIPVGGGPVGVAVSPDGRRLYV 214
|
170 180
....*....|....*....|
gi 1907443934 198 SDSLANH-------IRVFDV 210
Cdd:COG3391 215 ANRGSNTsnggsntVSVIDL 234
|
|
| NHL_like_3 |
cd14956 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
45-208 |
3.16e-05 |
|
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.
Pssm-ID: 271326 [Multi-domain] Cd Length: 274 Bit Score: 44.58 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 45 PAGRYLVwSDIPNDRLLRWDETTGAVGVFRSP------AGFPNGNTLDGQGRLVTCEQGNRRVTRTEHDGS-VTVIAER- 116
Cdd:cd14956 69 KDGWLYV-ADYWGDRIQVFTLTGELQTIGGSSgsgpgqFNAPRGVAVDADGNLYVADFGNQRIQKFDPDGSfLRQWGGTg 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 117 FEGKRLNSPNDAVVRSDGSVWFSDPE------FGIATDYEGHRGESEIG--------------ARNVYRVDPADGRV-RL 175
Cdd:cd14956 148 IEPGSFNYPRGVAVDPDGTLYVADTYndriqvFDNDGAFLRKWGGRGTGpgqfnypygiaidpDGNVFVADFGNNRIqKF 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907443934 176 VADG---------------FEGPNGLVFSPDeSRLYVSDSLANHIRVF 208
Cdd:cd14956 228 TADGtfltswgspgtgpgqFKNPWGVVVDAD-GTVYVADSNNNRVQRF 274
|
|
| PLN02919 |
PLN02919 |
haloacid dehalogenase-like hydrolase family protein |
159-224 |
1.20e-04 |
|
haloacid dehalogenase-like hydrolase family protein
Pssm-ID: 215497 [Multi-domain] Cd Length: 1057 Bit Score: 43.69 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 159 GARNVYRVDPADGRVRLVA-DGFE--------------GPNGLVFSPDESRLYVSDSLANHIRVFDVRDDGT--LGGGE- 220
Cdd:PLN02919 703 GQHQIWEYNISDGVTRVFSgDGYErnlngssgtstsfaQPSGISLSPDLKELYIADSESSSIRALDLKTGGSrlLAGGDp 782
|
....
gi 1907443934 221 VFAE 224
Cdd:PLN02919 783 TFSD 786
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
45-274 |
1.49e-04 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 42.98 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 45 PAGRYLVWSDipNDRLLR-WDETTGA-VGVFRSPAGF-------PNGNTL-----DGQGRLVTCEQGNRRVTRTEHDGSV 110
Cdd:COG2319 130 PDGKTLASGS--ADGTVRlWDLATGKlLRTLTGHSGAvtsvafsPDGKLLasgsdDGTVRLWDLATGKLLRTLTGHTGAV 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 111 TVIAERFEGKRLnspndAVVRSDGSVWFSDPEFG-IATDYEGHRGEseigarnVYRV---------------------DP 168
Cdd:COG2319 208 RSVAFSPDGKLL-----ASGSADGTVRLWDLATGkLLRTLTGHSGS-------VRSVafspdgrllasgsadgtvrlwDL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 169 ADGRVRLVADGFEGP-NGLVFSPDESRLyVSDSLANHIRVFDVRDDGTLGGGEVFAECANGnfdnIRFDDAGRLWAAALH 247
Cdd:COG2319 276 ATGELLRTLTGHSGGvNSVAFSPDGKLL-ASGSDDGTVRLWDLATGKLLRTLTGHTGAVRS----VAFSPDGKTLASGSD 350
|
250 260 270
....*....|....*....|....*....|
gi 1907443934 248 GG-VHCYDPDGTLLGRVLV--PGTVANVRF 274
Cdd:COG2319 351 DGtVRLWDLATGELLRTLTghTGAVTSVAF 380
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
132-257 |
2.29e-04 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 42.67 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 132 SDGSVWfsdpefgIATDYEGhrgeseigarnVYRVDPADGRVRLVADGFEGPNGLVFSPDESR-----------LYVSDS 200
Cdd:COG3292 323 SDGNLW-------IGTSGGG-----------LYRYDPKTGKFTKFSEDNGLSNNFIRSILEDSdgnlwvgtnggLYRLDP 384
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907443934 201 LANHIRVFD-VRDDGTLGGGEVFAecangnfdnIRFDDAGRLWAAALHGGVHCYDPDG 257
Cdd:COG3292 385 KTGKFTNFThDPDKNGLSSNYINS---------IFEDSDGRLWIGTDGGGLYRYDPKT 433
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
17-274 |
3.57e-04 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 41.82 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 17 RTGRCQAGDSALETLFEGCRWAEGPVYVPAGRYLVWSDIPNDRLLRWDET-------TGAVGVFRSPAGFPNGNTL---- 85
Cdd:COG2319 18 LALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAgallatlLGHTAAVLSVAFSPDGRLLasas 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 86 -DGQGRLVTCEQGNRRVTRTEHDGSVTVIAerF--EGKRLnspndAVVRSDGSVWFSDPEFG--IATdYEGHRGEseiga 160
Cdd:COG2319 98 aDGTVRLWDLATGLLLRTLTGHTGAVRSVA--FspDGKTL-----ASGSADGTVRLWDLATGklLRT-LTGHSGA----- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 161 rnVYRV--DP---------ADGRVRL--VADG-----FEGPNGLV----FSPDESRLyVSDSLANHIRVFDVRDD---GT 215
Cdd:COG2319 165 --VTSVafSPdgkllasgsDDGTVRLwdLATGkllrtLTGHTGAVrsvaFSPDGKLL-ASGSADGTVRLWDLATGkllRT 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907443934 216 LGG--GEVFAecangnfdnIRFDDAGRLWAAA-LHGGVHCYDPDGTLLGRVLV--PGTVANVRF 274
Cdd:COG2319 242 LTGhsGSVRS---------VAFSPDGRLLASGsADGTVRLWDLATGELLRTLTghSGGVNSVAF 296
|
|
| Pgl |
COG2706 |
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism]; |
163-263 |
4.69e-04 |
|
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];
Pssm-ID: 442025 [Multi-domain] Cd Length: 352 Bit Score: 41.43 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 163 VYRVDPADGRVRLV--ADGFEGPNGLVFSPDESRLYVSDSL-ANHIRVFDV-RDDGTLG-GGEVFAECANGNFdnIRFDD 237
Cdd:COG2706 25 VFRLDTATGELTLLglVAALGNPSFLALSPDGRFLYAVNEVdDGGVSAFRIdPADGTLTlLNTVSSGGASPCH--LSVDP 102
|
90 100 110
....*....|....*....|....*....|
gi 1907443934 238 AGR-LWAAALHGG---VHCYDPDGTLLGRV 263
Cdd:COG2706 103 DGRfLFVANYGGGsvsVFPIDADGSLGEPV 132
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
57-256 |
6.12e-04 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 41.51 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 57 NDRLLRWDETTGAVGVFRsPAGFPNGN----TLDGQGRLVTCEQGNRRVTrTEHDGSVTVIAERFEGKRLNSPNDAVVRS 132
Cdd:COG3292 142 SNGLYRYDPKTGKFKRFT-LDGLPSNTitslAEDADGNLWVDSDGNLWIG-TDGNGLYRLDPNTGKFEHITHDPDPNSLS 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 133 DGSVW--FSDPEfG---IATDYEGhrgeseigarnVYRVDPADGRVRLVADG-------------FEGPNG-----LVFS 189
Cdd:COG3292 220 SNSIYslFEDRE-GnlwVGTYGGG-----------LNYLDPNNSKFKSYRHNdpnglsgnsvrsiAEDSDGnlwirLWIG 287
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907443934 190 PDESRLYVSDSLANHIRVFDvrdDGTLGGGEVFAecangnfdnIRFDDAGRLWAAALHGGVHCYDPD 256
Cdd:COG3292 288 TYGGGLFRLDPKTGKFKRYN---PNGLPSNSVYS---------ILEDSDGNLWIGTSGGGLYRYDPK 342
|
|
| NHL_like_3 |
cd14956 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
176-291 |
8.72e-04 |
|
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.
Pssm-ID: 271326 [Multi-domain] Cd Length: 274 Bit Score: 40.34 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 176 VADG-FEGPNGLVFSPDEsRLYVSDSLANHIRVFD-----VRDDGTLGGGevfaecaNGNFD---NIRFDDAGRLWAAAL 246
Cdd:cd14956 7 SGPGqFKDPRGIAVDADD-NVYVADARNGRIQVFDkdgtfLRRFGTTGDG-------PGQFGrprGLAVDKDGWLYVADY 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907443934 247 HGG-VHCYDPDGTLLGRVLVPGTvANVRFGGARrnRMFIAADTTLY 291
Cdd:cd14956 79 WGDrIQVFTLTGELQTIGGSSGS-GPGQFNAPR--GVAVDADGNLY 121
|
|
| PQQ_ABC_repeats |
TIGR03866 |
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ... |
183-230 |
1.13e-03 |
|
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family consist of seven repeats each of the YVTN family beta-propeller repeat (see TIGR02276). Members occur invariably as part of a transport operon that is associated with PQQ-dependent catabolism of alcohols such as phenylethanol.
Pssm-ID: 274824 [Multi-domain] Cd Length: 310 Bit Score: 40.02 E-value: 1.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907443934 183 PNGLVFSPDESRLYVSDSLANHIRVFDVRDD---GTLGGG---EVFAECANGNF 230
Cdd:TIGR03866 43 PRGITFSKDGKLLYVCASDSDTIQVIDPATGevlHTLPSGpdpEQFALHPNGKI 96
|
|
| NHL_like_1 |
cd14953 |
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ... |
63-206 |
1.45e-03 |
|
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat domains is found in a variety of domain architectures. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.
Pssm-ID: 271323 [Multi-domain] Cd Length: 323 Bit Score: 39.82 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 63 WDETTGAVGVFRSPAGFpngnTLDGQGRLVTCEQGNRRVTRTEHDGSVTVIA----ERFEGK------RLNSPNDAVVRS 132
Cdd:cd14953 121 SDDGGATAAQFNYPTGV----AVDAAGNLYVADTGNHRIRKITPDGVVTTVAgtggAGYAGDgpataaQFNNPTGVAVDA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 133 DGSVWfsdpefgIAtDYEGHRgeseigarnVYRVDPaDGRVRLVA---------DG------FEGPNGLVFSPDESrLYV 197
Cdd:cd14953 197 AGNLY-------VA-DRGNHR---------IRKITP-DGVVTTVAgtgtagfsgDGgataaqLNNPTGVAVDAAGN-LYV 257
|
....*....
gi 1907443934 198 SDSLANHIR 206
Cdd:cd14953 258 ADSGNHRIR 266
|
|
| NHL_like_5 |
cd14963 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
68-260 |
1.63e-03 |
|
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.
Pssm-ID: 271333 [Multi-domain] Cd Length: 268 Bit Score: 39.20 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 68 GAVGVFRspagFPNGNTLDGQGRLVTCEQGNRRVTRTEHDGS-VTVIAERFEGKRLNSPNdAVVRSDGSVWFSD--PEFG 144
Cdd:cd14963 50 TGPGEFK----YPYGIAVDSDGNIYVADLYNGRIQVFDPDGKfLKYFPEKKDRVKLISPA-GLAIDDGKLYVSDvkKHKV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 145 IATDYEGhRGESEIGArnvyrvdPADGRVRLVAdgfegPNGLVFSPDeSRLYVSDSLANHIRVFDV------RDDGTLGG 218
Cdd:cd14963 125 IVFDLEG-KLLLEFGK-------PGSEPGELSY-----PNGIAVDED-GNIYVADSGNGRIQVFDKngkfikELNGSPDG 190
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907443934 219 GEVFAecangNFDNIRFDDAGRLWAA-ALHGGVHCYDPDGTLL 260
Cdd:cd14963 191 KSGFV-----NPRGIAVDPDGNLYVVdNLSHRVYVFDEQGKEL 228
|
|
| ScyE_fam |
NF033206 |
ScyD/ScyE family protein; This family includes ScyE, a protein involved in scytomenin ... |
159-197 |
4.09e-03 |
|
ScyD/ScyE family protein; This family includes ScyE, a protein involved in scytomenin biosynthesis and export, and its paralog ScyD. Some members of the family contain a C-terminal PEP-CTERM domain that predictions anchoring to the outer membrane.
Pssm-ID: 467996 [Multi-domain] Cd Length: 330 Bit Score: 38.41 E-value: 4.09e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1907443934 159 GARNVYRVDPaDGRVRLVADGFEGPNGLVFSPDEsRLYV 197
Cdd:NF033206 229 GRARVYRVDP-GGAPTVYATGFTGLTDLAFDPDG-NLYV 265
|
|
| NHL_TRIM32_like |
cd14961 |
NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; ... |
80-267 |
5.45e-03 |
|
NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; The E3 ubiquitin-protein ligase TRIM32 (HT2A) is widely expressed and is responsible for ubiquinating a large variety of targets, including dysbindin (DTNBP1), NPHP7/Glis2, TAp73, and others. TRIM32 promotes disassociation of the plakoglobin-PI3K complex and reduces PI3K-Akt-FoxO signaling. Mutations in TRIM32 have been implemented in the two diverse diseases limb-girdle muscular dystrophy type 2H (LGMD2H) or sarcotubular myopathy (STM) and Bardet-Biedl syndrome type 11 (BBS11). The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.
Pssm-ID: 271331 [Multi-domain] Cd Length: 273 Bit Score: 37.64 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 80 PNGNTLDGQGRLVTCEQGNRRVTRTEHDGSVtviaERFEGKRLNSPNDavVRSdgsvwfsdpEFGIATDYEGHRGESEIG 159
Cdd:cd14961 13 PTGVAVTPTGRVVVADDGNKRIQVFDSDGNC----LQQFGPKGDAGQD--IRY---------PLDVAVTPDGHIVVTDAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 160 ARNVYRVDPaDGRVRL-VADGFEGPNGLVFSPdESRLYVSDSLANHIRVFDVrdDGTLGG-GEVFAECanGNFDNIRFDD 237
Cdd:cd14961 78 DRSVKVFSF-DGRLKLfVRKSFSLPWGVAVNP-SGEILVTDSEAGKLFVLTV--DFKLGIlKKGQKLC--SQLCRPRFVA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907443934 238 AGRLWAAAL------------HGGVHCYDPDGTLLGRVLVPG 267
Cdd:cd14961 152 VSRLGAVAVtehlfangtrssSTRVKVFSSGGQLLGQIDSFG 193
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
45-212 |
6.45e-03 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 37.97 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 45 PAGRYLVWSDipNDRLLR-WDETTGA-VGVFRSPAGF-------PNGNTL-----DGQGRLVTCEQGNRRVTRTEHDGSV 110
Cdd:COG2319 214 PDGKLLASGS--ADGTVRlWDLATGKlLRTLTGHSGSvrsvafsPDGRLLasgsaDGTVRLWDLATGELLRTLTGHSGGV 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 111 TVIAerF--EGKRLnspndAVVRSDGSVWFSDPEFG-IATDYEGHRGE------SEIGAR--------NVYRVDPADGRV 173
Cdd:COG2319 292 NSVA--FspDGKLL-----ASGSDDGTVRLWDLATGkLLRTLTGHTGAvrsvafSPDGKTlasgsddgTVRLWDLATGEL 364
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907443934 174 RLVADGFEGP-NGLVFSPDESRLyVSDSLANHIRVFDVRD 212
Cdd:COG2319 365 LRTLTGHTGAvTSVAFSPDGRTL-ASGSADGTVRLWDLAT 403
|
|
| NHL_like_5 |
cd14963 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
40-208 |
7.47e-03 |
|
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.
Pssm-ID: 271333 [Multi-domain] Cd Length: 268 Bit Score: 37.27 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 40 GPVYVPAGRYLVwSDIPNDRLLRWDET------TGAVGVFRSPAGFPNGNTLDGQGRLVTCEQGNRRVTRTEHDGSVTvi 113
Cdd:cd14963 105 AGLAIDDGKLYV-SDVKKHKVIVFDLEgkllleFGKPGSEPGELSYPNGIAVDEDGNIYVADSGNGRIQVFDKNGKFI-- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 114 aerfegKRLNSpndavvRSDGSVWFSDPEfGIATDYEGHRGESEIGARNVYRVDPaDGRVRLVADG-------FEGPNGL 186
Cdd:cd14963 182 ------KELNG------SPDGKSGFVNPR-GIAVDPDGNLYVVDNLSHRVYVFDE-QGKELFTFGGrgkddgqFNLPNGL 247
|
170 180
....*....|....*....|..
gi 1907443934 187 vFSPDESRLYVSDSLANHIRVF 208
Cdd:cd14963 248 -FIDDDGRLYVTDRENNRVAVY 268
|
|
| NHL_like_3 |
cd14956 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
37-140 |
8.53e-03 |
|
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.
Pssm-ID: 271326 [Multi-domain] Cd Length: 274 Bit Score: 37.26 E-value: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907443934 37 WAEGPVYVPAGRYLVwSDIPNDR----------LLRWDETTGAVGVFRSPAGFpngnTLDGQGRLVTCEQGNRRVTRTEH 106
Cdd:cd14956 155 YPRGVAVDPDGTLYV-ADTYNDRiqvfdndgafLRKWGGRGTGPGQFNYPYGI----AIDPDGNVFVADFGNNRIQKFTA 229
|
90 100 110
....*....|....*....|....*....|....*....
gi 1907443934 107 DGsvtVIAERFEGK-----RLNSPNDAVVRSDGSVWFSD 140
Cdd:cd14956 230 DG---TFLTSWGSPgtgpgQFKNPWGVVVDADGTVYVAD 265
|
|
| |
