|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02241 |
PLN02241 |
glucose-1-phosphate adenylyltransferase |
82-518 |
0e+00 |
|
glucose-1-phosphate adenylyltransferase
Pssm-ID: 215133 [Multi-domain] Cd Length: 436 Bit Score: 925.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 82 PKNVASIILGGGAGTRLFPLTSKRAKPAVPIGGCYRLIDIPMSNCINSGIRKIFILTQFNSFSLNRHLSRTYNFGNGVNF 161
Cdd:PLN02241 1 PKSVAAIILGGGAGTRLFPLTKRRAKPAVPIGGNYRLIDIPMSNCINSGINKIYVLTQFNSASLNRHLSRAYNFGNGGNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 162 GDGFVEVLAATQTSGDAGkkWFQGTADAVRQFIWVFEDAKTKNVEHVLILSGDHLYRMDYMNFVQKHIESNADITVSCLP 241
Cdd:PLN02241 81 GDGFVEVLAATQTPGEKG--WFQGTADAVRQFLWLFEDAKNKNVEEVLILSGDHLYRMDYMDFVQKHRESGADITIACLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 242 MDESRASDFGLLKIDQSGKIIQFSEKPKGDDLKAMQVDTSILGLPPKEAAESPYIASMGVYVFRKEVLLKLLRSSYPTSN 321
Cdd:PLN02241 159 VDESRASDFGLMKIDDTGRIIEFSEKPKGDELKAMQVDTTVLGLSPEEAKEKPYIASMGIYVFKKDVLLKLLRWRFPTAN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 322 DFGSEIIPLAVGE-HNVQAFLFNDYWEDIGTIGSFFDANLALTEQPPKFQFYDQKTPFFTSPRFLPPTKVDKCRILDSIV 400
Cdd:PLN02241 239 DFGSEIIPGAIKEgYNVQAYLFDGYWEDIGTIKSFYEANLALTKQPPKFSFYDPDAPIYTSPRFLPPSKIEDCRITDSII 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 401 SHGCFLRECSVQHSIVGIRSRLESGVELQDTMMMGADFYQTEAEIASLLAEGKVPVGVGQNTKIKNCIIDKNAKIGKNVV 480
Cdd:PLN02241 319 SHGCFLRECKIEHSVVGLRSRIGEGVEIEDTVMMGADYYETEEEIASLLAEGKVPIGIGENTKIRNAIIDKNARIGKNVV 398
|
410 420 430
....*....|....*....|....*....|....*...
gi 259439172 481 IANADGVEEGDRPEEGFHIRSGITVVLKNATIRDGLHI 518
Cdd:PLN02241 399 IINKDGVQEADREEEGYYIRSGIVVILKNAVIPDGTVI 436
|
|
| glgC |
PRK02862 |
glucose-1-phosphate adenylyltransferase; Provisional |
83-515 |
0e+00 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179486 [Multi-domain] Cd Length: 429 Bit Score: 749.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 83 KNVASIILGGGAGTRLFPLTSKRAKPAVPIGGCYRLIDIPMSNCINSGIRKIFILTQFNSFSLNRHLSRTYNFGNgvnFG 162
Cdd:PRK02862 2 KRVLAIILGGGAGTRLYPLTKLRAKPAVPLAGKYRLIDIPISNCINSGINKIYVLTQFNSASLNRHISQTYNFDG---FS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 163 DGFVEVLAATQTsgDAGKKWFQGTADAVRQFIWVFEDaktKNVEHVLILSGDHLYRMDYMNFVQKHIESNADITVSCLPM 242
Cdd:PRK02862 79 GGFVEVLAAQQT--PENPSWFQGTADAVRKYLWHFQE---WDVDEYLILSGDQLYRMDYRLFVQHHRETGADITLAVLPV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 243 DESRASDFGLLKIDQSGKIIQFSEKPKGDDLKAMQVDTSILGLPPKEAAESPYIASMGVYVFRKEVLLKLLRSSyPTSND 322
Cdd:PRK02862 154 DEKDASGFGLMKTDDDGRITEFSEKPKGDELKAMAVDTSRLGLSPEEAKGKPYLASMGIYVFSRDVLFDLLNKN-PEYTD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 323 FGSEIIPLAVGEHNVQAFLFNDYWEDIGTIGSFFDANLALTEQP-PKFQFYDQKTPFFTSPRFLPPTKVDKCRILDSIVS 401
Cdd:PRK02862 233 FGKEIIPEAIRDYKVQSYLFDGYWEDIGTIEAFYEANLALTQQPnPPFSFYDEKAPIYTRARYLPPSKLLDATITESIIA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 402 HGCFLRECSVQHSIVGIRSRLESGVELQDTMMMGADFYQTEAEIASLLAEGKVPVGVGQNTKIKNCIIDKNAKIGKNVVI 481
Cdd:PRK02862 313 EGCIIKNCSIHHSVLGIRSRIESGCTIEDTLVMGADFYESSEEREELRKEGKPPLGIGEGTTIKRAIIDKNARIGNNVRI 392
|
410 420 430
....*....|....*....|....*....|....
gi 259439172 482 ANADGVEEGDRPEEGFHIRSGITVVLKNATIRDG 515
Cdd:PRK02862 393 VNKDNVEEADREDQGFYIRDGIVVVVKNAVIPDG 426
|
|
| glgC |
TIGR02091 |
glucose-1-phosphate adenylyltransferase; This enzyme, glucose-1-phosphate adenylyltransferase, ... |
87-483 |
0e+00 |
|
glucose-1-phosphate adenylyltransferase; This enzyme, glucose-1-phosphate adenylyltransferase, is also called ADP-glucose pyrophosphorylase. The plant form is an alpha2,beta2 heterodimer, allosterically regulated in plants. Both subunits are homologous and included in this model. In bacteria, both homomeric forms of GlgC and more active heterodimers of GlgC and GlgD have been described. This model describes the GlgC subunit only. This enzyme appears in variants of glycogen synthesis pathways that use ADP-glucose, rather than UDP-glucose as in animals. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
Pssm-ID: 273965 [Multi-domain] Cd Length: 361 Bit Score: 522.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 87 SIILGGGAGTRLFPLTSKRAKPAVPIGGCYRLIDIPMSNCINSGIRKIFILTQFNSFSLNRHLSRTYNFGNgvnFGDGFV 166
Cdd:TIGR02091 1 AMVLAGGRGSRLSPLTKRRAKPAVPFGGKYRIIDFPLSNCINSGIRRIGVLTQYKSHSLNRHIQRGWDFDG---FIDGFV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 167 EVLAATQTSGdaGKKWFQGTADAVRQFIWVFEDaktKNVEHVLILSGDHLYRMDYMNFVQKHIESNADITVSCLPMDESR 246
Cdd:TIGR02091 78 TLLPAQQRES--GTDWYQGTADAVYQNLDLIED---YDPEYVLILSGDHIYKMDYEKMLDYHIESGADVTIACIPVPRKE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 247 ASDFGLLKIDQSGKIIQFSEKP-KGDDLKAMQvdtsilglppkeaaeSPYIASMGVYVFRKEVLLKLLR---SSYPTSND 322
Cdd:TIGR02091 153 ASRFGVMQVDEDGRIVDFEEKPaNPPSIPGMP---------------DFALASMGIYIFDKDVLKELLEedaDDPESSHD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 323 FGSEIIPLAVGEHNVQAFLFNDYWEDIGTIGSFFDANLALTEQPPKFQFYDQKTPFFTSPRFLPPTKV--DKCRILDSIV 400
Cdd:TIGR02091 218 FGKDIIPRALEEGSVQAYLFSGYWRDVGTIDSFWEANMDLVSVVPPFDLYDRKWPIYTYNEFLPPAKFvdSDAQVVDSLV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 401 SHGCFLRECSVQHSIVGIRSRLESGVELQDTMMMGAdfyqteaeiasllaegkvpVGVGQNTKIKNCIIDKNAKIGKNVV 480
Cdd:TIGR02091 298 SEGCIISGATVSHSVLGIRVRIGSGSTVEDSVIMGD-------------------VGIGRGAVIRNAIIDKNVRIGEGVV 358
|
...
gi 259439172 481 IAN 483
Cdd:TIGR02091 359 IGN 361
|
|
| GlgC |
COG0448 |
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
84-511 |
7.68e-172 |
|
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];
Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 489.59 E-value: 7.68e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 84 NVASIILGGGAGTRLFPLTSKRAKPAVPIGGCYRLIDIPMSNCINSGIRKIFILTQFNSFSLNRHLSRT--YNFgngvNF 161
Cdd:COG0448 1 KVLAIILAGGRGSRLGPLTKDRAKPAVPFGGKYRIIDFPLSNCVNSGIRRVGVLTQYKSHSLNDHIGSGkpWDL----DR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 162 GDGFVEVLAATQTsgDAGKKWFQGTADAVRQFIWVFEDAktkNVEHVLILSGDHLYRMDYMNFVQKHIESNADITVSCLP 241
Cdd:COG0448 77 KRGGVFILPPYQQ--REGEDWYQGTADAVYQNLDFIERS---DPDYVLILSGDHIYKMDYRQMLDFHIESGADITVACIE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 242 MDESRASDFGLLKIDQSGKIIQFSEKPKGDDlkamqvdtsilglppkeaaesPYIASMGVYVFRKEVLLKLLRSSYPTS- 320
Cdd:COG0448 152 VPREEASRFGVMEVDEDGRITEFEEKPKDPK---------------------SALASMGIYVFNKDVLIELLEEDAPNSs 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 321 NDFGSEIIPLAVGEHNVQAFLFNDYWEDIGTIGSFFDANLALTEQPPKFQFYDQKTPFFTSPRFLPPTK-VDKCRILDSI 399
Cdd:COG0448 211 HDFGKDIIPRLLDRGKVYAYEFDGYWRDVGTIDSYYEANMDLLDPEPEFNLYDPEWPIYTKQKDLPPAKfVRGGKVKNSL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 400 VSHGCFLrECSVQHSIVGIRSRLESGVELQDTMMMGAdfyqteaeiasllaegkvpVGVGQNTKIKNCIIDKNAKIGKNV 479
Cdd:COG0448 291 VSNGCII-SGTVENSVLFRGVRVESGAVVENSVIMPG-------------------VVIGEGAVIENAIIDKNVVIPPGV 350
|
410 420 430
....*....|....*....|....*....|..
gi 259439172 480 VIanadgVEEGDRPEEGFHIRSGITVVLKNAT 511
Cdd:COG0448 351 VI-----GEDPEEDRKRFTVSSGIVVVGKGAV 377
|
|
| glgC |
PRK00844 |
glucose-1-phosphate adenylyltransferase; Provisional |
83-512 |
2.25e-122 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 364.53 E-value: 2.25e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 83 KNVASIILGGGAGTRLFPLTSKRAKPAVPIGGCYRLIDIPMSNCINSGIRKIFILTQFNSFSLNRHLSRTYNFgngVNFG 162
Cdd:PRK00844 4 PKVLAIVLAGGEGKRLMPLTADRAKPAVPFGGSYRLIDFVLSNLVNSGYLRIYVLTQYKSHSLDRHISQTWRL---SGLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 163 DGFVEVLAATQTSgdaGKKWFQGTADAVRQFIWVFEDAKTknvEHVLILSGDHLYRMDYMNFVQKHIESNADITVSCLPM 242
Cdd:PRK00844 81 GNYITPVPAQQRL---GKRWYLGSADAIYQSLNLIEDEDP---DYVVVFGADHVYRMDPRQMVDFHIESGAGVTVAAIRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 243 DESRASDFGLLKIDQSGKIIQFSEKPKgdDLKamqvdtsilGLP--PKEAaespyIASMGVYVFRKEVLLKLLR---SSY 317
Cdd:PRK00844 155 PREEASAFGVIEVDPDGRIRGFLEKPA--DPP---------GLPddPDEA-----LASMGNYVFTTDALVDALRrdaADE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 318 PTSNDFGSEIIPLAVGEHNVQAFLFND------------YWEDIGTIGSFFDANLALTEQPPKFQFYDQKTPFFTSPRFL 385
Cdd:PRK00844 219 DSSHDMGGDIIPRLVERGRAYVYDFSTnevpgaterdrgYWRDVGTIDAYYDAHMDLLSVHPVFNLYNREWPIYTSSPNL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 386 PPTKV-----DKCRILDSIVSHGCFLRECSVQHSIVGIRSRLESGVELQDTMMMGAdfyqteaeiasllaegkvpVGVGQ 460
Cdd:PRK00844 299 PPAKFvdgggRVGSAQDSLVSAGSIISGATVRNSVLSPNVVVESGAEVEDSVLMDG-------------------VRIGR 359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 259439172 461 NTKIKNCIIDKNAKIGKNVVIanadGVE-EGDRpeEGFHI-RSGITVVLKNATI 512
Cdd:PRK00844 360 GAVVRRAILDKNVVVPPGATI----GVDlEEDR--RRFTVsEGGIVVVPKGQRV 407
|
|
| glgC |
PRK00725 |
glucose-1-phosphate adenylyltransferase; Provisional |
69-506 |
2.63e-121 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234824 [Multi-domain] Cd Length: 425 Bit Score: 362.62 E-value: 2.63e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 69 ESHEPLLRTQNAdPKNVASIILGGGAGTRLFPLTSKRAKPAVPIGGCYRLIDIPMSNCINSGIRKIFILTQFNSFSLNRH 148
Cdd:PRK00725 1 EKNDSLMLARQL-TRDTLALILAGGRGSRLKELTDKRAKPAVYFGGKFRIIDFALSNCINSGIRRIGVLTQYKAHSLIRH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 149 LSRTYNFGNGvNFGDgFVEVLAATQTSgdAGKKWFQGTADAVRQFIWVFEDAktkNVEHVLILSGDHLYRMDYMNFVQKH 228
Cdd:PRK00725 80 IQRGWSFFRE-ELGE-FVDLLPAQQRV--DEENWYRGTADAVYQNLDIIRRY---DPKYVVILAGDHIYKMDYSRMLADH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 229 IESNADITVSCLPMDESRASDFGLLKIDQSGKIIQFSEKPKgdDLKAMQVDtsilglpPKEAaespyIASMGVYVFRKEV 308
Cdd:PRK00725 153 VESGADCTVACLEVPREEASAFGVMAVDENDRITAFVEKPA--NPPAMPGD-------PDKS-----LASMGIYVFNADY 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 309 LLKLLR---SSYPTSNDFGSEIIPLAVGEHNVQAFLFND-----------YWEDIGTIGSFFDANLALTEQPPKFQFYDQ 374
Cdd:PRK00725 219 LYELLEedaEDPNSSHDFGKDIIPKIVEEGKVYAHPFSDscvrsdpeeepYWRDVGTLDAYWQANLDLASVTPELDLYDR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 375 KTPFFTSPRFLPPTK----VDKCR--ILDSIVSHGCFLRECSVQHSIVGIRSRLESGVELQDTMMMgadfyqteaeiasl 448
Cdd:PRK00725 299 NWPIWTYQEQLPPAKfvfdRSGRRgmAINSLVSGGCIISGAVVRRSVLFSRVRVNSFSNVEDSVLL-------------- 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 259439172 449 laegkvP-VGVGQNTKIKNCIIDKNAKIGKNVVIanadgveeGDRPEEG---FHI-RSGITVV 506
Cdd:PRK00725 365 ------PdVNVGRSCRLRRCVIDRGCVIPEGMVI--------GEDPEEDakrFRRsEEGIVLV 413
|
|
| glgC |
PRK05293 |
glucose-1-phosphate adenylyltransferase; Provisional |
83-518 |
5.90e-99 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 303.71 E-value: 5.90e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 83 KNVASIILGGGAGTRLFPLTSKRAKPAVPIGGCYRLIDIPMSNCINSGIRKIFILTQFNSFSLNRHLsrtynfGNGVNFG 162
Cdd:PRK05293 2 KEMLAMILAGGQGTRLGKLTKNIAKPAVPFGGKYRIIDFTLSNCANSGIDTVGVLTQYQPLELNNHI------GIGSPWD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 163 ----DGFVEVLAATQTSgdAGKKWFQGTADAVRQFIWVFEDaktKNVEHVLILSGDHLYRMDYMNFVQKHIESNADITVS 238
Cdd:PRK05293 76 ldriNGGVTILPPYSES--EGGKWYKGTAHAIYQNIDYIDQ---YDPEYVLILSGDHIYKMDYDKMLDYHKEKEADVTIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 239 CL--PMDEsrASDFGLLKIDQSGKIIQFSEKPKGddlkamqvdtsilglpPKEAaespyIASMGVYVFRKEVLLKLLRSS 316
Cdd:PRK05293 151 VIevPWEE--ASRFGIMNTDENMRIVEFEEKPKN----------------PKSN-----LASMGIYIFNWKRLKEYLIED 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 317 YPT---SNDFGSEIIPLAVGE-HNVQAFLFNDYWEDIGTIGSFFDANLALTEQPPKFQFYDQKTPFFTSPRFLPPTKV-D 391
Cdd:PRK05293 208 EKNpnsSHDFGKNVIPLYLEEgEKLYAYPFKGYWKDVGTIESLWEANMELLRPENPLNLFDRNWRIYSVNPNLPPQYIaE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 392 KCRILDSIVSHGCFLrECSVQHSIvgirsrLESGVElqdtmmmgadfyqteaeiasllaegkvpvgVGQNTKIKNCIIDK 471
Cdd:PRK05293 288 NAKVKNSLVVEGCVV-YGTVEHSV------LFQGVQ------------------------------VGEGSVVKDSVIMP 330
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 259439172 472 NAKIGKNVVIANADgVEEGDRPEEGFHIRSG---ITVVLKNATIRDGLHI 518
Cdd:PRK05293 331 GAKIGENVVIERAI-IGENAVIGDGVIIGGGkevITVIGENEVIGVGTVI 379
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
88-363 |
3.32e-95 |
|
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.
Pssm-ID: 425709 [Multi-domain] Cd Length: 243 Bit Score: 289.15 E-value: 3.32e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 88 IILGGGAGTRLFPLTSKRAKPAVPIGGCYRLIDIPMSNCINSGIRK-IFILTQFNSFSLNRHLSRTYNFGngvnfgdgfV 166
Cdd:pfam00483 3 IILAGGSGTRLWPLTRTLAKPLVPVGGKYPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFG---------V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 167 EVLAATQTSGDagkkwfqGTADAVRQFIWVFEDAKTknveHVLILSGDHLYRMDYMNFVQKHIESNADITVSCLPMDESR 246
Cdd:pfam00483 74 QITYALQPEGK-------GTAPAVALAADFLGDEKS----DVLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGIVPVEP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 247 ASDFGLLKIDQSGKIIQFSEKPKGDDLkamqvdtsilglppkeaaesPYIASMGVYVFRKEVLLKLLR--SSYPTSNDFG 324
Cdd:pfam00483 143 PTGYGVVEFDDNGRVIRFVEKPKLPKA--------------------SNYASMGIYIFNSGVLDFLAKylEELKRGEDEI 202
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 259439172 325 SEIIPLAVGEHNVQ-AFLFNDY-WEDIGTIGSFFDANLALT 363
Cdd:pfam00483 203 TDILPKALEDGKLAyAFIFKGYaWLDVGTWDSLWEANLFLL 243
|
|
| ADP_Glucose_PP |
cd02508 |
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ... |
88-349 |
3.59e-86 |
|
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP. ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. While a homotetramer in bacteria, in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits. There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. It is a subfamily of a very diverse glycosy transferase family 2.
Pssm-ID: 133002 [Multi-domain] Cd Length: 200 Bit Score: 264.02 E-value: 3.59e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 88 IILGGGAGTRLFPLTSKRAKPAVPIGGCYRLIDIPMSNCINSGIRKIFILTQFNSFSLNRHLSRTYNFgnGVNFGDGFVE 167
Cdd:cd02508 2 IILAGGEGTRLSPLTKKRAKPAVPFGGRYRLIDFPLSNMVNSGIRNVGVLTQYKSRSLNDHLGSGKEW--DLDRKNGGLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 168 VLAATQtsgDAGKKWFQGTADAVRQFIWVFEDAKtknVEHVLILSGDHLYRMDYMNFVQKHIESNADITVSclpmdesra 247
Cdd:cd02508 80 ILPPQQ---RKGGDWYRGTADAIYQNLDYIERSD---PEYVLILSGDHIYNMDYREMLDFHIESGADITVV--------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 248 sdfgllkidqsgkiiqfsekpkgddlkamqvdtsilglppkeaaespYIASMGVYVFRKEVLLKLLRSSY-PTSNDFGSE 326
Cdd:cd02508 145 -----------------------------------------------YKASMGIYIFSKDLLIELLEEDAaDGSHDFGKD 177
|
250 260
....*....|....*....|...
gi 259439172 327 IIPLAVGEHNVQAFLFNDYWEDI 349
Cdd:cd02508 178 IIPAMLKKLKIYAYEFNGYWADI 200
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
88-350 |
7.51e-41 |
|
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.
Pssm-ID: 133024 [Multi-domain] Cd Length: 217 Bit Score: 146.19 E-value: 7.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 88 IILGGGAGTRLFPLTSKRAKPAVPIGGcYRLIDIPMSNCINSGIRKIFILTQFNSFSLNRHLSRTYNFGNGVNFgdgfve 167
Cdd:cd04181 2 VILAAGKGTRLRPLTDTRPKPLLPIAG-KPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVNIEY------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 168 vlaATQTSGdagkkwfQGTADAVRQFIWVFEDaktknvEHVLILSGDHLYRMDYMNFVQKHIESNADITVSCLPMDesRA 247
Cdd:cd04181 75 ---VVQEEP-------LGTAGAVRNAEDFLGD------DDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVE--DP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 248 SDFGLLKIDQSGKIIQFSEKPKgddlkamqvdtsilglppkeaAESPYIASMGVYVFRKEVlLKLLRSSYPTSNDFGSEI 327
Cdd:cd04181 137 SRYGVVELDDDGRVTRFVEKPT---------------------LPESNLANAGIYIFEPEI-LDYIPEILPRGEDELTDA 194
|
250 260
....*....|....*....|...
gi 259439172 328 IPLAVGEHNVQAFLFNDYWEDIG 350
Cdd:cd04181 195 IPLLIEEGKVYGYPVDGYWLDIG 217
|
|
| glgD |
TIGR02092 |
glucose-1-phosphate adenylyltransferase, GlgD subunit; This family is GlgD, an apparent ... |
83-482 |
2.38e-36 |
|
glucose-1-phosphate adenylyltransferase, GlgD subunit; This family is GlgD, an apparent regulatory protein that appears in an alpha2/beta2 heterotetramer with GlgC (glucose-1-phosphate adenylyltransferase, TIGR02091) in a subset of bacteria that use GlgC for glycogen biosynthesis. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
Pssm-ID: 273966 [Multi-domain] Cd Length: 369 Bit Score: 138.67 E-value: 2.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 83 KNVASIILGGGAGTRLFPLTSKRAKPAVPIGGCYRLIDIPMSNCINSGIRKIFILTQFNS-FSLNRHLsrtynfGNGVNF 161
Cdd:TIGR02092 1 NKMSAIINLTESSKNLSPLTKVRPLASLPFGGRYRLIDFPLSNMVNAGIRNVFIFFKNKErQSLFDHL------GSGREW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 162 G-----DG-FVEVLAATQTSGDAGKKWFQGTadavRQFIwvfedaKTKNVEHVLILSGDHLYRMDYMNFVQKHIESNADI 235
Cdd:TIGR02092 75 DlhrkrDGlFVFPYNDRDDLSEGGKRYFSQN----LEFL------KRSTSEYTVVLNSHMVCNIDLKAVLKYHEETGKDI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 236 TVSCLPMDESRASDF-GLLKIDQSGKIiqfsekpkgddlkamqvdTSILGLPPKEAAESpyiASMGVYVFRKEVLLKLLR 314
Cdd:TIGR02092 145 TVVYKKVKPADASEYdTILRFDESGKV------------------KSIGQNLNPEEEEN---ISLDIYIVSTDLLIELLY 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 315 SS----YPTSNdfgSEIIPLAVGEHNVQAFLFNDYWEDIGTIGSFFDANLALTEqPPKFQ--FYDQKTPFFTSPRFLPPT 388
Cdd:TIGR02092 204 ECiqrgKLTSL---EELIRENLKELNINAYEYTGYLANINSVKSYYKANMDLLD-PQNFQslFYSSQGPIYTKVKDEPPT 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 389 K-VDKCRILDSIVSHGCFLrECSVQHSIVGIRSRLESGVELQDTMMMgadfyqTEAEIasllaegkvpvgvGQNTKIKNC 467
Cdd:TIGR02092 280 YyAENSKVENSLVANGCII-EGKVENSILSRGVHVGKDALIKNCIIM------QRTVI-------------GEGAHLENV 339
|
410
....*....|....*
gi 259439172 468 IIDKNAKIGKNVVIA 482
Cdd:TIGR02092 340 IIDKDVVIEPNVKIA 354
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
88-362 |
3.70e-34 |
|
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440821 [Multi-domain] Cd Length: 238 Bit Score: 128.73 E-value: 3.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 88 IILGGGAGTRLFPLTSKRAKPAVPIGGcyR-LIDIPMSNCINSGIRKIFILTqfnsfslnRHLS---RTYnFGNGVNFGd 163
Cdd:COG1208 3 VILAGGLGTRLRPLTDTRPKPLLPVGG--KpLLEHILERLAAAGITEIVINV--------GYLAeqiEEY-FGDGSRFG- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 164 gfVEVLAATQtsgdaGKKWfqGTADAVRQFIWVFEDaktknvEHVLILSGDHLYRMDYMNFVQKHIESNADITVSCLPMD 243
Cdd:COG1208 71 --VRITYVDE-----GEPL--GTGGALKRALPLLGD------EPFLVLNGDILTDLDLAALLAFHREKGADATLALVPVP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 244 esRASDFGLLKIDQSGKIIQFSEKPKGddlkamqvdtsilglppkeaAESPYIaSMGVYVFRKEVLlkllrSSYPTSNDF 323
Cdd:COG1208 136 --DPSRYGVVELDGDGRVTRFVEKPEE--------------------PPSNLI-NAGIYVLEPEIF-----DYIPEGEPF 187
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 259439172 324 G-SEIIPLAVGEHNVQAFLFNDYWEDIGTIGSFFDANLAL 362
Cdd:COG1208 188 DlEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALL 227
|
|
| LbH_G1P_AT_C |
cd04651 |
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ... |
386-512 |
8.11e-30 |
|
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.
Pssm-ID: 100056 [Multi-domain] Cd Length: 104 Bit Score: 112.56 E-value: 8.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 386 PPTKVDKCRILDSIVSHGCFLRECSVQHSIVGIRSRLESGVELQDTMMMGAdfyqteaeiasllaegkvpVGVGQNTKIK 465
Cdd:cd04651 1 PPYIGRRGEVKNSLVSEGCIISGGTVENSVLFRGVRVGSGSVVEDSVIMPN-------------------VGIGRNAVIR 61
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 259439172 466 NCIIDKNAKIGKNVVIANADGVEEGdrpeEGFHIRSGITVVLKNATI 512
Cdd:cd04651 62 RAIIDKNVVIPDGVVIGGDPEEDRA----RFYVTEDGIVVVGKGMVI 104
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
88-358 |
2.83e-21 |
|
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars.
Pssm-ID: 133065 [Multi-domain] Cd Length: 223 Bit Score: 92.23 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 88 IILGGGAGTRLFPLTSKRAKPAVPIGGcYRLIDIPMSNCINSGIRKIFILTQFNSFSLNRHLSRTYNFGNGVNFGDGfvE 167
Cdd:cd06915 2 VILAGGLGTRLRSVVKDLPKPLAPVAG-RPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIYYVIE--P 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 168 VLAatqtsgdagkkwfqGTADAVRQFIWVFEDaktknvEHVLILSGDHLYRMDYMNFVQKHIESNADITVSCLPMDEsrA 247
Cdd:cd06915 79 EPL--------------GTGGAIKNALPKLPE------DQFLVLNGDTYFDVDLLALLAALRASGADATMALRRVPD--A 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 248 SDFGLLKIDQSGKIIQFSEKPKGddlkamqvdtsilglppkeaAESPYIASmGVYVFRKEVLLKLLRSSYptsnDFGSEI 327
Cdd:cd06915 137 SRYGNVTVDGDGRVIAFVEKGPG--------------------AAPGLING-GVYLLRKEILAEIPADAF----SLEADV 191
|
250 260 270
....*....|....*....|....*....|.
gi 259439172 328 IPLAVGEHNVQAFLFNDYWEDIGTIGSFFDA 358
Cdd:cd06915 192 LPALVKRGRLYGFEVDGYFIDIGIPEDYARA 222
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
88-359 |
3.08e-17 |
|
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.
Pssm-ID: 133048 [Multi-domain] Cd Length: 220 Bit Score: 80.63 E-value: 3.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 88 IILGGGAGTRLFPLTSKRAKPAVPIGGcYRLIDIPMSNCINSGIRKIFIltqfnsfSLNrHLSRT--YNFGNGVNFGDGF 165
Cdd:cd06426 2 VIMAGGKGTRLRPLTENTPKPMLKVGG-KPILETIIDRFIAQGFRNFYI-------SVN-YLAEMieDYFGDGSKFGVNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 166 VEVLaatqtsgdagKKWFQGTADAVRQFiwvfedaKTKNVEHVLILSGDHLYRMDYMNFVQKHIESNADITVSClpmdes 245
Cdd:cd06426 73 SYVR----------EDKPLGTAGALSLL-------PEKPTDPFLVMNGDILTNLNYEHLLDFHKENNADATVCV------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 246 RASD----FGLLKIDQsGKIIQFSEKPkgddlkamqvdtsilglppkeaaESPYIASMGVYVFRKEVLLKLLRSSYPTSN 321
Cdd:cd06426 130 REYEvqvpYGVVETEG-GRITSIEEKP-----------------------THSFLVNAGIYVLEPEVLDLIPKNEFFDMP 185
|
250 260 270
....*....|....*....|....*....|....*...
gi 259439172 322 DFGSEIIplAVGEhNVQAFLFNDYWEDIGTIGSFFDAN 359
Cdd:cd06426 186 DLIEKLI--KEGK-KVGVFPIHEYWLDIGRPEDYEKAN 220
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
88-359 |
1.77e-15 |
|
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.
Pssm-ID: 133032 [Multi-domain] Cd Length: 236 Bit Score: 75.68 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 88 IILGGGAGTRLFPLTSKRAKPAVPIGGcYRLIDIPMSNCINSGIRKIFILTqfnsfSLNRHLSRTYnFGNGVNFGDGFVE 167
Cdd:cd04189 4 LILAGGKGTRLRPLTYTRPKQLIPVAG-KPIIQYAIEDLREAGIEDIGIVV-----GPTGEEIKEA-LGDGSRFGVRITY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 168 VLAATQtsgdagkkwfQGTADAV---RQFIwvfedaktKNVEHVLILsGDHLYRMDYMNFVQKHIESNADITVSCLPMDE 244
Cdd:cd04189 77 ILQEEP----------LGLAHAVlaaRDFL--------GDEPFVVYL-GDNLIQEGISPLVRDFLEEDADASILLAEVED 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 245 SRAsdFGLLKIDQsGKIIQFSEKPKgddlkamqvdtsilglPPKeaaeSPYiASMGVYVFRKEVLlkllrssyptsnDFG 324
Cdd:cd04189 138 PRR--FGVAVVDD-GRIVRLVEKPK----------------EPP----SNL-ALVGVYAFTPAIF------------DAI 181
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 259439172 325 SEIIPLAVGE--------------HNVQAFLFNDYWEDIGTIGSFFDAN 359
Cdd:cd04189 182 SRLKPSWRGEleitdaiqwlidrgRRVGYSIVTGWWKDTGTPEDLLEAN 230
|
|
| rmlA_long |
TIGR01208 |
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ... |
88-478 |
1.06e-13 |
|
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced. Alternate name: dTDP-D-glucose synthase
Pssm-ID: 273500 [Multi-domain] Cd Length: 353 Bit Score: 72.43 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 88 IILGGGAGTRLFPLTSKRAKPAVPIGG----CYRLIDIpmsncINSGIRKI-FILTQFNSFSLNRHLsrtynfGNGVNFG 162
Cdd:TIGR01208 3 LILAAGKGTRLRPLTFTRPKQLIPVANkpilQYAIEDL-----AEAGITDIgIVVGPVTGEEIKEIV------GEGERFG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 163 DGFVEVLAATQtsgdagkkwfQGTADAVRQFI-WVFEDaktknvEHVLILsGDHLYRMDYMNFVqKHIEsNADITVSCLP 241
Cdd:TIGR01208 72 AKITYIVQGEP----------LGLAHAVYTARdFLGDD------DFVVYL-GDNLIQDGISRFV-KSFE-EKDYDALILL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 242 MDESRASDFGLLKIDQSGKIIQFSEKPKGddlkamqvdtsilglPPKEaaespyIASMGVYVFRkevllkllrssyPTSN 321
Cdd:TIGR01208 133 TKVRDPTAFGVAVLEDGKRILKLVEKPKE---------------PPSN------LAVVGLYMFR------------PLIF 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 322 DFGSEIIPLAVGEHNV----QAFLFNDY----------WEDIGTIGSFFDAN-LALTEQPPKFQFYDQKTpfftspRFLP 386
Cdd:TIGR01208 180 EAIKNIKPSWRGELEItdaiQWLIEKGYkvggskvtgwWKDTGKPEDLLDANrLILDEVEREVQGVDDES------KIRG 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 387 PTKVDK-CRILDSIVsHG-------CFLRECSVQH-SIVGIRSRLESGvELQDTMMMgadfyqTEAEIasllaegkvpvg 457
Cdd:TIGR01208 254 RVVVGEgAKIVNSVI-RGpavigedCIIENSYIGPyTSIGEGVVIRDA-EVEHSIVL------DESVI------------ 313
|
410 420
....*....|....*....|.
gi 259439172 458 VGQNTKIKNCIIDKNAKIGKN 478
Cdd:TIGR01208 314 EGVQARIVDSVIGKKVRIKGN 334
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
88-359 |
1.47e-12 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 68.19 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 88 IILGGGAGTRLFPLTSKRAKPAVPIGGcyR-LIDIPMSNCINSGIRKIFILTqfnsfslnrhlsrtynfgnGVNFGDGFV 166
Cdd:COG1209 4 IILAGGSGTRLRPLTLTVSKQLLPVYD--KpMIYYPLSTLMLAGIREILIIS-------------------TPEDGPQFE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 167 EVLaatqtsGDaGKKW-------FQ----GTADAV---RQFIwvfEDAKTknvehVLILsGDHLYRMDYM-NFVQKHIES 231
Cdd:COG1209 63 RLL------GD-GSQLgikisyaVQpeplGLAHAFiiaEDFI---GGDPV-----ALVL-GDNIFYGDGLsELLREAAAR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 232 NADITVSCLPMDESRAsdFGLLKIDQSGKIIQFSEKPKgddlkamqvdtsilglPPKeaaeSPYiASMGVYVFRKEVL-- 309
Cdd:COG1209 127 ESGATIFGYKVEDPER--YGVVEFDEDGRVVSLEEKPK----------------EPK----SNL-AVTGLYFYDNDVVei 183
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 259439172 310 LKLLRSS----YptsndfgsEI-----IPLAVGEHNVQAFLFNDYWEDIGTIGSFFDAN 359
Cdd:COG1209 184 AKNLKPSargeL--------EItdanqAYLERGKLVVELLGRGFAWLDTGTHESLLEAN 234
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
88-359 |
3.10e-11 |
|
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short form of glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.
Pssm-ID: 133019 [Multi-domain] Cd Length: 240 Bit Score: 63.36 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 88 IILGGGAGTRLFPLTSKRAKPAVPIGGcYRLIDIPMSNCINSGIRKIFILTQfnsfslNRHLSRTYN-FGNGVNFGdgfV 166
Cdd:cd02538 4 IILAGGSGTRLYPLTKVVSKQLLPVYD-KPMIYYPLSTLMLAGIREILIIST------PEDLPLFKElLGDGSDLG---I 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 167 EVLAATQTSGDagkkwfqGTADAV---RQFIwvfedaKTKNVehVLILsGDHLYR-MDYMNFVQKHIESNADITVSCLPM 242
Cdd:cd02538 74 RITYAVQPKPG-------GLAQAFiigEEFI------GDDPV--CLIL-GDNIFYgQGLSPILQRAAAQKEGATVFGYEV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 243 -DESRasdFGLLKIDQSGKIIQFSEKPKGddlkamqvdtsilglpPKeaaeSPYiASMGVYVFRKEVLlkllrssyptsn 321
Cdd:cd02538 138 nDPER---YGVVEFDENGRVLSIEEKPKK----------------PK----SNY-AVTGLYFYDNDVF------------ 181
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 259439172 322 DFGSEIIPLAVGEH---------------NVQAFLFNDYWEDIGTIGSFFDAN 359
Cdd:cd02538 182 EIAKQLKPSARGELeitdvnneylekgklSVELLGRGFAWLDTGTHESLLEAS 234
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
88-309 |
3.96e-08 |
|
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133041 [Multi-domain] Cd Length: 214 Bit Score: 53.82 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 88 IILGGGAGTRLFPLTSKRAKPAVPIGGcYRLIDIPMSNCINSGIRKIFILTQFNSFSLNRHLSRTYNFGNGVnfgdgfVE 167
Cdd:cd04198 4 VILAGGGGSRLYPLTDNIPKALLPVAN-KPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFPLNLKQ------KL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 168 VLAATQTSGDAgkkwfqGTADAVRQfiwvFEDAKTKNvehVLILSGD-----HLYRMdymnfVQKHIESNAdiTVSCLpM 242
Cdd:cd04198 77 DEVTIVLDEDM------GTADSLRH----IRKKIKKD---FLVLSCDlitdlPLIEL-----VDLHRSHDA--SLTVL-L 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 243 DESRASDFGLLKIDQSGKIIQfseKPKGDDLKAMQvdtSILGLPPKEAAESPYIASMG------------------VYVF 304
Cdd:cd04198 136 YPPPVSSEQKGGKGKSKKADE---RDVIGLDEKTQ---RLLFITSEEDLDEDLELRKSllkrhprvtittklldahVYIF 209
|
....*
gi 259439172 305 RKEVL 309
Cdd:cd04198 210 KRWVL 214
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
88-314 |
1.70e-07 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 52.17 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 88 IILGGGAGTRLFPLTSKRAKPAVPIGGcYRLIDIPMSNCINSGIRKIFILTqfnsfslnrhlsrtynfgngvnfgdGFve 167
Cdd:COG1213 3 VILAAGRGSRLGPLTDDIPKCLVEIGG-KTLLERQLEALAAAGIKDIVVVT-------------------------GY-- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 168 vlaatqtSGDAGKKWFQGTADAVRqfiWVFED--AKTKNV-----------EHVLILSGDHLYRmDYMnfVQKHIESNAD 234
Cdd:COG1213 55 -------KAELIEEALARPGPDVT---FVYNPdyDETNNIyslwlarealdEDFLLLNGDVVFD-PAI--LKRLLASDGD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 235 ITVSCLPMDESRASDFGLLKIDQSGKIIQFSEKPKGDDlkamqvdtsILGlppkEaaespyiaSMGVYVFRKEVLLKLLR 314
Cdd:COG1213 122 IVLLVDRKWEKPLDEEVKVRVDEDGRIVEIGKKLPPEE---------ADG----E--------YIGIFKFSAEGAAALRE 180
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
88-309 |
4.97e-07 |
|
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133001 [Multi-domain] Cd Length: 216 Bit Score: 50.71 E-value: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 88 IILGGGAGTRLFPLTSKRAKPAVPIGGCYrLIDIPMSNCINSGIRKIFILTQFNSFSLNRHLSRTynFGNGVNFGDGFVE 167
Cdd:cd02507 4 VVLADGFGSRFLPLTSDIPKALLPVANVP-LIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKS--KWSSLSSKMIVDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 168 VLAATQTSgdagkkwfQGTADAVRqfiwvfeDAKTKNVEHVLILSGDHLYRMDY--MNFVQKHIESNADITVSCL----- 240
Cdd:cd02507 81 ITSDLCES--------AGDALRLR-------DIRGLIRSDFLLLSCDLVSNIPLseLLEERRKKDKNAIATLTVLlaspp 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 259439172 241 -PMDESRASD----FGLLKIDQSGKIIQFSEKPKGDDLkaMQVDTSILGLPPKEAAESPYIASmGVYVFRKEVL 309
Cdd:cd02507 146 vSTEQSKKTEeedvIAVDSKTQRLLLLHYEEDLDEDLE--LIIRKSLLSKHPNVTIRTDLLDC-HIYICSPDVL 216
|
|
| LbH_eIF2B_epsilon |
cd05787 |
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
458-515 |
9.83e-07 |
|
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.
Pssm-ID: 100061 [Multi-domain] Cd Length: 79 Bit Score: 46.42 E-value: 9.83e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 259439172 458 VGQNTKIKNCIIDKNAKIGKNVVIANA---DGVEEGDrpeeGFHIRSGI----TVVLKNATIRDG 515
Cdd:cd05787 8 IGEGTTIKNSVIGRNCKIGKNVVIDNSyiwDDVTIED----GCTIHHSIvadgAVIGKGCTIPPG 68
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
88-350 |
1.38e-06 |
|
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.
Pssm-ID: 133020 [Multi-domain] Cd Length: 229 Bit Score: 49.44 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 88 IILGGGAGTRLFpltSKRAKPAVPIGGcyR-LIDIPMSNCINSGIRKIFILTQFNSFSLNRHLSrtynfGNGVNFgdgfv 166
Cdd:cd02540 2 VILAAGKGTRMK---SDLPKVLHPLAG--KpMLEHVLDAARALGPDRIVVVVGHGAEQVKKALA-----NPNVEF----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 167 eVLAATQtsgdagkkwfQGTADAVRQFIwvfeDAKTKNVEHVLILSGDH-LYRMDYM-NFVQKHIESNADITVSCLPMDe 244
Cdd:cd02540 67 -VLQEEQ----------LGTGHAVKQAL----PALKDFEGDVLVLYGDVpLITPETLqRLLEAHREAGADVTVLTAELE- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 245 sRASDFGLLKIDQSGKIIQFSEkpkgddlkamQVDTSILGLPPKEaaespyiASMGVYVFRKEVLLKLLRSsypTSND-- 322
Cdd:cd02540 131 -DPTGYGRIIRDGNGKVLRIVE----------EKDATEEEKAIRE-------VNAGIYAFDAEFLFEALPK---LTNNna 189
|
250 260 270
....*....|....*....|....*....|...
gi 259439172 323 ----FGSEIIPLAVGE-HNVQAFLFNDYWEDIG 350
Cdd:cd02540 190 qgeyYLTDIIALAVADgLKVAAVLADDEEEVLG 222
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
89-136 |
7.64e-06 |
|
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.
Pssm-ID: 133044 [Multi-domain] Cd Length: 221 Bit Score: 47.18 E-value: 7.64e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 259439172 89 ILGGGAGTRLFPLTSKRAKPAVPIGGcyR-LIDIPMSNCINSGIRKIFI 136
Cdd:cd06422 4 ILAAGLGTRMRPLTDTRPKPLVPVAG--KpLIDHALDRLAAAGIRRIVV 50
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
88-349 |
1.60e-05 |
|
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.
Pssm-ID: 133014 [Multi-domain] Cd Length: 229 Bit Score: 46.07 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 88 IILGGGAGTRLFPLTSKRAKPAVPIGGcYRLIDIPMSNCINSGIRKIFILTQFNSFSLNRHLSRTYNFGNGVNfgdgfvE 167
Cdd:cd02523 2 IILAAGRGSRLRPLTEDRPKCLLEING-KPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNIKFVYN------P 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 168 VLAATQTSGDAGKkwfqgtadavrqfiwvfedAKTKNVEHVLILSGDHLYRmdyMNFVQKHIESNADITVSCLPMDESRA 247
Cdd:cd02523 75 DYAETNNIYSLYL-------------------ARDFLDEDFLLLEGDVVFD---PSILERLLSSPADNAILVDKKTKEWE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 248 SDFGLLKIDQsGKIIQFSEKPKGDDlkamqvdtSILGlppkeaaespyiASMGVYVFRKE---VLLKLLRSSYPTSNDfg 324
Cdd:cd02523 133 DEYVKDLDDA-GVLLGIISKAKNLE--------EIQG------------EYVGISKFSPEdadRLAEALEELIEAGRV-- 189
|
250 260
....*....|....*....|....*
gi 259439172 325 seiiplavgehnvqaflfNDYWEDI 349
Cdd:cd02523 190 ------------------NLYYEDA 196
|
|
| LbH_G1P_AT_C_like |
cd03356 |
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
409-483 |
2.60e-05 |
|
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.
Pssm-ID: 100046 [Multi-domain] Cd Length: 79 Bit Score: 42.61 E-value: 2.60e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 259439172 409 CSVQHSIVGIRSRLESGVELQDTMMMGAdfyqteaeiasllaegkvpVGVGQNTKIKNCIIDKNAKIGKNVVIAN 483
Cdd:cd03356 12 AIIKNSVIGDNVRIGDGVTITNSILMDN-------------------VTIGANSVIVDSIIGDNAVIGENVRVVN 67
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
83-268 |
2.76e-05 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 46.21 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 83 KNVASIILGGGAGTRLFPLTSKRAKPAVPIGGcYRLIDIPMSNCINSGIRKIFILTQFNSFSLNRHLsrtynFGNGVNFG 162
Cdd:PRK15480 2 KTRKGIILAGGSGTRLYPVTMAVSKQLLPIYD-KPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQL-----LGDGSQWG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 163 DGFvevlaatqtsgdagKKWFQGTADAVRQFIWVFEDAKTKNvEHVLILSGDHLYRMDYMNFVQKHIESNADITVSCLPM 242
Cdd:PRK15480 76 LNL--------------QYKVQPSPDGLAQAFIIGEEFIGGD-DCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHV 140
|
170 180
....*....|....*....|....*.
gi 259439172 243 DESRAsdFGLLKIDQSGKIIQFSEKP 268
Cdd:PRK15480 141 NDPER--YGVVEFDQNGTAISLEEKP 164
|
|
| LbH_eIF2B_gamma_C |
cd04652 |
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
458-518 |
3.54e-04 |
|
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.
Pssm-ID: 100057 [Multi-domain] Cd Length: 81 Bit Score: 39.48 E-value: 3.54e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 259439172 458 VGQNTKIKNCIIDKNAKIGKNVVIANA---DGVEegdrPEEGFHIRSGItvVLKNATIRDGLHI 518
Cdd:cd04652 8 VGEKTSIKRSVIGANCKIGKRVKITNCvimDNVT----IEDGCTLENCI--IGNGAVIGEKCKL 65
|
|
| LbH_G1P_AT_C_like |
cd03356 |
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
458-515 |
1.34e-03 |
|
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.
Pssm-ID: 100046 [Multi-domain] Cd Length: 79 Bit Score: 37.61 E-value: 1.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 259439172 458 VGQNTKIKNCIIDKNAKIGKNVVIAN---ADGVEEGDrpeeGFHIRSgiTVVLKNATIRDG 515
Cdd:cd03356 8 IGENAIIKNSVIGDNVRIGDGVTITNsilMDNVTIGA----NSVIVD--SIIGDNAVIGEN 62
|
|
| LbH_eIF2B_gamma_C |
cd04652 |
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
399-496 |
2.72e-03 |
|
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.
Pssm-ID: 100057 [Multi-domain] Cd Length: 81 Bit Score: 36.79 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 399 IVSHGCFLRE-CSVQHSIVGIRSRLESGVELQDTMMMgaDFyqteaeiasllaegkvpVGVGQNTKIKNCIIDKNAKIGK 477
Cdd:cd04652 1 LVGENTQVGEkTSIKRSVIGANCKIGKRVKITNCVIM--DN-----------------VTIEDGCTLENCIIGNGAVIGE 61
|
90
....*....|....*....
gi 259439172 478 NVVIANADgVEEGDRPEEG 496
Cdd:cd04652 62 KCKLKDCL-VGSGYRVEAG 79
|
|
| LbH_GlmU_C |
cd03353 |
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ... |
425-515 |
2.75e-03 |
|
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.
Pssm-ID: 100044 [Multi-domain] Cd Length: 193 Bit Score: 38.94 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259439172 425 GVELQD--------TMMMGADfyqTEAEIASLLaEGKVPVG----VGQNTKIKNCIIDKNAKIGKNVVIANADGVEEGD- 491
Cdd:cd03353 1 GVTLIDpettyidgDVEIGVD---VVIDPGVIL-EGKTVIGedcvIGPNCVIKDSTIGDGVVIKASSVIEGAVIGNGATv 76
|
90 100 110
....*....|....*....|....*....|....
gi 259439172 492 ------RP----EEGFHIrsGITVVLKNATIRDG 515
Cdd:cd03353 77 gpfahlRPgtvlGEGVHI--GNFVEIKKSTIGEG 108
|
|
| |
