|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02241 |
PLN02241 |
glucose-1-phosphate adenylyltransferase |
86-521 |
0e+00 |
|
glucose-1-phosphate adenylyltransferase
Pssm-ID: 215133 [Multi-domain] Cd Length: 436 Bit Score: 868.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 86 PKNVAAIILGGGDGAKLFPLTKRAATPAVPVGGCYRMIDIPMSNCINSCINKIFVLTQFNSASLNRHLARTY-FGNGINF 164
Cdd:PLN02241 1 PKSVAAIILGGGAGTRLFPLTKRRAKPAVPIGGNYRLIDIPMSNCINSGINKIYVLTQFNSASLNRHLSRAYnFGNGGNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 165 GDGFVEVLAATQTPGEAGkkWFQGTADAVRKFLWVFEDAKNRNIENIIILSGDHLYRMNYMDFVQHHVDSKADITLSCAP 244
Cdd:PLN02241 81 GDGFVEVLAATQTPGEKG--WFQGTADAVRQFLWLFEDAKNKNVEEVLILSGDHLYRMDYMDFVQKHRESGADITIACLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 245 VDESRASEYGLVNIDRSGRVVHFSEKPTGIDLKSMQTDTTMHGLSHQEAAKSPYIASMGVYCFKTEALLKLLTWRYPSSN 324
Cdd:PLN02241 159 VDESRASDFGLMKIDDTGRIIEFSEKPKGDELKAMQVDTTVLGLSPEEAKEKPYIASMGIYVFKKDVLLKLLRWRFPTAN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 325 DFGSEIIPAAIKD-HNVQGYIYRDYWEDIGTIKSFYEANIALVEEHPKFEFYDQNTPFYTSPRFLPPTKTEKCRIVNSVI 403
Cdd:PLN02241 239 DFGSEIIPGAIKEgYNVQAYLFDGYWEDIGTIKSFYEANLALTKQPPKFSFYDPDAPIYTSPRFLPPSKIEDCRITDSII 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 404 SHGCFLGECSIQRSIIGERSRLDYGVELQDTLMLGADSYQTESEIASLLAEGNVPIGIGRDTKIRKCIIDKNAKIGKNVV 483
Cdd:PLN02241 319 SHGCFLRECKIEHSVVGLRSRIGEGVEIEDTVMMGADYYETEEEIASLLAEGKVPIGIGENTKIRNAIIDKNARIGKNVV 398
|
410 420 430
....*....|....*....|....*....|....*...
gi 1063727669 484 IMNKDDVKEADRPEEGFYIRSGITVVVEKATIKDGTVI 521
Cdd:PLN02241 399 IINKDGVQEADREEEGYYIRSGIVVILKNAVIPDGTVI 436
|
|
| glgC |
PRK02862 |
glucose-1-phosphate adenylyltransferase; Provisional |
87-521 |
0e+00 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179486 [Multi-domain] Cd Length: 429 Bit Score: 671.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 87 KNVAAIILGGGDGAKLFPLTKRAATPAVPVGGCYRMIDIPMSNCINSCINKIFVLTQFNSASLNRHLARTYfgNGINFGD 166
Cdd:PRK02862 2 KRVLAIILGGGAGTRLYPLTKLRAKPAVPLAGKYRLIDIPISNCINSGINKIYVLTQFNSASLNRHISQTY--NFDGFSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 167 GFVEVLAATQTPgeAGKKWFQGTADAVRKFLWVFEdakNRNIENIIILSGDHLYRMNYMDFVQHHVDSKADITLSCAPVD 246
Cdd:PRK02862 80 GFVEVLAAQQTP--ENPSWFQGTADAVRKYLWHFQ---EWDVDEYLILSGDQLYRMDYRLFVQHHRETGADITLAVLPVD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 247 ESRASEYGLVNIDRSGRVVHFSEKPTGIDLKSMQTDTTMHGLSHQEAAKSPYIASMGVYCFKTEALLKLLTwRYPSSNDF 326
Cdd:PRK02862 155 EKDASGFGLMKTDDDGRITEFSEKPKGDELKAMAVDTSRLGLSPEEAKGKPYLASMGIYVFSRDVLFDLLN-KNPEYTDF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 327 GSEIIPAAIKDHNVQGYIYRDYWEDIGTIKSFYEANIALVEE-HPKFEFYDQNTPFYTSPRFLPPTKTEKCRIVNSVISH 405
Cdd:PRK02862 234 GKEIIPEAIRDYKVQSYLFDGYWEDIGTIEAFYEANLALTQQpNPPFSFYDEKAPIYTRARYLPPSKLLDATITESIIAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 406 GCFLGECSIQRSIIGERSRLDYGVELQDTLMLGADSYQTESEIASLLAEGNVPIGIGRDTKIRKCIIDKNAKIGKNVVIM 485
Cdd:PRK02862 314 GCIIKNCSIHHSVLGIRSRIESGCTIEDTLVMGADFYESSEEREELRKEGKPPLGIGEGTTIKRAIIDKNARIGNNVRIV 393
|
410 420 430
....*....|....*....|....*....|....*.
gi 1063727669 486 NKDDVKEADRPEEGFYIRSGITVVVEKATIKDGTVI 521
Cdd:PRK02862 394 NKDNVEEADREDQGFYIRDGIVVVVKNAVIPDGTVI 429
|
|
| glgC |
TIGR02091 |
glucose-1-phosphate adenylyltransferase; This enzyme, glucose-1-phosphate adenylyltransferase, ... |
91-486 |
2.23e-171 |
|
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: 487.92 E-value: 2.23e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 91 AIILGGGDGAKLFPLTKRAATPAVPVGGCYRMIDIPMSNCINSCINKIFVLTQFNSASLNRHLARTYFGNGinFGDGFVE 170
Cdd:TIGR02091 1 AMVLAGGRGSRLSPLTKRRAKPAVPFGGKYRIIDFPLSNCINSGIRRIGVLTQYKSHSLNRHIQRGWDFDG--FIDGFVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 171 VLAATQTpgEAGKKWFQGTADAVRKFLWVFEDAknrNIENIIILSGDHLYRMNYMDFVQHHVDSKADITLSCAPVDESRA 250
Cdd:TIGR02091 79 LLPAQQR--ESGTDWYQGTADAVYQNLDLIEDY---DPEYVLILSGDHIYKMDYEKMLDYHIESGADVTIACIPVPRKEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 251 SEYGLVNIDRSGRVVHFSEKP-TGIDLKSMQtdttmhglshqeaakSPYIASMGVYCFKTEALLKLLTWR---YPSSNDF 326
Cdd:TIGR02091 154 SRFGVMQVDEDGRIVDFEEKPaNPPSIPGMP---------------DFALASMGIYIFDKDVLKELLEEDaddPESSHDF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 327 GSEIIPAAIKDHNVQGYIYRDYWEDIGTIKSFYEANIALVEEHPKFEFYDQNTPFYTSPRFLPPTKT--EKCRIVNSVIS 404
Cdd:TIGR02091 219 GKDIIPRALEEGSVQAYLFSGYWRDVGTIDSFWEANMDLVSVVPPFDLYDRKWPIYTYNEFLPPAKFvdSDAQVVDSLVS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 405 HGCFLGECSIQRSIIGERSRLDYGVELQDTLMLGAdsyqteseiasllaegnvpIGIGRDTKIRKCIIDKNAKIGKNVVI 484
Cdd:TIGR02091 299 EGCIISGATVSHSVLGIRVRIGSGSTVEDSVIMGD-------------------VGIGRGAVIRNAIIDKNVRIGEGVVI 359
|
..
gi 1063727669 485 MN 486
Cdd:TIGR02091 360 GN 361
|
|
| GlgC |
COG0448 |
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
88-509 |
9.50e-151 |
|
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];
Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 436.04 E-value: 9.50e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 88 NVAAIILGGGDGAKLFPLTKRAATPAVPVGGCYRMIDIPMSNCINSCINKIFVLTQFNSASLNRHLartyfGNGINFG-- 165
Cdd:COG0448 1 KVLAIILAGGRGSRLGPLTKDRAKPAVPFGGKYRIIDFPLSNCVNSGIRRVGVLTQYKSHSLNDHI-----GSGKPWDld 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 166 --DGFVEVLAATQTPgeAGKKWFQGTADAVRKFLWVFEDAknrNIENIIILSGDHLYRMNYMDFVQHHVDSKADITLSCA 243
Cdd:COG0448 76 rkRGGVFILPPYQQR--EGEDWYQGTADAVYQNLDFIERS---DPDYVLILSGDHIYKMDYRQMLDFHIESGADITVACI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 244 PVDESRASEYGLVNIDRSGRVVHFSEKPTGIDlksmqtdttmhglshqeaaksPYIASMGVYCFKTEALLKLLTWRYP-S 322
Cdd:COG0448 151 EVPREEASRFGVMEVDEDGRITEFEEKPKDPK---------------------SALASMGIYVFNKDVLIELLEEDAPnS 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 323 SNDFGSEIIPAAIKDHNVQGYIYRDYWEDIGTIKSFYEANIALVEEHPKFEFYDQNTPFYTSPRFLPPTK-TEKCRIVNS 401
Cdd:COG0448 210 SHDFGKDIIPRLLDRGKVYAYEFDGYWRDVGTIDSYYEANMDLLDPEPEFNLYDPEWPIYTKQKDLPPAKfVRGGKVKNS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 402 VISHGCFLgECSIQRSIIGERSRLDYGVELQDTLMLGAdsyqteseiasllaegnvpIGIGRDTKIRKCIIDKNAKIGKN 481
Cdd:COG0448 290 LVSNGCII-SGTVENSVLFRGVRVESGAVVENSVIMPG-------------------VVIGEGAVIENAIIDKNVVIPPG 349
|
410 420
....*....|....*....|....*...
gi 1063727669 482 VVIMNKDdvkEADRpeEGFYIRSGITVV 509
Cdd:COG0448 350 VVIGEDP---EEDR--KRFTVSSGIVVV 372
|
|
| glgC |
PRK00725 |
glucose-1-phosphate adenylyltransferase; Provisional |
73-512 |
2.07e-104 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234824 [Multi-domain] Cd Length: 425 Bit Score: 319.09 E-value: 2.07e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 73 KNQPSMFERRRadPKNVAAIILGGGDGAKLFPLTKRAATPAVPVGGCYRMIDIPMSNCINSCINKIFVLTQFNSASLNRH 152
Cdd:PRK00725 2 KNDSLMLARQL--TRDTLALILAGGRGSRLKELTDKRAKPAVYFGGKFRIIDFALSNCINSGIRRIGVLTQYKAHSLIRH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 153 LARtyfgnGINFGDG----FVEVLAATQTPGEagKKWFQGTADAVRKFLWVFEDAknrNIENIIILSGDHLYRMNYMDFV 228
Cdd:PRK00725 80 IQR-----GWSFFREelgeFVDLLPAQQRVDE--ENWYRGTADAVYQNLDIIRRY---DPKYVVILAGDHIYKMDYSRML 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 229 QHHVDSKADITLSCAPVDESRASEYGLVNIDRSGRVVHFSEKPTgiDLKSMQTDTTMHglshqeaakspyIASMGVYCFK 308
Cdd:PRK00725 150 ADHVESGADCTVACLEVPREEASAFGVMAVDENDRITAFVEKPA--NPPAMPGDPDKS------------LASMGIYVFN 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 309 TEALLKLLTW--RYP-SSNDFGSEIIPAAIKDHNVQGYIYRD-----------YWEDIGTIKSFYEANIALVEEHPKFEF 374
Cdd:PRK00725 216 ADYLYELLEEdaEDPnSSHDFGKDIIPKIVEEGKVYAHPFSDscvrsdpeeepYWRDVGTLDAYWQANLDLASVTPELDL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 375 YDQNTPFYTSPRFLPPTKT----EKCR--IVNSVISHGCFLGECSIQRSIIGERSRLDYGVELQDTLMLgadsyqtesei 448
Cdd:PRK00725 296 YDRNWPIWTYQEQLPPAKFvfdrSGRRgmAINSLVSGGCIISGAVVRRSVLFSRVRVNSFSNVEDSVLL----------- 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063727669 449 asllaegnvP-IGIGRDTKIRKCIIDKNAKIGKNVVI-MNkddvKEADRpeEGFYI-RSGITVVVEK 512
Cdd:PRK00725 365 ---------PdVNVGRSCRLRRCVIDRGCVIPEGMVIgED----PEEDA--KRFRRsEEGIVLVTRE 416
|
|
| glgC |
PRK00844 |
glucose-1-phosphate adenylyltransferase; Provisional |
87-509 |
5.25e-103 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 315.23 E-value: 5.25e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 87 KNVAAIILGGGDGAKLFPLTKRAATPAVPVGGCYRMIDIPMSNCINSCINKIFVLTQFNSASLNRHLARTYFGNGINfgD 166
Cdd:PRK00844 4 PKVLAIVLAGGEGKRLMPLTADRAKPAVPFGGSYRLIDFVLSNLVNSGYLRIYVLTQYKSHSLDRHISQTWRLSGLL--G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 167 GFVEVLAATQTpgeAGKKWFQGTADAVRKFLWVFEDAKNrniENIIILSGDHLYRMNYMDFVQHHVDSKADITLSCAPVD 246
Cdd:PRK00844 82 NYITPVPAQQR---LGKRWYLGSADAIYQSLNLIEDEDP---DYVVVFGADHVYRMDPRQMVDFHIESGAGVTVAAIRVP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 247 ESRASEYGLVNIDRSGRVVHFSEKPTgiDLKSMQTDTTMhglshqeaakspYIASMGVYCFKTEALLKLLTWRY---PSS 323
Cdd:PRK00844 156 REEASAFGVIEVDPDGRIRGFLEKPA--DPPGLPDDPDE------------ALASMGNYVFTTDALVDALRRDAadeDSS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 324 NDFGSEIIPAAIKDHNVQGYIY------------RDYWEDIGTIKSFYEANIALVEEHPKFEFYDQNTPFYTSPRFLPPT 391
Cdd:PRK00844 222 HDMGGDIIPRLVERGRAYVYDFstnevpgaterdRGYWRDVGTIDAYYDAHMDLLSVHPVFNLYNREWPIYTSSPNLPPA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 392 K-----TEKCRIVNSVISHGCFLGECSIQRSIIGERSRLDYGVELQDTLMLgadsyqteseiasllaeGNVPigIGRDTK 466
Cdd:PRK00844 302 KfvdggGRVGSAQDSLVSAGSIISGATVRNSVLSPNVVVESGAEVEDSVLM-----------------DGVR--IGRGAV 362
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1063727669 467 IRKCIIDKNAKIGKNVVI-MNkddvKEADRpeEGFYI-RSGITVV 509
Cdd:PRK00844 363 VRRAILDKNVVVPPGATIgVD----LEEDR--RRFTVsEGGIVVV 401
|
|
| glgC |
PRK05293 |
glucose-1-phosphate adenylyltransferase; Provisional |
87-521 |
1.14e-91 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 284.84 E-value: 1.14e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 87 KNVAAIILGGGDGAKLFPLTKRAATPAVPVGGCYRMIDIPMSNCINSCINKIFVLTQFNSASLNRHLartyfGNGINFG- 165
Cdd:PRK05293 2 KEMLAMILAGGQGTRLGKLTKNIAKPAVPFGGKYRIIDFTLSNCANSGIDTVGVLTQYQPLELNNHI-----GIGSPWDl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 166 ---DGFVEVLAATQtpGEAGKKWFQGTADAV---RKFLwvfedaKNRNIENIIILSGDHLYRMNYMDFVQHHVDSKADIT 239
Cdd:PRK05293 77 driNGGVTILPPYS--ESEGGKWYKGTAHAIyqnIDYI------DQYDPEYVLILSGDHIYKMDYDKMLDYHKEKEADVT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 240 LSCAPVDESRASEYGLVNIDRSGRVVHFSEKPtgidlksmqtdttmhglshqEAAKSPyIASMGVYCFKTEALLKLLTWR 319
Cdd:PRK05293 149 IAVIEVPWEEASRFGIMNTDENMRIVEFEEKP--------------------KNPKSN-LASMGIYIFNWKRLKEYLIED 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 320 YP---SSNDFGSEIIPAAIKD-HNVQGYIYRDYWEDIGTIKSFYEANIALVEEHPKFEFYDQNTPFYTSPRFLPPTK-TE 394
Cdd:PRK05293 208 EKnpnSSHDFGKNVIPLYLEEgEKLYAYPFKGYWKDVGTIESLWEANMELLRPENPLNLFDRNWRIYSVNPNLPPQYiAE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 395 KCRIVNSVISHGCFLgECSIQRSIIGERSRLDYGVELQDT-LMLGADsyqteseiasllaegnvpigIGRDTKIRKCIID 473
Cdd:PRK05293 288 NAKVKNSLVVEGCVV-YGTVEHSVLFQGVQVGEGSVVKDSvIMPGAK--------------------IGENVVIERAIIG 346
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1063727669 474 KNAKIGKNVVIMNKDDVkeadrpeegfyirsgITVVVEKATIKDGTVI 521
Cdd:PRK05293 347 ENAVIGDGVIIGGGKEV---------------ITVIGENEVIGVGTVI 379
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
91-365 |
7.45e-84 |
|
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: 259.88 E-value: 7.45e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 91 AIILGGGDGAKLFPLTKRAATPAVPVGGCYRMIDIPMSNCINSCINK-IFVLTQFNSASLNRHLartyfGNGINFGdgfV 169
Cdd:pfam00483 2 AIILAGGSGTRLWPLTRTLAKPLVPVGGKYPLIDYPLSRLANAGIREiIVILTQEHRFMLNELL-----GDGSKFG---V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 170 EVLAATQTPGEagkkwfqGTADAVRKFLWVFEDAKNrnieNIIILSGDHLYRMNYMDFVQHHVDSKADITLSCAPVDESR 249
Cdd:pfam00483 74 QITYALQPEGK-------GTAPAVALAADFLGDEKS----DVLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGIVPVEP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 250 ASEYGLVNIDRSGRVVHFSEKPtgidlksmqtdttmhglshqEAAKSPYIASMGVYCFKTEALLKLL--TWRYPSSNDFG 327
Cdd:pfam00483 143 PTGYGVVEFDDNGRVIRFVEKP--------------------KLPKASNYASMGIYIFNSGVLDFLAkyLEELKRGEDEI 202
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1063727669 328 SEIIPAAIKDHNVQGY-IYRDY-WEDIGTIKSFYEANIAL 365
Cdd:pfam00483 203 TDILPKALEDGKLAYAfIFKGYaWLDVGTWDSLWEANLFL 242
|
|
| ADP_Glucose_PP |
cd02508 |
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ... |
91-352 |
9.48e-75 |
|
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: 234.74 E-value: 9.48e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 91 AIILGGGDGAKLFPLTKRAATPAVPVGGCYRMIDIPMSNCINSCINKIFVLTQFNSASLNRHLARTYFGNGINFgDGFVE 170
Cdd:cd02508 1 AIILAGGEGTRLSPLTKKRAKPAVPFGGRYRLIDFPLSNMVNSGIRNVGVLTQYKSRSLNDHLGSGKEWDLDRK-NGGLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 171 VLAATQTPGEagkKWFQGTADAVRKFLWVFEDAKNrniENIIILSGDHLYRMNYMDFVQHHVDSKADITLScapvdesra 250
Cdd:cd02508 80 ILPPQQRKGG---DWYRGTADAIYQNLDYIERSDP---EYVLILSGDHIYNMDYREMLDFHIESGADITVV--------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 251 seyglvnidrsgrvvhfsekptgidlksmqtdttmhglshqeaakspYIASMGVYCFKTEALLKLLTWRY-PSSNDFGSE 329
Cdd:cd02508 145 -----------------------------------------------YKASMGIYIFSKDLLIELLEEDAaDGSHDFGKD 177
|
250 260
....*....|....*....|...
gi 1063727669 330 IIPAAIKDHNVQGYIYRDYWEDI 352
Cdd:cd02508 178 IIPAMLKKLKIYAYEFNGYWADI 200
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
91-367 |
1.87e-32 |
|
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: 124.11 E-value: 1.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 91 AIILGGGDGAKLFPLTKRAATPAVPVGGcyR-MIDIPMSNCINSCINKIFVLTqfnsaslnRHLA---RTYFGNGINFGd 166
Cdd:COG1208 2 AVILAGGLGTRLRPLTDTRPKPLLPVGG--KpLLEHILERLAAAGITEIVINV--------GYLAeqiEEYFGDGSRFG- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 167 gfVEVLAATQtpgeaGKKWfqGTADAVRKFLWVFEDaknrniENIIILSGDHLYRMNYMDFVQHHVDSKADITLSCAPVD 246
Cdd:COG1208 71 --VRITYVDE-----GEPL--GTGGALKRALPLLGD------EPFLVLNGDILTDLDLAALLAFHREKGADATLALVPVP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 247 esRASEYGLVNIDRSGRVVHFSEKPtgidlksmqtdttmhglshqEAAKSPYIaSMGVYCFKTEaLLKLLtwryPSSNDF 326
Cdd:COG1208 136 --DPSRYGVVELDGDGRVTRFVEKP--------------------EEPPSNLI-NAGIYVLEPE-IFDYI----PEGEPF 187
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1063727669 327 G-SEIIPAAIKDHNVQGYIYRDYWEDIGTIKSFYEANIALVE 367
Cdd:COG1208 188 DlEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229
|
|
| glgD |
TIGR02092 |
glucose-1-phosphate adenylyltransferase, GlgD subunit; This family is GlgD, an apparent ... |
87-484 |
9.81e-31 |
|
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: 122.88 E-value: 9.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 87 KNVAAIILGGGDGAKLFPLTKRAATPAVPVGGCYRMIDIPMSNCINSCINKIFVLTQFNS-ASLNRHLartyfGNGINFG 165
Cdd:TIGR02092 1 NKMSAIINLTESSKNLSPLTKVRPLASLPFGGRYRLIDFPLSNMVNAGIRNVFIFFKNKErQSLFDHL-----GSGREWD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 166 -----DG-FVEVLAATQTPGEAGKKWFQGTADAVRKflwvfedaknRNIENIIILSGDHLYRMNYMDFVQHHVDSKADIT 239
Cdd:TIGR02092 76 lhrkrDGlFVFPYNDRDDLSEGGKRYFSQNLEFLKR----------STSEYTVVLNSHMVCNIDLKAVLKYHEETGKDIT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 240 LSCAPVDESRASEY-GLVNIDRSGRVvhfsekpTGI-DLKSMQTDTTMhglshqeaakspyiaSMGVYCFKTEALLKLLT 317
Cdd:TIGR02092 146 VVYKKVKPADASEYdTILRFDESGKV-------KSIgQNLNPEEEENI---------------SLDIYIVSTDLLIELLY 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 318 wrypSSNDFG-----SEIIPAAIKDHNVQGYIYRDYWEDIGTIKSFYEANIALVEEHpKFE--FYDQNTPFYTSPRFLPP 390
Cdd:TIGR02092 204 ----ECIQRGkltslEELIRENLKELNINAYEYTGYLANINSVKSYYKANMDLLDPQ-NFQslFYSSQGPIYTKVKDEPP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 391 TK-TEKCRIVNSVISHGCFLgECSIQRSIIGERSRLDYGVELQDTLMLgadsyqTESEiasllaegnvpigIGRDTKIRK 469
Cdd:TIGR02092 279 TYyAENSKVENSLVANGCII-EGKVENSILSRGVHVGKDALIKNCIIM------QRTV-------------IGEGAHLEN 338
|
410
....*....|....*
gi 1063727669 470 CIIDKNAKIGKNVVI 484
Cdd:TIGR02092 339 VIIDKDVVIEPNVKI 353
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
91-353 |
2.14e-30 |
|
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: 118.07 E-value: 2.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 91 AIILGGGDGAKLFPLTKRAATPAVPVGGcYRMIDIPMSNCINSCINKIFVLTQFNsaslnRHLARTYFGNGINFGdgfVE 170
Cdd:cd04181 1 AVILAAGKGTRLRPLTDTRPKPLLPIAG-KPILEYIIERLARAGIDEIILVVGYL-----GEQIEEYFGDGSKFG---VN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 171 VLAATQTPGEagkkwfqGTADAVRKFLWVFEDaknrniENIIILSGDHLYRMNYMDFVQHHVDSKADITLSCAPVDesRA 250
Cdd:cd04181 72 IEYVVQEEPL-------GTAGAVRNAEDFLGD------DDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVE--DP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 251 SEYGLVNIDRSGRVVHFSEKPTgidlksmqtdttmHGLShqeaakspYIASMGVYCFKTEaLLKLLTWRYPSSNDFGSEI 330
Cdd:cd04181 137 SRYGVVELDDDGRVTRFVEKPT-------------LPES--------NLANAGIYIFEPE-ILDYIPEILPRGEDELTDA 194
|
250 260
....*....|....*....|...
gi 1063727669 331 IPAAIKDHNVQGYIYRDYWEDIG 353
Cdd:cd04181 195 IPLLIEEGKVYGYPVDGYWLDIG 217
|
|
| LbH_G1P_AT_C |
cd04651 |
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ... |
389-515 |
1.04e-27 |
|
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: 106.78 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 389 PPTKTEKCRIVNSVISHGCFLGECSIQRSIIGERSRLDYGVELQDTLMLGADsyqteseiasllaegnvpiGIGRDTKIR 468
Cdd:cd04651 1 PPYIGRRGEVKNSLVSEGCIISGGTVENSVLFRGVRVGSGSVVEDSVIMPNV-------------------GIGRNAVIR 61
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1063727669 469 KCIIDKNAKIGKNVVIMNKDDVKEAdrpeEGFYIRSGITVVVEKATI 515
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 ... |
91-361 |
4.71e-19 |
|
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: 86.07 E-value: 4.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 91 AIILGGGDGAKLFPLTKRAATPAVPVGGcYRMIDIPMSNCINSCINKIFVLTQfnsaslnrHLA---RTYFGNGinFGDG 167
Cdd:cd06915 1 AVILAGGLGTRLRSVVKDLPKPLAPVAG-RPFLEYLLEYLARQGISRIVLSVG--------YLAeqiEEYFGDG--YRGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 168 FVEVLAATQTPgeagkkwfQGTADAVRKFLWVFEDaknrniENIIILSGDHLYRMNYMDFVQHHVDSKADITLSCAPVDE 247
Cdd:cd06915 70 IRIYYVIEPEP--------LGTGGAIKNALPKLPE------DQFLVLNGDTYFDVDLLALLAALRASGADATMALRRVPD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 248 srASEYGLVNIDRSGRVVHFSEKPTGidlksmqtdttmhglshqeaAKSPYIASmGVYCFKTEAlLKLLTWRYPSsndFG 327
Cdd:cd06915 136 --ASRYGNVTVDGDGRVIAFVEKGPG--------------------AAPGLING-GVYLLRKEI-LAEIPADAFS---LE 188
|
250 260 270
....*....|....*....|....*....|....
gi 1063727669 328 SEIIPAAIKDHNVQGYIYRDYWEDIGTIKSFYEA 361
Cdd:cd06915 189 ADVLPALVKRGRLYGFEVDGYFIDIGIPEDYARA 222
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
91-362 |
3.17e-14 |
|
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: 71.77 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 91 AIILGGGDGAKLFPLTKRAATPAVPVGGcYRMIDIPMSNCINSCINKIFVltqfnsaSLNrHLART---YFGNGINFGDG 167
Cdd:cd06426 1 VVIMAGGKGTRLRPLTENTPKPMLKVGG-KPILETIIDRFIAQGFRNFYI-------SVN-YLAEMiedYFGDGSKFGVN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 168 FVEVlaatqtpgEAGKKWfqGTADAVrKFLwvfedaKNRNIENIIILSGDHLYRMNYMDFVQHHVDSKADITLSCAPVDE 247
Cdd:cd06426 72 ISYV--------REDKPL--GTAGAL-SLL------PEKPTDPFLVMNGDILTNLNYEHLLDFHKENNADATVCVREYEV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 248 SRAseYGLVNIDrSGRVVHFSEKPTgidlksmqtdttmhglsHQeaakspYIASMGVYCFKTEALlklltwRYPSSNDF- 326
Cdd:cd06426 135 QVP--YGVVETE-GGRITSIEEKPT-----------------HS------FLVNAGIYVLEPEVL------DLIPKNEFf 182
|
250 260 270
....*....|....*....|....*....|....*...
gi 1063727669 327 -GSEIIPAAIKD-HNVQGYIYRDYWEDIGTIKSFYEAN 362
Cdd:cd06426 183 dMPDLIEKLIKEgKKVGVFPIHEYWLDIGRPEDYEKAN 220
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
91-368 |
1.86e-13 |
|
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: 69.91 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 91 AIILGGGDGAKLFPLTKRAATPAVPVGGcYRMIDIPMSNCINSCINKIFVLTqfnsaSLNRHLARTYFGNGINFGDGFVE 170
Cdd:cd04189 3 GLILAGGKGTRLRPLTYTRPKQLIPVAG-KPIIQYAIEDLREAGIEDIGIVV-----GPTGEEIKEALGDGSRFGVRITY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 171 VLAATQtpgeagkkwfQGTADAV---RKFLwvfedaknrNIENIIILSGDHLYRMNYMDFVQHHVDSKADITLSCAPVDE 247
Cdd:cd04189 77 ILQEEP----------LGLAHAVlaaRDFL---------GDEPFVVYLGDNLIQEGISPLVRDFLEEDADASILLAEVED 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 248 SRAseYGLVNIDrSGRVVHFSEKPtgidlksmqtdttmhglshqEAAKSPYiASMGVYCFkTEALLKLL-----TWRyps 322
Cdd:cd04189 138 PRR--FGVAVVD-DGRIVRLVEKP--------------------KEPPSNL-ALVGVYAF-TPAIFDAIsrlkpSWR--- 189
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1063727669 323 sndfgSEI-IPAAIK---DHN--VQGYIYRDYWEDIGTIKSFYEANIALVEE 368
Cdd:cd04189 190 -----GELeITDAIQwliDRGrrVGYSIVTGWWKDTGTPEDLLEANRLLLDK 236
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
91-362 |
5.38e-08 |
|
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: 53.73 E-value: 5.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 91 AIILGGGDGAKLFPLTKRAATPAVPVGGcYRMIDIPMSNCINSCINKIFVLTQfnsaslNRHLARTY--FGNGINFGdgf 168
Cdd:cd02538 3 GIILAGGSGTRLYPLTKVVSKQLLPVYD-KPMIYYPLSTLMLAGIREILIIST------PEDLPLFKelLGDGSDLG--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 169 VEVLAATQ-TPGeagkkwfqGTADAV---RKFLwvfedaknrNIENIIILSGDHLYRMNYM-DFVQHHVDSKADITLSCA 243
Cdd:cd02538 73 IRITYAVQpKPG--------GLAQAFiigEEFI---------GDDPVCLILGDNIFYGQGLsPILQRAAAQKEGATVFGY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 244 PV-DESRaseYGLVNIDRSGRVVHFSEKPtgidlksmqtdttmhglshqEAAKSPYiASMGVYCFKTEALlklltwryps 322
Cdd:cd02538 136 EVnDPER---YGVVEFDENGRVLSIEEKP--------------------KKPKSNY-AVTGLYFYDNDVF---------- 181
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063727669 323 snDFGSEIIPAA-----IKDHNvQGYIYR-----------DYWEDIGTIKSFYEAN 362
Cdd:cd02538 182 --EIAKQLKPSArgeleITDVN-NEYLEKgklsvellgrgFAWLDTGTHESLLEAS 234
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
91-271 |
3.85e-06 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 48.55 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 91 AIILGGGDGAKLFPLTKRAATPAVPVGGcyR-MIDIPMSNCINSCINKI-FVLT-----QFnsaslnrhlaRTYFGNGIN 163
Cdd:COG1209 3 GIILAGGSGTRLRPLTLTVSKQLLPVYD--KpMIYYPLSTLMLAGIREIlIISTpedgpQF----------ERLLGDGSQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 164 FGdgfVEVLAATQ-TPgeagkkwfQGTADAV---RKFLwvfedaknRNIENIIILsGDHLYRMNYM-DFVQHHVDSKADI 238
Cdd:COG1209 71 LG---IKISYAVQpEP--------LGLAHAFiiaEDFI--------GGDPVALVL-GDNIFYGDGLsELLREAAARESGA 130
|
170 180 190
....*....|....*....|....*....|...
gi 1063727669 239 TLSCAPVDESRAseYGLVNIDRSGRVVHFSEKP 271
Cdd:COG1209 131 TIFGYKVEDPER--YGVVEFDEDGRVVSLEEKP 161
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
91-275 |
3.94e-06 |
|
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: 48.04 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 91 AIILGGGDGAKLFPLTKRAATPAVPVGGcYRMIDIPMSNCINSCINKIFVLTQFNSASLNRHLARTYFGNgiNFGDGFVE 170
Cdd:cd04198 3 AVILAGGGGSRLYPLTDNIPKALLPVAN-KPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFPLN--LKQKLDEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 171 VlaatqTPGEAGKkwfqGTADAVRKFLwvfedakNRNIENIIILSGDHLYRMNYMDFVQHHVDSKADIT-LSCAPVDESR 249
Cdd:cd04198 80 T-----IVLDEDM----GTADSLRHIR-------KKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTvLLYPPPVSSE 143
|
170 180 190
....*....|....*....|....*....|....*.
gi 1063727669 250 ----------ASEYGLVNIDRSGRVVHFSEKPTGID 275
Cdd:cd04198 144 qkggkgkskkADERDVIGLDEKTQRLLFITSEEDLD 179
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
91-361 |
5.53e-05 |
|
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: 44.48 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 91 AIILGGGDGAKLFPLTKRAATPAVPVGGcyR-MIDIPMSNCINSCINKIFVLTQFNSASLNRHLARTYFGNGINFGDGFV 169
Cdd:cd06422 2 AMILAAGLGTRMRPLTDTRPKPLVPVAG--KpLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDSRFGLRITISDEPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 170 EVLaatqtpgeagkkwfqGTADAVRK---FLwvfedaknrNIENIIILSGDHLYRMNYMDFVQHHVDsKADITLSCAPVD 246
Cdd:cd06422 80 ELL---------------ETGGGIKKalpLL---------GDEPFLVVNGDILWDGDLAPLLLLHAW-RMDALLLLLPLV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 247 ESRASE-YGLVNIDRSGRVVHFSEKPTGidlksmqtdttmhglshqeaaksPYIASmGVYCFKTEALLKLLTWRYPSsnd 325
Cdd:cd06422 135 RNPGHNgVGDFSLDADGRLRRGGGGAVA-----------------------PFTFT-GIQILSPELFAGIPPGKFSL--- 187
|
250 260 270
....*....|....*....|....*....|....*.
gi 1063727669 326 fgSEIIPAAIKDHNVQGYIYRDYWEDIGTIKSFYEA 361
Cdd:cd06422 188 --NPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
|
|
| LbH_eIF2B_epsilon |
cd05787 |
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
461-521 |
9.97e-05 |
|
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: 40.64 E-value: 9.97e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063727669 461 IGRDTKIRKCIIDKNAKIGKNVVIMNK---DDVKEADrpeeGFYIRSGI----TVVVEKATIKDGTVI 521
Cdd:cd05787 8 IGEGTTIKNSVIGRNCKIGKNVVIDNSyiwDDVTIED----GCTIHHSIvadgAVIGKGCTIPPGSLI 71
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
91-217 |
3.48e-04 |
|
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: 41.86 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 91 AIILGGGDGAKLFPLTKRAATPAVPVGGCYrMIDIPMSNCINSCINKIFVLTQFNSASLNRHLaRTYFGNGINFGDGFVE 170
Cdd:cd02507 3 AVVLADGFGSRFLPLTSDIPKALLPVANVP-LIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHL-LKSKWSSLSSKMIVDV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1063727669 171 VLAATQTPgeagkkwfQGTADAVRkflwvfeDAKNRNIENIIILSGD 217
Cdd:cd02507 81 ITSDLCES--------AGDALRLR-------DIRGLIRSDFLLLSCD 112
|
|
| LbH_G1P_AT_C_like |
cd03356 |
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
402-492 |
1.67e-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: 37.22 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727669 402 VISHGCFLGE-CSIQRSIIGERSRLDYGVELQDtlmlgadsyqteseiaSLLAEGNVpigIGRDTKIRKCIIDKNAKIGK 480
Cdd:cd03356 1 LIGESTVIGEnAIIKNSVIGDNVRIGDGVTITN----------------SILMDNVT---IGANSVIVDSIIGDNAVIGE 61
|
90
....*....|..
gi 1063727669 481 NVVIMNKDDVKE 492
Cdd:cd03356 62 NVRVVNLCIIGD 73
|
|
| |
