|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02241 |
PLN02241 |
glucose-1-phosphate adenylyltransferase |
87-522 |
0e+00 |
|
glucose-1-phosphate adenylyltransferase
Pssm-ID: 215133 [Multi-domain] Cd Length: 436 Bit Score: 894.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 87 PRTVASIILGGGAGTRLFPLTKRRAKPAVPIGGAYRLIDVPMSNCINSGINKVYILTQYNSASLNRHLARAYN-SNGLGF 165
Cdd:PLN02241 1 PKSVAAIILGGGAGTRLFPLTKRRAKPAVPIGGNYRLIDIPMSNCINSGINKIYVLTQFNSASLNRHLSRAYNfGNGGNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 166 GDGYVEVLAATQTPGESGkrWFQGTADAVRQFHWLFEDARSKDIEDVLILSGDHLYRMDYMDFIQDHRQSGADISISCIP 245
Cdd:PLN02241 81 GDGFVEVLAATQTPGEKG--WFQGTADAVRQFLWLFEDAKNKNVEEVLILSGDHLYRMDYMDFVQKHRESGADITIACLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 246 IDDRRASDFGLMKIDDKGRVISFSEKPKGDDLKAMAVDTTILGLSKEEAEKKPYIASMGVYVFKKEILLNLLRWRFPTAN 325
Cdd:PLN02241 159 VDESRASDFGLMKIDDTGRIIEFSEKPKGDELKAMQVDTTVLGLSPEEAKEKPYIASMGIYVFKKDVLLKLLRWRFPTAN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 326 DFGSEIIPFSAKEFY-VNAYLFNDYWEDIGTIRSFFEANLALTEHPGAFSFYDAAKPIYTSRRNLPPSKIDNSKLIDSII 404
Cdd:PLN02241 239 DFGSEIIPGAIKEGYnVQAYLFDGYWEDIGTIKSFYEANLALTKQPPKFSFYDPDAPIYTSPRFLPPSKIEDCRITDSII 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 405 SHGSFLTNCLIEHSIVGIRSRVGSNVQLKDTVMLGADYYETEAEVAALLAEGNVPIGIGENTKIQECIIDKNARVGKNVI 484
Cdd:PLN02241 319 SHGCFLRECKIEHSVVGLRSRIGEGVEIEDTVMMGADYYETEEEIASLLAEGKVPIGIGENTKIRNAIIDKNARIGKNVV 398
|
410 420 430
....*....|....*....|....*....|....*...
gi 15239684 485 IANSEGIQEADRSSDGFYIRSGITVILKNSVIKDGVVI 522
Cdd:PLN02241 399 IINKDGVQEADREEEGYYIRSGIVVILKNAVIPDGTVI 436
|
|
| glgC |
PRK02862 |
glucose-1-phosphate adenylyltransferase; Provisional |
88-522 |
0e+00 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179486 [Multi-domain] Cd Length: 429 Bit Score: 721.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 88 RTVASIILGGGAGTRLFPLTKRRAKPAVPIGGAYRLIDVPMSNCINSGINKVYILTQYNSASLNRHLARAYNSNGlgFGD 167
Cdd:PRK02862 2 KRVLAIILGGGAGTRLYPLTKLRAKPAVPLAGKYRLIDIPISNCINSGINKIYVLTQFNSASLNRHISQTYNFDG--FSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 168 GYVEVLAATQTPgESGKrWFQGTADAVRQFHWLFEDarsKDIEDVLILSGDHLYRMDYMDFIQDHRQSGADISISCIPID 247
Cdd:PRK02862 80 GFVEVLAAQQTP-ENPS-WFQGTADAVRKYLWHFQE---WDVDEYLILSGDQLYRMDYRLFVQHHRETGADITLAVLPVD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 248 DRRASDFGLMKIDDKGRVISFSEKPKGDDLKAMAVDTTILGLSKEEAEKKPYIASMGVYVFKKEILLNLLRwRFPTANDF 327
Cdd:PRK02862 155 EKDASGFGLMKTDDDGRITEFSEKPKGDELKAMAVDTSRLGLSPEEAKGKPYLASMGIYVFSRDVLFDLLN-KNPEYTDF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 328 GSEIIPFSAKEFYVNAYLFNDYWEDIGTIRSFFEANLALTEHPG-AFSFYDAAKPIYTSRRNLPPSKIDNSKLIDSIISH 406
Cdd:PRK02862 234 GKEIIPEAIRDYKVQSYLFDGYWEDIGTIEAFYEANLALTQQPNpPFSFYDEKAPIYTRARYLPPSKLLDATITESIIAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 407 GSFLTNCLIEHSIVGIRSRVGSNVQLKDTVMLGADYYETEAEVAALLAEGNVPIGIGENTKIQECIIDKNARVGKNVIIA 486
Cdd:PRK02862 314 GCIIKNCSIHHSVLGIRSRIESGCTIEDTLVMGADFYESSEEREELRKEGKPPLGIGEGTTIKRAIIDKNARIGNNVRIV 393
|
410 420 430
....*....|....*....|....*....|....*.
gi 15239684 487 NSEGIQEADRSSDGFYIRSGITVILKNSVIKDGVVI 522
Cdd:PRK02862 394 NKDNVEEADREDQGFYIRDGIVVVVKNAVIPDGTVI 429
|
|
| glgC |
TIGR02091 |
glucose-1-phosphate adenylyltransferase; This enzyme, glucose-1-phosphate adenylyltransferase, ... |
92-487 |
3.69e-169 |
|
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: 482.15 E-value: 3.69e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 92 SIILGGGAGTRLFPLTKRRAKPAVPIGGAYRLIDVPMSNCINSGINKVYILTQYNSASLNRHLARAYnsNGLGFGDGYVE 171
Cdd:TIGR02091 1 AMVLAGGRGSRLSPLTKRRAKPAVPFGGKYRIIDFPLSNCINSGIRRIGVLTQYKSHSLNRHIQRGW--DFDGFIDGFVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 172 VLAATQTpgESGKRWFQGTADAVRQFHWLFEDarsKDIEDVLILSGDHLYRMDYMDFIQDHRQSGADISISCIPIDDRRA 251
Cdd:TIGR02091 79 LLPAQQR--ESGTDWYQGTADAVYQNLDLIED---YDPEYVLILSGDHIYKMDYEKMLDYHIESGADVTIACIPVPRKEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 252 SDFGLMKIDDKGRVISFSEKPKgdDLKAMAvdttilglskeeAEKKPYIASMGVYVFKKEILLNLLRWR---FPTANDFG 328
Cdd:TIGR02091 154 SRFGVMQVDEDGRIVDFEEKPA--NPPSIP------------GMPDFALASMGIYIFDKDVLKELLEEDaddPESSHDFG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 329 SEIIPFSAKEFYVNAYLFNDYWEDIGTIRSFFEANLALTEHPGAFSFYDAAKPIYTSRRNLPPSKIDNS--KLIDSIISH 406
Cdd:TIGR02091 220 KDIIPRALEEGSVQAYLFSGYWRDVGTIDSFWEANMDLVSVVPPFDLYDRKWPIYTYNEFLPPAKFVDSdaQVVDSLVSE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 407 GSFLTNCLIEHSIVGIRSRVGSNVQLKDTVMLGAdyyeteaevaallaegnvpIGIGENTKIQECIIDKNARVGKNVIIA 486
Cdd:TIGR02091 300 GCIISGATVSHSVLGIRVRIGSGSTVEDSVIMGD-------------------VGIGRGAVIRNAIIDKNVRIGEGVVIG 360
|
.
gi 15239684 487 N 487
Cdd:TIGR02091 361 N 361
|
|
| GlgC |
COG0448 |
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
90-515 |
5.04e-161 |
|
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];
Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 462.24 E-value: 5.04e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 90 VASIILGGGAGTRLFPLTKRRAKPAVPIGGAYRLIDVPMSNCINSGINKVYILTQYNSASLNRHLAR--AYNSNGLgfgD 167
Cdd:COG0448 2 VLAIILAGGRGSRLGPLTKDRAKPAVPFGGKYRIIDFPLSNCVNSGIRRVGVLTQYKSHSLNDHIGSgkPWDLDRK---R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 168 GYVEVLAATQTPgeSGKRWFQGTADAVRQFHWLFEDARSkdiEDVLILSGDHLYRMDYMDFIQDHRQSGADISISCIPID 247
Cdd:COG0448 79 GGVFILPPYQQR--EGEDWYQGTADAVYQNLDFIERSDP---DYVLILSGDHIYKMDYRQMLDFHIESGADITVACIEVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 248 DRRASDFGLMKIDDKGRVISFSEKPKgddlkamavdttilglskeeaEKKPYIASMGVYVFKKEILLNLLRWRFPT-AND 326
Cdd:COG0448 154 REEASRFGVMEVDEDGRITEFEEKPK---------------------DPKSALASMGIYVFNKDVLIELLEEDAPNsSHD 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 327 FGSEIIPFSAKEFYVNAYLFNDYWEDIGTIRSFFEANLALTEHPGAFSFYDAAKPIYTSRRNLPPSKI-DNSKLIDSIIS 405
Cdd:COG0448 213 FGKDIIPRLLDRGKVYAYEFDGYWRDVGTIDSYYEANMDLLDPEPEFNLYDPEWPIYTKQKDLPPAKFvRGGKVKNSLVS 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 406 HGSFLTNClIEHSIVGIRSRVGSNVQLKDTVMLGAdyyeteaevaallaegnvpIGIGENTKIQECIIDKNARVGKNVII 485
Cdd:COG0448 293 NGCIISGT-VENSVLFRGVRVESGAVVENSVIMPG-------------------VVIGEGAVIENAIIDKNVVIPPGVVI 352
|
410 420 430
....*....|....*....|....*....|
gi 15239684 486 ANSEgiqEADRssDGFYIRSGITVILKNSV 515
Cdd:COG0448 353 GEDP---EEDR--KRFTVSSGIVVVGKGAV 377
|
|
| glgC |
PRK00844 |
glucose-1-phosphate adenylyltransferase; Provisional |
90-516 |
5.29e-111 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 335.64 E-value: 5.29e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 90 VASIILGGGAGTRLFPLTKRRAKPAVPIGGAYRLIDVPMSNCINSGINKVYILTQYNSASLNRHLARAYNSNGLgfGDGY 169
Cdd:PRK00844 6 VLAIVLAGGEGKRLMPLTADRAKPAVPFGGSYRLIDFVLSNLVNSGYLRIYVLTQYKSHSLDRHISQTWRLSGL--LGNY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 170 VEVLAATQTpgeSGKRWFQGTADAVRQFHWLFEDARSkDIedVLILSGDHLYRMDYMDFIQDHRQSGADISISCIPIDDR 249
Cdd:PRK00844 84 ITPVPAQQR---LGKRWYLGSADAIYQSLNLIEDEDP-DY--VVVFGADHVYRMDPRQMVDFHIESGAGVTVAAIRVPRE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 250 RASDFGLMKIDDKGRVISFSEKPKgdDLKAMAVDTtilglskEEAekkpyIASMGVYVFKKEILLNLLRWRF---PTAND 326
Cdd:PRK00844 158 EASAFGVIEVDPDGRIRGFLEKPA--DPPGLPDDP-------DEA-----LASMGNYVFTTDALVDALRRDAadeDSSHD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 327 FGSEIIPFSAKEFYVNAYLFND------------YWEDIGTIRSFFEANLAL-TEHPgAFSFYDAAKPIYTSRRNLPPSK 393
Cdd:PRK00844 224 MGGDIIPRLVERGRAYVYDFSTnevpgaterdrgYWRDVGTIDAYYDAHMDLlSVHP-VFNLYNREWPIYTSSPNLPPAK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 394 I-----DNSKLIDSIISHGSFLTNCLIEHSIVGIRSRVGSNVQLKDTVMLgadyyeteaevaallaeGNVPigIGENTKI 468
Cdd:PRK00844 303 FvdgggRVGSAQDSLVSAGSIISGATVRNSVLSPNVVVESGAEVEDSVLM-----------------DGVR--IGRGAVV 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 15239684 469 QECIIDKNARVGKNVIIanseGI-QEADRssDGFYI-RSGITVILKNSVI 516
Cdd:PRK00844 364 RRAILDKNVVVPPGATI----GVdLEEDR--RRFTVsEGGIVVVPKGQRV 407
|
|
| glgC |
PRK00725 |
glucose-1-phosphate adenylyltransferase; Provisional |
89-510 |
8.70e-108 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234824 [Multi-domain] Cd Length: 425 Bit Score: 327.95 E-value: 8.70e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 89 TVAsIILGGGAGTRLFPLTKRRAKPAVPIGGAYRLIDVPMSNCINSGINKVYILTQYNSASLNRHLARAYNSNGLGFGDg 168
Cdd:PRK00725 16 TLA-LILAGGRGSRLKELTDKRAKPAVYFGGKFRIIDFALSNCINSGIRRIGVLTQYKAHSLIRHIQRGWSFFREELGE- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 169 YVEVLAATQ-TPGESgkrWFQGTADAVRQFHWLFedaRSKDIEDVLILSGDHLYRMDYMDFIQDHRQSGADISISCIPID 247
Cdd:PRK00725 94 FVDLLPAQQrVDEEN---WYRGTADAVYQNLDII---RRYDPKYVVILAGDHIYKMDYSRMLADHVESGADCTVACLEVP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 248 DRRASDFGLMKIDDKGRVISFSEKPKgdDLKAMAVDTTILglskeeaekkpyIASMGVYVFKKEILLNLLRWRFPTAN-- 325
Cdd:PRK00725 168 REEASAFGVMAVDENDRITAFVEKPA--NPPAMPGDPDKS------------LASMGIYVFNADYLYELLEEDAEDPNss 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 326 -DFGSEIIPFSAKEFYVNAYLFND-----------YWEDIGTIRSFFEANLALTEHPGAFSFYDAAKPIYTSRRNLPPSK 393
Cdd:PRK00725 234 hDFGKDIIPKIVEEGKVYAHPFSDscvrsdpeeepYWRDVGTLDAYWQANLDLASVTPELDLYDRNWPIWTYQEQLPPAK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 394 I----DNSK--LIDSIISHGSFLTNCLIEHSIVGIRSRVGSNVQLKDTVMLgaDYYEteaevaallaegnvpigIGENTK 467
Cdd:PRK00725 314 FvfdrSGRRgmAINSLVSGGCIISGAVVRRSVLFSRVRVNSFSNVEDSVLL--PDVN-----------------VGRSCR 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 15239684 468 IQECIIDKNARVGKNVIIanseGIQ-EADRSSdgFYI-RSGITVI 510
Cdd:PRK00725 375 LRRCVIDRGCVIPEGMVI----GEDpEEDAKR--FRRsEEGIVLV 413
|
|
| glgC |
PRK05293 |
glucose-1-phosphate adenylyltransferase; Provisional |
93-522 |
1.63e-98 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 302.56 E-value: 1.63e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 93 IILGGGAGTRLFPLTKRRAKPAVPIGGAYRLIDVPMSNCINSGINKVYILTQYNSASLNRHLAraynsNGLGFG----DG 168
Cdd:PRK05293 7 MILAGGQGTRLGKLTKNIAKPAVPFGGKYRIIDFTLSNCANSGIDTVGVLTQYQPLELNNHIG-----IGSPWDldriNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 169 YVEVLAATQtpGESGKRWFQGTADAVRQ-FHWLfedaRSKDIEDVLILSGDHLYRMDYMDFIQDHRQSGADISISCIPID 247
Cdd:PRK05293 82 GVTILPPYS--ESEGGKWYKGTAHAIYQnIDYI----DQYDPEYVLILSGDHIYKMDYDKMLDYHKEKEADVTIAVIEVP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 248 DRRASDFGLMKIDDKGRVISFSEKPKgddlkamavdttilglskeeaEKKPYIASMGVYVFKKEILLNLLRWRFPTAN-- 325
Cdd:PRK05293 156 WEEASRFGIMNTDENMRIVEFEEKPK---------------------NPKSNLASMGIYIFNWKRLKEYLIEDEKNPNss 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 326 -DFGSEIIPFSAKEFY-VNAYLFNDYWEDIGTIRSFFEANLALTEHPGAFSFYDAAKPIYTSRRNLPPSKI-DNSKLIDS 402
Cdd:PRK05293 215 hDFGKNVIPLYLEEGEkLYAYPFKGYWKDVGTIESLWEANMELLRPENPLNLFDRNWRIYSVNPNLPPQYIaENAKVKNS 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 403 IISHGSFLTNcLIEHSIVGIRSRVGSNVQLKDTV-MLGADyyeteaevaallaegnvpigIGENTKIQECIIDKNARVGK 481
Cdd:PRK05293 295 LVVEGCVVYG-TVEHSVLFQGVQVGEGSVVKDSViMPGAK--------------------IGENVVIERAIIGENAVIGD 353
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 15239684 482 NVIIANSEGIqeadrssdgfyirsgITVILKNSVIKDGVVI 522
Cdd:PRK05293 354 GVIIGGGKEV---------------ITVIGENEVIGVGTVI 379
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
93-367 |
1.51e-88 |
|
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: 271.82 E-value: 1.51e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 93 IILGGGAGTRLFPLTKRRAKPAVPIGGAYRLIDVPMSNCINSGINK-VYILTQYNSASLNRHLARAYNsnglgFGdgyVE 171
Cdd:pfam00483 3 IILAGGSGTRLWPLTRTLAKPLVPVGGKYPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSK-----FG---VQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 172 VLAATQTPGEsgkrwfqGTADAVRQFHWLFEDARSkdieDVLILSGDHLYRMDYMDFIQDHRQSGADISISCIPIDDRRA 251
Cdd:pfam00483 75 ITYALQPEGK-------GTAPAVALAADFLGDEKS----DVLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGIVPVEPP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 252 SDFGLMKIDDKGRVISFSEKPKGDDLkamavdttilglskeeaekkPYIASMGVYVFKKEILLNLLR--WRFPTANDFGS 329
Cdd:pfam00483 144 TGYGVVEFDDNGRVIRFVEKPKLPKA--------------------SNYASMGIYIFNSGVLDFLAKylEELKRGEDEIT 203
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15239684 330 EIIPFSAKEFYVN-AYLFNDY-WEDIGTIRSFFEANLALT 367
Cdd:pfam00483 204 DILPKALEDGKLAyAFIFKGYaWLDVGTWDSLWEANLFLL 243
|
|
| ADP_Glucose_PP |
cd02508 |
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ... |
93-353 |
2.90e-80 |
|
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: 249.00 E-value: 2.90e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 93 IILGGGAGTRLFPLTKRRAKPAVPIGGAYRLIDVPMSNCINSGINKVYILTQYNSASLNRHLARAYNSnGLGFGDGYVEV 172
Cdd:cd02508 2 IILAGGEGTRLSPLTKKRAKPAVPFGGRYRLIDFPLSNMVNSGIRNVGVLTQYKSRSLNDHLGSGKEW-DLDRKNGGLFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 173 LAATQTPGEsgkRWFQGTADAVRQFHWLFEDArskDIEDVLILSGDHLYRMDYMDFIQDHRQSGADISIScipiddrras 252
Cdd:cd02508 81 LPPQQRKGG---DWYRGTADAIYQNLDYIERS---DPEYVLILSGDHIYNMDYREMLDFHIESGADITVV---------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 253 dfglmkiddkgrvisfsekpkgddlkamavdttilglskeeaekkpYIASMGVYVFKKEILLNLLRWRF-PTANDFGSEI 331
Cdd:cd02508 145 ----------------------------------------------YKASMGIYIFSKDLLIELLEEDAaDGSHDFGKDI 178
|
250 260
....*....|....*....|..
gi 15239684 332 IPFSAKEFYVNAYLFNDYWEDI 353
Cdd:cd02508 179 IPAMLKKLKIYAYEFNGYWADI 200
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
93-354 |
6.51e-40 |
|
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: 143.88 E-value: 6.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 93 IILGGGAGTRLFPLTKRRAKPAVPIGGaYRLIDVPMSNCINSGINKVYILTQYNSASLNRHlaraynsnglgFGDGY--- 169
Cdd:cd04181 2 VILAAGKGTRLRPLTDTRPKPLLPIAG-KPILEYIIERLARAGIDEIILVVGYLGEQIEEY-----------FGDGSkfg 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 170 VEVLAATQTPGEsgkrwfqGTADAVRQFHWLFEDarskdiEDVLILSGDHLYRMDYMDFIQDHRQSGADISISCIPIDDr 249
Cdd:cd04181 70 VNIEYVVQEEPL-------GTAGAVRNAEDFLGD------DDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVED- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 250 rASDFGLMKIDDKGRVISFSEKPKgddlkamavdttilglskeeaEKKPYIASMGVYVFKKEIlLNLLRWRFPTANDFGS 329
Cdd:cd04181 136 -PSRYGVVELDDDGRVTRFVEKPT---------------------LPESNLANAGIYIFEPEI-LDYIPEILPRGEDELT 192
|
250 260
....*....|....*....|....*
gi 15239684 330 EIIPFSAKEFYVNAYLFNDYWEDIG 354
Cdd:cd04181 193 DAIPLLIEEGKVYGYPVDGYWLDIG 217
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
93-366 |
2.75e-36 |
|
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: 134.90 E-value: 2.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 93 IILGGGAGTRLFPLTKRRAKPAVPIGGayR-LIDVPMSNCINSGINKVYILTQYNSASLNRHLAraynsNGLGFGdgyVE 171
Cdd:COG1208 3 VILAGGLGTRLRPLTDTRPKPLLPVGG--KpLLEHILERLAAAGITEIVINVGYLAEQIEEYFG-----DGSRFG---VR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 172 VLAATQtpgesGKRWfqGTADAVRQFHWLFEDarskdiEDVLILSGDHLYRMDYMDFIQDHRQSGADISISCIPIDDRra 251
Cdd:COG1208 73 ITYVDE-----GEPL--GTGGALKRALPLLGD------EPFLVLNGDILTDLDLAALLAFHREKGADATLALVPVPDP-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 252 SDFGLMKIDDKGRVISFSEKPKGDdlkamavdttilglskeeaekKPYIASMGVYVFKKEILLNLlrwrfPTANDFG-SE 330
Cdd:COG1208 138 SRYGVVELDGDGRVTRFVEKPEEP---------------------PSNLINAGIYVLEPEIFDYI-----PEGEPFDlED 191
|
250 260 270
....*....|....*....|....*....|....*.
gi 15239684 331 IIPFSAKEFYVNAYLFNDYWEDIGTIRSFFEANLAL 366
Cdd:COG1208 192 LLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALL 227
|
|
| glgD |
TIGR02092 |
glucose-1-phosphate adenylyltransferase, GlgD subunit; This family is GlgD, an apparent ... |
103-489 |
5.84e-35 |
|
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: 134.82 E-value: 5.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 103 LFPLTKRRAKPAVPIGGAYRLIDVPMSNCINSGINKVYILTQYNS-ASLNRHLaRAYNSNGL-GFGDGYVEVLAATQTPG 180
Cdd:TIGR02092 16 LSPLTKVRPLASLPFGGRYRLIDFPLSNMVNAGIRNVFIFFKNKErQSLFDHL-GSGREWDLhRKRDGLFVFPYNDRDDL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 181 ESGKRwfqgtadavRQFHWLFEDARSKDIEDVLILSGDHLYRMDYMDFIQDHRQSGADISISCIPIDDRRASDF-GLMKI 259
Cdd:TIGR02092 95 SEGGK---------RYFSQNLEFLKRSTSEYTVVLNSHMVCNIDLKAVLKYHEETGKDITVVYKKVKPADASEYdTILRF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 260 DDKGRVISFSEKpkgddlkamavdttilgLSKEEAEKKpyiaSMGVYVFKKEILLNLLRwrfpTANDFG-----SEIIPF 334
Cdd:TIGR02092 166 DESGKVKSIGQN-----------------LNPEEEENI----SLDIYIVSTDLLIELLY----ECIQRGkltslEELIRE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 335 SAKEFYVNAYLFNDYWEDIGTIRSFFEANLALTEhPGAFS--FYDAAKPIYTSRRNLPPSK-IDNSKLIDSIISHGSFLt 411
Cdd:TIGR02092 221 NLKELNINAYEYTGYLANINSVKSYYKANMDLLD-PQNFQslFYSSQGPIYTKVKDEPPTYyAENSKVENSLVANGCII- 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15239684 412 NCLIEHSIVGIRSRVGSNVQLKDTVMLgadyyeTEAEvaallaegnvpigIGENTKIQECIIDKNARVGKNVIIANSE 489
Cdd:TIGR02092 299 EGKVENSILSRGVHVGKDALIKNCIIM------QRTV-------------IGEGAHLENVIIDKDVVIEPNVKIAGTS 357
|
|
| LbH_G1P_AT_C |
cd04651 |
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ... |
390-516 |
1.61e-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: 106.01 E-value: 1.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 390 PPSKIDNSKLIDSIISHGSFLTNCLIEHSIVGIRSRVGSNVQLKDTVMLGADyyeteaevaallaegnvpiGIGENTKIQ 469
Cdd:cd04651 1 PPYIGRRGEVKNSLVSEGCIISGGTVENSVLFRGVRVGSGSVVEDSVIMPNV-------------------GIGRNAVIR 61
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15239684 470 ECIIDKNARVGKNVIIANSEGIQEAdrssDGFYIRSGITVILKNSVI 516
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 ... |
93-362 |
2.94e-24 |
|
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: 100.71 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 93 IILGGGAGTRLFPLTKRRAKPAVPIGGaYRLIDVPMSNCINSGINKVYILTQYNSASLNRHLARaynsnglGFGDGYVEV 172
Cdd:cd06915 2 VILAGGLGTRLRSVVKDLPKPLAPVAG-RPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGD-------GYRGGIRIY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 173 LAATQTPgesgkrwfQGTADAVRQFhwlfedARSKDIEDVLILSGDHLYRMDYMDFIQDHRQSGADISISCIPIDDRraS 252
Cdd:cd06915 74 YVIEPEP--------LGTGGAIKNA------LPKLPEDQFLVLNGDTYFDVDLLALLAALRASGADATMALRRVPDA--S 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 253 DFGLMKIDDKGRVISFSEKPKGDDLKamavdttilglskeeaekkpYIASmGVYVFKKEILLNLLRWRFptanDFGSEII 332
Cdd:cd06915 138 RYGNVTVDGDGRVIAFVEKGPGAAPG--------------------LING-GVYLLRKEILAEIPADAF----SLEADVL 192
|
250 260 270
....*....|....*....|....*....|
gi 15239684 333 PFSAKEFYVNAYLFNDYWEDIGTIRSFFEA 362
Cdd:cd06915 193 PALVKRGRLYGFEVDGYFIDIGIPEDYARA 222
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
93-363 |
1.14e-18 |
|
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: 84.87 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 93 IILGGGAGTRLFPLTKRRAKPAVPIGGAyRLIDVPMSNCINSGINKVYILTQYNSaslnrHLARAYNSNGLGFGDG--YV 170
Cdd:cd06426 2 VIMAGGKGTRLRPLTENTPKPMLKVGGK-PILETIIDRFIAQGFRNFYISVNYLA-----EMIEDYFGDGSKFGVNisYV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 171 evlaatqtpgESGKRWfqGTADAVRQFhwlfedaRSKDIEDVLILSGDHLYRMDYMDFIQDHRQSGADISISC------I 244
Cdd:cd06426 76 ----------REDKPL--GTAGALSLL-------PEKPTDPFLVMNGDILTNLNYEHLLDFHKENNADATVCVreyevqV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 245 PiddrrasdFGLMKIDDkGRVISFSEKPkgddlkamavdttilglskeeaeKKPYIASMGVYVFKKEILLNLLRWRFPTA 324
Cdd:cd06426 137 P--------YGVVETEG-GRITSIEEKP-----------------------THSFLVNAGIYVLEPEVLDLIPKNEFFDM 184
|
250 260 270
....*....|....*....|....*....|....*....
gi 15239684 325 NDFGSEIIPFSAKefyVNAYLFNDYWEDIGTIRSFFEAN 363
Cdd:cd06426 185 PDLIEKLIKEGKK---VGVFPIHEYWLDIGRPEDYEKAN 220
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
93-363 |
1.16e-17 |
|
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: 82.23 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 93 IILGGGAGTRLFPLTKRRAKPAVPIGGAyRLIDVPMSNCINSGINKVYILTQYNSASLNRHLaraynsnglgfGDGYVEV 172
Cdd:cd04189 4 LILAGGKGTRLRPLTYTRPKQLIPVAGK-PIIQYAIEDLREAGIEDIGIVVGPTGEEIKEAL-----------GDGSRFG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 173 LAATQTPGESGKrwfqGTADAVrqfhwlfedARSKDI---EDVLILSGDHLYRMDYMDFIQDHRQSGADISISCIPIDDR 249
Cdd:cd04189 72 VRITYILQEEPL----GLAHAV---------LAARDFlgdEPFVVYLGDNLIQEGISPLVRDFLEEDADASILLAEVEDP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 250 RAsdFGLMKIDDkGRVISFSEKPKgddlkamavdttilglskeeaEKKPYIASMGVYVFKKEIL--LNLLR--WR----F 321
Cdd:cd04189 139 RR--FGVAVVDD-GRIVRLVEKPK---------------------EPPSNLALVGVYAFTPAIFdaISRLKpsWRgeleI 194
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15239684 322 PTAndfgseIIPFSAKEFYVNAYLFNDYWEDIGTIRSFFEAN 363
Cdd:cd04189 195 TDA------IQWLIDRGRRVGYSIVTGWWKDTGTPEDLLEAN 230
|
|
| rmlA_long |
TIGR01208 |
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ... |
93-482 |
1.89e-15 |
|
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: 77.83 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 93 IILGGGAGTRLFPLTKRRAKPAVPIGGAyRLIDVPMSNCINSGINKVYILTQYNSASLNRHLARaynsNGLGFGdgyvev 172
Cdd:TIGR01208 3 LILAAGKGTRLRPLTFTRPKQLIPVANK-PILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVG----EGERFG------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 173 laATQTPGESGKRwfQGTADAVRQFHWLFEDarskdiEDVLILSGDHLYRMDYMDFIQDHRQSGADISISCIPIDDRRAs 252
Cdd:TIGR01208 72 --AKITYIVQGEP--LGLAHAVYTARDFLGD------DDFVVYLGDNLIQDGISRFVKSFEEKDYDALILLTKVRDPTA- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 253 dFGLMKIDDKGRVISFSEKPKgddlkamavdttilglskeeaEKKPYIASMGVYVFKK---EILLNLL-RWRfpTANDFG 328
Cdd:TIGR01208 141 -FGVAVLEDGKRILKLVEKPK---------------------EPPSNLAVVGLYMFRPlifEAIKNIKpSWR--GELEIT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 329 SEIIPFSAKEFYVNAYLFNDYWEDIGTIRSFFEAN-LALTEHPGAFSFYDAAKPIyTSRRNLPPSkidnSKLIDSIIsHG 407
Cdd:TIGR01208 197 DAIQWLIEKGYKVGGSKVTGWWKDTGKPEDLLDANrLILDEVEREVQGVDDESKI-RGRVVVGEG----AKIVNSVI-RG 270
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15239684 408 SFLT--NCLIEHSIVGIRSRVGSNVQLKDtvmlgadyyeTEAEVAALLAEGNVpigIGENTKIQECIIDKNARVGKN 482
Cdd:TIGR01208 271 PAVIgeDCIIENSYIGPYTSIGEGVVIRD----------AEVEHSIVLDESVI---EGVQARIVDSVIGKKVRIKGN 334
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
93-273 |
7.65e-12 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 66.27 E-value: 7.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 93 IILGGGAGTRLFPLTKRRAKPAVPIGGA---YRLIDVPMSncinSGINKVY-ILTQYNSASLNRHLaraynsnglgfGDG 168
Cdd:COG1209 4 IILAGGSGTRLRPLTLTVSKQLLPVYDKpmiYYPLSTLML----AGIREILiISTPEDGPQFERLL-----------GDG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 169 --------YVEvlaatQ-TPgesgkrwfQGTADAVrqfhWLFEDArskdIED---VLILsGDHLYRMDYM-DFIQDHRQS 235
Cdd:COG1209 69 sqlgikisYAV-----QpEP--------LGLAHAF----IIAEDF----IGGdpvALVL-GDNIFYGDGLsELLREAAAR 126
|
170 180 190
....*....|....*....|....*....|....*...
gi 15239684 236 GADISISCIPIDDRRAsdFGLMKIDDKGRVISFSEKPK 273
Cdd:COG1209 127 ESGATIFGYKVEDPER--YGVVEFDEDGRVVSLEEKPK 162
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
93-313 |
5.50e-10 |
|
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: 59.21 E-value: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 93 IILGGGAGTRLFPLTKRRAKPAVPIGGaYRLIDVPMSNCINSGINKVYILTQYNSASLNRHLARAYNSNGLGFGDGYVEV 172
Cdd:cd04198 4 VILAGGGGSRLYPLTDNIPKALLPVAN-KPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFPLNLKQKLDEVTIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 173 LaATQTpgesgkrwfqGTADAVRQFHwlfedarSKDIEDVLILSGDHLYRMDYMDFIQDHRQSGAdiSISCI----PIDD 248
Cdd:cd04198 83 L-DEDM----------GTADSLRHIR-------KKIKKDFLVLSCDLITDLPLIELVDLHRSHDA--SLTVLlyppPVSS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 249 RRASDFGLMKIDDKGRVISFSEKpkgddlkamavDTTILGLSKEEAEKKPYIASMG------------------VYVFKK 310
Cdd:cd04198 143 EQKGGKGKSKKADERDVIGLDEK-----------TQRLLFITSEEDLDEDLELRKSllkrhprvtittklldahVYIFKR 211
|
...
gi 15239684 311 EIL 313
Cdd:cd04198 212 WVL 214
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
93-273 |
1.37e-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: 55.66 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 93 IILGGGAGTRLFPLTKRRAKPAVPIgGAYRLIDVPMSNCINSGINKVYILTQYNSASLNRHLaraynsnglgFGDG---- 168
Cdd:cd02538 4 IILAGGSGTRLYPLTKVVSKQLLPV-YDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKEL----------LGDGsdlg 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 169 ----YvevlAATQTPGesgkrwfqGTADAVrqfhWLFEDARSKDieDVLILSGDHLYR-MDYMDFIQDHRQSGADISISC 243
Cdd:cd02538 73 iritY----AVQPKPG--------GLAQAF----IIGEEFIGDD--PVCLILGDNIFYgQGLSPILQRAAAQKEGATVFG 134
|
170 180 190
....*....|....*....|....*....|
gi 15239684 244 IPIDDrrASDFGLMKIDDKGRVISFSEKPK 273
Cdd:cd02538 135 YEVND--PERYGVVEFDENGRVLSIEEKPK 162
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
93-296 |
5.88e-08 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 53.71 E-value: 5.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 93 IILGGGAGTRLFPLTKRRAKPAVPIGGaYRLIDVPMSNCINSGINKVYILTQYNSASLNRHLAR-------AYNSNGLGF 165
Cdd:COG1213 3 VILAAGRGSRLGPLTDDIPKCLVEIGG-KTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARpgpdvtfVYNPDYDET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 166 GDGYVeVLAAtqtpgesgKRWFQgtadavrqfhwlfedarskdiEDVLILSGDHLYRMDYMDFIQDHRQSgadisiSCIP 245
Cdd:COG1213 82 NNIYS-LWLA--------REALD---------------------EDFLLLNGDVVFDPAILKRLLASDGD------IVLL 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15239684 246 IDDRRASDFG---LMKIDDKGRVISFSEKPKGDDlkAMAVDTTILGLSKEEAEK 296
Cdd:COG1213 126 VDRKWEKPLDeevKVRVDEDGRIVEIGKKLPPEE--ADGEYIGIFKFSAEGAAA 177
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
93-218 |
1.74e-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: 51.87 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 93 IILGGGAGTRLFPLTKRRAKPAVPIGGAYrLIDVPMSNCINSGINKVYILTQYNSASLNRHLARAYNSNGLGFGDGYVEV 172
Cdd:cd02507 4 VVLADGFGSRFLPLTSDIPKALLPVANVP-LIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKWSSLSSKMIVDVIT 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 15239684 173 LAATQTpgesgkrwfQGTADAVRqfhwlfeDARSKDIEDVLILSGD 218
Cdd:cd02507 83 SDLCES---------AGDALRLR-------DIRGLIRSDFLLLSCD 112
|
|
| LbH_G1P_AT_C_like |
cd03356 |
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
412-488 |
2.40e-06 |
|
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: 45.31 E-value: 2.40e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15239684 412 NCLIEHSIVGIRSRVGSNVQLKDTVMLGADYyeteaevaallaegnvpigIGENTKIQECIIDKNARVGKNVIIANS 488
Cdd:cd03356 11 NAIIKNSVIGDNVRIGDGVTITNSILMDNVT-------------------IGANSVIVDSIIGDNAVIGENVRVVNL 68
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
94-362 |
8.08e-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: 8.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 94 ILGGGAGTRLFPLTKRRAKPAVPIGGAyRLIDVPMSNCINSGINKVYILTQYNSASLNRHLARAYNSNGLGFGDGYVEVL 173
Cdd:cd06422 4 ILAAGLGTRMRPLTDTRPKPLVPVAGK-PLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDSRFGLRITISDEPDELL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 174 aatqtpgesgkrwfqGTADAVRQfhwlfedARSK-DIEDVLILSGDHLYRMDYMDFIqDHRQSGADISISCIPIDDRRAS 252
Cdd:cd06422 83 ---------------ETGGGIKK-------ALPLlGDEPFLVVNGDILWDGDLAPLL-LLHAWRMDALLLLLPLVRNPGH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 253 ----DFGLmkiDDKGRVIsfsekpkgddlkamavdttilglSKEEAEKKPYIASmGVYVFKKEILLNLLRWRFPtandfg 328
Cdd:cd06422 140 ngvgDFSL---DADGRLR-----------------------RGGGGAVAPFTFT-GIQILSPELFAGIPPGKFS------ 186
|
250 260 270
....*....|....*....|....*....|....*..
gi 15239684 329 seIIPF---SAKEFYVNAYLFNDYWEDIGTIRSFFEA 362
Cdd:cd06422 187 --LNPLwdrAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
93-159 |
1.02e-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: 46.84 E-value: 1.02e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15239684 93 IILGGGAGTRLFPLTKRRAKPAVPIGGAyRLIDVPMSNCINSGINKVYILTQYNSASLNRHLARAYN 159
Cdd:cd02523 2 IILAAGRGSRLRPLTEDRPKCLLEINGK-PLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPN 67
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
88-272 |
2.55e-05 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 46.21 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 88 RTVASIILGGGAGTRLFPLTKRRAKPAVPIGGAyRLIDVPMSNCINSGINKVYILTQYNSASLNRHLaraynsnglgFGD 167
Cdd:PRK15480 2 KTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDK-PMIYYPLSTLMLAGIRDILIISTPQDTPRFQQL----------LGD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 168 GyvevlaatQTPGESGKRWFQGTADAVRQFHWLFEDARSKDiEDVLILSGDHLYRMDYMDFIQD--HRQSGADISISCIP 245
Cdd:PRK15480 71 G--------SQWGLNLQYKVQPSPDGLAQAFIIGEEFIGGD-DCALVLGDNIFYGHDLPKLMEAavNKESGATVFAYHVN 141
|
170 180
....*....|....*....|....*..
gi 15239684 246 IDDRrasdFGLMKIDDKGRVISFSEKP 272
Cdd:PRK15480 142 DPER----YGVVEFDQNGTAISLEEKP 164
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
189-318 |
4.90e-05 |
|
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: 44.81 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 189 GTADAVRQFhwlfEDARSKDIEDVLILSGDH-LYRMDYM-DFIQDHRQSGADISISCIPIDDrrASDFGLMKIDDKGRVI 266
Cdd:cd02540 74 GTGHAVKQA----LPALKDFEGDVLVLYGDVpLITPETLqRLLEAHREAGADVTVLTAELED--PTGYGRIIRDGNGKVL 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15239684 267 SFSEkpkgddlkamAVDTTilglskeEAEKKPYIASMGVYVFKKEILLNLLR 318
Cdd:cd02540 148 RIVE----------EKDAT-------EEEKAIREVNAGIYAFDAEFLFEALP 182
|
|
| LbH_eIF2B_epsilon |
cd05787 |
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
462-522 |
1.07e-04 |
|
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: 1.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15239684 462 IGENTKIQECIIDKNARVGKNVIIANSegiqeadrssdgfYIRSGITV----ILKNSVIKDGVVI 522
Cdd:cd05787 8 IGEGTTIKNSVIGRNCKIGKNVVIDNS-------------YIWDDVTIedgcTIHHSIVADGAVI 59
|
|
| GT2_BcE_like |
cd04183 |
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ... |
212-310 |
3.57e-04 |
|
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.
Pssm-ID: 133026 [Multi-domain] Cd Length: 231 Bit Score: 42.24 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239684 212 VLILSGDHLYRMDYMDFIQDHRQSGADISI-SCIPIDDRrasdFGLMKIDDKGRVIsfsekpkgddlkamavdttilgls 290
Cdd:cd04183 101 LLIFNCDQIVESDLLAFLAAFRERDLDGGVlTFFSSHPR----WSYVKLDENGRVI------------------------ 152
|
90 100
....*....|....*....|..
gi 15239684 291 kEEAEKKPY--IASMGVYVFKK 310
Cdd:cd04183 153 -ETAEKEPIsdLATAGLYYFKS 173
|
|
| LbH_eIF2B_gamma_C |
cd04652 |
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
462-522 |
1.70e-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: 37.56 E-value: 1.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15239684 462 IGENTKIQECIIDKNARVGKNVIIANSegiqeadrssdgfyirsgitVILKNSVIKDGVVI 522
Cdd:cd04652 8 VGEKTSIKRSVIGANCKIGKRVKITNC--------------------VIMDNVTIEDGCTL 48
|
|
| LbH_eIF2B_epsilon |
cd05787 |
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
411-485 |
3.09e-03 |
|
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: 36.79 E-value: 3.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15239684 411 TNCLIEHSIVGIRSRVGSNVQLKDtvmlgadyyeteaevaALLAEGNVpigIGENTKIQECIIDKNARVGKNVII 485
Cdd:cd05787 10 EGTTIKNSVIGRNCKIGKNVVIDN----------------SYIWDDVT---IEDGCTIHHSIVADGAVIGKGCTI 65
|
|
| LbH_G1P_AT_C_like |
cd03356 |
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
462-520 |
4.56e-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: 36.07 E-value: 4.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 15239684 462 IGENTKIQECIIDKNARVGKNVIIANSEgIQEADRSSDGFYIRSgiTVILKNSVIKDGV 520
Cdd:cd03356 8 IGENAIIKNSVIGDNVRIGDGVTITNSI-LMDNVTIGANSVIVD--SIIGDNAVIGENV 63
|
|
| |
