|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02241 |
PLN02241 |
glucose-1-phosphate adenylyltransferase |
101-520 |
0e+00 |
|
glucose-1-phosphate adenylyltransferase
Pssm-ID: 215133 [Multi-domain] Cd Length: 436 Bit Score: 841.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 101 TRLYPLTKKRAKPAVPLGANYRLIDIPVSNCLNSNISKIYVLTQFNSASLNRHLSRAYASNMGGYKNEGFVEVLAAQQSP 180
Cdd:PLN02241 15 TRLFPLTKRRAKPAVPIGGNYRLIDIPMSNCINSGINKIYVLTQFNSASLNRHLSRAYNFGNGGNFGDGFVEVLAATQTP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 181 ENPNWFQGTADAVRQYLWLFEEH---NVLEYLILAGDHLYRMDYEKFIQAHRETDADITVAALPMDEQRATAFGLMKIDE 257
Cdd:PLN02241 95 GEKGWFQGTADAVRQFLWLFEDAknkNVEEVLILSGDHLYRMDYMDFVQKHRESGADITIACLPVDESRASDFGLMKIDD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 258 EGRIIEFAEKPKGEHLKAMKVDTTILGLDDQRAKEMPFIASMGIYVVSRDVMLDLLRNQFPGANDFGSEVIPGATSLGLR 337
Cdd:PLN02241 175 TGRIIEFSEKPKGDELKAMQVDTTVLGLSPEEAKEKPYIASMGIYVFKKDVLLKLLRWRFPTANDFGSEIIPGAIKEGYN 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 338 VQAYLYDGYWEDIGTIEAFYNANLGITKKPvPDFSFYDRSAPIYTQPRYLPPSKMLDADVTDSVIGEGCVIKNCKIHHSV 417
Cdd:PLN02241 255 VQAYLFDGYWEDIGTIKSFYEANLALTKQP-PKFSFYDPDAPIYTSPRFLPPSKIEDCRITDSIISHGCFLRECKIEHSV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 418 VGLRSCISEGAIIEDSLLMGADYYETATEKSLLSAKGSVPIGIGKNSHIKRAIIDKNARIGDNVKIINSDNVQEAARETD 497
Cdd:PLN02241 334 VGLRSRIGEGVEIEDTVMMGADYYETEEEIASLLAEGKVPIGIGENTKIRNAIIDKNARIGKNVVIINKDGVQEADREEE 413
|
410 420
....*....|....*....|...
gi 15238933 498 GYFIKSGIVTVIKDALIPTGTVI 520
Cdd:PLN02241 414 GYYIRSGIVVILKNAVIPDGTVI 436
|
|
| glgC |
PRK02862 |
glucose-1-phosphate adenylyltransferase; Provisional |
101-520 |
0e+00 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179486 [Multi-domain] Cd Length: 429 Bit Score: 763.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 101 TRLYPLTKKRAKPAVPLGANYRLIDIPVSNCLNSNISKIYVLTQFNSASLNRHLSRAYasNMGGYkNEGFVEVLAAQQSP 180
Cdd:PRK02862 15 TRLYPLTKLRAKPAVPLAGKYRLIDIPISNCINSGINKIYVLTQFNSASLNRHISQTY--NFDGF-SGGFVEVLAAQQTP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 181 ENPNWFQGTADAVRQYLWLFEEHNVLEYLILAGDHLYRMDYEKFIQAHRETDADITVAALPMDEQRATAFGLMKIDEEGR 260
Cdd:PRK02862 92 ENPSWFQGTADAVRKYLWHFQEWDVDEYLILSGDQLYRMDYRLFVQHHRETGADITLAVLPVDEKDASGFGLMKTDDDGR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 261 IIEFAEKPKGEHLKAMKVDTTILGLDDQRAKEMPFIASMGIYVVSRDVMLDLLRNQfPGANDFGSEVIPGATSlGLRVQA 340
Cdd:PRK02862 172 ITEFSEKPKGDELKAMAVDTSRLGLSPEEAKGKPYLASMGIYVFSRDVLFDLLNKN-PEYTDFGKEIIPEAIR-DYKVQS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 341 YLYDGYWEDIGTIEAFYNANLGITKKPVPDFSFYDRSAPIYTQPRYLPPSKMLDADVTDSVIGEGCVIKNCKIHHSVVGL 420
Cdd:PRK02862 250 YLFDGYWEDIGTIEAFYEANLALTQQPNPPFSFYDEKAPIYTRARYLPPSKLLDATITESIIAEGCIIKNCSIHHSVLGI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 421 RSCISEGAIIEDSLLMGADYYETATEKSLLSAKGSVPIGIGKNSHIKRAIIDKNARIGDNVKIINSDNVQEAARETDGYF 500
Cdd:PRK02862 330 RSRIESGCTIEDTLVMGADFYESSEEREELRKEGKPPLGIGEGTTIKRAIIDKNARIGNNVRIVNKDNVEEADREDQGFY 409
|
410 420
....*....|....*....|
gi 15238933 501 IKSGIVTVIKDALIPTGTVI 520
Cdd:PRK02862 410 IRDGIVVVVKNAVIPDGTVI 429
|
|
| GlgC |
COG0448 |
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
101-513 |
5.35e-166 |
|
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];
Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 474.56 E-value: 5.35e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 101 TRLYPLTKKRAKPAVPLGANYRLIDIPVSNCLNSNISKIYVLTQFNSASLNRHLSRAYASNMGGYKneGFVEVLAAQQSP 180
Cdd:COG0448 13 SRLGPLTKDRAKPAVPFGGKYRIIDFPLSNCVNSGIRRVGVLTQYKSHSLNDHIGSGKPWDLDRKR--GGVFILPPYQQR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 181 ENPNWFQGTADAVRQYLWLFEEHNVLEYLILAGDHLYRMDYEKFIQAHRETDADITVAALPMDEQRATAFGLMKIDEEGR 260
Cdd:COG0448 91 EGEDWYQGTADAVYQNLDFIERSDPDYVLILSGDHIYKMDYRQMLDFHIESGADITVACIEVPREEASRFGVMEVDEDGR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 261 IIEFAEKPKgehlkamkvdttilglddqraKEMPFIASMGIYVVSRDVMLDLL-RNQFPGANDFGSEVIPGATSlGLRVQ 339
Cdd:COG0448 171 ITEFEEKPK---------------------DPKSALASMGIYVFNKDVLIELLeEDAPNSSHDFGKDIIPRLLD-RGKVY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 340 AYLYDGYWEDIGTIEAFYNANLGITkKPVPDFSFYDRSAPIYTQPRYLPPSKML-DADVTDSVIGEGCVIKNcKIHHSVV 418
Cdd:COG0448 229 AYEFDGYWRDVGTIDSYYEANMDLL-DPEPEFNLYDPEWPIYTKQKDLPPAKFVrGGKVKNSLVSNGCIISG-TVENSVL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 419 GLRSCISEGAIIEDSLLMGAdyyetateksllsakgsvpIGIGKNSHIKRAIIDKNARIGDNVKIINSDNvqeaaRETDG 498
Cdd:COG0448 307 FRGVRVESGAVVENSVIMPG-------------------VVIGEGAVIENAIIDKNVVIPPGVVIGEDPE-----EDRKR 362
|
410
....*....|....*
gi 15238933 499 YFIKSGIVTVIKDAL 513
Cdd:COG0448 363 FTVSSGIVVVGKGAV 377
|
|
| glgC |
TIGR02091 |
glucose-1-phosphate adenylyltransferase; This enzyme, glucose-1-phosphate adenylyltransferase, ... |
101-485 |
5.49e-166 |
|
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: 474.06 E-value: 5.49e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 101 TRLYPLTKKRAKPAVPLGANYRLIDIPVSNCLNSNISKIYVLTQFNSASLNRHLSRAYasNMGGYKNeGFVEVLAAQQSP 180
Cdd:TIGR02091 10 SRLSPLTKRRAKPAVPFGGKYRIIDFPLSNCINSGIRRIGVLTQYKSHSLNRHIQRGW--DFDGFID-GFVTLLPAQQRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 181 ENPNWFQGTADAVRQYLWLFEEHNVLEYLILAGDHLYRMDYEKFIQAHRETDADITVAALPMDEQRATAFGLMKIDEEGR 260
Cdd:TIGR02091 87 SGTDWYQGTADAVYQNLDLIEDYDPEYVLILSGDHIYKMDYEKMLDYHIESGADVTIACIPVPRKEASRFGVMQVDEDGR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 261 IIEFAEKPKGEhlKAMkvdttilglddqRAKEMPFIASMGIYVVSRDVMLDLLR---NQFPGANDFGSEVIPGATSLGlR 337
Cdd:TIGR02091 167 IVDFEEKPANP--PSI------------PGMPDFALASMGIYIFDKDVLKELLEedaDDPESSHDFGKDIIPRALEEG-S 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 338 VQAYLYDGYWEDIGTIEAFYNANLGITkKPVPDFSFYDRSAPIYTQPRYLPPSKMLDAD--VTDSVIGEGCVIKNCKIHH 415
Cdd:TIGR02091 232 VQAYLFSGYWRDVGTIDSFWEANMDLV-SVVPPFDLYDRKWPIYTYNEFLPPAKFVDSDaqVVDSLVSEGCIISGATVSH 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 416 SVVGLRSCISEGAIIEDSLLMGAdyyetateksllsakgsvpIGIGKNSHIKRAIIDKNARIGDNVKIIN 485
Cdd:TIGR02091 311 SVLGIRVRIGSGSTVEDSVIMGD-------------------VGIGRGAVIRNAIIDKNVRIGEGVVIGN 361
|
|
| glgC |
PRK00725 |
glucose-1-phosphate adenylyltransferase; Provisional |
101-513 |
9.43e-117 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234824 [Multi-domain] Cd Length: 425 Bit Score: 351.07 E-value: 9.43e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 101 TRLYPLTKKRAKPAVPLGANYRLIDIPVSNCLNSNISKIYVLTQFNSASLNRHLSRAYaSNMGGYKNEgFVEVLAAQQSP 180
Cdd:PRK00725 27 SRLKELTDKRAKPAVYFGGKFRIIDFALSNCINSGIRRIGVLTQYKAHSLIRHIQRGW-SFFREELGE-FVDLLPAQQRV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 181 ENPNWFQGTADAVRQYLWLFEEHNVlEY-LILAGDHLYRMDYEKFIQAHRETDADITVAALPMDEQRATAFGLMKIDEEG 259
Cdd:PRK00725 105 DEENWYRGTADAVYQNLDIIRRYDP-KYvVILAGDHIYKMDYSRMLADHVESGADCTVACLEVPREEASAFGVMAVDEND 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 260 RIIEFAEKPKgeHLKAM--KVDTTilglddqrakempfIASMGIYVVSRDVMLDLLR--NQFPGAN-DFGSEVIPGATSL 334
Cdd:PRK00725 184 RITAFVEKPA--NPPAMpgDPDKS--------------LASMGIYVFNADYLYELLEedAEDPNSShDFGKDIIPKIVEE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 335 GlRVQAYLY-----------DGYWEDIGTIEAFYNANLGITkKPVPDFSFYDRSAPIYTQPRYLPPSK-MLDAD-----V 397
Cdd:PRK00725 248 G-KVYAHPFsdscvrsdpeeEPYWRDVGTLDAYWQANLDLA-SVTPELDLYDRNWPIWTYQEQLPPAKfVFDRSgrrgmA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 398 TDSVIGEGCVIKNCKIHHSVVGLRSCISEGAIIEDSLLMgaDYYEtateksllsakgsvpigIGKNSHIKRAIIDKNARI 477
Cdd:PRK00725 326 INSLVSGGCIISGAVVRRSVLFSRVRVNSFSNVEDSVLL--PDVN-----------------VGRSCRLRRCVIDRGCVI 386
|
410 420 430
....*....|....*....|....*....|....*..
gi 15238933 478 GDNVkIINSDNVQEAARetdgYFI-KSGIVTVIKDAL 513
Cdd:PRK00725 387 PEGM-VIGEDPEEDAKR----FRRsEEGIVLVTREML 418
|
|
| glgC |
PRK00844 |
glucose-1-phosphate adenylyltransferase; Provisional |
101-514 |
5.47e-114 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 343.35 E-value: 5.47e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 101 TRLYPLTKKRAKPAVPLGANYRLIDIPVSNCLNSNISKIYVLTQFNSASLNRHLSRAYasNMGGYKNEgFVEVLAAQQSp 180
Cdd:PRK00844 17 KRLMPLTADRAKPAVPFGGSYRLIDFVLSNLVNSGYLRIYVLTQYKSHSLDRHISQTW--RLSGLLGN-YITPVPAQQR- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 181 ENPNWFQGTADAVRQYLWLFEEHNVlEY-LILAGDHLYRMDYEKFIQAHRETDADITVAALPMDEQRATAFGLMKIDEEG 259
Cdd:PRK00844 93 LGKRWYLGSADAIYQSLNLIEDEDP-DYvVVFGADHVYRMDPRQMVDFHIESGAGVTVAAIRVPREEASAFGVIEVDPDG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 260 RIIEFAEKPKGehlkamkvdttilglddqrAKEMP-----FIASMGIYVVSRDVMLDLLRNQF---PGANDFGSEVIPGA 331
Cdd:PRK00844 172 RIRGFLEKPAD-------------------PPGLPddpdeALASMGNYVFTTDALVDALRRDAadeDSSHDMGGDIIPRL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 332 TSLGlrvQAYLYD--------------GYWEDIGTIEAFYNANLGITkKPVPDFSFYDRSAPIYTQPRYLPPSKMLDAD- 396
Cdd:PRK00844 233 VERG---RAYVYDfstnevpgaterdrGYWRDVGTIDAYYDAHMDLL-SVHPVFNLYNREWPIYTSSPNLPPAKFVDGGg 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 397 ----VTDSVIGEGCVIKNCKIHHSVVGLRSCISEGAIIEDSLLMGadyyetateksllsakGSVpigIGKNSHIKRAIID 472
Cdd:PRK00844 309 rvgsAQDSLVSAGSIISGATVRNSVLSPNVVVESGAEVEDSVLMD----------------GVR---IGRGAVVRRAILD 369
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 15238933 473 KNARIGDNVKIinSDNVQEAARetdGYFI-KSGIVTVIKDALI 514
Cdd:PRK00844 370 KNVVVPPGATI--GVDLEEDRR---RFTVsEGGIVVVPKGQRV 407
|
|
| glgC |
PRK05293 |
glucose-1-phosphate adenylyltransferase; Provisional |
101-520 |
2.69e-96 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 296.78 E-value: 2.69e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 101 TRLYPLTKKRAKPAVPLGANYRLIDIPVSNCLNSNISKIYVLTQFNSASLNRHLSRAYASNMGGyKNEGfVEVLAAQQSP 180
Cdd:PRK05293 15 TRLGKLTKNIAKPAVPFGGKYRIIDFTLSNCANSGIDTVGVLTQYQPLELNNHIGIGSPWDLDR-INGG-VTILPPYSES 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 181 ENPNWFQGTADAVRQYLWLFEEHNVlEY-LILAGDHLYRMDYEKFIQAHRETDADITVAAL--PMDEqrATAFGLMKIDE 257
Cdd:PRK05293 93 EGGKWYKGTAHAIYQNIDYIDQYDP-EYvLILSGDHIYKMDYDKMLDYHKEKEADVTIAVIevPWEE--ASRFGIMNTDE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 258 EGRIIEFAEKPKgeHLKAMKvdttilglddqrakempfiASMGIYVVSRDVMLDLLRNQFPGAN---DFGSEVIPGATSL 334
Cdd:PRK05293 170 NMRIVEFEEKPK--NPKSNL-------------------ASMGIYIFNWKRLKEYLIEDEKNPNsshDFGKNVIPLYLEE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 335 GLRVQAYLYDGYWEDIGTIEAFYNANLGITkKPVPDFSFYDRSAPIYTQPRYLPPSKML-DADVTDSVIGEGCVIkNCKI 413
Cdd:PRK05293 229 GEKLYAYPFKGYWKDVGTIESLWEANMELL-RPENPLNLFDRNWRIYSVNPNLPPQYIAeNAKVKNSLVVEGCVV-YGTV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 414 HHSVVGLRSCISEGAIIEDSLLMgadyyeTATEksllsakgsvpigIGKNSHIKRAIIDKNARIGDNVKIINSDNvqeaa 493
Cdd:PRK05293 307 EHSVLFQGVQVGEGSVVKDSVIM------PGAK-------------IGENVVIERAIIGENAVIGDGVIIGGGKE----- 362
|
410 420
....*....|....*....|....*...
gi 15238933 494 retdgyfiksgIVTVI-KDALIPTGTVI 520
Cdd:PRK05293 363 -----------VITVIgENEVIGVGTVI 379
|
|
| ADP_Glucose_PP |
cd02508 |
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ... |
101-350 |
4.65e-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: 248.61 E-value: 4.65e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 101 TRLYPLTKKRAKPAVPLGANYRLIDIPVSNCLNSNISKIYVLTQFNSASLNRHLSRAYASNMGGYKneGFVEVLAAQQSP 180
Cdd:cd02508 10 TRLSPLTKKRAKPAVPFGGRYRLIDFPLSNMVNSGIRNVGVLTQYKSRSLNDHLGSGKEWDLDRKN--GGLFILPPQQRK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 181 eNPNWFQGTADAVRQYLWLFEEHNVLEYLILAGDHLYRMDYEKFIQAHRETDADITVAAlpmdeqratafglmkideegr 260
Cdd:cd02508 88 -GGDWYRGTADAIYQNLDYIERSDPEYVLILSGDHIYNMDYREMLDFHIESGADITVVY--------------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 261 iiefaekpkgehlkamkvdttilglddqrakempfIASMGIYVVSRDVMLDLLRN-QFPGANDFGSEVIPGATSLGlRVQ 339
Cdd:cd02508 146 -----------------------------------KASMGIYIFSKDLLIELLEEdAADGSHDFGKDIIPAMLKKL-KIY 189
|
250
....*....|.
gi 15238933 340 AYLYDGYWEDI 350
Cdd:cd02508 190 AYEFNGYWADI 200
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
101-364 |
2.26e-69 |
|
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: 222.51 E-value: 2.26e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 101 TRLYPLTKKRAKPAVPLGANYRLIDIPVSNCLNSNISK-IYVLTQFNSASLNRHLSRayasnmgGYKNEgfVEVLAAQQS 179
Cdd:pfam00483 11 TRLWPLTRTLAKPLVPVGGKYPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGD-------GSKFG--VQITYALQP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 180 PENpnwfqGTADAVRQYLWLFEEHNVlEYLILAGDHLYRMDYEKFIQAHRETDADITVAALPMDEQRATAFGLMKIDEEG 259
Cdd:pfam00483 82 EGK-----GTAPAVALAADFLGDEKS-DVLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGIVPVEPPTGYGVVEFDDNG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 260 RIIEFAEKPKGEhlkamkvdttilglddqrakEMPFIASMGIYVVSRDVMLDLLRNQFPGA--NDFGSEVIPGATSLGLR 337
Cdd:pfam00483 156 RVIRFVEKPKLP--------------------KASNYASMGIYIFNSGVLDFLAKYLEELKrgEDEITDILPKALEDGKL 215
|
250 260
....*....|....*....|....*...
gi 15238933 338 VQAYLYDGY-WEDIGTIEAFYNANLGIT 364
Cdd:pfam00483 216 AYAFIFKGYaWLDVGTWDSLWEANLFLL 243
|
|
| glgD |
TIGR02092 |
glucose-1-phosphate adenylyltransferase, GlgD subunit; This family is GlgD, an apparent ... |
103-486 |
1.11e-34 |
|
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: 134.05 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 103 LYPLTKKRAKPAVPLGANYRLIDIPVSNCLNSNISKIYVLTQFNS-ASLNRHLSRAYASNMGGYKNEGFVevlaAQQSPE 181
Cdd:TIGR02092 16 LSPLTKVRPLASLPFGGRYRLIDFPLSNMVNAGIRNVFIFFKNKErQSLFDHLGSGREWDLHRKRDGLFV----FPYNDR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 182 NPNWFQGtadaVRQYlwlfeeHNVLEYL---------ILAGDHLYRMDYEKFIQAHRETDADITVAALPMDEQratafgl 252
Cdd:TIGR02092 92 DDLSEGG----KRYF------SQNLEFLkrstseytvVLNSHMVCNIDLKAVLKYHEETGKDITVVYKKVKPA------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 253 mKIDEEGRIIEFAEKPKgehlkamkvdttILGLDDQRAKEMPFIASMGIYVVSRDVMLDLLRnqfpGANDFG-----SEV 327
Cdd:TIGR02092 155 -DASEYDTILRFDESGK------------VKSIGQNLNPEEEENISLDIYIVSTDLLIELLY----ECIQRGkltslEEL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 328 IPGATSlGLRVQAYLYDGYWEDIGTIEAFYNANLGITKKPVPDFSFYDRSAPIYTQPRYLPPSKMLD-ADVTDSVIGEGC 406
Cdd:TIGR02092 218 IRENLK-ELNINAYEYTGYLANINSVKSYYKANMDLLDPQNFQSLFYSSQGPIYTKVKDEPPTYYAEnSKVENSLVANGC 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 407 VIkNCKIHHSVVGLRSCISEGAIIEDSLLMGADYyetateksllsakgsvpigIGKNSHIKRAIIDKNARIGDNVKIINS 486
Cdd:TIGR02092 297 II-EGKVENSILSRGVHVGKDALIKNCIIMQRTV-------------------IGEGAHLENVIIDKDVVIEPNVKIAGT 356
|
|
| LbH_G1P_AT_C |
cd04651 |
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ... |
388-514 |
1.87e-34 |
|
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: 125.27 E-value: 1.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 388 PPSKMLDADVTDSVIGEGCVIKNCKIHHSVVGLRSCISEGAIIEDSLLMGADyyetateksllsakgsvpiGIGKNSHIK 467
Cdd:cd04651 1 PPYIGRRGEVKNSLVSEGCIISGGTVENSVLFRGVRVGSGSVVEDSVIMPNV-------------------GIGRNAVIR 61
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15238933 468 RAIIDKNARIGDNVKIINSDNVQEAaretDGYFIKSGIVTVIKDALI 514
Cdd:cd04651 62 RAIIDKNVVIPDGVVIGGDPEEDRA----RFYVTEDGIVVVGKGMVI 104
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
101-351 |
7.32e-34 |
|
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: 127.31 E-value: 7.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 101 TRLYPLTKKRAKPAVPLgANYRLIDIPVSNCLNSNISKIYVLTQFNSASLNRHLSRAYASNmggyKNEGFVEvlaaQQSP 180
Cdd:cd04181 10 TRLRPLTDTRPKPLLPI-AGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFG----VNIEYVV----QEEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 181 EnpnwfqGTADAVRQ-YLWLFEEHnvleYLILAGDHLYRMDYEKFIQAHRETDADITVAALPMDEQRatAFGLMKIDEEG 259
Cdd:cd04181 81 L------GTAGAVRNaEDFLGDDD----FLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVEDPS--RYGVVELDDDG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 260 RIIEFAEKPKGEHlkamkvdttilglddqrakemPFIASMGIYVVSRDVmLDLLRNQFPGANDFGSEVIPGATSlGLRVQ 339
Cdd:cd04181 149 RVTRFVEKPTLPE---------------------SNLANAGIYIFEPEI-LDYIPEILPRGEDELTDAIPLLIE-EGKVY 205
|
250
....*....|..
gi 15238933 340 AYLYDGYWEDIG 351
Cdd:cd04181 206 GYPVDGYWLDIG 217
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
101-360 |
1.23e-30 |
|
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: 119.10 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 101 TRLYPLTKKRAKPAVPLGaNYRLIDIPVSNCLNSNISKIYVLTqfnsaslnrhlsrayasnmgGYKNEGFVEVLAAQQ-- 178
Cdd:COG1208 11 TRLRPLTDTRPKPLLPVG-GKPLLEHILERLAAAGITEIVINV--------------------GYLAEQIEEYFGDGSrf 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 179 ------SPENPNWfqGTADAVRQYLWLFEEHNVleyLILAGDHLYRMDYEKFIQAHRETDADITVAALPMDEQRatAFGL 252
Cdd:COG1208 70 gvrityVDEGEPL--GTGGALKRALPLLGDEPF---LVLNGDILTDLDLAALLAFHREKGADATLALVPVPDPS--RYGV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 253 MKIDEEGRIIEFAEKPKGEHlkamkvdttilglddqrakemPFIASMGIYVVSRDVmLDLLRnqfPGAN-DFGsEVIPGA 331
Cdd:COG1208 143 VELDGDGRVTRFVEKPEEPP---------------------SNLINAGIYVLEPEI-FDYIP---EGEPfDLE-DLLPRL 196
|
250 260
....*....|....*....|....*....
gi 15238933 332 TSLGlRVQAYLYDGYWEDIGTIEAFYNAN 360
Cdd:COG1208 197 IAEG-RVYGYVHDGYWLDIGTPEDLLEAN 224
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
101-360 |
4.49e-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: 82.94 E-value: 4.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 101 TRLYPLTKKRAKPAVPLGaNYRLIDIPVSNCLNSNISKIYVltqfnsaSLN--RHLSRAYASNMG--GYKNEGFVEvlaa 176
Cdd:cd06426 10 TRLRPLTENTPKPMLKVG-GKPILETIIDRFIAQGFRNFYI-------SVNylAEMIEDYFGDGSkfGVNISYVRE---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 177 qqspENPnwfQGTADAvrqyLWLFEEHNVLEYLILAGDHLYRMDYEKFIQAHRETDADITVAALPMDEQraTAFGLMKID 256
Cdd:cd06426 78 ----DKP---LGTAGA----LSLLPEKPTDPFLVMNGDILTNLNYEHLLDFHKENNADATVCVREYEVQ--VPYGVVETE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 257 eEGRIIEFAEKPkgehlkamkvdttilglddqrakEMPFIASMGIYVVSRDVmLDLL-RNQFPGANDFGSEVIpgatSLG 335
Cdd:cd06426 145 -GGRITSIEEKP-----------------------THSFLVNAGIYVLEPEV-LDLIpKNEFFDMPDLIEKLI----KEG 195
|
250 260
....*....|....*....|....*
gi 15238933 336 LRVQAYLYDGYWEDIGTIEAFYNAN 360
Cdd:cd06426 196 KKVGVFPIHEYWLDIGRPEDYEKAN 220
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
101-359 |
1.31e-17 |
|
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: 81.83 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 101 TRLYPLTKKRAKPAVPLgANYRLIDIPVSNCLNSNISKIYVLTqfnsaslnrhlsrayasnmgGYKNEGFVEVLAAQQSP 180
Cdd:cd06915 10 TRLRSVVKDLPKPLAPV-AGRPFLEYLLEYLARQGISRIVLSV--------------------GYLAEQIEEYFGDGYRG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 181 ENPNWFQ------GTADAVRQYLWLFEEHNVLeylILAGDHLYRMDYEKFIQAHRETDADITVAALPMDEqrATAFGLMK 254
Cdd:cd06915 69 GIRIYYViepeplGTGGAIKNALPKLPEDQFL---VLNGDTYFDVDLLALLAALRASGADATMALRRVPD--ASRYGNVT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 255 IDEEGRIIEFAEkpKGEHLKamkvdttilglddqrakeMPFIASmGIYVVSRDVMLDLLRNQFpganDFGSEVIPGATSL 334
Cdd:cd06915 144 VDGDGRVIAFVE--KGPGAA------------------PGLING-GVYLLRKEILAEIPADAF----SLEADVLPALVKR 198
|
250 260
....*....|....*....|....*
gi 15238933 335 GlRVQAYLYDGYWEDIGTIEAFYNA 359
Cdd:cd06915 199 G-RLYGFEVDGYFIDIGIPEDYARA 222
|
|
| LbH_G1P_AT_C_like |
cd03356 |
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
401-486 |
4.47e-17 |
|
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: 75.74 E-value: 4.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 401 VIGEGCVIK-NCKIHHSVVGLRSCISEGAIIEDSLLMGADYyetateksllsakgsvpigIGKNSHIKRAIIDKNARIGD 479
Cdd:cd03356 1 LIGESTVIGeNAIIKNSVIGDNVRIGDGVTITNSILMDNVT-------------------IGANSVIVDSIIGDNAVIGE 61
|
....*..
gi 15238933 480 NVKIINS 486
Cdd:cd03356 62 NVRVVNL 68
|
|
| rmlA_long |
TIGR01208 |
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ... |
101-477 |
1.42e-12 |
|
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: 68.97 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 101 TRLYPLTKKRAKPAVPLgANYRLIDIPVSNCLNSNISKIYVLtqfnsasLNRHLSRAYASNMGGYKNEGFVEVLAAQQSP 180
Cdd:TIGR01208 11 TRLRPLTFTRPKQLIPV-ANKPILQYAIEDLAEAGITDIGIV-------VGPVTGEEIKEIVGEGERFGAKITYIVQGEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 181 enpnwfQGTADAV-RQYLWLFEEHNVLeYLilaGDHLYRMDYEKFIQAHRETDADITVAALPMDEqrATAFGLMKIDEEG 259
Cdd:TIGR01208 83 ------LGLAHAVyTARDFLGDDDFVV-YL---GDNLIQDGISRFVKSFEEKDYDALILLTKVRD--PTAFGVAVLEDGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 260 RIIEFAEKPKgEHLKAMKVdttilglddqrakempfiasMGIYVVsRDVMLDLLRNQFPGANdfG----SEVIPGATSLG 335
Cdd:TIGR01208 151 RILKLVEKPK-EPPSNLAV--------------------VGLYMF-RPLIFEAIKNIKPSWR--GeleiTDAIQWLIEKG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 336 LRVQAYLYDGYWEDIGTIEAFYNANLGITKKPVPDFSFYDRSAPIYTQPRYLPPSKMLDADVTD-SVIGEGCVIKNCKI- 413
Cdd:TIGR01208 207 YKVGGSKVTGWWKDTGKPEDLLDANRLILDEVEREVQGVDDESKIRGRVVVGEGAKIVNSVIRGpAVIGEDCIIENSYIg 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15238933 414 HHSVVGLRSCIsEGAIIEDSLLMgadyyetateksllsaKGSVPIGIGKnsHIKRAIIDKNARI 477
Cdd:TIGR01208 287 PYTSIGEGVVI-RDAEVEHSIVL----------------DESVIEGVQA--RIVDSVIGKKVRI 331
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
101-360 |
1.18e-10 |
|
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: 61.82 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 101 TRLYPLTKKRAKPAVPLgANYRLIDIPVSNCLNSNISKIYVLTQFNSASLNRHLSRAYASNMggykNEGFVEvlaaQQSP 180
Cdd:cd04189 12 TRLRPLTYTRPKQLIPV-AGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFGV----RITYIL----QEEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 181 enpnwfQGTADAV-RQYLWLFEEHNVLeYLilaGDHLYRMDYEKFIQAHRETDADITVAALPMDEQRatAFGLMKIDeEG 259
Cdd:cd04189 83 ------LGLAHAVlAARDFLGDEPFVV-YL---GDNLIQEGISPLVRDFLEEDADASILLAEVEDPR--RFGVAVVD-DG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 260 RIIEFAEKPKgehlkamkvdttilglddqraKEMPFIASMGIYVVSRDVmLDLLRNQFPGANdfGSEVIPGATSL----G 335
Cdd:cd04189 150 RIVRLVEKPK---------------------EPPSNLALVGVYAFTPAI-FDAISRLKPSWR--GELEITDAIQWlidrG 205
|
250 260
....*....|....*....|....*
gi 15238933 336 LRVQAYLYDGYWEDIGTIEAFYNAN 360
Cdd:cd04189 206 RRVGYSIVTGWWKDTGTPEDLLEAN 230
|
|
| LbetaH |
cd00208 |
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ... |
400-485 |
5.34e-09 |
|
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.
Pssm-ID: 100038 [Multi-domain] Cd Length: 78 Bit Score: 53.02 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 400 SVIGEGCVIKnckiHHSVVGLRSCISEGAIIEDSLLMGADYYETateksllsakGSVPIGIGKNSHIK-RAIIDKNARIG 478
Cdd:cd00208 1 VFIGEGVKIH----PKAVIRGPVVIGDNVNIGPGAVIGAATGPN----------EKNPTIIGDNVEIGaNAVIHGGVKIG 66
|
....*..
gi 15238933 479 DNVKIIN 485
Cdd:cd00208 67 DNAVIGA 73
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
101-269 |
1.34e-08 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 56.25 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 101 TRLYPLTKKRAKPAVPLgANYRLIDIPVSNCLNSNISKIYVLTqfnsaslnrhlsrayasnmGGYKNEGFVEVL------ 174
Cdd:COG1209 12 TRLRPLTLTVSKQLLPV-YDKPMIYYPLSTLMLAGIREILIIS-------------------TPEDGPQFERLLgdgsql 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 175 ------AAQQSPEnpnwfqGTADAVrqylWLFEEH----NVLeyLILaGDHLYRMD-YEKFIQAHRETDADITVAALPMD 243
Cdd:COG1209 72 gikisyAVQPEPL------GLAHAF----IIAEDFiggdPVA--LVL-GDNIFYGDgLSELLREAAARESGATIFGYKVE 138
|
170 180
....*....|....*....|....*.
gi 15238933 244 EQRatAFGLMKIDEEGRIIEFAEKPK 269
Cdd:COG1209 139 DPE--RYGVVEFDEDGRVVSLEEKPK 162
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
188-483 |
2.83e-07 |
|
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440820 [Multi-domain] Cd Length: 457 Bit Score: 52.72 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 188 GTADAVRQYLWLFEEHN--VLeylILAGDH-LYRMD-YEKFIQAHRETDADITVAALPMDEqratAFGLMKI--DEEG-- 259
Cdd:COG1207 78 GTGHAVQQALPALPGDDgtVL---VLYGDVpLIRAEtLKALLAAHRAAGAAATVLTAELDD----PTGYGRIvrDEDGrv 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 260 -RIIEfaEKpkgehlkamkvDTTilglDDQRA-KEmpfIASmGIYVVSRDVMLDLLRnQFPGANDFG----SEVIPGATS 333
Cdd:COG1207 151 lRIVE--EK-----------DAT----EEQRAiRE---INT-GIYAFDAAALREALP-KLSNDNAQGeyylTDVIAIARA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 334 LGLRVQAYLYDGYWEDIG--------TIEAFYNANL-------GITkkpvpdfsFYDrsapiytqprylPPSKMLDADVT 398
Cdd:COG1207 209 DGLKVAAVQPEDPWEVLGvndrvqlaEAERILQRRIaerlmraGVT--------IID------------PATTYIDGDVE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 399 ---------------------DSVIGEGCVIKNCKIHHSVVGLRSCIsEGAIIEDsllmGADyyetateksllsakgsvp 457
Cdd:COG1207 269 igrdvvidpnvilegktvigeGVVIGPNCTLKDSTIGDGVVIKYSVI-EDAVVGA----GAT------------------ 325
|
330 340 350
....*....|....*....|....*....|....*.
gi 15238933 458 IG----------IGKNSHIkraiidKNARIGDNVKI 483
Cdd:COG1207 326 VGpfarlrpgtvLGEGVKIgnfvevKNSTIGEGSKV 361
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
99-360 |
6.40e-07 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 50.62 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 99 AGTRLYPLTKKRAKPAVPLGaNYRLIDIPVSNCLNSNISKIYVLTqfnsaslnrhlsrayasnmgGYKNEGFVEVLAAQQ 178
Cdd:COG1213 9 RGSRLGPLTDDIPKCLVEIG-GKTLLERQLEALAAAGIKDIVVVT--------------------GYKAELIEEALARPG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 179 SP----ENPNWFQ-GTAdavrqY-LWLFEEHNVLEYLILAGDHLYRmdyEKFIQAHRETDADITVAA------LPMDEqr 246
Cdd:COG1213 68 PDvtfvYNPDYDEtNNI-----YsLWLAREALDEDFLLLNGDVVFD---PAILKRLLASDGDIVLLVdrkwekPLDEE-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 247 atafglMK--IDEEGRIIEFAEKPKGEhlkamkvdtTILGlddqrakEmpfiaSMGIYVVSRDvMLDLLRNQF------P 318
Cdd:COG1213 138 ------VKvrVDEDGRIVEIGKKLPPE---------EADG-------E-----YIGIFKFSAE-GAAALREALealideG 189
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15238933 319 GANDFGSEVIPGATSLGLRVQAYLYDG-YWEDIGTIEAFYNAN 360
Cdd:COG1213 190 GPNLYYEDALQELIDEGGPVKAVDIGGlPWVEIDTPEDLERAE 232
|
|
| LbH_LpxD |
cd03352 |
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ... |
399-490 |
1.20e-06 |
|
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).
Pssm-ID: 100043 [Multi-domain] Cd Length: 205 Bit Score: 49.33 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 399 DSVIGEGCVIK-NCKIHH-SVVGLRSCISEGAIIedsllmGADYYETATEK-------SLlsakGSVPIG----IGKNSH 465
Cdd:cd03352 37 GVVIGDDCVIHpNVTIYEgCIIGDRVIIHSGAVI------GSDGFGFAPDGggwvkipQL----GGVIIGddveIGANTT 106
|
90 100
....*....|....*....|....*.
gi 15238933 466 IKRAIIDkNARIGDNVKIinsDN-VQ 490
Cdd:cd03352 107 IDRGALG-DTVIGDGTKI---DNlVQ 128
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
101-356 |
1.82e-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: 49.11 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 101 TRLYPLTKKRAKPAVPLgANYRLIDIPVSNCLNSNISKIYVltqfnsaslNRHlsrayasnmggYKNEGFVEVLAAQQ-- 178
Cdd:cd06422 11 TRMRPLTDTRPKPLVPV-AGKPLIDHALDRLAAAGIRRIVV---------NTH-----------HLADQIEAHLGDSRfg 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 179 -----SPENPNwFQGTADAVRQYLWLFEEHNVleyLILAGDHLYRMDYEKFIQAHREtDADITVAALPM----DEQRATA 249
Cdd:cd06422 70 lritiSDEPDE-LLETGGGIKKALPLLGDEPF---LVVNGDILWDGDLAPLLLLHAW-RMDALLLLLPLvrnpGHNGVGD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 250 FGLmkiDEEGRIIEFAEKPKGehlkamkvdttilglddqrakemPFIASmGIYVVSRDVMLDLLRNQFPgANDFGSEVIP 329
Cdd:cd06422 145 FSL---DADGRLRRGGGGAVA-----------------------PFTFT-GIQILSPELFAGIPPGKFS-LNPLWDRAIA 196
|
250 260
....*....|....*....|....*..
gi 15238933 330 GAtslglRVQAYLYDGYWEDIGTIEAF 356
Cdd:cd06422 197 AG-----RLFGLVYDGLWFDVGTPERL 218
|
|
| LpxD |
COG1044 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ... |
399-490 |
1.59e-05 |
|
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis
Pssm-ID: 440666 [Multi-domain] Cd Length: 335 Bit Score: 46.93 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 399 DSVIGEGCVIK-NCKI-HHSVVGLRSCISEGAIIedsllmGAD---YYETATEKSLlsaK----GSVPIG----IGKNSH 465
Cdd:COG1044 144 GVVIGDDCVLHpNVTIyERCVIGDRVIIHSGAVI------GADgfgFAPDEDGGWV---KipqlGRVVIGddveIGANTT 214
|
90 100
....*....|....*....|....*.
gi 15238933 466 IKRAIIDkNARIGDNVKIinsDN-VQ 490
Cdd:COG1044 215 IDRGALG-DTVIGDGTKI---DNlVQ 236
|
|
| LbH_GlmU_C |
cd03353 |
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ... |
387-486 |
3.32e-05 |
|
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.
Pssm-ID: 100044 [Multi-domain] Cd Length: 193 Bit Score: 44.72 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 387 LPPSKMLDADVT---DSVIGEGCVIKNCKIHHSVVGLRSCISEGAIIEDsllmGADyyetateksllsakgsvpigIGKN 463
Cdd:cd03353 24 IDPGVILEGKTVigeDCVIGPNCVIKDSTIGDGVVIKASSVIEGAVIGN----GAT--------------------VGPF 79
|
90 100
....*....|....*....|....
gi 15238933 464 SHIKR-AIIDKNARIGDNVKIINS 486
Cdd:cd03353 80 AHLRPgTVLGEGVHIGNFVEIKKS 103
|
|
| LbH_eIF2B_epsilon |
cd05787 |
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
398-483 |
1.96e-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: 39.87 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 398 TDSVIGEGCVIKNckihhSVVGLRSCISEGAIIEDSLLmgadyYETATeksllsakgsvpigIGKNSHIKRAIIDKNARI 477
Cdd:cd05787 4 RGTSIGEGTTIKN-----SVIGRNCKIGKNVVIDNSYI-----WDDVT--------------IEDGCTIHHSIVADGAVI 59
|
....*.
gi 15238933 478 GDNVKI 483
Cdd:cd05787 60 GKGCTI 65
|
|
| lpxD |
PRK00892 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional |
358-490 |
2.91e-04 |
|
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
Pssm-ID: 234858 [Multi-domain] Cd Length: 343 Bit Score: 43.20 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 358 NANLGITKKPVPDFS-----FYDRSAPIYTQ----PRYLPPSKMLDADVT---------DSVIGEGCVI-------KNCK 412
Cdd:PRK00892 71 GNALLVVKNPYLAFArlaqlFDPPATPSPAAgihpSAVIDPSAKIGEGVSigpnavigaGVVIGDGVVIgagavigDGVK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 413 I-------------HHSVVGLRSCISEGAIIedsllmGADYYETATEKSL---LSAKGSVPIG----IGKNSHIKRAIID 472
Cdd:PRK00892 151 IgadcrlhanvtiyHAVRIGNRVIIHSGAVI------GSDGFGFANDRGGwvkIPQLGRVIIGddveIGANTTIDRGALD 224
|
170
....*....|....*....
gi 15238933 473 kNARIGDNVKIinsDN-VQ 490
Cdd:PRK00892 225 -DTVIGEGVKI---DNlVQ 239
|
|
| LbH_eIF2B_epsilon |
cd05787 |
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
397-479 |
2.95e-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: 39.48 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 397 VTDSVIGEGCVI-KNCKIHHSVVGLRSCISEGAIIEDSLLmgadyyetateksllsAKGSVpigIGKNSHIK-RAIIDKN 474
Cdd:cd05787 14 IKNSVIGRNCKIgKNVVIDNSYIWDDVTIEDGCTIHHSIV----------------ADGAV---IGKGCTIPpGSLISFG 74
|
....*
gi 15238933 475 ARIGD 479
Cdd:cd05787 75 VVIGD 79
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
188-351 |
3.51e-04 |
|
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: 42.12 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 188 GTADAVRQYLWLFEEHN--VleyLILAGDH-LYRMD-YEKFIQAHRETDADITVAALPMDeqRATAFGLMKIDEEG---R 260
Cdd:cd02540 74 GTGHAVKQALPALKDFEgdV---LVLYGDVpLITPEtLQRLLEAHREAGADVTVLTAELE--DPTGYGRIIRDGNGkvlR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 261 IIEfaEKpkgehlkamkvDTTilglDDQRA-KEmpfiASMGIYVVSRDVM---LDLLRNQfpgaNDFG----SEVIPGAT 332
Cdd:cd02540 149 IVE--EK-----------DAT----EEEKAiRE----VNAGIYAFDAEFLfeaLPKLTNN----NAQGeyylTDIIALAV 203
|
170
....*....|....*....
gi 15238933 333 SLGLRVQAYLYDGYWEDIG 351
Cdd:cd02540 204 ADGLKVAAVLADDEEEVLG 222
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
101-237 |
4.59e-04 |
|
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: 41.49 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 101 TRLYPLTKKRAKPAVPLGaNYRLIDIPVSNCLNSNISKIYVLTQFNSASLNRHLSRAYASNmggYKNEGFVEVLAAQQSp 180
Cdd:cd04198 12 SRLYPLTDNIPKALLPVA-NKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFPLN---LKQKLDEVTIVLDED- 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15238933 181 enpnwfQGTADAVRQYLWLFEEhnvlEYLILAGDHLYRMDYEKFIQAHRETDADITV 237
Cdd:cd04198 87 ------MGTADSLRHIRKKIKK----DFLVLSCDLITDLPLIELVDLHRSHDASLTV 133
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
101-269 |
6.26e-04 |
|
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: 41.41 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 101 TRLYPLTKKRAKPAVPLGaNYRLIDIPVSNCLNSNISKIYVLTQfnsaslNRHLSRayasnmggyknegFVEVL------ 174
Cdd:cd02538 12 TRLYPLTKVVSKQLLPVY-DKPMIYYPLSTLMLAGIREILIIST------PEDLPL-------------FKELLgdgsdl 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 175 ------AAQQSPEnpnwfqGTADAvrqyLWLFEE----HNVLeyLILaGDHLYR-MDYEKFIQAHRETDADITVAALPM- 242
Cdd:cd02538 72 girityAVQPKPG------GLAQA----FIIGEEfigdDPVC--LIL-GDNIFYgQGLSPILQRAAAQKEGATVFGYEVn 138
|
170 180
....*....|....*....|....*..
gi 15238933 243 DEQRataFGLMKIDEEGRIIEFAEKPK 269
Cdd:cd02538 139 DPER---YGVVEFDENGRVLSIEEKPK 162
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
101-237 |
2.05e-03 |
|
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: 39.54 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 101 TRLYPLTKKRAKPAVPLgANYRLIDIPVSNCLNSNISKIYVLTQFNSASLNRHLSRAYASNmGGYKNEGFVEVLAAQQSp 180
Cdd:cd02507 12 SRFLPLTSDIPKALLPV-ANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKWSS-LSSKMIVDVITSDLCES- 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15238933 181 enpnwfQGTADAVRQYLWLFEEHnvleYLILAGDHLYRMDY----EKFIQAHRETDADITV 237
Cdd:cd02507 89 ------AGDALRLRDIRGLIRSD----FLLLSCDLVSNIPLsellEERRKKDKNAIATLTV 139
|
|
| LbH_eIF2B_epsilon |
cd05787 |
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
460-520 |
2.25e-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: 37.17 E-value: 2.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15238933 460 IGKNSHIKRAIIDKNARIGDNVKIINS---DNVQ-EAARETDGYFIKSGiVTVIKDALIPTGTVI 520
Cdd:cd05787 8 IGEGTTIKNSVIGRNCKIGKNVVIDNSyiwDDVTiEDGCTIHHSIVADG-AVIGKGCTIPPGSLI 71
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
188-520 |
3.09e-03 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 40.13 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 188 GTADAVRQYLWLFEEHNVLeyLILAGD--HLYRMDYEKFIQAHRETDADITVAALPMDEqrATAFGLMkIDEEG--RIIE 263
Cdd:PRK14357 74 GTAHAVMCARDFIEPGDDL--LILYGDvpLISENTLKRLIEEHNRKGADVTILVADLED--PTGYGRI-IRDGGkyRIVE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 264 faEKPKGEHLKAMKVDTTilglddqrakempfiasmGIYVVSRDVMLdllrnqfpgandfgsEVIPGATSLGLRVQAYLY 343
Cdd:PRK14357 149 --DKDAPEEEKKIKEINT------------------GIYVFSGDFLL---------------EVLPKIKNENAKGEYYLT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 344 D--GYWEDIGTIeafynanlgITKKPVPDFSFYDRS--APIYTQPRYL--------------PPSKMLDADVT---DSVI 402
Cdd:PRK14357 194 DavNFAEKVRVV---------KTEDLLEITGVNTRIqlAWLEKQLRMRileelmengvtildPNTTYIHYDVEigmDTII 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 403 ------------GEGCV------IKNCKIHHSVVGLRSCIsEGAIIEDSLLMGAdyYETATEKSLLsaKGSVPIG----- 459
Cdd:PRK14357 265 ypmtfiegktriGEDCEigpmtrIVDCEIGNNVKIIRSEC-EKSVIEDDVSVGP--FSRLREGTVL--KKSVKIGnfvei 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15238933 460 ----IGKNS------HIKRAIIDKNARIGDNVKIINSDNVQEaaRET---DGYFIKSGI-----VTVIKDALIPTGTVI 520
Cdd:PRK14357 340 kkstIGENTkaqhltYLGDATVGKNVNIGAGTITCNYDGKKK--NPTfieDGAFIGSNSslvapVRIGKGALIGAGSVI 416
|
|
| LbH_G1P_AT_C_like |
cd03356 |
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
397-439 |
4.28e-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: 4.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 15238933 397 VTDSVIGEGCVI-KNCKIHHSVVGLRSCISEGAIIEDSLLMGAD 439
Cdd:cd03356 31 ITNSILMDNVTIgANSVIVDSIIGDNAVIGENVRVVNLCIIGDD 74
|
|
| LbH_eIF2B_gamma_C |
cd04652 |
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
460-489 |
9.48e-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: 35.25 E-value: 9.48e-03
10 20 30
....*....|....*....|....*....|...
gi 15238933 460 IGKNSHIKRAIIDKNARIGDNVKIINS---DNV 489
Cdd:cd04652 8 VGEKTSIKRSVIGANCKIGKRVKITNCvimDNV 40
|
|
| LbH_eIF2B_gamma_C |
cd04652 |
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
401-485 |
9.96e-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: 35.25 E-value: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238933 401 VIGEGCVIKN-CKIHHSVVGlRSC-ISEGAIIEDSLLMgadyyETATeksllsakgsvpigIGKNSHIKRAIIDKNARIG 478
Cdd:cd04652 1 LVGENTQVGEkTSIKRSVIG-ANCkIGKRVKITNCVIM-----DNVT--------------IEDGCTLENCIIGNGAVIG 60
|
....*..
gi 15238933 479 DNVKIIN 485
Cdd:cd04652 61 EKCKLKD 67
|
|
| |
