|
Name |
Accession |
Description |
Interval |
E-value |
| glgC |
PRK00844 |
glucose-1-phosphate adenylyltransferase; Provisional |
2-406 |
0e+00 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 742.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 2 IRQPNVLAIVLAGGEGKRLFPLTLDRAKPAVPFGGNYRLIDFVLSNLVNAGYNRIAVLTQYKSHSLDRHVATAWNFSGPT 81
Cdd:PRK00844 1 RAMPKVLAIVLAGGEGKRLMPLTADRAKPAVPFGGSYRLIDFVLSNLVNSGYLRIYVLTQYKSHSLDRHISQTWRLSGLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 82 HQYIASVPAQQRLGKRWYQGSADALLQSLNLIFDESPDYVLVFGADHVYRMDPSQMVENHIASGKACTVAGIRVPRSEAS 161
Cdd:PRK00844 81 GNYITPVPAQQRLGKRWYLGSADAIYQSLNLIEDEDPDYVVVFGADHVYRMDPRQMVDFHIESGAGVTVAAIRVPREEAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 162 QFGCIQSDENGAITEFLEKPADPPGTPDDPDTTFASMGNYCFSTEALIQALRDDTENDDSDHDMGGDIIPYFVERGEANV 241
Cdd:PRK00844 161 AFGVIEVDPDGRIRGFLEKPADPPGLPDDPDEALASMGNYVFTTDALVDALRRDAADEDSSHDMGGDIIPRLVERGRAYV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 242 YDFSSNEVPGATERDKAYWRDVGTIDSFYEAHMDLISIHPVFNLYNKAWPIHsTEDENLPPAKFVSG----GLAQESIIA 317
Cdd:PRK00844 241 YDFSTNEVPGATERDRGYWRDVGTIDAYYDAHMDLLSVHPVFNLYNREWPIY-TSSPNLPPAKFVDGggrvGSAQDSLVS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 318 PGSIISGSTVRNSVLSTDVYVEDGAVVESSVLMPGVRVGKGAIVRHAILDKNVYVSDGAAVGTHRADDeRRGFTISAEGV 397
Cdd:PRK00844 320 AGSIISGATVRNSVLSPNVVVESGAEVEDSVLMDGVRIGRGAVVRRAILDKNVVVPPGATIGVDLEED-RRRFTVSEGGI 398
|
....*....
gi 736655208 398 VVVGKGEFV 406
Cdd:PRK00844 399 VVVPKGQRV 407
|
|
| GlgC |
COG0448 |
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
6-404 |
0e+00 |
|
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];
Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 565.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 6 NVLAIVLAGGEGKRLFPLTLDRAKPAVPFGGNYRLIDFVLSNLVNAGYNRIAVLTQYKSHSLDRHVAT--AWNFSGpTHQ 83
Cdd:COG0448 1 KVLAIILAGGRGSRLGPLTKDRAKPAVPFGGKYRIIDFPLSNCVNSGIRRVGVLTQYKSHSLNDHIGSgkPWDLDR-KRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 84 YIASVPA-QQRLGKRWYQGSADALLQSLNLIFDESPDYVLVFGADHVYRMDPSQMVENHIASGKACTVAGIRVPRSEASQ 162
Cdd:COG0448 80 GVFILPPyQQREGEDWYQGTADAVYQNLDFIERSDPDYVLILSGDHIYKMDYRQMLDFHIESGADITVACIEVPREEASR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 163 FGCIQSDENGAITEFLEKPAdppgtpdDPDTTFASMGNYCFSTEALIQALRDDTENddSDHDMGGDIIPYFVERGEANVY 242
Cdd:COG0448 160 FGVMEVDEDGRITEFEEKPK-------DPKSALASMGIYVFNKDVLIELLEEDAPN--SSHDFGKDIIPRLLDRGKVYAY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 243 DFssnevpgaterdKAYWRDVGTIDSFYEAHMDLISIHPVFNLYNKAWPIHsTEDENLPPAKFVSGGLAQESIIAPGSII 322
Cdd:COG0448 231 EF------------DGYWRDVGTIDSYYEANMDLLDPEPEFNLYDPEWPIY-TKQKDLPPAKFVRGGKVKNSLVSNGCII 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 323 SGsTVRNSVLSTDVYVEDGAVVESSVLMPGVRVGKGAIVRHAILDKNVYVSDGAAVGTHRADDERRgFTISaEGVVVVGK 402
Cdd:COG0448 298 SG-TVENSVLFRGVRVESGAVVENSVIMPGVVIGEGAVIENAIIDKNVVIPPGVVIGEDPEEDRKR-FTVS-SGIVVVGK 374
|
..
gi 736655208 403 GE 404
Cdd:COG0448 375 GA 376
|
|
| glgC |
PRK00725 |
glucose-1-phosphate adenylyltransferase; Provisional |
6-400 |
0e+00 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234824 [Multi-domain] Cd Length: 425 Bit Score: 509.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 6 NVLAIVLAGGEGKRLFPLTLDRAKPAVPFGGNYRLIDFVLSNLVNAGYNRIAVLTQYKSHSLDRHVATAWNF-SGPTHQY 84
Cdd:PRK00725 15 DTLALILAGGRGSRLKELTDKRAKPAVYFGGKFRIIDFALSNCINSGIRRIGVLTQYKAHSLIRHIQRGWSFfREELGEF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 85 IASVPAQQRL-GKRWYQGSADALLQSLNLIFDESPDYVLVFGADHVYRMDPSQMVENHIASGKACTVAGIRVPRSEASQF 163
Cdd:PRK00725 95 VDLLPAQQRVdEENWYRGTADAVYQNLDIIRRYDPKYVVILAGDHIYKMDYSRMLADHVESGADCTVACLEVPREEASAF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 164 GCIQSDENGAITEFLEKPADPPGTPDDPDTTFASMGNYCFSTEALIQALRDDTENDDSDHDMGGDIIPYFVERGEANVYD 243
Cdd:PRK00725 175 GVMAVDENDRITAFVEKPANPPAMPGDPDKSLASMGIYVFNADYLYELLEEDAEDPNSSHDFGKDIIPKIVEEGKVYAHP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 244 FSSNEVPGATERDkAYWRDVGTIDSFYEAHMDLISIHPVFNLYNKAWPIHsTEDENLPPAKFVSG-----GLAQESIIAP 318
Cdd:PRK00725 255 FSDSCVRSDPEEE-PYWRDVGTLDAYWQANLDLASVTPELDLYDRNWPIW-TYQEQLPPAKFVFDrsgrrGMAINSLVSG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 319 GSIISGSTVRNSVLSTDVYVEDGAVVESSVLMPGVRVGKGAIVRHAILDKNVYVSDGAAVGTHRADDERRgFTISAEGVV 398
Cdd:PRK00725 333 GCIISGAVVRRSVLFSRVRVNSFSNVEDSVLLPDVNVGRSCRLRRCVIDRGCVIPEGMVIGEDPEEDAKR-FRRSEEGIV 411
|
..
gi 736655208 399 VV 400
Cdd:PRK00725 412 LV 413
|
|
| glgC |
TIGR02091 |
glucose-1-phosphate adenylyltransferase; This enzyme, glucose-1-phosphate adenylyltransferase, ... |
9-379 |
4.41e-179 |
|
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: 502.95 E-value: 4.41e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 9 AIVLAGGEGKRLFPLTLDRAKPAVPFGGNYRLIDFVLSNLVNAGYNRIAVLTQYKSHSLDRHVATAWNFSGPTHQYIASV 88
Cdd:TIGR02091 1 AMVLAGGRGSRLSPLTKRRAKPAVPFGGKYRIIDFPLSNCINSGIRRIGVLTQYKSHSLNRHIQRGWDFDGFIDGFVTLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 89 PAQQR-LGKRWYQGSADALLQSLNLIFDESPDYVLVFGADHVYRMDPSQMVENHIASGKACTVAGIRVPRSEASQFGCIQ 167
Cdd:TIGR02091 81 PAQQReSGTDWYQGTADAVYQNLDLIEDYDPEYVLILSGDHIYKMDYEKMLDYHIESGADVTIACIPVPRKEASRFGVMQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 168 SDENGAITEFLEKPADPPGTPDDPDTTFASMGNYCFSTEALIQALRDDTENDDSDHDMGGDIIPYFVERGEANVYDFSsn 247
Cdd:TIGR02091 161 VDEDGRIVDFEEKPANPPSIPGMPDFALASMGIYIFDKDVLKELLEEDADDPESSHDFGKDIIPRALEEGSVQAYLFS-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 248 evpgaterdkAYWRDVGTIDSFYEAHMDLISIHPVFNLYNKAWPIHsTEDENLPPAKFV-SGGLAQESIIAPGSIISGST 326
Cdd:TIGR02091 239 ----------GYWRDVGTIDSFWEANMDLVSVVPPFDLYDRKWPIY-TYNEFLPPAKFVdSDAQVVDSLVSEGCIISGAT 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 736655208 327 VRNSVLSTDVYVEDGAVVESSVLMPGVRVGKGAIVRHAILDKNVYVSDGAAVG 379
Cdd:TIGR02091 308 VSHSVLGIRVRIGSGSTVEDSVIMGDVGIGRGAVIRNAIIDKNVRIGEGVVIG 360
|
|
| glgC |
PRK05293 |
glucose-1-phosphate adenylyltransferase; Provisional |
6-407 |
3.16e-124 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 364.19 E-value: 3.16e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 6 NVLAIVLAGGEGKRLFPLTLDRAKPAVPFGGNYRLIDFVLSNLVNAGYNRIAVLTQYKSHSLDRHV--ATAWNF----SG 79
Cdd:PRK05293 3 EMLAMILAGGQGTRLGKLTKNIAKPAVPFGGKYRIIDFTLSNCANSGIDTVGVLTQYQPLELNNHIgiGSPWDLdrinGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 80 PThqyIASvPAQQRLGKRWYQGSADALLQSLNLIFDESPDYVLVFGADHVYRMDPSQMVENHIASGKACTVAGIRVPRSE 159
Cdd:PRK05293 83 VT---ILP-PYSESEGGKWYKGTAHAIYQNIDYIDQYDPEYVLILSGDHIYKMDYDKMLDYHKEKEADVTIAVIEVPWEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 160 ASQFGCIQSDENGAITEFLEKPAdppgtpdDPDTTFASMGNYCFSTEALIQALRDDTENDDSDHDMGGDIIPYFVERGEa 239
Cdd:PRK05293 159 ASRFGIMNTDENMRIVEFEEKPK-------NPKSNLASMGIYIFNWKRLKEYLIEDEKNPNSSHDFGKNVIPLYLEEGE- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 240 NVYDFssnevpgateRDKAYWRDVGTIDSFYEAHMDLISIHPVFNLYNKAWPIHSTeDENLPPAKFVSGGLAQESIIAPG 319
Cdd:PRK05293 231 KLYAY----------PFKGYWKDVGTIESLWEANMELLRPENPLNLFDRNWRIYSV-NPNLPPQYIAENAKVKNSLVVEG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 320 SIISGsTVRNSVLSTDVYVEDGAVVESSVLMPGVRVGKGAIVRHAILDKNVYVSDGAAVGThradderrgftiSAEGVVV 399
Cdd:PRK05293 300 CVVYG-TVEHSVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVIIGG------------GKEVITV 366
|
....*...
gi 736655208 400 VGKGEFVE 407
Cdd:PRK05293 367 IGENEVIG 374
|
|
| glgC |
PRK02862 |
glucose-1-phosphate adenylyltransferase; Provisional |
6-403 |
1.16e-112 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179486 [Multi-domain] Cd Length: 429 Bit Score: 336.47 E-value: 1.16e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 6 NVLAIVLAGGEGKRLFPLTLDRAKPAVPFGGNYRLIDFVLSNLVNAGYNRIAVLTQYKSHSLDRHVATAWNFSGPTHQYI 85
Cdd:PRK02862 3 RVLAIILGGGAGTRLYPLTKLRAKPAVPLAGKYRLIDIPISNCINSGINKIYVLTQFNSASLNRHISQTYNFDGFSGGFV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 86 ASVPAQQRL-GKRWYQGSADALLQSLNLIFDESPDYVLVFGADHVYRMDPSQMVENHIASGKACTVAGIRVPRSEASQFG 164
Cdd:PRK02862 83 EVLAAQQTPeNPSWFQGTADAVRKYLWHFQEWDVDEYLILSGDQLYRMDYRLFVQHHRETGADITLAVLPVDEKDASGFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 165 CIQSDENGAITEFLEKPA--------------DPPGTPDDPDTTFASMGNYCFSTEALIQALrddtENDDSDHDMGGDII 230
Cdd:PRK02862 163 LMKTDDDGRITEFSEKPKgdelkamavdtsrlGLSPEEAKGKPYLASMGIYVFSRDVLFDLL----NKNPEYTDFGKEII 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 231 PYFVERGEANVYDFssnevpgaterdKAYWRDVGTIDSFYEAHMDL-ISIHPVFNLYNKAWPIHsTEDENLPPAKFVSGG 309
Cdd:PRK02862 239 PEAIRDYKVQSYLF------------DGYWEDIGTIEAFYEANLALtQQPNPPFSFYDEKAPIY-TRARYLPPSKLLDAT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 310 LaQESIIAPGSIISGSTVRNSVLSTDVYVEDGAVVESSVLM-------------------PGVRVGKGAIVRHAILDKNV 370
Cdd:PRK02862 306 I-TESIIAEGCIIKNCSIHHSVLGIRSRIESGCTIEDTLVMgadfyesseereelrkegkPPLGIGEGTTIKRAIIDKNA 384
|
410 420 430
....*....|....*....|....*....|....*..
gi 736655208 371 YVSDGAAVGT----HRADDERRGFTISaEGVVVVGKG 403
Cdd:PRK02862 385 RIGNNVRIVNkdnvEEADREDQGFYIR-DGIVVVVKN 420
|
|
| PLN02241 |
PLN02241 |
glucose-1-phosphate adenylyltransferase |
6-403 |
1.12e-104 |
|
glucose-1-phosphate adenylyltransferase
Pssm-ID: 215133 [Multi-domain] Cd Length: 436 Bit Score: 316.41 E-value: 1.12e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 6 NVLAIVLAGGEGKRLFPLTLDRAKPAVPFGGNYRLIDFVLSNLVNAGYNRIAVLTQYKSHSLDRHVATAWNFS--GPTHQ 83
Cdd:PLN02241 3 SVAAIILGGGAGTRLFPLTKRRAKPAVPIGGNYRLIDIPMSNCINSGINKIYVLTQFNSASLNRHLSRAYNFGngGNFGD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 84 -YIASVPAQQRLG-KRWYQGSADALLQSLNLiFDESP----DYVLVFGADHVYRMDPSQMVENHIASGKACTVAGIRVPR 157
Cdd:PLN02241 83 gFVEVLAATQTPGeKGWFQGTADAVRQFLWL-FEDAKnknvEEVLILSGDHLYRMDYMDFVQKHRESGADITIACLPVDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 158 SEASQFGCIQSDENGAITEFLEKPADPPGTPDDPDTTF--------------ASMGNYCFSTEALIQALRDDTEnddSDH 223
Cdd:PLN02241 162 SRASDFGLMKIDDTGRIIEFSEKPKGDELKAMQVDTTVlglspeeakekpyiASMGIYVFKKDVLLKLLRWRFP---TAN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 224 DMGGDIIPYFVERGeANV--YDFssnevpgaterdKAYWRDVGTIDSFYEAHMDLISIHPVFNLYNKAWPIHsTEDENLP 301
Cdd:PLN02241 239 DFGSEIIPGAIKEG-YNVqaYLF------------DGYWEDIGTIKSFYEANLALTKQPPKFSFYDPDAPIY-TSPRFLP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 302 PAKFVSGGLAqESIIAPGSIISGSTVRNSVLSTDVYVEDGAVVESSVLM-----------------PGVR--VGKGAIVR 362
Cdd:PLN02241 305 PSKIEDCRIT-DSIISHGCFLRECKIEHSVVGLRSRIGEGVEIEDTVMMgadyyeteeeiasllaeGKVPigIGENTKIR 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 736655208 363 HAILDKNVYVsdGAAV------GTHRADDERRGFTISaEGVVVVGKG 403
Cdd:PLN02241 384 NAIIDKNARI--GKNVviinkdGVQEADREEEGYYIR-SGIVVILKN 427
|
|
| ADP_Glucose_PP |
cd02508 |
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ... |
9-263 |
4.14e-85 |
|
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: 257.86 E-value: 4.14e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 9 AIVLAGGEGKRLFPLTLDRAKPAVPFGGNYRLIDFVLSNLVNAGYNRIAVLTQYKSHSLDRHVATAWNFSGP-THQYIAS 87
Cdd:cd02508 1 AIILAGGEGTRLSPLTKKRAKPAVPFGGRYRLIDFPLSNMVNSGIRNVGVLTQYKSRSLNDHLGSGKEWDLDrKNGGLFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 88 VPAQQRLGKRWYQGSADALLQSLNLIFDESPDYVLVFGADHVYRMDPSQMVENHIASGKACTVAGIrvprseasqfgciq 167
Cdd:cd02508 81 LPPQQRKGGDWYRGTADAIYQNLDYIERSDPEYVLILSGDHIYNMDYREMLDFHIESGADITVVYK-------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 168 sdengaiteflekpadppgtpddpdttfASMGNYCFSTEALIQALRDDteNDDSDHDMGGDIIPYFVERGEANVYDFssn 247
Cdd:cd02508 147 ----------------------------ASMGIYIFSKDLLIELLEED--AADGSHDFGKDIIPAMLKKLKIYAYEF--- 193
|
250
....*....|....*.
gi 736655208 248 evpgaterdKAYWRDV 263
Cdd:cd02508 194 ---------NGYWADI 200
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
8-276 |
1.15e-79 |
|
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: 245.63 E-value: 1.15e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 8 LAIVLAGGEGKRLFPLTLDRAKPAVPFGGNYRLIDFVLSNLVNAGYNRIA-VLTQYKSHSLDRHVATAWNFSgpthqyIA 86
Cdd:pfam00483 1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKYPLIDYPLSRLANAGIREIIvILTQEHRFMLNELLGDGSKFG------VQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 87 SVPAQQRLGKrwyqGSADALLQSLNLIFDESPDyVLVFGADHVYRMDPSQMVENHIASGKACTVAGIRVPRSEASQFGCI 166
Cdd:pfam00483 75 ITYALQPEGK----GTAPAVALAADFLGDEKSD-VLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGIVPVEPPTGYGVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 167 QSDENGAITEFLEKPAdppgtpDDPDTTFASMGNYCFSTEALIQALRDDtENDDSDHDMGGDIIPYFVERGEaNVYDFss 246
Cdd:pfam00483 150 EFDDNGRVIRFVEKPK------LPKASNYASMGIYIFNSGVLDFLAKYL-EELKRGEDEITDILPKALEDGK-LAYAF-- 219
|
250 260 270
....*....|....*....|....*....|
gi 736655208 247 nevpgatERDKAYWRDVGTIDSFYEAHMDL 276
Cdd:pfam00483 220 -------IFKGYAWLDVGTWDSLWEANLFL 242
|
|
| glgD |
TIGR02092 |
glucose-1-phosphate adenylyltransferase, GlgD subunit; This family is GlgD, an apparent ... |
6-375 |
9.24e-49 |
|
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: 169.48 E-value: 9.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 6 NVLAIVLAGGEGKRLFPLTLDRAKPAVPFGGNYRLIDFVLSNLVNAGYNRIAVLTQYKS-HSLDRHVATA--WNFSGPTH 82
Cdd:TIGR02092 2 KMSAIINLTESSKNLSPLTKVRPLASLPFGGRYRLIDFPLSNMVNAGIRNVFIFFKNKErQSLFDHLGSGreWDLHRKRD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 83 QYIASvPAQQRlgKRWYQGSADALLQSLNLIFDESPDYVLVFGADHVYRMDPSQMVENHIASGKACTVAGIRVPRSEASQ 162
Cdd:TIGR02092 82 GLFVF-PYNDR--DDLSEGGKRYFSQNLEFLKRSTSEYTVVLNSHMVCNIDLKAVLKYHEETGKDITVVYKKVKPADASE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 163 FGCI-QSDENGAITeflekpaDPPGTPDDPDTTFASMGNYCFSTEALIQALRDdtENDDSDHDMGGDIIPYFVERGEANV 241
Cdd:TIGR02092 159 YDTIlRFDESGKVK-------SIGQNLNPEEEENISLDIYIVSTDLLIELLYE--CIQRGKLTSLEELIRENLKELNINA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 242 YDFssnevpgaterdKAYWRDVGTIDSFYEAHMDLIS---IHPVFnlYNKAWPIHsTEDENLPPAKFVSGGLAQESIIAP 318
Cdd:TIGR02092 230 YEY------------TGYLANINSVKSYYKANMDLLDpqnFQSLF--YSSQGPIY-TKVKDEPPTYYAENSKVENSLVAN 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 736655208 319 GSIISGsTVRNSVLSTDVYVEDGAVVESSVLMPGVRVGKGAIVRHAILDKNVYVSDG 375
Cdd:TIGR02092 295 GCIIEG-KVENSILSRGVHVGKDALIKNCIIMQRTVIGEGAHLENVIIDKDVVIEPN 350
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
9-264 |
3.59e-38 |
|
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: 136.94 E-value: 3.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 9 AIVLAGGEGKRLFPLTLDRAKPAVPFGGnYRLIDFVLSNLVNAGYNRIAVLTQYKSHSLDRHVATAWNFsGPTHQYIasv 88
Cdd:cd04181 1 AVILAAGKGTRLRPLTDTRPKPLLPIAG-KPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKF-GVNIEYV--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 89 paqqrlgkrwYQ----GSADALLQSLNLIFDespDYVLVFGADHVYRMDPSQMVENHIASGKACTVAGIRVPRseASQFG 164
Cdd:cd04181 76 ----------VQeeplGTAGAVRNAEDFLGD---DDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVED--PSRYG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 165 CIQSDENGAITEFLEKPAdppgtpdDPDTTFASMGNYCFSTEALiQALRddtENDDSDHDMGGDIIPYFVERGEANVYDF 244
Cdd:cd04181 141 VVELDDDGRVTRFVEKPT-------LPESNLANAGIYIFEPEIL-DYIP---EILPRGEDELTDAIPLLIEEGKVYGYPV 209
|
250 260
....*....|....*....|
gi 736655208 245 ssnevpgaterdKAYWRDVG 264
Cdd:cd04181 210 ------------DGYWLDIG 217
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
9-282 |
3.33e-37 |
|
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: 3.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 9 AIVLAGGEGKRLFPLTLDRAKPAVPFGGnyR-LIDFVLSNLVNAGYNRIAVLTQYKSHSLDRHVATAWNFsGPTHQYias 87
Cdd:COG1208 2 AVILAGGLGTRLRPLTDTRPKPLLPVGG--KpLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRF-GVRITY--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 88 VPAQQRLgkrwyqGSADALLQSLNLIFDEspdYVLVFGADHVYRMDPSQMVENHIASGKACTVAGIRVPRseASQFGCIQ 167
Cdd:COG1208 76 VDEGEPL------GTGGALKRALPLLGDE---PFLVLNGDILTDLDLAALLAFHREKGADATLALVPVPD--PSRYGVVE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 168 SDENGAITEFLEKPAdppgtpdDPDTTFASMGNYCFSTEALiqalrdDTENDDSDHDMgGDIIPYFVERGEANVYDFSsn 247
Cdd:COG1208 145 LDGDGRVTRFVEKPE-------EPPSNLINAGIYVLEPEIF------DYIPEGEPFDL-EDLLPRLIAEGRVYGYVHD-- 208
|
250 260 270
....*....|....*....|....*....|....*.
gi 736655208 248 evpgaterdkAYWRDVGTIDSFYEAHMDLIS-IHPV 282
Cdd:COG1208 209 ----------GYWLDIGTPEDLLEANALLLSgKAPV 234
|
|
| LbH_G1P_AT_C |
cd04651 |
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ... |
302-404 |
2.29e-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: 122.96 E-value: 2.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 302 PAKFVSGGLAQESIIAPGSIISGSTVRNSVLSTDVYVEDGAVVESSVLMPGVRVGKGAIVRHAILDKNVYVSDGAAVGtH 381
Cdd:cd04651 1 PPYIGRRGEVKNSLVSEGCIISGGTVENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIPDGVVIG-G 79
|
90 100
....*....|....*....|...
gi 736655208 382 RADDERRGFTISAEGVVVVGKGE 404
Cdd:cd04651 80 DPEEDRARFYVTEDGIVVVGKGM 102
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
9-180 |
3.73e-15 |
|
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: 74.13 E-value: 3.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 9 AIVLAGGEGKRLFPLTLDRAKPAVPFGGnYRLIDFVLSNLVNAGYNRIAVLTQYKSHSLDRHVATAWNFsGPTHQY-IAS 87
Cdd:cd06915 1 AVILAGGLGTRLRSVVKDLPKPLAPVAG-RPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRG-GIRIYYvIEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 88 VPAqqrlgkrwyqGSADALLQSLNLIFDespDYVLVFGADHVYRMDPSQMVENHIASGKACTVAGIRVPrsEASQFGCIQ 167
Cdd:cd06915 79 EPL----------GTGGAIKNALPKLPE---DQFLVLNGDTYFDVDLLALLAALRASGADATMALRRVP--DASRYGNVT 143
|
170
....*....|...
gi 736655208 168 SDENGAITEFLEK 180
Cdd:cd06915 144 VDGDGRVIAFVEK 156
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
7-272 |
3.78e-15 |
|
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.
Pssm-ID: 133032 [Multi-domain] Cd Length: 236 Bit Score: 74.14 E-value: 3.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 7 VLAIVLAGGEGKRLFPLTLDRAKPAVPFGGNyRLIDFVLSNLVNAGYNRIAVLTQYKSHSLDRHVATAWNFSGPthqyIA 86
Cdd:cd04189 1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGK-PIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFGVR----IT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 87 SVPAQQRLgkrwyqGSADALLQSLNLIFDEspDYVLVFGaDHVYRMDPSQMVENHIASGKACTVAGIRVPrsEASQFGCI 166
Cdd:cd04189 76 YILQEEPL------GLAHAVLAARDFLGDE--PFVVYLG-DNLIQEGISPLVRDFLEEDADASILLAEVE--DPRRFGVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 167 QSDeNGAITEFLEKPAdppgtpdDPDTTFASMGNYCFSTEAL--IQAL----RDDTENDDSdhdmggdiIPYFVERGean 240
Cdd:cd04189 145 VVD-DGRIVRLVEKPK-------EPPSNLALVGVYAFTPAIFdaISRLkpswRGELEITDA--------IQWLIDRG--- 205
|
250 260 270
....*....|....*....|....*....|..
gi 736655208 241 vYDFSSNEVPGaterdkaYWRDVGTIDSFYEA 272
Cdd:cd04189 206 -RRVGYSIVTG-------WWKDTGTPEDLLEA 229
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
9-272 |
5.46e-13 |
|
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: 67.60 E-value: 5.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 9 AIVLAGGEGKRLFPLTLDRAKPAVPFGGNyRLIDFVLSNLVNAGYNRIAVLTQYKSHSLDRHVATAWnfSGPTHQYIASV 88
Cdd:cd06422 2 AMILAAGLGTRMRPLTDTRPKPLVPVAGK-PLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDSR--FGLRITISDEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 89 PaqQRLgkrwyqGSADALLQSLNLiFDESPdyVLVFGADHVYRMDPSQMVENHIASGKACTVAGIRVPRSEASQFGCIQS 168
Cdd:cd06422 79 D--ELL------ETGGGIKKALPL-LGDEP--FLVVNGDILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFSL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 169 DENGAITEFLEKpadppgtpddPDTTFASMGNYCFSTEaLIQALRDDTENddsdhdmggdIIPYF---VERGE--ANVYD 243
Cdd:cd06422 148 DADGRLRRGGGG----------AVAPFTFTGIQILSPE-LFAGIPPGKFS----------LNPLWdraIAAGRlfGLVYD 206
|
250 260
....*....|....*....|....*....
gi 736655208 244 fssnevpgaterdkAYWRDVGTIDSFYEA 272
Cdd:cd06422 207 --------------GLWFDVGTPERLLAA 221
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
9-181 |
1.28e-12 |
|
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.
Pssm-ID: 133047 [Multi-domain] Cd Length: 233 Bit Score: 66.85 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 9 AIVLAGGEGKRLFPLTLDRAKPAVPFgGNYRLIDFVLSNLVNAGYNRIAVLTQYKSHSLDRHVAtawnfsgpthqyiasv 88
Cdd:cd06425 3 ALILVGGYGTRLRPLTLTVPKPLVEF-CNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLK---------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 89 PAQQRLGKRWY-------QGSADALLQSLNLIFDESPDYvLVFGADHVYRMDPSQMVENHIASGKACTVAGIRVprSEAS 161
Cdd:cd06425 66 EYEKKLGIKITfsietepLGTAGPLALARDLLGDDDEPF-FVLNSDVICDFPLAELLDFHKKHGAEGTILVTKV--EDPS 142
|
170 180
....*....|....*....|.
gi 736655208 162 QFGCIQSDEN-GAITEFLEKP 181
Cdd:cd06425 143 KYGVVVHDENtGRIERFVEKP 163
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
9-273 |
3.86e-12 |
|
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: 65.23 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 9 AIVLAGGEGKRLFPLTLDRAKPAVPFGGNyRLIDFVLSNLVNAGYNRIAVLTQYKSHSLDRHVAT--AWNFSgpthqyIA 86
Cdd:cd06426 1 VVIMAGGKGTRLRPLTENTPKPMLKVGGK-PILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDgsKFGVN------IS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 87 SVPAQQRLgkrwyqGSADALlqSLnliFDESP-DYVLVFGADHVYRMDPSQMVENHIASGKACTVAG----IRVPrseas 161
Cdd:cd06426 74 YVREDKPL------GTAGAL--SL---LPEKPtDPFLVMNGDILTNLNYEHLLDFHKENNADATVCVreyeVQVP----- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 162 qFGCIQSDeNGAITEFLEKPadppgtpddPDTTFASMGNYCFSTEALiqalrdDTENDDSDHDMgGDIIPYFVERGE-AN 240
Cdd:cd06426 138 -YGVVETE-GGRITSIEEKP---------THSFLVNAGIYVLEPEVL------DLIPKNEFFDM-PDLIEKLIKEGKkVG 199
|
250 260 270
....*....|....*....|....*....|...
gi 736655208 241 VYDFSSnevpgaterdkaYWRDVGTIDSFYEAH 273
Cdd:cd06426 200 VFPIHE------------YWLDIGRPEDYEKAN 220
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
9-272 |
1.43e-10 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 61.64 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 9 AIVLAGGEGKRLFPLTLDRAKPAVPFGGNyRLIDFVLSNLVNAGYNRIAVLTqykshsldrhvatawnfsGPTHQyiasv 88
Cdd:COG1209 3 GIILAGGSGTRLRPLTLTVSKQLLPVYDK-PMIYYPLSTLMLAGIREILIIS------------------TPEDG----- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 89 PAQQRL---GKRW-------YQ----GSADALLQSLNLIFDEspDYVLVFGaDHVYRMDP-SQMVENHIASGKACTVAGI 153
Cdd:COG1209 59 PQFERLlgdGSQLgikisyaVQpeplGLAHAFIIAEDFIGGD--PVALVLG-DNIFYGDGlSELLREAAARESGATIFGY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 154 RVprSEASQFGCIQSDENGAITEFLEKPAdppgtpdDPDTTFASMGNYCFsTEALIQALRdDTENDDsdhdmGG-----D 228
Cdd:COG1209 136 KV--EDPERYGVVEFDEDGRVVSLEEKPK-------EPKSNLAVTGLYFY-DNDVVEIAK-NLKPSA-----RGeleitD 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 736655208 229 IIPYFVERGEANVYDFSSNevpgaterdkAYWRDVGTIDSFYEA 272
Cdd:COG1209 200 ANQAYLERGKLVVELLGRG----------FAWLDTGTHESLLEA 233
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
9-72 |
7.55e-10 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 58.71 E-value: 7.55e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736655208 9 AIVLAGGEGKRLFPLTLDRAKPAVPFGGnYRLIDFVLSNLVNAGYNRIAVLTQYKSHSLDRHVA 72
Cdd:COG1213 2 AVILAAGRGSRLGPLTDDIPKCLVEIGG-KTLLERQLEALAAAGIKDIVVVTGYKAELIEEALA 64
|
|
| LbH_G1P_AT_C_like |
cd03356 |
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
315-407 |
3.81e-09 |
|
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: 53.01 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 315 IIAPGSIIS-GSTVRNSVLSTDVYVEDGAVVESSVLMPGVRVGKGAIVRHAILDKNVYVSDGAAVgthradderrgftis 393
Cdd:cd03356 1 LIGESTVIGeNAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRV--------------- 65
|
90
....*....|....
gi 736655208 394 aEGVVVVGKGEFVE 407
Cdd:cd03356 66 -VNLCIIGDDVVVE 78
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
9-68 |
4.76e-09 |
|
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: 56.47 E-value: 4.76e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 9 AIVLAGGEGKRLFPLTLDRAKPAVPFGGNyRLIDFVLSNLVNAGYNRIAVLTQYKSHSLD 68
Cdd:cd02523 1 AIILAAGRGSRLRPLTEDRPKCLLEINGK-PLLERQIETLKEAGIDDIVIVTGYKKEQIE 59
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
9-144 |
8.15e-08 |
|
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: 52.64 E-value: 8.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 9 AIVLAGGEGKRLFPLTLDRAKPAVPFgGNYRLIDFVLSNLVNAGYNRIAVLTQYKSHSLDRHV-ATAWNFSGPT--HQYI 85
Cdd:cd02507 3 AVVLADGFGSRFLPLTSDIPKALLPV-ANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLlKSKWSSLSSKmiVDVI 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736655208 86 ASVPAQQrlgkrwyQGSADALLQSLNLIFDespDYVLVFGaDHVYRMDPSQMVE-------NHIAS 144
Cdd:cd02507 82 TSDLCES-------AGDALRLRDIRGLIRS---DFLLLSC-DLVSNIPLSELLEerrkkdkNAIAT 136
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
9-150 |
2.07e-07 |
|
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: 51.12 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 9 AIVLAGGEGKRLFPLTLDRAKPAVPFgGNYRLIDFVLSNLVNAGYNRIAVLTQYKSH-SLDRHVATAWNFSGPTHQYIAS 87
Cdd:cd04198 3 AVILAGGGGSRLYPLTDNIPKALLPV-ANKPMIWYPLDWLEKAGFEDVIVVVPEEEQaEISTYLRSFPLNLKQKLDEVTI 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 736655208 88 VPAQQrlgkrwyQGSADALLqslnLIFDESPDYVLVFGADHVYRMDPSQMVENHIASGKACTV 150
Cdd:cd04198 82 VLDED-------MGTADSLR----HIRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTV 133
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
9-182 |
6.70e-07 |
|
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: 49.88 E-value: 6.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 9 AIVLAGGEGKRLFPLTLDRAKPAVPFgGNYRLIDFVLSNLVNAGYNRIAVLtqykshsldrhvatawnfSGPTHqyiasV 88
Cdd:cd02538 3 GIILAGGSGTRLYPLTKVVSKQLLPV-YDKPMIYYPLSTLMLAGIREILII------------------STPED-----L 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 89 PAQQRL---GKRW-----YQ------GSADALLQSLNLIFDESpdYVLVFGADHVYRMDPSQMVENHIASGKACTVAGIR 154
Cdd:cd02538 59 PLFKELlgdGSDLgiritYAvqpkpgGLAQAFIIGEEFIGDDP--VCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYE 136
|
170 180
....*....|....*....|....*...
gi 736655208 155 VprSEASQFGCIQSDENGAITEFLEKPA 182
Cdd:cd02538 137 V--NDPERYGVVEFDENGRVLSIEEKPK 162
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
9-181 |
7.94e-06 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 47.36 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 9 AIVLAGGEGKRLFPLTLDRAKPAVPFgGNYRLIDFVLSNLVNAGYNRIAVLTQYKshsldrhvatawnfSGPTHQYIASV 88
Cdd:PRK15480 6 GIILAGGSGTRLYPVTMAVSKQLLPI-YDKPMIYYPLSTLMLAGIRDILIISTPQ--------------DTPRFQQLLGD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 89 PAQQRLGKRW-YQGSADALLQSLNL--IFDESPDYVLVFGADHVYRMDPSQMVENHIASGKACTVAGIRVprSEASQFGC 165
Cdd:PRK15480 71 GSQWGLNLQYkVQPSPDGLAQAFIIgeEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHV--NDPERYGV 148
|
170
....*....|....*.
gi 736655208 166 IQSDENGAITEFLEKP 181
Cdd:PRK15480 149 VEFDQNGTAISLEEKP 164
|
|
| LbH_eIF2B_epsilon |
cd05787 |
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
315-379 |
5.99e-05 |
|
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.
Pssm-ID: 100061 [Multi-domain] Cd Length: 79 Bit Score: 41.02 E-value: 5.99e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736655208 315 IIAPGSII-SGSTVRNSVLSTDVYVEDGAVVESSVLMPGVRVGKGAIVRHAILDKNVYVSDGAAVG 379
Cdd:cd05787 1 VIGRGTSIgEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIP 66
|
|
| G1P_cytidylyltransferase |
cd02524 |
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ... |
138-181 |
7.07e-05 |
|
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.
Pssm-ID: 133015 [Multi-domain] Cd Length: 253 Bit Score: 44.10 E-value: 7.07e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 736655208 138 VENHIASGKACTVAGIRVPrseaSQFGCIQSDENGAITEFLEKP 181
Cdd:cd02524 138 IEFHRSHGKLATVTAVHPP----GRFGELDLDDDGQVTSFTEKP 177
|
|
| LbH_eIF2B_gamma_C |
cd04652 |
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
315-376 |
8.59e-05 |
|
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: 40.64 E-value: 8.59e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 736655208 315 IIAPGSIISGST-VRNSVLSTDVYVEDGAVVESSVLMPGVRVGKGAIVRHAILDKNVYVSDGA 376
Cdd:cd04652 1 LVGENTQVGEKTsIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKC 63
|
|
| Fucokinase |
pfam07959 |
L-fucokinase; In the salvage pathway of GDP-L-fucose, free cytosolic fucose is phosphorylated ... |
311-369 |
2.26e-04 |
|
L-fucokinase; In the salvage pathway of GDP-L-fucose, free cytosolic fucose is phosphorylated by L-fucokinase to form L-fucose-L-phosphate, which is then further converted to GDP-L-fucose in the reaction catalyzed by GDP-L-fucose pyrophosphorylase.
Pssm-ID: 462323 Cd Length: 405 Bit Score: 43.02 E-value: 2.26e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 736655208 311 AQESIIAPGSIISGSTVRNSVLSTDVYVEDGAVVESSVLMPGVRVGKGAIVRHAILDKN 369
Cdd:pfam07959 259 AFSVIANARQLKAGASVINSVLEPGVSVGPGSVIEYCHLGGPVSIGSGCILSGLDLSSS 317
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
9-213 |
4.24e-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: 41.35 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 9 AIVLAGGEGKRLFPltlDRAKPAVPFGGnyR-LIDFVLSNLVNAGYNRIAVLTQYKSHSLDRHVAtawnfsGPTHQYIas 87
Cdd:cd02540 1 AVILAAGKGTRMKS---DLPKVLHPLAG--KpMLEHVLDAARALGPDRIVVVVGHGAEQVKKALA------NPNVEFV-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 88 VPAQQRlgkrwyqGSADALLQSLNLIfDESPDYVLVFGADHvyrmdP-------SQMVENHIASGKACTVAGIRVPRseA 160
Cdd:cd02540 68 LQEEQL-------GTGHAVKQALPAL-KDFEGDVLVLYGDV-----PlitpetlQRLLEAHREAGADVTVLTAELED--P 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 736655208 161 SQFGCIQSDENGAITEFLE-KPAdppgTPDDPDTTFASMGNYCFSTEALIQALR 213
Cdd:cd02540 133 TGYGRIIRDGNGKVLRIVEeKDA----TEEEKAIREVNAGIYAFDAEFLFEALP 182
|
|
| eIF-2B_epsilon_N |
cd04197 |
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
9-141 |
5.32e-04 |
|
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of epsilon 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 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: 133040 [Multi-domain] Cd Length: 217 Bit Score: 41.05 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 9 AIVLAGGEGKRLFPLTLDRAKPAVPFgGNYRLIDFVLSNLVNAGYNRIAVLTQYKSHSLDRHVATA-WN---FSGPTHQY 84
Cdd:cd04197 3 AVVLADSFNRRFRPLTKEKPRCLLPL-ANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKSkWSkpkSSLMIVII 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 736655208 85 IASvPAQQRLGkrwyqgsaDAL--LQSLNLIFDespDYVLVFGaDHVYRMDPSQMVENH 141
Cdd:cd04197 82 IMS-EDCRSLG--------DALrdLDAKGLIRG---DFILVSG-DVVSNIDLKEILEEH 127
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
9-159 |
8.17e-04 |
|
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.
Pssm-ID: 463715 [Multi-domain] Cd Length: 159 Bit Score: 39.87 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 9 AIVLAGGEGKRlfpltLDRAKPAVPFGGNyRLIDFVLSNLVNAGyNRIAVLTQYKshsldrhvatawnfsgPTHQYIASV 88
Cdd:pfam12804 1 AVILAGGRSSR-----MGGDKALLPLGGK-PLLERVLERLRPAG-DEVVVVANDE----------------EVLAALAGL 57
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736655208 89 PAQQRLGKRWYQGSADALLQSLNliFDESPDYVLVFGADHVYrMDPS---QMVENHIASGKACTVAGIRVPRSE 159
Cdd:pfam12804 58 GVPVVPDPDPGQGPLAGLLAALR--AAPGADAVLVLACDMPF-LTPEllrRLLAAAEESGADIVVPVYDGGRGH 128
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
6-361 |
1.85e-03 |
|
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: 40.40 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 6 NVLAIVLAGGEGKRLfpltldR-AKPAV--PFGGnyR-LIDFVLSNLVNAGYNRIAVLT-----QYKSHSLDRHVATAwn 76
Cdd:COG1207 2 PLAVVILAAGKGTRM------KsKLPKVlhPLAG--KpMLEHVLDAARALGPDRIVVVVghgaeQVRAALADLDVEFV-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 77 fsgptHQyiasvpAQQRlgkrwyqGSADALLQSLNLIfDESPDYVLVFGADHvyrmdP-------SQMVENHIASGKACT 149
Cdd:COG1207 72 -----LQ------EEQL-------GTGHAVQQALPAL-PGDDGTVLVLYGDV-----PliraetlKALLAAHRAAGAAAT 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 150 VAGIRVPrsEASQFGCIQSDENG---AITEflEKPAdppgtpddpdttfaSM----------GNYCFSTEALIQALRD-D 215
Cdd:COG1207 128 VLTAELD--DPTGYGRIVRDEDGrvlRIVE--EKDA--------------TEeqraireintGIYAFDAAALREALPKlS 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 216 TENDDsdhdmgG-----DIIPYFVERGEA-NVYDFS-SNEVPGATER------DKAYWRDVGtidsfyEAHMD----LIS 278
Cdd:COG1207 190 NDNAQ------GeyyltDVIAIARADGLKvAAVQPEdPWEVLGVNDRvqlaeaERILQRRIA------ERLMRagvtIID 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655208 279 ihpvfnlynkawpihstedenlpPAKF-VSGGL--AQESIIAPGSIISGSTV--------RNSVLsTDVYVEDGAVVESS 347
Cdd:COG1207 258 -----------------------PATTyIDGDVeiGRDVVIDPNVILEGKTVigegvvigPNCTL-KDSTIGDGVVIKYS 313
|
410
....*....|....
gi 736655208 348 VLMpGVRVGKGAIV 361
Cdd:COG1207 314 VIE-DAVVGAGATV 326
|
|
| |
