|
Name |
Accession |
Description |
Interval |
E-value |
| glgC |
PRK00844 |
glucose-1-phosphate adenylyltransferase; Provisional |
3-413 |
0e+00 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 764.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 3 KSNPKILSIVLAGGEGTRLMPLTRDRAKPAVPFGGVFRLVDFPLSNLVNSGYQQVIVLTQYKSHSLDRHISLTWRFSPLL 82
Cdd:PRK00844 1 RAMPKVLAIVLAGGEGKRLMPLTADRAKPAVPFGGSYRLIDFVLSNLVNSGYLRIYVLTQYKSHSLDRHISQTWRLSGLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 83 GNYVSPVPAQQRLGKHWYLGSADAIYQTINIIEDVQPDIVVIVGADHVYRMDFSQMVQQHIESGAEFTVAGIRQPISQSN 162
Cdd:PRK00844 81 GNYITPVPAQQRLGKRWYLGSADAIYQSLNLIEDEDPDYVVVFGADHVYRMDPRQMVDFHIESGAGVTVAAIRVPREEAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 163 QFGVIEVDPDHpnMIKSFQEKPETATGLPDDPNSFLASMGNYVANTDALFAALAQDEKAENTKHDMGGDIAPYFASRNEA 242
Cdd:PRK00844 161 AFGVIEVDPDG--RIRGFLEKPADPPGLPDDPDEALASMGNYVFTTDALVDALRRDAADEDSSHDMGGDIIPRLVERGRA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 243 GVYDFNTNEIPGSTSTDHAYWRDVGTLKQFYDAHMDLISYVPEFNLYNSEWPIYTMSGNLPPAKFVHAGRDRlGHATDSI 322
Cdd:PRK00844 239 YVYDFSTNEVPGATERDRGYWRDVGTIDAYYDAHMDLLSVHPVFNLYNREWPIYTSSPNLPPAKFVDGGGRV-GSAQDSL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 323 ISPGVIVSGGEVHHSVLSPNVRIHSWSQVVDSILFDGVVVNRRARVYKAILDKNVVLTENSTVGIDTEHDlARGFTVTPD 402
Cdd:PRK00844 318 VSAGSIISGATVRNSVLSPNVVVESGAEVEDSVLMDGVRIGRGAVVRRAILDKNVVVPPGATIGVDLEED-RRRFTVSEG 396
|
410
....*....|.
gi 705426897 403 GITVVPKNTIV 413
Cdd:PRK00844 397 GIVVVPKGQRV 407
|
|
| GlgC |
COG0448 |
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
7-412 |
0e+00 |
|
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];
Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 547.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 7 KILSIVLAGGEGTRLMPLTRDRAKPAVPFGGVFRLVDFPLSNLVNSGYQQVIVLTQYKSHSLDRHISLT--WRFSPLLGn 84
Cdd:COG0448 1 KVLAIILAGGRGSRLGPLTKDRAKPAVPFGGKYRIIDFPLSNCVNSGIRRVGVLTQYKSHSLNDHIGSGkpWDLDRKRG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 85 YVSPVPA-QQRLGKHWYLGSADAIYQTINIIEDVQPDIVVIVGADHVYRMDFSQMVQQHIESGAEFTVAGIRQPISQSNQ 163
Cdd:COG0448 80 GVFILPPyQQREGEDWYQGTADAVYQNLDFIERSDPDYVLILSGDHIYKMDYRQMLDFHIESGADITVACIEVPREEASR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 164 FGVIEVDPDhpNMIKSFQEKPEtatglpdDPNSFLASMGNYVANTDALFAALAQDekAENTKHDMGGDIAPYFASRNEAG 243
Cdd:COG0448 160 FGVMEVDED--GRITEFEEKPK-------DPKSALASMGIYVFNKDVLIELLEED--APNSSHDFGKDIIPRLLDRGKVY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 244 VYDFNtneipgststdhAYWRDVGTLKQFYDAHMDLISYVPEFNLYNSEWPIYTMSGNLPPAKFVhagrdRLGHATDSII 323
Cdd:COG0448 229 AYEFD------------GYWRDVGTIDSYYEANMDLLDPEPEFNLYDPEWPIYTKQKDLPPAKFV-----RGGKVKNSLV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 324 SPGVIVSgGEVHHSVLSPNVRIHSWSQVVDSILFDGVVVNRRARVYKAILDKNVVLTENSTVGIDTEHDLARgFTVTpDG 403
Cdd:COG0448 292 SNGCIIS-GTVENSVLFRGVRVESGAVVENSVIMPGVVIGEGAVIENAIIDKNVVIPPGVVIGEDPEEDRKR-FTVS-SG 368
|
....*....
gi 705426897 404 ITVVPKNTI 412
Cdd:COG0448 369 IVVVGKGAV 377
|
|
| glgC |
PRK00725 |
glucose-1-phosphate adenylyltransferase; Provisional |
7-408 |
0e+00 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234824 [Multi-domain] Cd Length: 425 Bit Score: 519.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 7 KILSIVLAGGEGTRLMPLTRDRAKPAVPFGGVFRLVDFPLSNLVNSGYQQVIVLTQYKSHSLDRHISLTWRF-SPLLGNY 85
Cdd:PRK00725 15 DTLALILAGGRGSRLKELTDKRAKPAVYFGGKFRIIDFALSNCINSGIRRIGVLTQYKAHSLIRHIQRGWSFfREELGEF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 86 VSPVPAQQRL-GKHWYLGSADAIYQTINIIEDVQPDIVVIVGADHVYRMDFSQMVQQHIESGAEFTVAGIRQPISQSNQF 164
Cdd:PRK00725 95 VDLLPAQQRVdEENWYRGTADAVYQNLDIIRRYDPKYVVILAGDHIYKMDYSRMLADHVESGADCTVACLEVPREEASAF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 165 GVIEVDPDhpNMIKSFQEKPETATGLPDDPNSFLASMGNYVANTDALFAALAQDEKAENTKHDMGGDIAPYFASRNEAGV 244
Cdd:PRK00725 175 GVMAVDEN--DRITAFVEKPANPPAMPGDPDKSLASMGIYVFNADYLYELLEEDAEDPNSSHDFGKDIIPKIVEEGKVYA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 245 YDFNTNEIpGSTSTDHAYWRDVGTLKQFYDAHMDLISYVPEFNLYNSEWPIYTMSGNLPPAKFVHAGRDRLGHATDSIIS 324
Cdd:PRK00725 253 HPFSDSCV-RSDPEEEPYWRDVGTLDAYWQANLDLASVTPELDLYDRNWPIWTYQEQLPPAKFVFDRSGRRGMAINSLVS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 325 PGVIVSGGEVHHSVLSPNVRIHSWSQVVDSILFDGVVVNRRARVYKAILDKNVVLTENSTVGIDTEHDlARGFTVTPDGI 404
Cdd:PRK00725 332 GGCIISGAVVRRSVLFSRVRVNSFSNVEDSVLLPDVNVGRSCRLRRCVIDRGCVIPEGMVIGEDPEED-AKRFRRSEEGI 410
|
....
gi 705426897 405 TVVP 408
Cdd:PRK00725 411 VLVT 414
|
|
| glgC |
TIGR02091 |
glucose-1-phosphate adenylyltransferase; This enzyme, glucose-1-phosphate adenylyltransferase, ... |
10-387 |
7.42e-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: 469.43 E-value: 7.42e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 10 SIVLAGGEGTRLMPLTRDRAKPAVPFGGVFRLVDFPLSNLVNSGYQQVIVLTQYKSHSLDRHISLTWRFSPLLGNYVSPV 89
Cdd:TIGR02091 1 AMVLAGGRGSRLSPLTKRRAKPAVPFGGKYRIIDFPLSNCINSGIRRIGVLTQYKSHSLNRHIQRGWDFDGFIDGFVTLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 90 PAQQR-LGKHWYLGSADAIYQTINIIEDVQPDIVVIVGADHVYRMDFSQMVQQHIESGAEFTVAGIRQPISQSNQFGVIE 168
Cdd:TIGR02091 81 PAQQReSGTDWYQGTADAVYQNLDLIEDYDPEYVLILSGDHIYKMDYEKMLDYHIESGADVTIACIPVPRKEASRFGVMQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 169 VDPDhpNMIKSFQEKPETATGLPDDPNSFLASMGNYVANTDALFAALAQDEKAENTKHDMGGDIAPYFASRNEAGVYDFn 248
Cdd:TIGR02091 161 VDED--GRIVDFEEKPANPPSIPGMPDFALASMGIYIFDKDVLKELLEEDADDPESSHDFGKDIIPRALEEGSVQAYLF- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 249 tneipgststdHAYWRDVGTLKQFYDAHMDLISYVPEFNLYNSEWPIYTMSGNLPPAKFVHAGrdrlGHATDSIISPGVI 328
Cdd:TIGR02091 238 -----------SGYWRDVGTIDSFWEANMDLVSVVPPFDLYDRKWPIYTYNEFLPPAKFVDSD----AQVVDSLVSEGCI 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 705426897 329 VSGGEVHHSVLSPNVRIHSWSQVVDSILFDGVVVNRRARVYKAILDKNVVLTENSTVGI 387
Cdd:TIGR02091 303 ISGATVSHSVLGIRVRIGSGSTVEDSVIMGDVGIGRGAVIRNAIIDKNVRIGEGVVIGN 361
|
|
| glgC |
PRK05293 |
glucose-1-phosphate adenylyltransferase; Provisional |
7-415 |
4.19e-112 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 333.76 E-value: 4.19e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 7 KILSIVLAGGEGTRLMPLTRDRAKPAVPFGGVFRLVDFPLSNLVNSGYQQVIVLTQYKSHSLDRHISL--TWRFSPLLGN 84
Cdd:PRK05293 3 EMLAMILAGGQGTRLGKLTKNIAKPAVPFGGKYRIIDFTLSNCANSGIDTVGVLTQYQPLELNNHIGIgsPWDLDRINGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 85 YVSPVPAQQRLGKHWYLGSADAIYQTINIIEDVQPDIVVIVGADHVYRMDFSQMVQQHIESGAEFTVAGIRQPISQSNQF 164
Cdd:PRK05293 83 VTILPPYSESEGGKWYKGTAHAIYQNIDYIDQYDPEYVLILSGDHIYKMDYDKMLDYHKEKEADVTIAVIEVPWEEASRF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 165 GVIEVDPDhpNMIKSFQEKPETatglpddPNSFLASMGNYVANTDALFAALAQDEKAENTKHDMGGDIAPYFASRNEAgV 244
Cdd:PRK05293 163 GIMNTDEN--MRIVEFEEKPKN-------PKSNLASMGIYIFNWKRLKEYLIEDEKNPNSSHDFGKNVIPLYLEEGEK-L 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 245 YDFNTNeipgststdhAYWRDVGTLKQFYDAHMDLISYVPEFNLYNSEWPIYTMSGNLPPAkFVHAGrdrlGHATDSIIS 324
Cdd:PRK05293 233 YAYPFK----------GYWKDVGTIESLWEANMELLRPENPLNLFDRNWRIYSVNPNLPPQ-YIAEN----AKVKNSLVV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 325 PGVIVSgGEVHHSVLSPNVRIHSWSQVVDSILFDGVVVNRRARVYKAILDKNVVLTENSTVGidtehdlargftVTPDGI 404
Cdd:PRK05293 298 EGCVVY-GTVEHSVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVIIG------------GGKEVI 364
|
410
....*....|.
gi 705426897 405 TVVPKNTIVDD 415
Cdd:PRK05293 365 TVIGENEVIGV 375
|
|
| glgC |
PRK02862 |
glucose-1-phosphate adenylyltransferase; Provisional |
7-415 |
5.78e-104 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179486 [Multi-domain] Cd Length: 429 Bit Score: 314.52 E-value: 5.78e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 7 KILSIVLAGGEGTRLMPLTRDRAKPAVPFGGVFRLVDFPLSNLVNSGYQQVIVLTQYKSHSLDRHISLTWRFSPLLGNYV 86
Cdd:PRK02862 3 RVLAIILGGGAGTRLYPLTKLRAKPAVPLAGKYRLIDIPISNCINSGINKIYVLTQFNSASLNRHISQTYNFDGFSGGFV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 87 SPVPAQQRL-GKHWYLGSADAIYQTINIIEDVQPDIVVIVGADHVYRMDFSQMVQQHIESGAEFTVAGIrqPIS--QSNQ 163
Cdd:PRK02862 83 EVLAAQQTPeNPSWFQGTADAVRKYLWHFQEWDVDEYLILSGDQLYRMDYRLFVQHHRETGADITLAVL--PVDekDASG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 164 FGVIEVDPDHpnMIKSFQEKP-----------ETATGLPDDP---NSFLASMGNYVANTDALFAALAQDEkaenTKHDMG 229
Cdd:PRK02862 161 FGLMKTDDDG--RITEFSEKPkgdelkamavdTSRLGLSPEEakgKPYLASMGIYVFSRDVLFDLLNKNP----EYTDFG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 230 GDIAPYFASRNEAGVYDFNtneipgststdhAYWRDVGTLKQFYDAHMDL-ISYVPEFNLYNSEWPIYTMSGNLPPAKFV 308
Cdd:PRK02862 235 KEIIPEAIRDYKVQSYLFD------------GYWEDIGTIEAFYEANLALtQQPNPPFSFYDEKAPIYTRARYLPPSKLL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 309 HAgrdrlgHATDSIISPGVIVSGGEVHHSVLSPNVRIHSWSQVVDSILF-------------------DGVVVNRRARVY 369
Cdd:PRK02862 303 DA------TITESIIAEGCIIKNCSIHHSVLGIRSRIESGCTIEDTLVMgadfyesseereelrkegkPPLGIGEGTTIK 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 705426897 370 KAILDKNVVLTENST-VGIDT----EHDLaRGFTVTpDGITVVPKNTIVDD 415
Cdd:PRK02862 377 RAIIDKNARIGNNVRiVNKDNveeaDRED-QGFYIR-DGIVVVVKNAVIPD 425
|
|
| PLN02241 |
PLN02241 |
glucose-1-phosphate adenylyltransferase |
7-415 |
3.02e-102 |
|
glucose-1-phosphate adenylyltransferase
Pssm-ID: 215133 [Multi-domain] Cd Length: 436 Bit Score: 310.25 E-value: 3.02e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 7 KILSIVLAGGEGTRLMPLTRDRAKPAVPFGGVFRLVDFPLSNLVNSGYQQVIVLTQYKSHSLDRHISLTWRFSPLLGN-- 84
Cdd:PLN02241 3 SVAAIILGGGAGTRLFPLTKRRAKPAVPIGGNYRLIDIPMSNCINSGINKIYVLTQFNSASLNRHLSRAYNFGNGGNFgd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 85 -YVSPVPAQQRLG-KHWYLGSADAIYQTINIIEDVQ---PDIVVIVGADHVYRMDFSQMVQQHIESGAEFTVAGIRQPIS 159
Cdd:PLN02241 83 gFVEVLAATQTPGeKGWFQGTADAVRQFLWLFEDAKnknVEEVLILSGDHLYRMDYMDFVQKHRESGADITIACLPVDES 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 160 QSNQFGVIEVdpDHPNMIKSFQEKPE-----------TATGL-PDDPNS--FLASMGNYVANTDALFAALAQDekaENTK 225
Cdd:PLN02241 163 RASDFGLMKI--DDTGRIIEFSEKPKgdelkamqvdtTVLGLsPEEAKEkpYIASMGIYVFKKDVLLKLLRWR---FPTA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 226 HDMGGDIapyfasrneagvydfntneIPGSTSTDHA--------YWRDVGTLKQFYDAHMDLISYVPEFNLYNSEWPIYT 297
Cdd:PLN02241 238 NDFGSEI-------------------IPGAIKEGYNvqaylfdgYWEDIGTIKSFYEANLALTKQPPKFSFYDPDAPIYT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 298 MSGNLPPAKFVHAgrdrlgHATDSIISPGVIVSGGEVHHSVLSPNVRIHSWSQVVDSILF----------------DGVV 361
Cdd:PLN02241 299 SPRFLPPSKIEDC------RITDSIISHGCFLRECKIEHSVVGLRSRIGEGVEIEDTVMMgadyyeteeeiasllaEGKV 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 705426897 362 ---VNRRARVYKAILDKNVVLTEN----STVGIDtEHDL-ARGFTVTpDGITVVPKNTIVDD 415
Cdd:PLN02241 373 pigIGENTKIRNAIIDKNARIGKNvviiNKDGVQ-EADReEEGYYIR-SGIVVILKNAVIPD 432
|
|
| ADP_Glucose_PP |
cd02508 |
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ... |
11-266 |
4.50e-76 |
|
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP. ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. While a homotetramer in bacteria, in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits. There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. It is a subfamily of a very diverse glycosy transferase family 2.
Pssm-ID: 133002 [Multi-domain] Cd Length: 200 Bit Score: 234.74 E-value: 4.50e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 11 IVLAGGEGTRLMPLTRDRAKPAVPFGGVFRLVDFPLSNLVNSGYQQVIVLTQYKSHSLDRHISLTWRFS-PLLGNYVSPV 89
Cdd:cd02508 2 IILAGGEGTRLSPLTKKRAKPAVPFGGRYRLIDFPLSNMVNSGIRNVGVLTQYKSRSLNDHLGSGKEWDlDRKNGGLFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 90 PAQQRLGKHWYLGSADAIYQTINIIEDVQPDIVVIVGADHVYRMDFSQMVQQHIESGAEFTVAgirqpisqsnqfgviev 169
Cdd:cd02508 82 PPQQRKGGDWYRGTADAIYQNLDYIERSDPEYVLILSGDHIYNMDYREMLDFHIESGADITVV----------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 170 dpdhpnmiksfqekpetatglpddpnsFLASMGNYVANTDALFAALaqDEKAENTKHDMGGDIAPYFASRNEAGVYDFNt 249
Cdd:cd02508 145 ---------------------------YKASMGIYIFSKDLLIELL--EEDAADGSHDFGKDIIPAMLKKLKIYAYEFN- 194
|
250
....*....|....*..
gi 705426897 250 neipgststdhAYWRDV 266
Cdd:cd02508 195 -----------GYWADI 200
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
11-279 |
2.93e-71 |
|
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: 224.05 E-value: 2.93e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 11 IVLAGGEGTRLMPLTRDRAKPAVPFGGVFRLVDFPLSNLVNSGYQQ-VIVLTQYKSHSLDRHISLTWRFSpllgnyVSPV 89
Cdd:pfam00483 3 IILAGGSGTRLWPLTRTLAKPLVPVGGKYPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFG------VQIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 90 PAQQRLGKhwylGSADAIYQTINIIEDvQPDIVVIVGADHVYRMDFSQMVQQHIESGAEFTVAGIRQPISQSNQFGVIEV 169
Cdd:pfam00483 77 YALQPEGK----GTAPAVALAADFLGD-EKSDVLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGIVPVEPPTGYGVVEF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 170 DPDhpNMIKSFQEKPETATGlpddpnSFLASMGNYVANTDALFAALAQDEKAeNTKHDMGGDIAP-YFASRNEAGVYDFN 248
Cdd:pfam00483 152 DDN--GRVIRFVEKPKLPKA------SNYASMGIYIFNSGVLDFLAKYLEEL-KRGEDEITDILPkALEDGKLAYAFIFK 222
|
250 260 270
....*....|....*....|....*....|.
gi 705426897 249 TNEipgststdhayWRDVGTLKQFYDAHMDL 279
Cdd:pfam00483 223 GYA-----------WLDVGTWDSLWEANLFL 242
|
|
| LbH_G1P_AT_C |
cd04651 |
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ... |
309-413 |
2.39e-37 |
|
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: 131.05 E-value: 2.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 309 HAGRDRLGHATDSIISPGVIVSGGEVHHSVLSPNVRIHSWSQVVDSILFDGVVVNRRARVYKAILDKNVVLTENSTVGID 388
Cdd:cd04651 1 PPYIGRRGEVKNSLVSEGCIISGGTVENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIPDGVVIGGD 80
|
90 100
....*....|....*....|....*
gi 705426897 389 TEHDLARgFTVTPDGITVVPKNTIV 413
Cdd:cd04651 81 PEEDRAR-FYVTEDGIVVVGKGMVI 104
|
|
| glgD |
TIGR02092 |
glucose-1-phosphate adenylyltransferase, GlgD subunit; This family is GlgD, an apparent ... |
21-382 |
1.02e-36 |
|
glucose-1-phosphate adenylyltransferase, GlgD subunit; This family is GlgD, an apparent regulatory protein that appears in an alpha2/beta2 heterotetramer with GlgC (glucose-1-phosphate adenylyltransferase, TIGR02091) in a subset of bacteria that use GlgC for glycogen biosynthesis. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
Pssm-ID: 273966 [Multi-domain] Cd Length: 369 Bit Score: 137.51 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 21 LMPLTRDRAKPAVPFGGVFRLVDFPLSNLVNSGYQQVIVLTQYKS-HSLDRHISL--TWRFSPLLGNY-VSPvpaqQRLG 96
Cdd:TIGR02092 16 LSPLTKVRPLASLPFGGRYRLIDFPLSNMVNAGIRNVFIFFKNKErQSLFDHLGSgrEWDLHRKRDGLfVFP----YNDR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 97 KHWYLGSADAIYQTINIIEDVQPDIVVIVGADHVYRMDFSQMVQQHIESGAEFTVagIRQPISQSnqfgvievDPDHPNM 176
Cdd:TIGR02092 92 DDLSEGGKRYFSQNLEFLKRSTSEYTVVLNSHMVCNIDLKAVLKYHEETGKDITV--VYKKVKPA--------DASEYDT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 177 IKSFQEKPETAT---GLPDDPNSFLaSMGNYVANTDALFAALaqdeKAENTKHDMggDIAPYFASRNeAGVYDFNTNEIP 253
Cdd:TIGR02092 162 ILRFDESGKVKSigqNLNPEEEENI-SLDIYIVSTDLLIELL----YECIQRGKL--TSLEELIREN-LKELNINAYEYT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 254 GststdhaYWRDVGTLKQFYDAHMDLISyvPEFN---LYNSEWPIYTMSGNLPPAKFVHAGRdrlghATDSIISPGVIVS 330
Cdd:TIGR02092 234 G-------YLANINSVKSYYKANMDLLD--PQNFqslFYSSQGPIYTKVKDEPPTYYAENSK-----VENSLVANGCIIE 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 705426897 331 gGEVHHSVLSPNVRIHSWSQVVDSILFDGVVVNRRARVYKAILDKNVVLTEN 382
Cdd:TIGR02092 300 -GKVENSILSRGVHVGKDALIKNCIIMQRTVIGEGAHLENVIIDKDVVIEPN 350
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
11-267 |
1.90e-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: 1.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 11 IVLAGGEGTRLMPLTRDRAKPAVPFGGVfRLVDFPLSNLVNSGYQQVIVLTQYKSHSLDRHISLTWRFspllGNYVSPVP 90
Cdd:cd04181 2 VILAAGKGTRLRPLTDTRPKPLLPIAGK-PILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKF----GVNIEYVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 91 aQQRLgkhwyLGSADAIYQTINIIEDvqpDIVVIVGADHVYRMDFSQMVQQHIESGAEFTVAGIRQPISQsnQFGVIEVD 170
Cdd:cd04181 77 -QEEP-----LGTAGAVRNAEDFLGD---DDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVEDPS--RYGVVELD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 171 PDhpNMIKSFQEKpetatglPDDPNSFLASMGNYVANTDaLFAALAQDEKAEntkHDMGGDIAPYFASRNEAGVYDFNtn 250
Cdd:cd04181 146 DD--GRVTRFVEK-------PTLPESNLANAGIYIFEPE-ILDYIPEILPRG---EDELTDAIPLLIEEGKVYGYPVD-- 210
|
250
....*....|....*..
gi 705426897 251 eipgststdhAYWRDVG 267
Cdd:cd04181 211 ----------GYWLDIG 217
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
11-279 |
1.76e-31 |
|
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: 119.87 E-value: 1.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 11 IVLAGGEGTRLMPLTRDRAKPAVPFGGVfRLVDFPLSNLVNSGYQQVIVLTQYKSHSLDRHisltwrfsplLGNyvspvp 90
Cdd:COG1208 3 VILAGGLGTRLRPLTDTRPKPLLPVGGK-PLLEHILERLAAAGITEIVINVGYLAEQIEEY----------FGD------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 91 aQQRLGKH-WY------LGSADAIYQTINIIEDvqpDIVVIVGADHVYRMDFSQMVQQHIESGAEFTVAGIRQPisQSNQ 163
Cdd:COG1208 66 -GSRFGVRiTYvdegepLGTGGALKRALPLLGD---EPFLVLNGDILTDLDLAALLAFHREKGADATLALVPVP--DPSR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 164 FGVIEVDPDhpNMIKSFQEKPEtatglpdDPNSFLASMGNYVANTDaLFAALAQDEKAentkhDMgGDIAPYFASRNEAG 243
Cdd:COG1208 140 YGVVELDGD--GRVTRFVEKPE-------EPPSNLINAGIYVLEPE-IFDYIPEGEPF-----DL-EDLLPRLIAEGRVY 203
|
250 260 270
....*....|....*....|....*....|....*.
gi 705426897 244 VYDFntneipgststdHAYWRDVGTLKQFYDAHMDL 279
Cdd:COG1208 204 GYVH------------DGYWLDIGTPEDLLEANALL 227
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
11-276 |
2.56e-16 |
|
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: 77.55 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 11 IVLAGGEGTRLMPLTRDRAKPAVPFGGVfRLVDFPLSNLVNSGYQQVIVLTQYKSHSLDRHisltwrfsplLGNyvspvp 90
Cdd:cd06426 2 VIMAGGKGTRLRPLTENTPKPMLKVGGK-PILETIIDRFIAQGFRNFYISVNYLAEMIEDY----------FGD------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 91 aqqrlGKHW-----------YLGSADAiyqtINIIEDVQPDIVVIVGADHVYRMDFSQMVQQHIESGAEFTVAGIrqPIS 159
Cdd:cd06426 65 -----GSKFgvnisyvredkPLGTAGA----LSLLPEKPTDPFLVMNGDILTNLNYEHLLDFHKENNADATVCVR--EYE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 160 QSNQFGVIEVDPDHpnmIKSFQEKPEtatglpddpNSFLASMGNYVANTDALfaalaqDEKAENTKHDMGGDIAPYFASR 239
Cdd:cd06426 134 VQVPYGVVETEGGR---ITSIEEKPT---------HSFLVNAGIYVLEPEVL------DLIPKNEFFDMPDLIEKLIKEG 195
|
250 260 270
....*....|....*....|....*....|....*..
gi 705426897 240 NEAGVYdfntnEIpgststdHAYWRDVGTLKQFYDAH 276
Cdd:cd06426 196 KKVGVF-----PI-------HEYWLDIGRPEDYEKAN 220
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
11-188 |
2.10e-13 |
|
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: 69.12 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 11 IVLAGGEGTRLMPLTRDRAKPAVPFGG-VFrlVDFPLSNLVNSGYQQVIVLTQYKSHSLDRHISLTWRFSPLLGNYVSPV 89
Cdd:cd06915 2 VILAGGLGTRLRSVVKDLPKPLAPVAGrPF--LEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 90 PaqqrlgkhwyLGSADAIYQTINIIEDvqPDIVVIVGaDHVYRMDFSQMVQQHIESGAEFTVAGIRQPISQsnQFGVIEV 169
Cdd:cd06915 80 P----------LGTGGAIKNALPKLPE--DQFLVLNG-DTYFDVDLLALLAALRASGADATMALRRVPDAS--RYGNVTV 144
|
170
....*....|....*....
gi 705426897 170 DPDhpNMIKSFQEKPETAT 188
Cdd:cd06915 145 DGD--GRVIAFVEKGPGAA 161
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
11-216 |
2.14e-13 |
|
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.
Pssm-ID: 133032 [Multi-domain] Cd Length: 236 Bit Score: 69.13 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 11 IVLAGGEGTRLMPLTRDRAKPAVPFGGVfRLVDFPLSNLVNSGYQQVIVLTQYKSHSLDRHISLTWRFspllGNYVSPVP 90
Cdd:cd04189 4 LILAGGKGTRLRPLTYTRPKQLIPVAGK-PIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRF----GVRITYIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 91 AQQRlgkhwyLGSADAIYQTINIIEDvqPDIVVIVGaDHVYRMDFSQMVQQHIESGAEftvAGIR-QPISQSNQFGVIEV 169
Cdd:cd04189 79 QEEP------LGLAHAVLAARDFLGD--EPFVVYLG-DNLIQEGISPLVRDFLEEDAD---ASILlAEVEDPRRFGVAVV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 705426897 170 DpdhPNMIKSFQEKPEtatglpdDPNSFLASMGNYVAnTDALFAALA 216
Cdd:cd04189 147 D---DGRIVRLVEKPK-------EPPSNLALVGVYAF-TPAIFDAIS 182
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
10-272 |
2.04e-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: 66.47 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 10 SIVLAGGEGTRLMPLTRDRAKPAVPFGGVfRLVDFPLSNLVNSGYQQVIVLTQYKSHSLDRHISltwrfspllgnyvspv 89
Cdd:cd06425 3 ALILVGGYGTRLRPLTLTVPKPLVEFCNK-PMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLK---------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 90 PAQQRLG-KHWY------LGSADAIYQTINIIEDVQPDIVVIvGADHVYRMDFSQMVQQHIESGAEFTVAGIRqpISQSN 162
Cdd:cd06425 66 EYEKKLGiKITFsietepLGTAGPLALARDLLGDDDEPFFVL-NSDVICDFPLAELLDFHKKHGAEGTILVTK--VEDPS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 163 QFGVIEVDPDHpNMIKSFQEKPEtatglpdDPNSFLASMGNYVANTDALfaALAQDEKAENTKhdmggDIAPYFASRNEA 242
Cdd:cd06425 143 KYGVVVHDENT-GRIERFVEKPK-------VFVGNKINAGIYILNPSVL--DRIPLRPTSIEK-----EIFPKMASEGQL 207
|
250 260 270
....*....|....*....|....*....|
gi 705426897 243 GVYdfntnEIPGststdhaYWRDVGTLKQF 272
Cdd:cd06425 208 YAY-----ELPG-------FWMDIGQPKDF 225
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
11-185 |
2.95e-11 |
|
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short form of glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.
Pssm-ID: 133019 [Multi-domain] Cd Length: 240 Bit Score: 62.98 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 11 IVLAGGEGTRLMPLTRDRAKPAVPfggVFR--LVDFPLSNLVNSGYQQVIVLTQykshslDRHISltwRFSPLLGNyvsp 88
Cdd:cd02538 4 IILAGGSGTRLYPLTKVVSKQLLP---VYDkpMIYYPLSTLMLAGIREILIIST------PEDLP---LFKELLGD---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 89 vpaqqrlGKHWYLG-------SADAIYQTINIIED-VQPD-IVVIVGADHVYRMDFSQMVQQ--HIESGAefTVAGirQP 157
Cdd:cd02538 68 -------GSDLGIRityavqpKPGGLAQAFIIGEEfIGDDpVCLILGDNIFYGQGLSPILQRaaAQKEGA--TVFG--YE 136
|
170 180
....*....|....*....|....*...
gi 705426897 158 ISQSNQFGVIEVDPDhpNMIKSFQEKPE 185
Cdd:cd02538 137 VNDPERYGVVEFDEN--GRVLSIEEKPK 162
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
11-186 |
4.01e-11 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 63.57 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 11 IVLAGGEGTRLMPLTRDRAKPAVPFGG---VFRlvdfPLSNLVNSGYQQVIVLTqykshsldrhislTWRFSP----LLG 83
Cdd:COG1209 4 IILAGGSGTRLRPLTLTVSKQLLPVYDkpmIYY----PLSTLMLAGIREILIIS-------------TPEDGPqferLLG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 84 NyvspvpaqqrlGKHW-----Y------LGSADAIYQTINIIEDvqpDIVVIVGADHVYRMD-FSQMVQQHIESGAEFTV 151
Cdd:COG1209 67 D-----------GSQLgikisYavqpepLGLAHAFIIAEDFIGG---DPVALVLGDNIFYGDgLSELLREAAARESGATI 132
|
170 180 190
....*....|....*....|....*....|....*
gi 705426897 152 AGirQPISQSNQFGVIEVDPDhpNMIKSFQEKPET 186
Cdd:COG1209 133 FG--YKVEDPERYGVVEFDED--GRVVSLEEKPKE 163
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
11-72 |
1.79e-09 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 57.56 E-value: 1.79e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 705426897 11 IVLAGGEGTRLMPLTRDRAKPAVPFGGVfRLVDFPLSNLVNSGYQQVIVLTQYKSHSLDRHI 72
Cdd:COG1213 3 VILAAGRGSRLGPLTDDIPKCLVEIGGK-TLLERQLEALAAAGIKDIVVVTGYKAELIEEAL 63
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
12-77 |
2.27e-09 |
|
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: 57.20 E-value: 2.27e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 705426897 12 VLAGGEGTRLMPLTRDRAKPAVPFGGVfRLVDFPLSNLVNSGYQQVIVLTQYKSHSLDRHISLTWR 77
Cdd:cd06422 4 ILAAGLGTRMRPLTDTRPKPLVPVAGK-PLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDSRF 68
|
|
| M1P_guanylylT_A_like_N |
cd06428 |
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ... |
11-186 |
6.08e-09 |
|
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. 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 that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH 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 including cell lysis, defective cell wall, and failure of polarized growth and cell separation.
Pssm-ID: 133050 [Multi-domain] Cd Length: 257 Bit Score: 56.49 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 11 IVLAGGE--GTRLMPLTRDRAKPAVPFGGvFRLVDFPLSNLVN-SGYQQVIVLTQYKSHSLDRHISLTWRFSPLLGNYvs 87
Cdd:cd06428 2 VILVGGPqkGTRFRPLSLDVPKPLFPVAG-KPMIHHHIEACAKvPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRY-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 88 pvpaqqrLGKHWYLGSADAIYQTINIIEDVQPDIVVIVGADHVYRMDFSQMVQQHIESGAEFTVAGIRQPISQSNQFGVI 167
Cdd:cd06428 79 -------LQEYKPLGTAGGLYHFRDQILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEASREQASNYGCI 151
|
170
....*....|....*....
gi 705426897 168 EVDPDHPNMIKsFQEKPET 186
Cdd:cd06428 152 VEDPSTGEVLH-YVEKPET 169
|
|
| LbH_G1P_AT_C_like |
cd03356 |
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
322-385 |
1.29e-08 |
|
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: 51.47 E-value: 1.29e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 705426897 322 IISPGVIVSGG-EVHHSVLSPNVRIHSWSQVVDSILFDGVVVNRRARVYKAILDKNVVLTENSTV 385
Cdd:cd03356 1 LIGESTVIGENaIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRV 65
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
11-232 |
6.13e-08 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 53.91 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 11 IVLAGGEGTRLMPLTRDRAKPAVPFGGVfRLVDFPLSNLVNSGYQQVIVLTQYKShsldrhislTWRFSPLLGNyvspvp 90
Cdd:PRK15480 7 IILAGGSGTRLYPVTMAVSKQLLPIYDK-PMIYYPLSTLMLAGIRDILIISTPQD---------TPRFQQLLGD------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 91 aqqrlGKHWYLG-------SADAIYQTINIIEDV--QPDIVVIVGADHVYRMDFSQMVQQHI--ESGAEFTVAGIRQPis 159
Cdd:PRK15480 71 -----GSQWGLNlqykvqpSPDGLAQAFIIGEEFigGDDCALVLGDNIFYGHDLPKLMEAAVnkESGATVFAYHVNDP-- 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 705426897 160 qsNQFGVIEVDPDHPNMikSFQEKPEtatglpdDPNSFLASMGNYVANTDALfaalaqdEKAENTKHDMGGDI 232
Cdd:PRK15480 144 --ERYGVVEFDQNGTAI--SLEEKPL-------QPKSNYAVTGLYFYDNDVV-------EMAKNLKPSARGEL 198
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
11-73 |
9.38e-08 |
|
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: 52.62 E-value: 9.38e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 705426897 11 IVLAGGEGTRLMPLTRDRAKPAVPFGGVfRLVDFPLSNLVNSGYQQVIVLTQYKSHSLDRHIS 73
Cdd:cd02523 2 IILAAGRGSRLRPLTEDRPKCLLEINGK-PLLERQIETLKEAGIDDIVIVTGYKKEQIEELLK 63
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
11-141 |
1.10e-06 |
|
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: 49.17 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 11 IVLAGGEGTRLMPLTRDRAKPAVPFGGVfRLVDFPLSNLVNSGYQQVIVLTQYKSHSLDRHI--SLTWRFSPLLGNYVSP 88
Cdd:cd02507 4 VVLADGFGSRFLPLTSDIPKALLPVANV-PLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLlkSKWSSLSSKMIVDVIT 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 705426897 89 VPAQQRlgkhwyLGSADAIYQTINIIEDvqpDIVViVGADHVYRMDFSQMVQQ 141
Cdd:cd02507 83 SDLCES------AGDALRLRDIRGLIRS---DFLL-LSCDLVSNIPLSELLEE 125
|
|
| LbH_G1P_AT_C_like |
cd03356 |
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
321-381 |
1.15e-06 |
|
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.
Pssm-ID: 100046 [Multi-domain] Cd Length: 79 Bit Score: 46.08 E-value: 1.15e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 705426897 321 SIISPGVIV-SGGEVHHSVLSPNVRIHSWSQVVDSILFDGVVVNRRARVY-KAILDKNVVLTE 381
Cdd:cd03356 17 SVIGDNVRIgDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVnLCIIGDDVVVED 79
|
|
| rmlA_long |
TIGR01208 |
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ... |
11-372 |
1.23e-06 |
|
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: 50.09 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 11 IVLAGGEGTRLMPLTRDRAKPAVPFGGVfRLVDFPLSNLVNSGYQQV-IVLTQYKSHSLDRHISLTWRFSPLLGNYVSPV 89
Cdd:TIGR01208 3 LILAAGKGTRLRPLTFTRPKQLIPVANK-PILQYAIEDLAEAGITDIgIVVGPVTGEEIKEIVGEGERFGAKITYIVQGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 90 PaqqrlgkhwyLGSADAIYQTINIIEDvqPDIVVIVGaDHVYRMDFSQMVQQHIESGAEFTVAgiRQPISQSNQFGVIEV 169
Cdd:TIGR01208 82 P----------LGLAHAVYTARDFLGD--DDFVVYLG-DNLIQDGISRFVKSFEEKDYDALIL--LTKVRDPTAFGVAVL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 170 DPDhpNMIKSFQEKPEtatglpdDPNSFLASMGNYvantdaLFAalaqdekaeNTKHDMGGDIAPyfASRNEAGVYDF-- 247
Cdd:TIGR01208 147 EDG--KRILKLVEKPK-------EPPSNLAVVGLY------MFR---------PLIFEAIKNIKP--SWRGELEITDAiq 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 248 ----NTNEIPGSTSTdhAYWRDVGTLKQFYDAH---MDLISYVPEFNLYNSEwpiytMSGNL---PPAKFVHA------- 310
Cdd:TIGR01208 201 wlieKGYKVGGSKVT--GWWKDTGKPEDLLDANrliLDEVEREVQGVDDESK-----IRGRVvvgEGAKIVNSvirgpav 273
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 311 -GRDrlGHATDSIISP------GVIVSGGEVHHS-VLSPNVRIHSWSQVVDSILFDGVVVNRRARVYKAI 372
Cdd:TIGR01208 274 iGED--CIIENSYIGPytsigeGVVIRDAEVEHSiVLDESVIEGVQARIVDSVIGKKVRIKGNRRRPGDL 341
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
11-163 |
2.33e-06 |
|
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133041 [Multi-domain] Cd Length: 214 Bit Score: 48.04 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 11 IVLAGGEGTRLMPLTRDRAKPAVPFGGVfRLVDFPLSNLVNSGYQQVIVLTqykSHSLDRHISLTWRFSPlLGNYVSPVP 90
Cdd:cd04198 4 VILAGGGGSRLYPLTDNIPKALLPVANK-PMIWYPLDWLEKAGFEDVIVVV---PEEEQAEISTYLRSFP-LNLKQKLDE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 705426897 91 AQQRLGKHWylGSADAIYQtiniIEDVQPDIVVIVGADHVYRMDFSQMVQQHIESGAEFTVAgIRQPISQSNQ 163
Cdd:cd04198 79 VTIVLDEDM--GTADSLRH----IRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTVL-LYPPPVSSEQ 144
|
|
| eIF-2B_epsilon_N |
cd04197 |
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
11-142 |
7.71e-05 |
|
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: 43.75 E-value: 7.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705426897 11 IVLAGGEGTRLMPLTRDRAKPAVPFGGVfRLVDFPLSNLVNSGYQQVIVLTQYKSHSLDRHI-SLTWRFSPLLGNYVSPV 89
Cdd:cd04197 4 VVLADSFNRRFRPLTKEKPRCLLPLANV-PLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIeKSKWSKPKSSLMIVIII 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 705426897 90 --PAQQRLGkhwylgsaDA---IYQTiniiEDVQPDIvVIVGADHVYRMDFSQMVQQH 142
Cdd:cd04197 83 msEDCRSLG--------DAlrdLDAK----GLIRGDF-ILVSGDVVSNIDLKEILEEH 127
|
|
| LbH_eIF2B_epsilon |
cd05787 |
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
322-386 |
2.56e-03 |
|
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.
Pssm-ID: 100061 [Multi-domain] Cd Length: 79 Bit Score: 36.40 E-value: 2.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 705426897 322 IISPG-VIVSGGEVHHSVLSPNVRIHSWSQVVDSILFDGVVVNRRARVYKAILDKNVVLTENSTVG 386
Cdd:cd05787 1 VIGRGtSIGEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIP 66
|
|
| |
