|
Name |
Accession |
Description |
Interval |
E-value |
| glgC |
PRK00844 |
glucose-1-phosphate adenylyltransferase; Provisional |
1-403 |
0e+00 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 777.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 1 MAGVLGMILAGGEGSRLRPLTESRSKPSVPFGGSYRLIDFALNNFVNADLMRIYVLTQFKSQSLFHHLKKGWNINGITDR 80
Cdd:PRK00844 3 MPKVLAIVLAGGEGKRLMPLTADRAKPAVPFGGSYRLIDFVLSNLVNSGYLRIYVLTQYKSHSLDRHISQTWRLSGLLGN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 81 FIDPIPAQMRTGKRWYEGTADAIYQNLRFMELAEPDQVCIFGSDHIYKMDIKQMLAFHQEKEASLTVSALRMPLSEASQF 160
Cdd:PRK00844 83 YITPVPAQQRLGKRWYLGSADAIYQSLNLIEDEDPDYVVVFGADHVYRMDPRQMVDFHIESGAGVTVAAIRVPREEASAF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 161 GVIEVDNEGRMIGFEEKPANPKSIPGDPEHALVSMGNYIFEAQTLFAELIEDADNEASTHDFGKDIIPKMFPRGDVFVYD 240
Cdd:PRK00844 163 GVIEVDPDGRIRGFLEKPADPPGLPDDPDEALASMGNYVFTTDALVDALRRDAADEDSSHDMGGDIIPRLVERGRAYVYD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 241 FSTNRITG--EKEEVYWRDVGTIDAYWQAHMDLLEKDAPFSLYNRKWPLHTYYPPLPPATFTDSVNGRVQIIDSLVCNGS 318
Cdd:PRK00844 243 FSTNEVPGatERDRGYWRDVGTIDAYYDAHMDLLSVHPVFNLYNREWPIYTSSPNLPPAKFVDGGGRVGSAQDSLVSAGS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 319 YVRGSRIEKSVLGFRSNIASACDISQCILLGDVKVGEGCVLRRVIVDKDADIAPGTQIGVNLQEDKKHYHVSDDGIVVIP 398
Cdd:PRK00844 323 IISGATVRNSVLSPNVVVESGAEVEDSVLMDGVRIGRGAVVRRAILDKNVVVPPGATIGVDLEEDRRRFTVSEGGIVVVP 402
|
....*
gi 491592802 399 KGARV 403
Cdd:PRK00844 403 KGQRV 407
|
|
| glgC |
TIGR02091 |
glucose-1-phosphate adenylyltransferase; This enzyme, glucose-1-phosphate adenylyltransferase, ... |
6-378 |
0e+00 |
|
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: 580.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 6 GMILAGGEGSRLRPLTESRSKPSVPFGGSYRLIDFALNNFVNADLMRIYVLTQFKSQSLFHHLKKGWNINGITDRFIDPI 85
Cdd:TIGR02091 1 AMVLAGGRGSRLSPLTKRRAKPAVPFGGKYRIIDFPLSNCINSGIRRIGVLTQYKSHSLNRHIQRGWDFDGFIDGFVTLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 86 PAQMRT-GKRWYEGTADAIYQNLRFMELAEPDQVCIFGSDHIYKMDIKQMLAFHQEKEASLTVSALRMPLSEASQFGVIE 164
Cdd:TIGR02091 81 PAQQREsGTDWYQGTADAVYQNLDLIEDYDPEYVLILSGDHIYKMDYEKMLDYHIESGADVTIACIPVPRKEASRFGVMQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 165 VDNEGRMIGFEEKPANPKSIPGDPEHALVSMGNYIFEAQTLFAELIEDADNEASTHDFGKDIIPKMFPRGDVFVYDFSTn 244
Cdd:TIGR02091 161 VDEDGRIVDFEEKPANPPSIPGMPDFALASMGIYIFDKDVLKELLEEDADDPESSHDFGKDIIPRALEEGSVQAYLFSG- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 245 ritgekeevYWRDVGTIDAYWQAHMDLLEKDAPFSLYNRKWPLHTYYPPLPPATFTDSvngRVQIIDSLVCNGSYVRGSR 324
Cdd:TIGR02091 240 ---------YWRDVGTIDSFWEANMDLVSVVPPFDLYDRKWPIYTYNEFLPPAKFVDS---DAQVVDSLVSEGCIISGAT 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 491592802 325 IEKSVLGFRSNIASACDISQCILLGDVKVGEGCVLRRVIVDKDADIAPGTQIGV 378
Cdd:TIGR02091 308 VSHSVLGIRVRIGSGSTVEDSVIMGDVGIGRGAVIRNAIIDKNVRIGEGVVIGN 361
|
|
| GlgC |
COG0448 |
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
4-402 |
0e+00 |
|
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];
Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 556.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 4 VLGMILAGGEGSRLRPLTESRSKPSVPFGGSYRLIDFALNNFVNADLMRIYVLTQFKSQSLFHHLKKG--WNINGITDrF 81
Cdd:COG0448 2 VLAIILAGGRGSRLGPLTKDRAKPAVPFGGKYRIIDFPLSNCVNSGIRRVGVLTQYKSHSLNDHIGSGkpWDLDRKRG-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 82 IDPIPA-QMRTGKRWYEGTADAIYQNLRFMELAEPDQVCIFGSDHIYKMDIKQMLAFHQEKEASLTVSALRMPLSEASQF 160
Cdd:COG0448 81 VFILPPyQQREGEDWYQGTADAVYQNLDFIERSDPDYVLILSGDHIYKMDYRQMLDFHIESGADITVACIEVPREEASRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 161 GVIEVDNEGRMIGFEEKPANPKSipgdpehALVSMGNYIFEAQTLFAELIEDADNeaSTHDFGKDIIPKMFPRGDVFVYD 240
Cdd:COG0448 161 GVMEVDEDGRITEFEEKPKDPKS-------ALASMGIYVFNKDVLIELLEEDAPN--SSHDFGKDIIPRLLDRGKVYAYE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 241 FstnriTGekeevYWRDVGTIDAYWQAHMDLLEKDAPFSLYNRKWPLHTYYPPLPPATFTDsvngRVQIIDSLVCNGSYV 320
Cdd:COG0448 232 F-----DG-----YWRDVGTIDSYYEANMDLLDPEPEFNLYDPEWPIYTKQKDLPPAKFVR----GGKVKNSLVSNGCII 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 321 RGsRIEKSVLGFRSNIASACDISQCILLGDVKVGEGCVLRRVIVDKDADIAPGTQIGVNLQEDKKHYHVSdDGIVVIPKG 400
Cdd:COG0448 298 SG-TVENSVLFRGVRVESGAVVENSVIMPGVVIGEGAVIENAIIDKNVVIPPGVVIGEDPEEDRKRFTVS-SGIVVVGKG 375
|
..
gi 491592802 401 AR 402
Cdd:COG0448 376 AV 377
|
|
| glgC |
PRK00725 |
glucose-1-phosphate adenylyltransferase; Provisional |
5-398 |
0e+00 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234824 [Multi-domain] Cd Length: 425 Bit Score: 540.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 5 LGMILAGGEGSRLRPLTESRSKPSVPFGGSYRLIDFALNNFVNADLMRIYVLTQFKSQSLFHHLKKGWNI-NGITDRFID 83
Cdd:PRK00725 17 LALILAGGRGSRLKELTDKRAKPAVYFGGKFRIIDFALSNCINSGIRRIGVLTQYKAHSLIRHIQRGWSFfREELGEFVD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 84 PIPAQMRT-GKRWYEGTADAIYQNLRFMELAEPDQVCIFGSDHIYKMDIKQMLAFHQEKEASLTVSALRMPLSEASQFGV 162
Cdd:PRK00725 97 LLPAQQRVdEENWYRGTADAVYQNLDIIRRYDPKYVVILAGDHIYKMDYSRMLADHVESGADCTVACLEVPREEASAFGV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 163 IEVDNEGRMIGFEEKPANPKSIPGDPEHALVSMGNYIFEAQTLFAELIEDADNEASTHDFGKDIIPKMFPRGDVFVYDFS 242
Cdd:PRK00725 177 MAVDENDRITAFVEKPANPPAMPGDPDKSLASMGIYVFNADYLYELLEEDAEDPNSSHDFGKDIIPKIVEEGKVYAHPFS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 243 TNRITGEKE-EVYWRDVGTIDAYWQAHMDLLEKDAPFSLYNRKWPLHTYYPPLPPATFT-DSVNGRVQIIDSLVCNGSYV 320
Cdd:PRK00725 257 DSCVRSDPEeEPYWRDVGTLDAYWQANLDLASVTPELDLYDRNWPIWTYQEQLPPAKFVfDRSGRRGMAINSLVSGGCII 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491592802 321 RGSRIEKSVLGFRSNIASACDISQCILLGDVKVGEGCVLRRVIVDKDADIAPGTQIGVNLQEDKKHYHVSDDGIVVIP 398
Cdd:PRK00725 337 SGAVVRRSVLFSRVRVNSFSNVEDSVLLPDVNVGRSCRLRRCVIDRGCVIPEGMVIGEDPEEDAKRFRRSEEGIVLVT 414
|
|
| glgC |
PRK05293 |
glucose-1-phosphate adenylyltransferase; Provisional |
4-405 |
3.64e-127 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 371.51 E-value: 3.64e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 4 VLGMILAGGEGSRLRPLTESRSKPSVPFGGSYRLIDFALNNFVNADLMRIYVLTQFKSQSLFHHLKKG--WNIN----GI 77
Cdd:PRK05293 4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKYRIIDFTLSNCANSGIDTVGVLTQYQPLELNNHIGIGspWDLDringGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 78 TdrfIDPiPAQMRTGKRWYEGTADAIYQNLRFMELAEPDQVCIFGSDHIYKMDIKQMLAFHQEKEASLTVSALRMPLSEA 157
Cdd:PRK05293 84 T---ILP-PYSESEGGKWYKGTAHAIYQNIDYIDQYDPEYVLILSGDHIYKMDYDKMLDYHKEKEADVTIAVIEVPWEEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 158 SQFGVIEVDNEGRMIGFEEKPANPKSipgdpehALVSMGNYIFEAQTLFAELIEDADNEASTHDFGKDIIPKMFPRGD-V 236
Cdd:PRK05293 160 SRFGIMNTDENMRIVEFEEKPKNPKS-------NLASMGIYIFNWKRLKEYLIEDEKNPNSSHDFGKNVIPLYLEEGEkL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 237 FVYDFstnritgekeEVYWRDVGTIDAYWQAHMDLLEKDAPFSLYNRKWPLHTYYPPLPPATFTDSVNgrvqIIDSLVCN 316
Cdd:PRK05293 233 YAYPF----------KGYWKDVGTIESLWEANMELLRPENPLNLFDRNWRIYSVNPNLPPQYIAENAK----VKNSLVVE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 317 GSYVRGSrIEKSVLGFRSNIASACDISQCILLGDVKVGEGCVLRRVIVDKDADIAPGTQIGvnlqedkkhyhVSDDGIVV 396
Cdd:PRK05293 299 GCVVYGT-VEHSVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVIIG-----------GGKEVITV 366
|
....*....
gi 491592802 397 IPKGARVGY 405
Cdd:PRK05293 367 IGENEVIGV 375
|
|
| glgC |
PRK02862 |
glucose-1-phosphate adenylyltransferase; Provisional |
1-403 |
3.89e-114 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179486 [Multi-domain] Cd Length: 429 Bit Score: 340.32 E-value: 3.89e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 1 MAGVLGMILAGGEGSRLRPLTESRSKPSVPFGGSYRLIDFALNNFVNADLMRIYVLTQFKSQSLFHHLKKGWNINGITDR 80
Cdd:PRK02862 1 MKRVLAIILGGGAGTRLYPLTKLRAKPAVPLAGKYRLIDIPISNCINSGINKIYVLTQFNSASLNRHISQTYNFDGFSGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 81 FIDPIPA-QMRTGKRWYEGTADAIYQNLRFMELAEPDQVCIFGSDHIYKMDIKQMLAFHQEKEASLTVSALRMPLSEASQ 159
Cdd:PRK02862 81 FVEVLAAqQTPENPSWFQGTADAVRKYLWHFQEWDVDEYLILSGDQLYRMDYRLFVQHHRETGADITLAVLPVDEKDASG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 160 FGVIEVDNEGRMIGFEEKPA---------NPKSIPGDPEHA-----LVSMGNYIFEAQTLFaELIedaDNEASTHDFGKD 225
Cdd:PRK02862 161 FGLMKTDDDGRITEFSEKPKgdelkamavDTSRLGLSPEEAkgkpyLASMGIYVFSRDVLF-DLL---NKNPEYTDFGKE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 226 IIPKMFPRGDVFVYDFSTnritgekeevYWRDVGTIDAYWQAHMDLLEKDAP-FSLYNRKWPLHTYYPPLPPATFTDSvn 304
Cdd:PRK02862 237 IIPEAIRDYKVQSYLFDG----------YWEDIGTIEAFYEANLALTQQPNPpFSFYDEKAPIYTRARYLPPSKLLDA-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 305 grvQIIDSLVCNGSYVRGSRIEKSVLGFRSNIASACDISQCILLG-------------------DVKVGEGCVLRRVIVD 365
Cdd:PRK02862 305 ---TITESIIAEGCIIKNCSIHHSVLGIRSRIESGCTIEDTLVMGadfyesseereelrkegkpPLGIGEGTTIKRAIID 381
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 491592802 366 KDADIAPGTQIGV--NLQE---DKKHYHVSdDGIVVIPKGARV 403
Cdd:PRK02862 382 KNARIGNNVRIVNkdNVEEadrEDQGFYIR-DGIVVVVKNAVI 423
|
|
| PLN02241 |
PLN02241 |
glucose-1-phosphate adenylyltransferase |
4-401 |
8.37e-100 |
|
glucose-1-phosphate adenylyltransferase
Pssm-ID: 215133 [Multi-domain] Cd Length: 436 Bit Score: 303.70 E-value: 8.37e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 4 VLGMILAGGEGSRLRPLTESRSKPSVPFGGSYRLIDFALNNFVNADLMRIYVLTQFKSQSLFHHLKKGWNI-NGI--TDR 80
Cdd:PLN02241 4 VAAIILGGGAGTRLFPLTKRRAKPAVPIGGNYRLIDIPMSNCINSGINKIYVLTQFNSASLNRHLSRAYNFgNGGnfGDG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 81 FIDPIPAQMRTG-KRWYEGTADAIYQNLRFME---LAEPDQVCIFGSDHIYKMDIKQMLAFHQEKEASLTVSALRMPLSE 156
Cdd:PLN02241 84 FVEVLAATQTPGeKGWFQGTADAVRQFLWLFEdakNKNVEEVLILSGDHLYRMDYMDFVQKHRESGADITIACLPVDESR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 157 ASQFGVIEVDNEGRMIGFEEKP--------ANPKSIPG-DPEHA-----LVSMGNYIFEAQTLfAELIEDADNEAstHDF 222
Cdd:PLN02241 164 ASDFGLMKIDDTGRIIEFSEKPkgdelkamQVDTTVLGlSPEEAkekpyIASMGIYVFKKDVL-LKLLRWRFPTA--NDF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 223 GKDIIPKMFPRG-DVFVYDFSTnritgekeevYWRDVGTIDAYWQAHMDLLEKDAPFSLYNRKWPLHTYYPPLPPATFTD 301
Cdd:PLN02241 241 GSEIIPGAIKEGyNVQAYLFDG----------YWEDIGTIKSFYEANLALTKQPPKFSFYDPDAPIYTSPRFLPPSKIED 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 302 SVngrvqIIDSLVCNGSYVRGSRIEKSVLGFRSNIASACDISQCILLGD-------------------VKVGEGCVLRRV 362
Cdd:PLN02241 311 CR-----ITDSIISHGCFLRECKIEHSVVGLRSRIGEGVEIEDTVMMGAdyyeteeeiasllaegkvpIGIGENTKIRNA 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 491592802 363 IVDKDADIAPGTQIgVNLQEDKKHYHVSD-----DGIVVIPKGA 401
Cdd:PLN02241 386 IIDKNARIGKNVVI-INKDGVQEADREEEgyyirSGIVVILKNA 428
|
|
| ADP_Glucose_PP |
cd02508 |
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ... |
6-258 |
3.04e-87 |
|
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: 263.25 E-value: 3.04e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 6 GMILAGGEGSRLRPLTESRSKPSVPFGGSYRLIDFALNNFVNADLMRIYVLTQFKSQSLFHHLKKGWNINGI-TDRFIDP 84
Cdd:cd02508 1 AIILAGGEGTRLSPLTKKRAKPAVPFGGRYRLIDFPLSNMVNSGIRNVGVLTQYKSRSLNDHLGSGKEWDLDrKNGGLFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 85 IPAQMRTGKRWYEGTADAIYQNLRFMELAEPDQVCIFGSDHIYKMDIKQMLAFHQEKEASLTVSalrmplseasqfgvie 164
Cdd:cd02508 81 LPPQQRKGGDWYRGTADAIYQNLDYIERSDPEYVLILSGDHIYNMDYREMLDFHIESGADITVV---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 165 vdnegrmigfeekpanpksipgdpehALVSMGNYIFEAQTLFAELIEDADNEAstHDFGKDIIPKMFPRGDVFVYDFSTn 244
Cdd:cd02508 145 --------------------------YKASMGIYIFSKDLLIELLEEDAADGS--HDFGKDIIPAMLKKLKIYAYEFNG- 195
|
250
....*....|....
gi 491592802 245 ritgekeevYWRDV 258
Cdd:cd02508 196 ---------YWADI 200
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
5-272 |
1.87e-70 |
|
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: 221.74 E-value: 1.87e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 5 LGMILAGGEGSRLRPLTESRSKPSVPFGGSYRLIDFALNNFVNADLMR-IYVLTQFKSQSLFHHLKKGWNINgitdrfID 83
Cdd:pfam00483 1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKYPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFG------VQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 84 PIPAQMRTGKrwyeGTADAIYQNLRFMElAEPDQVCIFGSDHIYKMDIKQMLAFHQEKEASLTVSALRMPLSEASQFGVI 163
Cdd:pfam00483 75 ITYALQPEGK----GTAPAVALAADFLG-DEKSDVLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGIVPVEPPTGYGVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 164 EVDNEGRMIGFEEKPANPKSIpgdpehALVSMGNYIFEAQtLFAELIEDADNEASTHDFGKDIIPKMFPRGDVFVYdfst 243
Cdd:pfam00483 150 EFDDNGRVIRFVEKPKLPKAS------NYASMGIYIFNSG-VLDFLAKYLEELKRGEDEITDILPKALEDGKLAYA---- 218
|
250 260
....*....|....*....|....*....
gi 491592802 244 nrITGEKEEvyWRDVGTIDAYWQAHMDLL 272
Cdd:pfam00483 219 --FIFKGYA--WLDVGTWDSLWEANLFLL 243
|
|
| glgD |
TIGR02092 |
glucose-1-phosphate adenylyltransferase, GlgD subunit; This family is GlgD, an apparent ... |
1-403 |
3.02e-46 |
|
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: 162.94 E-value: 3.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 1 MAGVLGMIlaggEGSR-LRPLTESRSKPSVPFGGSYRLIDFALNNFVNADLMRIYVLTQFKS-QSLFHHLKKG--WNING 76
Cdd:TIGR02092 3 MSAIINLT----ESSKnLSPLTKVRPLASLPFGGRYRLIDFPLSNMVNAGIRNVFIFFKNKErQSLFDHLGSGreWDLHR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 77 ITDR-FIDPipaqMRTGKRWYEGTADAIYQNLRFMELAEPDQVCIFGSDHIYKMDIKQMLAFHQEKEASLTVSALRM-PL 154
Cdd:TIGR02092 79 KRDGlFVFP----YNDRDDLSEGGKRYFSQNLEFLKRSTSEYTVVLNSHMVCNIDLKAVLKYHEETGKDITVVYKKVkPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 155 SEASQFGVIEVDNEGRMIGFeekpanpKSIPGDPEHALVSMGNYIFEaQTLFAELIEDAdNEASTHDFGKDIIPKMFPRG 234
Cdd:TIGR02092 155 DASEYDTILRFDESGKVKSI-------GQNLNPEEEENISLDIYIVS-TDLLIELLYEC-IQRGKLTSLEELIRENLKEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 235 DVFVYDFstnriTGekeevYWRDVGTIDAYWQAHMDLLEKDAPFSL-YNRKWPLHTYYPPLPPATFTDSvngrVQIIDSL 313
Cdd:TIGR02092 226 NINAYEY-----TG-----YLANINSVKSYYKANMDLLDPQNFQSLfYSSQGPIYTKVKDEPPTYYAEN----SKVENSL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 314 VCNGSYVRGsRIEKSVLGFRSNIASACDISQCILLGDVKVGEGCVLRRVIVDKDADIAPGTQIgVNLQEDKkhyhvsddg 393
Cdd:TIGR02092 292 VANGCIIEG-KVENSILSRGVHVGKDALIKNCIIMQRTVIGEGAHLENVIIDKDVVIEPNVKI-AGTSEQP--------- 360
|
410
....*....|
gi 491592802 394 iVVIPKGARV 403
Cdd:TIGR02092 361 -LVISKGTVV 369
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
7-277 |
1.64e-44 |
|
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: 154.16 E-value: 1.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 7 MILAGGEGSRLRPLTESRSKPSVPFGGsyR-LIDFALNNFVNADLMRIYVLTQFKSQSLFHHLKK----GWNIngitdRF 81
Cdd:COG1208 3 VILAGGLGTRLRPLTDTRPKPLLPVGG--KpLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDgsrfGVRI-----TY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 82 IDpipaqmrTGKRWyeGTADAIyqnLRFMELAEPDQVCIFGSDHIYKMDIKQMLAFHQEKEASLTVSALRMPlsEASQFG 161
Cdd:COG1208 76 VD-------EGEPL--GTGGAL---KRALPLLGDEPFLVLNGDILTDLDLAALLAFHREKGADATLALVPVP--DPSRYG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 162 VIEVDNEGRMIGFEEKPANPKSipgdpehALVSMGNYIFEAQtLFAELIEDAdneasTHDFGkDIIPKMFPRGDVFVYdf 241
Cdd:COG1208 142 VVELDGDGRVTRFVEKPEEPPS-------NLINAGIYVLEPE-IFDYIPEGE-----PFDLE-DLLPRLIAEGRVYGY-- 205
|
250 260 270
....*....|....*....|....*....|....*.
gi 491592802 242 stnRITGekeevYWRDVGTIDAYWQAHMDLLEKDAP 277
Cdd:COG1208 206 ---VHDG-----YWLDIGTPEDLLEANALLLSGKAP 233
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
6-259 |
1.72e-42 |
|
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: 148.50 E-value: 1.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 6 GMILAGGEGSRLRPLTESRSKPSVPFGGsYRLIDFALNNFVNADLMRIYVLTQFKSQSLFHHLKKGWNINGITDRFIDPI 85
Cdd:cd04181 1 AVILAAGKGTRLRPLTDTRPKPLLPIAG-KPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVNIEYVVQEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 86 PaqmrtgkrwyEGTADAIYQNLRFMelaEPDQVCIFGSDHIYKMDIKQMLAFHQEKEASLTVSALRMPlsEASQFGVIEV 165
Cdd:cd04181 80 P----------LGTAGAVRNAEDFL---GDDDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVE--DPSRYGVVEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 166 DNEGRMIGFEEKPANPKSipgdpehALVSMGNYIFEAQTLfaELIEdaDNEASTHDFGKDIIPKMFPRGDVFVYDFstnr 245
Cdd:cd04181 145 DDDGRVTRFVEKPTLPES-------NLANAGIYIFEPEIL--DYIP--EILPRGEDELTDAIPLLIEEGKVYGYPV---- 209
|
250
....*....|....
gi 491592802 246 itgekeEVYWRDVG 259
Cdd:cd04181 210 ------DGYWLDIG 217
|
|
| LbH_G1P_AT_C |
cd04651 |
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ... |
301-403 |
7.60e-35 |
|
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: 124.50 E-value: 7.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 301 DSVNGRVQIIDSLVCNGSYVRGSRIEKSVLGFRSNIASACDISQCILLGDVKVGEGCVLRRVIVDKDADIAPGTQIGVNL 380
Cdd:cd04651 2 PYIGRRGEVKNSLVSEGCIISGGTVENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIPDGVVIGGDP 81
|
90 100
....*....|....*....|...
gi 491592802 381 QEDKKHYHVSDDGIVVIPKGARV 403
Cdd:cd04651 82 EEDRARFYVTEDGIVVVGKGMVI 104
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
7-268 |
2.16e-21 |
|
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: 91.85 E-value: 2.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 7 MILAGGEGSRLRPLTESRSKPSVPFGGsYRLIDFALNNFVNADLMRIYVLTQFKSQSLFHHLKKGWnINGITDRFID-PI 85
Cdd:cd06915 2 VILAGGLGTRLRSVVKDLPKPLAPVAG-RPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGY-RGGIRIYYVIePE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 86 PAqmrtgkrwyeGTADAIYqnlRFMELAEPDQVCIFGSDHIYKMDIKQMLAFHQEKEASLTVSALRMPlsEASQFGVIEV 165
Cdd:cd06915 80 PL----------GTGGAIK---NALPKLPEDQFLVLNGDTYFDVDLLALLAALRASGADATMALRRVP--DASRYGNVTV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 166 DNEGRMIGFEEKPANPKSipgdpehALVSMGNYIFEAQtLFAELiedADNEASthdFGKDIIPKMFPRGDVFVYdfstnr 245
Cdd:cd06915 145 DGDGRVIAFVEKGPGAAP-------GLINGGVYLLRKE-ILAEI---PADAFS---LEADVLPALVKRGRLYGF------ 204
|
250 260
....*....|....*....|...
gi 491592802 246 itgEKEEvYWRDVGTIDAYWQAH 268
Cdd:cd06915 205 ---EVDG-YFIDIGIPEDYARAQ 223
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
7-268 |
2.11e-18 |
|
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.
Pssm-ID: 133048 [Multi-domain] Cd Length: 220 Bit Score: 83.33 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 7 MILAGGEGSRLRPLTESRSKPSVPFGGSyRLIDFALNNFVNADLMRIYVLTQFKSQSLFHHLKKG--WNINgitdrfIDP 84
Cdd:cd06426 2 VIMAGGKGTRLRPLTENTPKPMLKVGGK-PILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGskFGVN------ISY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 85 IpaqmRTGKRWyeGTADAiyqnLRFMELAEPDQVCIFGSDHIYKMDIKQMLAFHQEKEASLTVSA----LRMPlseasqF 160
Cdd:cd06426 75 V----REDKPL--GTAGA----LSLLPEKPTDPFLVMNGDILTNLNYEHLLDFHKENNADATVCVreyeVQVP------Y 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 161 GVIEVDNeGRMIGFEEKPAnpksipgdpEHALVSMGNYIFEAQTLfaELIEDadNEasTHDFgKDIIPKMFPRGD-VFVY 239
Cdd:cd06426 139 GVVETEG-GRITSIEEKPT---------HSFLVNAGIYVLEPEVL--DLIPK--NE--FFDM-PDLIEKLIKEGKkVGVF 201
|
250 260
....*....|....*....|....*....
gi 491592802 240 DfstnrITGekeevYWRDVGTIDAYWQAH 268
Cdd:cd06426 202 P-----IHE-----YWLDIGRPEDYEKAN 220
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
4-273 |
9.05e-18 |
|
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: 81.85 E-value: 9.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 4 VLGMILAGGEGSRLRPLTESRSKPSVPFGGSyRLIDFALNNFVNADLMRIYVLTQFKSQSLFHHLKKG--WNINgITdrF 81
Cdd:cd04189 1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGK-PIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGsrFGVR-IT--Y 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 82 IdpipaqmRTGKRwyEGTADAIYQNLRFmeLAEPDQVCIFGsDHIYKMDIKQML-AFHQEK-EASLTVSALRMPlseaSQ 159
Cdd:cd04189 77 I-------LQEEP--LGLAHAVLAARDF--LGDEPFVVYLG-DNLIQEGISPLVrDFLEEDaDASILLAEVEDP----RR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 160 FGVIEVDNeGRMIGFEEKPANPKSipgdpEHALVsmGNYifeaqtLFAELIEDADNEASTHDFGK----DIIPKMFPRGd 235
Cdd:cd04189 141 FGVAVVDD-GRIVRLVEKPKEPPS-----NLALV--GVY------AFTPAIFDAISRLKPSWRGEleitDAIQWLIDRG- 205
|
250 260 270
....*....|....*....|....*....|....*...
gi 491592802 236 vfvYDFSTNRITGekeevYWRDVGTIDaywqahmDLLE 273
Cdd:cd04189 206 ---RRVGYSIVTG-----WWKDTGTPE-------DLLE 228
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
6-186 |
4.07e-17 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 80.90 E-value: 4.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 6 GMILAGGEGSRLRPLTESRSKPSVPFGG---SYRLIDfalnnfvnaDLMR-----IYVLT------QFKsqslfHHLKKG 71
Cdd:COG1209 3 GIILAGGSGTRLRPLTLTVSKQLLPVYDkpmIYYPLS---------TLMLagireILIIStpedgpQFE-----RLLGDG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 72 --WNINGitdRFID-PIPaqmrtgkrwyEGTADAIYqnlrfmeLAEP----DQVCIFGSDHIYKMD-IKQMLAFHQEKEA 143
Cdd:COG1209 69 sqLGIKI---SYAVqPEP----------LGLAHAFI-------IAEDfiggDPVALVLGDNIFYGDgLSELLREAAARES 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491592802 144 SLTVSALRmpLSEASQFGVIEVDNEGRMIGFEEKPANPKS---IPG 186
Cdd:COG1209 129 GATIFGYK--VEDPERYGVVEFDEDGRVVSLEEKPKEPKSnlaVTG 172
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
7-264 |
2.00e-16 |
|
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: 78.02 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 7 MILAGGEGSRLRPLTESRSKPSVPFGGSyRLIDFALNNFVNADLMRIYVLTQFKSQSLFHHLK---KGWNINGITDRFID 83
Cdd:cd06425 4 LILVGGYGTRLRPLTLTVPKPLVEFCNK-PMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKeyeKKLGIKITFSIETE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 84 PIpaqmrtgkrwyeGTADAIyqnlrfmELAEpDQVC-------IFGSDHIYKMDIKQMLAFHQE--KEASLTVSALrmpl 154
Cdd:cd06425 83 PL------------GTAGPL-------ALAR-DLLGdddepffVLNSDVICDFPLAELLDFHKKhgAEGTILVTKV---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 155 SEASQFGVIEVD-NEGRMIGFEEKPANPKSipgdpehALVSMGNYIFEAQTLfaELIEDADNEasthdFGKDIIPKMFPR 233
Cdd:cd06425 139 EDPSKYGVVVHDeNTGRIERFVEKPKVFVG-------NKINAGIYILNPSVL--DRIPLRPTS-----IEKEIFPKMASE 204
|
250 260 270
....*....|....*....|....*....|.
gi 491592802 234 GDVFVYDFstnritgekeEVYWRDVGTIDAY 264
Cdd:cd06425 205 GQLYAYEL----------PGFWMDIGQPKDF 225
|
|
| rmlA_long |
TIGR01208 |
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ... |
6-403 |
3.65e-15 |
|
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced. Alternate name: dTDP-D-glucose synthase
Pssm-ID: 273500 [Multi-domain] Cd Length: 353 Bit Score: 76.29 E-value: 3.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 6 GMILAGGEGSRLRPLTESRSKPSVPFGGSyRLIDFALNNFVNADLMRIYVLTQFKSQSLFHHLKKGWNINGITDRFI--- 82
Cdd:TIGR01208 2 ALILAAGKGTRLRPLTFTRPKQLIPVANK-PILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIvqg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 83 DPIpaqmrtgkrwyeGTADAIYQNLRFMelaEPDQVCIFGSDHIYKMDIKQMLA-FHqekEASLTVSALRMPLSEASQFG 161
Cdd:TIGR01208 81 EPL------------GLAHAVYTARDFL---GDDDFVVYLGDNLIQDGISRFVKsFE---EKDYDALILLTKVRDPTAFG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 162 VIEVDNEGRMIGFEEKPANPKSipgdpEHALVsmGNYIFEAQtlFAELIEDADNEASTHDFGKDIIPKMFPRGDvfvydf 241
Cdd:TIGR01208 143 VAVLEDGKRILKLVEKPKEPPS-----NLAVV--GLYMFRPL--IFEAIKNIKPSWRGELEITDAIQWLIEKGY------ 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 242 stnRITGEKEEVYWRDVGTIDaywqahmDLLEKdapfslyNRkwplhtyypplppaTFTDSVNGRVQiidslvcngsyvr 321
Cdd:TIGR01208 208 ---KVGGSKVTGWWKDTGKPE-------DLLDA-------NR--------------LILDEVEREVQ------------- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 322 GSRIEKSVLGfRSNIASACDISQCILLGDVKVGEGCVLRrvivdkDADIAPGTQIG--VNLQEDKKHYHVSDDGIVVIPK 399
Cdd:TIGR01208 244 GVDDESKIRG-RVVVGEGAKIVNSVIRGPAVIGEDCIIE------NSYIGPYTSIGegVVIRDAEVEHSIVLDESVIEGV 316
|
....
gi 491592802 400 GARV 403
Cdd:TIGR01208 317 QARI 320
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
6-267 |
2.95e-14 |
|
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: 71.84 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 6 GMILAGGEGSRLRPLTESRSKPSVPFGgSYRLIDFALNNFVNADLMRIYVLTQFKSQSLFHHL---KKGWNINgITDRfI 82
Cdd:cd02538 3 GIILAGGSGTRLYPLTKVVSKQLLPVY-DKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELlgdGSDLGIR-ITYA-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 83 DPIPaqmrtgkrwyEGTADAIYqnlrfmeLAEP----DQVC-IFGSDHIYKMDIKQMLAFHQEKEASLTVsaLRMPLSEA 157
Cdd:cd02538 80 QPKP----------GGLAQAFI-------IGEEfigdDPVClILGDNIFYGQGLSPILQRAAAQKEGATV--FGYEVNDP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 158 SQFGVIEVDNEGRMIGFEEKPANPKSipgdpehALVSMGNYIFeaqtlfaeliedaDNEASthDFGKDIIPKmfPRGDVF 237
Cdd:cd02538 141 ERYGVVEFDENGRVLSIEEKPKKPKS-------NYAVTGLYFY-------------DNDVF--EIAKQLKPS--ARGELE 196
|
250 260 270
....*....|....*....|....*....|....*....
gi 491592802 238 VYDfsTNRITGEKEEV---------YWRDVGTIDAYWQA 267
Cdd:cd02538 197 ITD--VNNEYLEKGKLsvellgrgfAWLDTGTHESLLEA 233
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
7-267 |
6.42e-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: 6.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 7 MILAGGEGSRLRPLTESRSKPSVPFGGSyRLIDFALNNFVNADLMRIYVLTqfksqslfHHLKkgwningitdrfiDPIP 86
Cdd:cd06422 3 MILAAGLGTRMRPLTDTRPKPLVPVAGK-PLIDHALDRLAAAGIRRIVVNT--------HHLA-------------DQIE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 87 AQMRTgKRW-------YE-----GTADAIYQNLRFmeLAEpDQVCIFGSDHIYKMDIKQMLAFHQEKEASLTVSALRMPL 154
Cdd:cd06422 61 AHLGD-SRFglritisDEpdellETGGGIKKALPL--LGD-EPFLVVNGDILWDGDLAPLLLLHAWRMDALLLLLPLVRN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 155 SEASQFGVIEVDNEGRMIGFEEKPANPksipgdpehaLVSMGNYIFEAqTLFAELIEDAdneASTHDFGKDIIPKmfprg 234
Cdd:cd06422 137 PGHNGVGDFSLDADGRLRRGGGGAVAP----------FTFTGIQILSP-ELFAGIPPGK---FSLNPLWDRAIAA----- 197
|
250 260 270
....*....|....*....|....*....|...
gi 491592802 235 dvfvydfstNRITGEKEEVYWRDVGTIDAYWQA 267
Cdd:cd06422 198 ---------GRLFGLVYDGLWFDVGTPERLLAA 221
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
6-183 |
1.45e-10 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 61.61 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 6 GMILAGGEGSRLRPLTESRSKPSVPFGGSyRLIDFALNNFVNADLMRIYVLTQFKSQSLFHHLKKGWNINGITDRF-IDP 84
Cdd:PRK15480 6 GIILAGGSGTRLYPVTMAVSKQLLPIYDK-PMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYkVQP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 85 IPaqmrtgkrwyEGTADAIYQNLRFmeLAEPDQVCIFGSDHIYKMDIKQMLAFHQEKEASLTVSALRmpLSEASQFGVIE 164
Cdd:PRK15480 85 SP----------DGLAQAFIIGEEF--IGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYH--VNDPERYGVVE 150
|
170
....*....|....*....
gi 491592802 165 VDNEGRMIGFEEKPANPKS 183
Cdd:PRK15480 151 FDQNGTAISLEEKPLQPKS 169
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
7-246 |
2.98e-10 |
|
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: 59.94 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 7 MILAGGEGSRLRPLTESRSKPSVPFGGSyRLIDFALNNFVNADLMRIYVLTQFKSQSLFHHLKKGWNIngitdRFIDpip 86
Cdd:cd02523 2 IILAAGRGSRLRPLTEDRPKCLLEINGK-PLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNI-----KFVY--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 87 aqmrtGKRWYE-GTADAIYQNLRFMElaepDQVCIFGSDHIYKMDIKQMLAfHQEKEASLTVSAlrmPLSEASQFGVIEV 165
Cdd:cd02523 73 -----NPDYAEtNNIYSLYLARDFLD----EDFLLLEGDVVFDPSILERLL-SSPADNAILVDK---KTKEWEDEYVKDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 166 DNEGRMIGFEEKPANPKSIPGdpehalVSMGNYIFEAQTL--FAELIEDADNEASTHDFGKDIIPKMFPRGDVFVYDFST 243
Cdd:cd02523 140 DDAGVLLGIISKAKNLEEIQG------EYVGISKFSPEDAdrLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKDISD 213
|
...
gi 491592802 244 NRI 246
Cdd:cd02523 214 GFW 216
|
|
| G1P_cytidylyltransferase |
cd02524 |
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ... |
7-178 |
1.10e-09 |
|
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: 58.35 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 7 MILAGGEGSRLRPLTESRSKPSVPFGG------------SYRLIDFAL----------NNFVNADLMRIYVLTQFKSQSL 64
Cdd:cd02524 2 VILAGGLGTRLSEETELKPKPMVEIGGrpilwhimkiysHYGHNDFILclgykghvikEYFLNYFLHNSDVTIDLGTNRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 65 FHHLKK--GWNINgitdrFIDPIPAQMrTGKRwyegtadaIYQNLRFMELAEPdqVCIFGSDHIYKMDIKQMLAFHQEKE 142
Cdd:cd02524 82 ELHNSDieDWKVT-----LVDTGLNTM-TGGR--------LKRVRRYLGDDET--FMLTYGDGVSDVNINALIEFHRSHG 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 491592802 143 ASLTVSALRMPlseaSQFGVIEVDNEGRMIGFEEKP 178
Cdd:cd02524 146 KLATVTAVHPP----GRFGELDLDDDGQVTSFTEKP 177
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
6-61 |
9.46e-08 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 52.55 E-value: 9.46e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 491592802 6 GMILAGGEGSRLRPLTESRSKPSVPFGGSyRLIDFALNNFVNADLMRIYVLTQFKS 61
Cdd:COG1213 2 AVILAAGRGSRLGPLTDDIPKCLVEIGGK-TLLERQLEALAAAGIKDIVVVTGYKA 56
|
|
| GDP-M1P_Guanylyltransferase |
cd02509 |
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ... |
8-263 |
4.66e-06 |
|
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.
Pssm-ID: 133003 [Multi-domain] Cd Length: 274 Bit Score: 47.96 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 8 ILAGGEGSRLRPL-TESRSKPSVPFGGSYRLIDFALNNFVNADL-MRIYVLTQFKSQSLFH-HLKKGWNINGItdrFIDP 84
Cdd:cd02509 5 ILAGGSGTRLWPLsRESYPKQFLKLFGDKSLLQQTLDRLKGLVPpDRILVVTNEEYRFLVReQLPEGLPEENI---ILEP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 85 ipaqmrTGKrwyeGTADAIYQNLRFMELAEPDQV-CIFGSDHIykmdIKQMLAFHQE-KEAsltVSALRM---------P 153
Cdd:cd02509 82 ------EGR----NTAPAIALAALYLAKRDPDAVlLVLPSDHL----IEDVEAFLKAvKKA---VEAAEEgylvtfgikP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 154 LSEASQFGVIEVDNEGRMIGFE-----EKPanpksipgDPEHA--LVSMGNY-------IFEAQTLFAEL---------- 209
Cdd:cd02509 145 TRPETGYGYIEAGEKLGGGVYRvkrfvEKP--------DLETAkeYLESGNYlwnsgifLFRAKTFLEELkkhapdiyea 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491592802 210 IEDADNEASTHDFGKDI------IPK-------MFPRGDVFVYDFSTNritgekeevyWRDVGTIDA 263
Cdd:cd02509 217 LEKALAAAGTDDFLRLLeeafakIPSisidyavMEKTKKVAVVPADFG----------WSDLGSWDA 273
|
|
| M1P_guanylylT_A_like_N |
cd06428 |
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ... |
8-239 |
1.59e-05 |
|
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: 46.09 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 8 ILAGGE--GSRLRPLTESRSKPSVPFGGS---YRLIDfALNNFvnADLMRIYVLTQFKSQSLFHHLKKGWNINGITDRFI 82
Cdd:cd06428 3 ILVGGPqkGTRFRPLSLDVPKPLFPVAGKpmiHHHIE-ACAKV--PDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 83 DPiPAQMrtgkrwyeGTADAIYqNLRFMELAE-PDQVCIFGSDHIYKMDIKQMLAFHQEKEASLTVSALRMPLSEASQFG 161
Cdd:cd06428 80 QE-YKPL--------GTAGGLY-HFRDQILAGnPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEASREQASNYG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 162 -VIEVDNEGRMIGFEEKPANPKSipgdpehALVSMGNYIFEAQTLF--AELIEDADNEASTHD------------FGKDI 226
Cdd:cd06428 150 cIVEDPSTGEVLHYVEKPETFVS-------DLINCGVYLFSPEIFDtiKKAFQSRQQEAQLGDdnnregraevirLEQDV 222
|
250
....*....|...
gi 491592802 227 IPKMFPRGDVFVY 239
Cdd:cd06428 223 LTPLAGSGKLYVY 235
|
|
| LbH_eIF2B_gamma_C |
cd04652 |
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
325-376 |
3.57e-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: 41.79 E-value: 3.57e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 491592802 325 IEKSVLGFRSNIASACDISQCILLGDVKVGEGCVLRRVIVDKDADIAPGTQI 376
Cdd:cd04652 14 IKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKL 65
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
8-182 |
6.41e-05 |
|
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: 43.78 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 8 ILAGGEGSRLRPLTESRSKPSVPFGGsYRLIDFALNNFVNADLMRIYVLT-QFKSQSLFHHLKKGWNINGIT-DRFIDPI 85
Cdd:cd02507 5 VLADGFGSRFLPLTSDIPKALLPVAN-VPLIDYTLEWLEKAGVEEVFVVCcEHSQAIIEHLLKSKWSSLSSKmIVDVITS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 86 PAQMRTgkrwyeGTADAIYQNLRFMelaEPDQVCIFGsDHIYKMDIKQMLA--FHQEKEASLTVSAL---RMPLSEASQF 160
Cdd:cd02507 84 DLCESA------GDALRLRDIRGLI---RSDFLLLSC-DLVSNIPLSELLEerRKKDKNAIATLTVLlasPPVSTEQSKK 153
|
170 180
....*....|....*....|....*....
gi 491592802 161 G----VIEVDN---EGRMIGFEEKPANPK 182
Cdd:cd02507 154 TeeedVIAVDSktqRLLLLHYEEDLDEDL 182
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
8-147 |
8.75e-05 |
|
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: 43.42 E-value: 8.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 8 ILAGGEGSRLRPLTESRSKPSVPFGGsYRLIDFALNNFVNADLMRIYVLTQFKSQSLFHHLKKGWNINGITDRFIDPIPA 87
Cdd:cd04198 5 ILAGGGGSRLYPLTDNIPKALLPVAN-KPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFPLNLKQKLDEVTIVL 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491592802 88 QMRTgkrwyeGTADAiyqnLRFMELAEPDQVCIFGSDHIYKMDIKQMLAFHQEKEASLTV 147
Cdd:cd04198 84 DEDM------GTADS----LRHIRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTV 133
|
|
| LbH_G1P_AT_C_like |
cd03356 |
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
321-376 |
1.90e-04 |
|
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: 39.53 E-value: 1.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 491592802 321 RGSRIEKSVLGFRSNIASACDISQCILLGDVKVGEGCVLRRVIVDKDADIAPGTQI 376
Cdd:cd03356 10 ENAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRV 65
|
|
| LbH_eIF2B_epsilon |
cd05787 |
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
313-379 |
5.00e-04 |
|
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.
Pssm-ID: 100061 [Multi-domain] Cd Length: 79 Bit Score: 38.33 E-value: 5.00e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491592802 313 LVCNGSYV-RGSRIEKSVLGFRSNIASACDISQCILLGDVKVGEGCVLRR------VIVDKDADIAPGTQIGVN 379
Cdd:cd05787 1 VIGRGTSIgEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHsivadgAVIGKGCTIPPGSLISFG 74
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
1-69 |
8.42e-03 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 37.06 E-value: 8.42e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491592802 1 MAGVLGMILAGGEGSRLrplteSRSKPSVPFGGSyRLIDFALNNFVNADLMRIYVLTQFKSQSLFHHLK 69
Cdd:COG2068 1 MSKVAAIILAAGASSRM-----GRPKLLLPLGGK-PLLERAVEAALAAGLDPVVVVLGADAEEVAAALA 63
|
|
| |
