|
Name |
Accession |
Description |
Interval |
E-value |
| glgC |
PRK00725 |
glucose-1-phosphate adenylyltransferase; Provisional |
6-418 |
0e+00 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234824 [Multi-domain] Cd Length: 425 Bit Score: 828.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 6 QPIARDAMAYVLAGGRGSRLAELTDRRAKPAVHFGGKARIIDFALSNALNSGIRRIGVATQYKAHSLIRHLQRGWNFFRT 85
Cdd:PRK00725 10 RQLTRDTLALILAGGRGSRLKELTDKRAKPAVYFGGKFRIIDFALSNCINSGIRRIGVLTQYKAHSLIRHIQRGWSFFRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 86 ERNESFDILPASQRVSESQWYEGTADAVFQNIDIIESYAPEYMVILAGDHVYKMDYELMLQQHVDSGADVTIGCMEVPVK 165
Cdd:PRK00725 90 ELGEFVDLLPAQQRVDEENWYRGTADAVYQNLDIIRRYDPKYVVILAGDHIYKMDYSRMLADHVESGADCTVACLEVPRE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 166 EASGFGVMHVDEQDVVTAFVEKPKKPPHIPGSPGMALASMGIYVFRTALLIEELRRDADDPDSKRDFGGDIIPHIVKHGK 245
Cdd:PRK00725 170 EASAFGVMAVDENDRITAFVEKPANPPAMPGDPDKSLASMGIYVFNADYLYELLEEDAEDPNSSHDFGKDIIPKIVEEGK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 246 AVAHRFSSSCVRAESEPVPYWRDVGTIDAYWQANIDLTDVVPSLDLYDRSWPLWTYSEVTPPAKFVHNEEGRRGSATSSL 325
Cdd:PRK00725 250 VYAHPFSDSCVRSDPEEEPYWRDVGTLDAYWQANLDLASVTPELDLYDRNWPIWTYQEQLPPAKFVFDRSGRRGMAINSL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 326 IAGGCIVSGSSLHRSLLFTGVRTHSFSSVTESVIMPDCVIGRGARLHKCVLDSGVIVPPGLIVGEHPEHDAQRFRRTEGG 405
Cdd:PRK00725 330 VSGGCIISGAVVRRSVLFSRVRVNSFSNVEDSVLLPDVNVGRSCRLRRCVIDRGCVIPEGMVIGEDPEEDAKRFRRSEEG 409
|
410
....*....|...
gi 494962724 406 VTLITQYMIERLA 418
Cdd:PRK00725 410 IVLVTREMLDKLG 422
|
|
| GlgC |
COG0448 |
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
11-414 |
0e+00 |
|
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];
Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 600.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 11 DAMAYVLAGGRGSRLAELTDRRAKPAVHFGGKARIIDFALSNALNSGIRRIGVATQYKAHSLIRHLQRG--WNFFRteRN 88
Cdd:COG0448 1 KVLAIILAGGRGSRLGPLTKDRAKPAVPFGGKYRIIDFPLSNCVNSGIRRVGVLTQYKSHSLNDHIGSGkpWDLDR--KR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 89 ESFDILPASQRVSESQWYEGTADAVFQNIDIIESYAPEYMVILAGDHVYKMDYELMLQQHVDSGADVTIGCMEVPVKEAS 168
Cdd:COG0448 79 GGVFILPPYQQREGEDWYQGTADAVYQNLDFIERSDPDYVLILSGDHIYKMDYRQMLDFHIESGADITVACIEVPREEAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 169 GFGVMHVDEQDVVTAFVEKPKKpphipgsPGMALASMGIYVFRTALLIEELRRDAddPDSKRDFGGDIIPHIVKHGKAVA 248
Cdd:COG0448 159 RFGVMEVDEDGRITEFEEKPKD-------PKSALASMGIYVFNKDVLIELLEEDA--PNSSHDFGKDIIPRLLDRGKVYA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 249 HRFSsscvraesepvPYWRDVGTIDAYWQANIDLTDVVPSLDLYDRSWPLWTYSEVTPPAKFVhneegRRGSATSSLIAG 328
Cdd:COG0448 230 YEFD-----------GYWRDVGTIDSYYEANMDLLDPEPEFNLYDPEWPIYTKQKDLPPAKFV-----RGGKVKNSLVSN 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 329 GCIVSGsSLHRSLLFTGVRTHSFSSVTESVIMPDCVIGRGARLHKCVLDSGVIVPPGLIVGEHPEHDAQRFRRTeGGVTL 408
Cdd:COG0448 294 GCIISG-TVENSVLFRGVRVESGAVVENSVIMPGVVIGEGAVIENAIIDKNVVIPPGVVIGEDPEEDRKRFTVS-SGIVV 371
|
....*.
gi 494962724 409 ITQYMI 414
Cdd:COG0448 372 VGKGAV 377
|
|
| glgC |
TIGR02091 |
glucose-1-phosphate adenylyltransferase; This enzyme, glucose-1-phosphate adenylyltransferase, ... |
14-390 |
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: 573.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 14 AYVLAGGRGSRLAELTDRRAKPAVHFGGKARIIDFALSNALNSGIRRIGVATQYKAHSLIRHLQRGWNFFRTeRNESFDI 93
Cdd:TIGR02091 1 AMVLAGGRGSRLSPLTKRRAKPAVPFGGKYRIIDFPLSNCINSGIRRIGVLTQYKSHSLNRHIQRGWDFDGF-IDGFVTL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 94 LPASQRVSESQWYEGTADAVFQNIDIIESYAPEYMVILAGDHVYKMDYELMLQQHVDSGADVTIGCMEVPVKEASGFGVM 173
Cdd:TIGR02091 80 LPAQQRESGTDWYQGTADAVYQNLDLIEDYDPEYVLILSGDHIYKMDYEKMLDYHIESGADVTIACIPVPRKEASRFGVM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 174 HVDEQDVVTAFVEKPKKPPHIPGSPGMALASMGIYVFRTALLIEELRRDADDPDSKRDFGGDIIPHIVKHGKAVAHRFSs 253
Cdd:TIGR02091 160 QVDEDGRIVDFEEKPANPPSIPGMPDFALASMGIYIFDKDVLKELLEEDADDPESSHDFGKDIIPRALEEGSVQAYLFS- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 254 scvraesepvPYWRDVGTIDAYWQANIDLTDVVPSLDLYDRSWPLWTYSEVTPPAKFVHNEEgrrgSATSSLIAGGCIVS 333
Cdd:TIGR02091 239 ----------GYWRDVGTIDSFWEANMDLVSVVPPFDLYDRKWPIYTYNEFLPPAKFVDSDA----QVVDSLVSEGCIIS 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 494962724 334 GSSLHRSLLFTGVRTHSFSSVTESVIMPDCVIGRGARLHKCVLDSGVIVPPGLIVGE 390
Cdd:TIGR02091 305 GATVSHSVLGIRVRIGSGSTVEDSVIMGDVGIGRGAVIRNAIIDKNVRIGEGVVIGN 361
|
|
| glgC |
PRK00844 |
glucose-1-phosphate adenylyltransferase; Provisional |
14-409 |
0e+00 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 538.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 14 AYVLAGGRGSRLAELTDRRAKPAVHFGGKARIIDFALSNALNSGIRRIGVATQYKAHSLIRHLQRGWNFFrTERNESFDI 93
Cdd:PRK00844 8 AIVLAGGEGKRLMPLTADRAKPAVPFGGSYRLIDFVLSNLVNSGYLRIYVLTQYKSHSLDRHISQTWRLS-GLLGNYITP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 94 LPASQRVSESqWYEGTADAVFQNIDIIESYAPEYMVILAGDHVYKMDYELMLQQHVDSGADVTIGCMEVPVKEASGFGVM 173
Cdd:PRK00844 87 VPAQQRLGKR-WYLGSADAIYQSLNLIEDEDPDYVVVFGADHVYRMDPRQMVDFHIESGAGVTVAAIRVPREEASAFGVI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 174 HVDEQDVVTAFVEKPKKPPHIPGSPGMALASMGIYVFRTALLIEELRRDADDPDSKRDFGGDIIPHIVKHGKAVAHRFSS 253
Cdd:PRK00844 166 EVDPDGRIRGFLEKPADPPGLPDDPDEALASMGNYVFTTDALVDALRRDAADEDSSHDMGGDIIPRLVERGRAYVYDFST 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 254 SCVR-AESEPVPYWRDVGTIDAYWQANIDLTDVVPSLDLYDRSWPLWTYSEVTPPAKFVHNEEGrRGSATSSLIAGGCIV 332
Cdd:PRK00844 246 NEVPgATERDRGYWRDVGTIDAYYDAHMDLLSVHPVFNLYNREWPIYTSSPNLPPAKFVDGGGR-VGSAQDSLVSAGSII 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494962724 333 SGSSLHRSLLFTGVRTHSFSSVTESVIMPDCVIGRGARLHKCVLDSGVIVPPGLIVGEHPEHDAQRFRRTEGGVTLI 409
Cdd:PRK00844 325 SGATVRNSVLSPNVVVESGAEVEDSVLMDGVRIGRGAVVRRAILDKNVVVPPGATIGVDLEEDRRRFTVSEGGIVVV 401
|
|
| glgC |
PRK05293 |
glucose-1-phosphate adenylyltransferase; Provisional |
14-411 |
4.13e-151 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 433.14 E-value: 4.13e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 14 AYVLAGGRGSRLAELTDRRAKPAVHFGGKARIIDFALSNALNSGIRRIGVATQYKAHSLIRHLQRG--WNFFRteRNESF 91
Cdd:PRK05293 6 AMILAGGQGTRLGKLTKNIAKPAVPFGGKYRIIDFTLSNCANSGIDTVGVLTQYQPLELNNHIGIGspWDLDR--INGGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 92 DILPASQRVSESQWYEGTADAVFQNIDIIESYAPEYMVILAGDHVYKMDYELMLQQHVDSGADVTIGCMEVPVKEASGFG 171
Cdd:PRK05293 84 TILPPYSESEGGKWYKGTAHAIYQNIDYIDQYDPEYVLILSGDHIYKMDYDKMLDYHKEKEADVTIAVIEVPWEEASRFG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 172 VMHVDEQDVVTAFVEKPKKPPHipgspgmALASMGIYVFRTALLIEELRRDADDPDSKRDFGGDIIPHIVKHGKAV-AHR 250
Cdd:PRK05293 164 IMNTDENMRIVEFEEKPKNPKS-------NLASMGIYIFNWKRLKEYLIEDEKNPNSSHDFGKNVIPLYLEEGEKLyAYP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 251 FSSscvraesepvpYWRDVGTIDAYWQANIDLTDVVPSLDLYDRSWPLWTYSEVTPPAkFVhneeGRRGSATSSLIAGGC 330
Cdd:PRK05293 237 FKG-----------YWKDVGTIESLWEANMELLRPENPLNLFDRNWRIYSVNPNLPPQ-YI----AENAKVKNSLVVEGC 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 331 IVSGSSLHrSLLFTGVRTHSFSSVTESVIMPDCVIGRGARLHKCVLDSGVIVPPGLIVGEhpehdaqrfrrTEGGVTLIT 410
Cdd:PRK05293 301 VVYGTVEH-SVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVIIGG-----------GKEVITVIG 368
|
.
gi 494962724 411 Q 411
Cdd:PRK05293 369 E 369
|
|
| glgC |
PRK02862 |
glucose-1-phosphate adenylyltransferase; Provisional |
14-365 |
5.61e-105 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179486 [Multi-domain] Cd Length: 429 Bit Score: 317.21 E-value: 5.61e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 14 AYVLAGGRGSRLAELTDRRAKPAVHFGGKARIIDFALSNALNSGIRRIGVATQYKAHSLIRHLQRGWNF--FrterNESF 91
Cdd:PRK02862 6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKYRLIDIPISNCINSGINKIYVLTQFNSASLNRHISQTYNFdgF----SGGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 92 -DILPASQRVSESQWYEGTADAVFQNIDIIESYAPEYMVILAGDHVYKMDYELMLQQHVDSGADVTIGCMEVPVKEASGF 170
Cdd:PRK02862 82 vEVLAAQQTPENPSWFQGTADAVRKYLWHFQEWDVDEYLILSGDQLYRMDYRLFVQHHRETGADITLAVLPVDEKDASGF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 171 GVMHVDEQDVVTAFVEKPKK--------PPHIPGSPGMA------LASMGIYVFRTALLIEELRrdaDDPDSKrDFGGDI 236
Cdd:PRK02862 162 GLMKTDDDGRITEFSEKPKGdelkamavDTSRLGLSPEEakgkpyLASMGIYVFSRDVLFDLLN---KNPEYT-DFGKEI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 237 IPHIVKHGKAVAHRFSSscvraesepvpYWRDVGTIDAYWQANIDLT-DVVPSLDLYDRSWPLWTYSEVTPPAKFVHnee 315
Cdd:PRK02862 238 IPEAIRDYKVQSYLFDG-----------YWEDIGTIEAFYEANLALTqQPNPPFSFYDEKAPIYTRARYLPPSKLLD--- 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 494962724 316 grrGSATSSLIAGGCIVSGSSLHRSLLftGVRthsfssvteSVIMPDCVI 365
Cdd:PRK02862 304 ---ATITESIIAEGCIIKNCSIHHSVL--GIR---------SRIESGCTI 339
|
|
| PLN02241 |
PLN02241 |
glucose-1-phosphate adenylyltransferase |
9-378 |
2.94e-101 |
|
glucose-1-phosphate adenylyltransferase
Pssm-ID: 215133 [Multi-domain] Cd Length: 436 Bit Score: 307.94 E-value: 2.94e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 9 ARDAMAYVLAGGRGSRLAELTDRRAKPAVHFGGKARIIDFALSNALNSGIRRIGVATQYKAHSLIRHLQRGWNF-----F 83
Cdd:PLN02241 1 PKSVAAIILGGGAGTRLFPLTKRRAKPAVPIGGNYRLIDIPMSNCINSGINKIYVLTQFNSASLNRHLSRAYNFgnggnF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 84 rterNESF-DILPASQRVSESQWYEGTADAVFQNIDIIESY---APEYMVILAGDHVYKMDYELMLQQHVDSGADVTIGC 159
Cdd:PLN02241 81 ----GDGFvEVLAATQTPGEKGWFQGTADAVRQFLWLFEDAknkNVEEVLILSGDHLYRMDYMDFVQKHRESGADITIAC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 160 MEVPVKEASGFGVMHVDEQDVVTAFVEKPKK----------------PPHIPGSPgmALASMGIYVFRTALLIEELRRDA 223
Cdd:PLN02241 157 LPVDESRASDFGLMKIDDTGRIIEFSEKPKGdelkamqvdttvlglsPEEAKEKP--YIASMGIYVFKKDVLLKLLRWRF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 224 ddPDSKrDFGGDIIPHIVKHGKAV-AHRFSSscvraesepvpYWRDVGTIDAYWQANIDLTDVVPSLDLYDRSWPLWTYS 302
Cdd:PLN02241 235 --PTAN-DFGSEIIPGAIKEGYNVqAYLFDG-----------YWEDIGTIKSFYEANLALTKQPPKFSFYDPDAPIYTSP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 303 EVTPPAKFVHneegrrGSATSSLIAGGCIVSGSSLHRSLLftGVRTHSFSSVT--ESVIM----------------PDCV 364
Cdd:PLN02241 301 RFLPPSKIED------CRITDSIISHGCFLRECKIEHSVV--GLRSRIGEGVEieDTVMMgadyyeteeeiasllaEGKV 372
|
410
....*....|....*..
gi 494962724 365 ---IGRGARLHKCVLDS 378
Cdd:PLN02241 373 pigIGENTKIRNAIIDK 389
|
|
| ADP_Glucose_PP |
cd02508 |
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ... |
14-269 |
5.10e-95 |
|
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: 283.28 E-value: 5.10e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 14 AYVLAGGRGSRLAELTDRRAKPAVHFGGKARIIDFALSNALNSGIRRIGVATQYKAHSLIRHLQRGWNFFRTERNESFDI 93
Cdd:cd02508 1 AIILAGGEGTRLSPLTKKRAKPAVPFGGRYRLIDFPLSNMVNSGIRNVGVLTQYKSRSLNDHLGSGKEWDLDRKNGGLFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 94 LPASQRVSESqWYEGTADAVFQNIDIIESYAPEYMVILAGDHVYKMDYELMLQQHVDSGADVTIGCMevpvkeasgfgvm 173
Cdd:cd02508 81 LPPQQRKGGD-WYRGTADAIYQNLDYIERSDPEYVLILSGDHIYNMDYREMLDFHIESGADITVVYK------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 174 hvdeqdvvtafvekpkkpphipgspgmalASMGIYVFRTALLIEELRRDADdpDSKRDFGGDIIPHIVKHGKAVAHRFSs 253
Cdd:cd02508 147 -----------------------------ASMGIYIFSKDLLIELLEEDAA--DGSHDFGKDIIPAMLKKLKIYAYEFN- 194
|
250
....*....|....*.
gi 494962724 254 scvraesepvPYWRDV 269
Cdd:cd02508 195 ----------GYWADI 200
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
16-283 |
7.94e-74 |
|
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: 230.99 E-value: 7.94e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 16 VLAGGRGSRLAELTDRRAKPAVHFGGKARIIDFALSNALNSGIRR-IGVATQYKAHSLIRHLQRGWNFfrterneSFDIL 94
Cdd:pfam00483 4 ILAGGSGTRLWPLTRTLAKPLVPVGGKYPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKF-------GVQIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 95 PASQRVSEsqwyeGTADAVFQNIDIIESYAPEyMVILAGDHVYKMDYELMLQQHVDSGADVTIGCMEVPVKEASGFGVMH 174
Cdd:pfam00483 77 YALQPEGK-----GTAPAVALAADFLGDEKSD-VLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGIVPVEPPTGYGVVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 175 VDEQDVVTAFVEKPKKPPHIpgspgmALASMGIYVFRTALLiEELRRDADDPDSKRDFGGDIIPHIVKHGK-AVAHRFSS 253
Cdd:pfam00483 151 FDDNGRVIRFVEKPKLPKAS------NYASMGIYIFNSGVL-DFLAKYLEELKRGEDEITDILPKALEDGKlAYAFIFKG 223
|
250 260 270
....*....|....*....|....*....|
gi 494962724 254 SCvraesepvpyWRDVGTIDAYWQANIDLT 283
Cdd:pfam00483 224 YA----------WLDVGTWDSLWEANLFLL 243
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
16-270 |
5.13e-43 |
|
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: 150.04 E-value: 5.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 16 VLAGGRGSRLAELTDRRAKPAVHFGGKArIIDFALSNALNSGIRRIGVATQYKAHSLIRHLQRGWNFFrternesFDILP 95
Cdd:cd04181 3 ILAAGKGTRLRPLTDTRPKPLLPIAGKP-ILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFG-------VNIEY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 96 ASQrvsESQWyeGTADAVFQNIDIIESyapEYMVILAGDHVYKMDYELMLQQHVDSGADVTIGCmeVPVKEASGFGVMHV 175
Cdd:cd04181 75 VVQ---EEPL--GTAGAVRNAEDFLGD---DDFLVVNGDVLTDLDLSELLRFHREKGADATIAV--KEVEDPSRYGVVEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 176 DEQDVVTAFVEKPKKPPHipgspgmALASMGIYVFRTALLiEELRRdadDPDSKRDFGGDIIPHIVKHGKAVAHRFSSsc 255
Cdd:cd04181 145 DDDGRVTRFVEKPTLPES-------NLANAGIYIFEPEIL-DYIPE---ILPRGEDELTDAIPLLIEEGKVYGYPVDG-- 211
|
250
....*....|....*
gi 494962724 256 vraesepvpYWRDVG 270
Cdd:cd04181 212 ---------YWLDIG 217
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
16-282 |
3.30e-41 |
|
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: 146.07 E-value: 3.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 16 VLAGGRGSRLAELTDRRAKPAVHFGGKArIIDFALSNALNSGIRRIGVATQYKAHSLIRHLQRGWNF-----FRTERnes 90
Cdd:COG1208 4 ILAGGLGTRLRPLTDTRPKPLLPVGGKP-LLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFgvritYVDEG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 91 fDILpasqrvsesqwyeGTADAVFQNIDIIESyapEYMVILAGDHVYKMDYELMLQQHVDSGADVTIGCmeVPVKEASGF 170
Cdd:COG1208 80 -EPL-------------GTGGALKRALPLLGD---EPFLVLNGDILTDLDLAALLAFHREKGADATLAL--VPVPDPSRY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 171 GVMHVDEQDVVTAFVEKPKKPPHipgspgmALASMGIYVFRTALLieelrrDADDPDSKRDFgGDIIPHIVKHGKAVAHR 250
Cdd:COG1208 141 GVVELDGDGRVTRFVEKPEEPPS-------NLINAGIYVLEPEIF------DYIPEGEPFDL-EDLLPRLIAEGRVYGYV 206
|
250 260 270
....*....|....*....|....*....|..
gi 494962724 251 FSSscvraesepvpYWRDVGTIDAYWQANIDL 282
Cdd:COG1208 207 HDG-----------YWLDIGTPEDLLEANALL 227
|
|
| glgD |
TIGR02092 |
glucose-1-phosphate adenylyltransferase, GlgD subunit; This family is GlgD, an apparent ... |
25-392 |
6.64e-41 |
|
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: 149.07 E-value: 6.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 25 LAELTDRRAKPAVHFGGKARIIDFALSNALNSGIRRIGVATQYKA-HSLIRHLQRG--WNFFRteRNESFDILPASQRVs 101
Cdd:TIGR02092 16 LSPLTKVRPLASLPFGGRYRLIDFPLSNMVNAGIRNVFIFFKNKErQSLFDHLGSGreWDLHR--KRDGLFVFPYNDRD- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 102 esQWYEGTADAVFQNIDIIESYAPEYMVILAGDHVYKMDYELMLQQHVDSGADVTIGCMEVPVKEASGF-GVMHVDEQDV 180
Cdd:TIGR02092 93 --DLSEGGKRYFSQNLEFLKRSTSEYTVVLNSHMVCNIDLKAVLKYHEETGKDITVVYKKVKPADASEYdTILRFDESGK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 181 VTAFV--EKPKKPPHIpgspgmalaSMGIYVFRTALLIEELRRDAD--DPDSKRdfggDIIPHIVKHGKAVAHRFSSscv 256
Cdd:TIGR02092 171 VKSIGqnLNPEEEENI---------SLDIYIVSTDLLIELLYECIQrgKLTSLE----ELIRENLKELNINAYEYTG--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 257 raesepvpYWRDVGTIDAYWQANIDLTD--VVPSLdLYDRSWPLWTYSEVTPPAKFVHNEEgrrgsATSSLIAGGCIVSG 334
Cdd:TIGR02092 235 --------YLANINSVKSYYKANMDLLDpqNFQSL-FYSSQGPIYTKVKDEPPTYYAENSK-----VENSLVANGCIIEG 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494962724 335 sSLHRSLLFTGVRTHSFSSVTESVIMPDCVIGRGARLHKCVLDSGVIVPPGL-IVG--EHP 392
Cdd:TIGR02092 301 -KVENSILSRGVHVGKDALIKNCIIMQRTVIGEGAHLENVIIDKDVVIEPNVkIAGtsEQP 360
|
|
| LbH_G1P_AT_C |
cd04651 |
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ... |
312-414 |
4.88e-39 |
|
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: 135.67 E-value: 4.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 312 HNEEGRRGSATSSLIAGGCIVSGSSLHRSLLFTGVRTHSFSSVTESVIMPDCVIGRGARLHKCVLDSGVIVPPGLIVGEH 391
Cdd:cd04651 1 PPYIGRRGEVKNSLVSEGCIISGGTVENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIPDGVVIGGD 80
|
90 100
....*....|....*....|...
gi 494962724 392 PEHDAQRFRRTEGGVTLITQYMI 414
Cdd:cd04651 81 PEEDRARFYVTEDGIVVVGKGMV 103
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
16-279 |
8.14e-20 |
|
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: 87.57 E-value: 8.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 16 VLAGGRGSRLAELTDRRAKPAVHFGGKArIIDFALSNALNSGIRRIGVATQYKAHSLIRHLQRGWNFfrterneSFDIlp 95
Cdd:cd06426 3 IMAGGKGTRLRPLTENTPKPMLKVGGKP-ILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKF-------GVNI-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 96 asQRVSESQwYEGTADAVfqnidiieSYAPE----YMVILAGDHVYKMDYELMLQQHVDSGADVTIGC----MEVPvkea 167
Cdd:cd06426 73 --SYVREDK-PLGTAGAL--------SLLPEkptdPFLVMNGDILTNLNYEHLLDFHKENNADATVCVreyeVQVP---- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 168 sgFGVMHVDeQDVVTAFVEKPKKPphipgspgmALASMGIYVFRTALLiEELrrdadDPDSKRDFgGDIIPHIVKHGKAV 247
Cdd:cd06426 138 --YGVVETE-GGRITSIEEKPTHS---------FLVNAGIYVLEPEVL-DLI-----PKNEFFDM-PDLIEKLIKEGKKV 198
|
250 260 270
....*....|....*....|....*....|...
gi 494962724 248 AhrfssscvraeSEPV-PYWRDVGTIDAYWQAN 279
Cdd:cd06426 199 G-----------VFPIhEYWLDIGRPEDYEKAN 220
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
14-279 |
1.13e-19 |
|
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: 87.24 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 14 AYVLAGGRGSRLAELTDRRAKPAVHFGGKArIIDFALSNALNSGIRRIGVATQYKAHSLIRHLQRGWNFfrterNESFDI 93
Cdd:cd04189 3 GLILAGGKGTRLRPLTYTRPKQLIPVAGKP-IIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRF-----GVRITY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 94 LPASQRVsesqwyeGTADAVFQNIDIIESyaPEYMVILaGDHVYKMDYELMLQQHVDSGADVTIGCmeVPVKEASGFGVM 173
Cdd:cd04189 77 ILQEEPL-------GLAHAVLAARDFLGD--EPFVVYL-GDNLIQEGISPLVRDFLEEDADASILL--AEVEDPRRFGVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 174 HVDEQDVVtAFVEKPKKPPHipgspgmALASMGIYVFRTALL--IEELRrdaddPdSKRdfgG-----DIIPHIVKHGKA 246
Cdd:cd04189 145 VVDDGRIV-RLVEKPKEPPS-------NLALVGVYAFTPAIFdaISRLK-----P-SWR---GeleitDAIQWLIDRGRR 207
|
250 260 270
....*....|....*....|....*....|...
gi 494962724 247 VAHRFSSScvraesepvpYWRDVGTIDAYWQAN 279
Cdd:cd04189 208 VGYSIVTG----------WWKDTGTPEDLLEAN 230
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
14-278 |
6.10e-16 |
|
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: 76.44 E-value: 6.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 14 AYVLAGGRGSRLAELTDRRAKPAVHFGGKaRIIDFALSNALNSGIRRIGVATQYKAHSLIRHLQRGWNFfrternesfdi 93
Cdd:cd06915 1 AVILAGGLGTRLRSVVKDLPKPLAPVAGR-PFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRG----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 94 lPASQRVSESQWYEGTADAVFQNIDIIEsyAPEYMViLAGDHVYKMDYELMLQQHVDSGADVTIGCmeVPVKEASGFGVM 173
Cdd:cd06915 69 -GIRIYYVIEPEPLGTGGAIKNALPKLP--EDQFLV-LNGDTYFDVDLLALLAALRASGADATMAL--RRVPDASRYGNV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 174 HVDEQDVVTAFVEKPKKpphipgsPGMALASMGIYVFRTALLieelrrdADDPDSKRDFGGDIIPHIVKHGKAVAHrfss 253
Cdd:cd06915 143 TVDGDGRVIAFVEKGPG-------AAPGLINGGVYLLRKEIL-------AEIPADAFSLEADVLPALVKRGRLYGF---- 204
|
250 260
....*....|....*....|....*
gi 494962724 254 sCVRAesepvpYWRDVGTIDAYWQA 278
Cdd:cd06915 205 -EVDG------YFIDIGIPEDYARA 222
|
|
| rmlA_long |
TIGR01208 |
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ... |
14-385 |
2.14e-15 |
|
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced. Alternate name: dTDP-D-glucose synthase
Pssm-ID: 273500 [Multi-domain] Cd Length: 353 Bit Score: 77.06 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 14 AYVLAGGRGSRLAELTDRRAKPAVHFGGKArIIDFALSNALNSGIRRIGVATQYKAHSLIRHLqrgwnffrTERNESFDI 93
Cdd:TIGR01208 2 ALILAAGKGTRLRPLTFTRPKQLIPVANKP-ILQYAIEDLAEAGITDIGIVVGPVTGEEIKEI--------VGEGERFGA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 94 lpasqRVSESQWYE--GTADAVFQNIDIIESyaPEYMVILaGDHVYKMDYELMLQQHVDSGADVTIgcMEVPVKEASGFG 171
Cdd:TIGR01208 73 -----KITYIVQGEplGLAHAVYTARDFLGD--DDFVVYL-GDNLIQDGISRFVKSFEEKDYDALI--LLTKVRDPTAFG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 172 VMHVDEQDVVTAFVEKPKKPPHipgspgmALASMGIYVFRTalLIEELRRDAddPDSKRdfgG-----DIIPHIVKHGKA 246
Cdd:TIGR01208 143 VAVLEDGKRILKLVEKPKEPPS-------NLAVVGLYMFRP--LIFEAIKNI--KPSWR---GeleitDAIQWLIEKGYK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 247 VahrfSSSCVRAesepvpYWRDVGTIDAYWQAN-IDLTDVVPSLDLYDRSWPLWTYSEVTPPAKFVhnEEGRRGSAtssL 325
Cdd:TIGR01208 209 V----GGSKVTG------WWKDTGKPEDLLDANrLILDEVEREVQGVDDESKIRGRVVVGEGAKIV--NSVIRGPA---V 273
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494962724 326 IAGGCIVSGSSL-HRSLLFTGVRTHSfSSVTESVIMPDCVI-GRGARLHKCVLDSGVIVPPG 385
Cdd:TIGR01208 274 IGEDCIIENSYIgPYTSIGEGVVIRD-AEVEHSIVLDESVIeGVQARIVDSVIGKKVRIKGN 334
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
12-278 |
1.29e-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: 69.52 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 12 AMayVLAGGRGSRLAELTDRRAKPAVHFGGKArIIDFALSNALNSGIRRIGVATQYKAHSLIRHLQRGWNFFRTE-RNES 90
Cdd:cd06422 2 AM--ILAAGLGTRMRPLTDTRPKPLVPVAGKP-LIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDSRFGLRITiSDEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 91 FDILpasqrvsesqwyeGTADAVFQNIDIIesyAPEYMVILAGDHVYKMDYELMLQQHVD--SGADVTIgcMEVPVKEAS 168
Cdd:cd06422 79 DELL-------------ETGGGIKKALPLL---GDEPFLVVNGDILWDGDLAPLLLLHAWrmDALLLLL--PLVRNPGHN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 169 GFGVMHVDEQDVVTAFVEKPKKPphipgspgmaLASMGIYVFRTALLieelrrdADDPDSKrdfgGDIIPH---IVKHGK 245
Cdd:cd06422 141 GVGDFSLDADGRLRRGGGGAVAP----------FTFTGIQILSPELF-------AGIPPGK----FSLNPLwdrAIAAGR 199
|
250 260 270
....*....|....*....|....*....|...
gi 494962724 246 AVAHRFSSscvraesepvpYWRDVGTIDAYWQA 278
Cdd:cd06422 200 LFGLVYDG-----------LWFDVGTPERLLAA 221
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
16-279 |
1.20e-12 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 67.19 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 16 VLAGGRGSRLAELTDRRAKPAVHFGGKArIIDFALSNALNSGIRRIGVATQYKAHSLIRHLQRGWNFFRTERNESFDilp 95
Cdd:COG1213 4 ILAAGRGSRLGPLTDDIPKCLVEIGGKT-LLERQLEALAAAGIKDIVVVTGYKAELIEEALARPGPDVTFVYNPDYD--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 96 asqrvsesqwyegtadavfqNIDIIES--YAPEYM----VILAGDHVYKmdyELMLQQHVDSGADVTIGC---MEVPVKE 166
Cdd:COG1213 80 --------------------ETNNIYSlwLAREALdedfLLLNGDVVFD---PAILKRLLASDGDIVLLVdrkWEKPLDE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 167 AsgfgvMHV--DEQDVVTAFVekpKKPPhipgsPGMALA-SMGIYVFR---TALLIEELRRDADDPDSKRDFgGDIIPHI 240
Cdd:COG1213 137 E-----VKVrvDEDGRIVEIG---KKLP-----PEEADGeYIGIFKFSaegAAALREALEALIDEGGPNLYY-EDALQEL 202
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 494962724 241 VKHGKAV-AHRFSSScvraesepvpYWRDVGTIDAYWQAN 279
Cdd:COG1213 203 IDEGGPVkAVDIGGL----------PWVEIDTPEDLERAE 232
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
16-279 |
1.28e-12 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 67.81 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 16 VLAGGRGSRLAELTDRRAKPAVHFGGKArIIDFALSNALNSGIRRIG-VATQYKAHSLIRHLQRGwnffrternESFDIl 94
Cdd:COG1209 5 ILAGGSGTRLRPLTLTVSKQLLPVYDKP-MIYYPLSTLMLAGIREILiISTPEDGPQFERLLGDG---------SQLGI- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 95 PASQRVSESQwyEGTADAVfqnidIIesyAPEY------MVILaGDHVYKMD-YELMLQQHVDSGADVTIGCmeVPVKEA 167
Cdd:COG1209 74 KISYAVQPEP--LGLAHAF-----II---AEDFiggdpvALVL-GDNIFYGDgLSELLREAAARESGATIFG--YKVEDP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 168 SGFGVMHVDEQDVVTAFVEKPKKPPhipgSPgmaLASMGIYVFrTALLIEELRRdaDDPdSKRdfgG-----DIIPHIVK 242
Cdd:COG1209 141 ERYGVVEFDEDGRVVSLEEKPKEPK----SN---LAVTGLYFY-DNDVVEIAKN--LKP-SAR---GeleitDANQAYLE 206
|
250 260 270
....*....|....*....|....*....|....*..
gi 494962724 243 HGKAVAHRFSSSCvraesepvpYWRDVGTIDAYWQAN 279
Cdd:COG1209 207 RGKLVVELLGRGF---------AWLDTGTHESLLEAN 234
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
14-275 |
1.26e-11 |
|
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: 64.15 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 14 AYVLAGGRGSRLAELTDRRAKPAVHFGGKArIIDFALSNALNSGIRRIGVATQYKAHSLIRHLQrgwnffrtERNESFDI 93
Cdd:cd06425 3 ALILVGGYGTRLRPLTLTVPKPLVEFCNKP-MIEHQIEALAKAGVKEIILAVNYRPEDMVPFLK--------EYEKKLGI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 94 lpasqRVSESQWYE--GTADAVFQNIDIIESYAPEYMViLAGDHVYKMDYELMLQQHVDSGADVTIgcMEVPVKEASGFG 171
Cdd:cd06425 74 -----KITFSIETEplGTAGPLALARDLLGDDDEPFFV-LNSDVICDFPLAELLDFHKKHGAEGTI--LVTKVEDPSKYG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 172 VMHVDEQD-VVTAFVEKPKKPPHipgspgmALASMGIYVFRTALlieeLRRDADDPDSkrdFGGDIIPHIVKHGKAVAHR 250
Cdd:cd06425 146 VVVHDENTgRIERFVEKPKVFVG-------NKINAGIYILNPSV----LDRIPLRPTS---IEKEIFPKMASEGQLYAYE 211
|
250 260
....*....|....*....|....*
gi 494962724 251 FSSscvraesepvpYWRDVGTIDAY 275
Cdd:cd06425 212 LPG-----------FWMDIGQPKDF 225
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
14-225 |
1.23e-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: 61.09 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 14 AYVLAGGRGSRLAELTDRRAKPAVHFGGKaRIIDFALSNALNSGIRRIGVATQYKAHSLIRHLQRGWNfFRTERNESFDI 93
Cdd:cd02523 1 AIILAAGRGSRLRPLTEDRPKCLLEINGK-PLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPN-IKFVYNPDYAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 94 lpasqrvsesqwyEGTADAVFQNIDIIEsyapEYMVILAGDHVYkmdYELMLQQHVDSGADVTIGCMEvPVKEASGFGVM 173
Cdd:cd02523 79 -------------TNNIYSLYLARDFLD----EDFLLLEGDVVF---DPSILERLLSSPADNAILVDK-KTKEWEDEYVK 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494962724 174 HVDEQDVVTAFVEKPKKPPHIPGspgmalASMGIYVFRTALL------IEELRRDADD 225
Cdd:cd02523 138 DLDDAGVLLGIISKAKNLEEIQG------EYVGISKFSPEDAdrlaeaLEELIEAGRV 189
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
45-282 |
5.95e-09 |
|
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose Pyrophosphorylase (UGPase) catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans. UGPase is found in both prokaryotes and eukaryotes, although prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity.
Pssm-ID: 133021 [Multi-domain] Cd Length: 267 Bit Score: 56.77 E-value: 5.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 45 IIDFALSNALNSGIRRIGVATQYKAHSLIRHLQRgwNFF---------RTERNESFDILPASQRVSESQWYE--GTADAV 113
Cdd:cd02541 33 VIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDR--SYEleetlekkgKTDLLEEVRIISDLANIHYVRQKEplGLGHAV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 114 FQNIDII--ESYApeymVILAGDHVYKMDYEL--MLQQHVDSGADVtIGCMEVPVKEASGFGVMHVDEQD----VVTAFV 185
Cdd:cd02541 111 LCAKPFIgdEPFA----VLLGDDLIDSKEPCLkqLIEAYEKTGASV-IAVEEVPPEDVSKYGIVKGEKIDgdvfKVKGLV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 186 EKPKkpphiPGSPGMALASMGIYVFrTALLIEELRRdaddpdSKRDFGGDI-----IPHIVKHGKAVAHRFSSScvraes 260
Cdd:cd02541 186 EKPK-----PEEAPSNLAIVGRYVL-TPDIFDILEN------TKPGKGGEIqltdaIAKLLEEEPVYAYVFEGK------ 247
|
250 260
....*....|....*....|..
gi 494962724 261 epvpyWRDVGTIDAYWQANIDL 282
Cdd:cd02541 248 -----RYDCGNKLGYLKATVEF 264
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
16-248 |
6.96e-07 |
|
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.
Pssm-ID: 133020 [Multi-domain] Cd Length: 229 Bit Score: 49.82 E-value: 6.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 16 VLAGGRGSRLaeltdRRAKPAV-H-FGGKArIIDFALSNALNSGIRRIGVATQYKAHSLIRHLQrgwnffrterneSFDI 93
Cdd:cd02540 3 ILAAGKGTRM-----KSDLPKVlHpLAGKP-MLEHVLDAARALGPDRIVVVVGHGAEQVKKALA------------NPNV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 94 LPASQrvsESQwyEGTADAVFQNIDIIESYApEYMVILAGDH--VYKMDYELMLQQHVDSGADVTIGCMEVPvkEASGFG 171
Cdd:cd02540 65 EFVLQ---EEQ--LGTGHAVKQALPALKDFE-GDVLVLYGDVplITPETLQRLLEAHREAGADVTVLTAELE--DPTGYG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 172 VMHVDEQDVVTAFVE---------KPKkpphipgspgmaLASMGIYVFRTALLIEELRRDADDPDSKRDFGGDIIPHIVK 242
Cdd:cd02540 137 RIIRDGNGKVLRIVEekdateeekAIR------------EVNAGIYAFDAEFLFEALPKLTNNNAQGEYYLTDIIALAVA 204
|
....*.
gi 494962724 243 HGKAVA 248
Cdd:cd02540 205 DGLKVA 210
|
|
| LbH_G1P_AT_C_like |
cd03356 |
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
316-384 |
2.12e-06 |
|
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.
Pssm-ID: 100046 [Multi-domain] Cd Length: 79 Bit Score: 45.31 E-value: 2.12e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494962724 316 GRRGSATSSLIAGGCIV-SGSSLHRSLLFTGVRTHSFSSVTESVIMPDCVIGRGARL-HKCVLDSGVIVPP 384
Cdd:cd03356 9 GENAIIKNSVIGDNVRIgDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVvNLCIIGDDVVVED 79
|
|
| glmU |
PRK14356 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
89-382 |
9.24e-05 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237686 [Multi-domain] Cd Length: 456 Bit Score: 44.33 E-value: 9.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 89 ESFDILPASQRVSESQWyeGTADAVFQNIDIIESYAPEYMVILAGDhvYKMDYELMLQQHVDSGADVTIGCMEVPVKEAS 168
Cdd:PRK14356 64 AAFPDEDARFVLQEQQL--GTGHALQCAWPSLTAAGLDRVLVVNGD--TPLVTTDTIDDFLKEAAGADLAFMTLTLPDPG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 169 GFGVMhVDEQDVVTAFVEKPKKPPHIPGsPGMALASMGIYVFRTALLIEELRRDADDPDSKRDFGGDIIphivkhGKAVA 248
Cdd:PRK14356 140 AYGRV-VRRNGHVAAIVEAKDYDEALHG-PETGEVNAGIYYLRLDAVESLLPRLTNANKSGEYYITDLV------GLAVA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 249 HRFSSSCVRAESEP----VPYWRDVGTIDAYWQANIDLTdvvpsldlydrswplWTYSEVTppakfVHNEEGRRGSATSS 324
Cdd:PRK14356 212 EGMNVLGVNCGEDPnllgVNTPAELVRSEELLRARIVEK---------------HLESGVL-----IHAPESVRIGPRAT 271
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494962724 325 L-----IAGGCIVSGSS-------------LHRSLLFTGVRTHSFSSVTESVIMPDCVIGRGARLHK-CVLDSGVIV 382
Cdd:PRK14356 272 IepgaeIYGPCEIYGASriargavihshcwLRDAVVSSGATIHSFSHLEGAEVGDGCSVGPYARLRPgAVLEEGARV 348
|
|
| GalU |
COG1210 |
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
126-282 |
3.55e-04 |
|
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 42.33 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 126 EYMVILAGDHVYKMDYEL---MLQQHVDSGADVtIGCMEVPVKEASGFGVMHVDEQD----VVTAFVEKPKkpphipgsP 198
Cdd:COG1210 123 EPFAVLLGDDLIDSEKPClkqMIEVYEETGGSV-IAVQEVPPEEVSKYGIVDGEEIEggvyRVTGLVEKPA--------P 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 199 GMA---LASMGIYVFRTAL--LIEELRRDAddpdskrdfGG-----DIIPHIVKHGKAVAHRFSSScvraesepvpyWRD 268
Cdd:COG1210 194 EEApsnLAIVGRYILTPEIfdILEKTKPGA---------GGeiqltDAIAALAKEEPVYAYEFEGK-----------RYD 253
|
170
....*....|....
gi 494962724 269 VGTIDAYWQANIDL 282
Cdd:COG1210 254 CGDKLGYLKATVEF 267
|
|
| COG2266 |
COG2266 |
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
17-65 |
9.78e-04 |
|
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441867 [Multi-domain] Cd Length: 185 Bit Score: 39.87 E-value: 9.78e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 494962724 17 LAGGRGSRLaeltDRRAKPAVHFGGKaRIIDFALSNALNSGIRRIGVAT 65
Cdd:COG2266 1 MAGGKGTRL----GGGEKPLLEICGK-PMIDRVIDALEESCIDKIYVAV 44
|
|
| LbH_G1P_AT_C_like |
cd03356 |
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
325-391 |
1.25e-03 |
|
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.
Pssm-ID: 100046 [Multi-domain] Cd Length: 79 Bit Score: 37.61 E-value: 1.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494962724 325 LIAGGCIVS-GSSLHRSLLFTGVRTHSFSSVTESVIMPDCVIGRGARLH------KCVLDSGVIVPPGLIVGEH 391
Cdd:cd03356 1 LIGESTVIGeNAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVdsiigdNAVIGENVRVVNLCIIGDD 74
|
|
| M1P_guanylylT_A_like_N |
cd06428 |
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ... |
108-249 |
1.30e-03 |
|
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: 40.31 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 108 GTADAVFQNIDIIESYAPEYMVILAGDHVYKMDYELMLQQHVDSGADVTIGCMEVPVKEASGFGVMHVDEQD-VVTAFVE 186
Cdd:cd06428 86 GTAGGLYHFRDQILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEASREQASNYGCIVEDPSTgEVLHYVE 165
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494962724 187 KpkkpphiPGSPGMALASMGIYVFRTALL------IEELRRDADDPDSKRDFGG--------DIIPHIVKHGKAVAH 249
Cdd:cd06428 166 K-------PETFVSDLINCGVYLFSPEIFdtikkaFQSRQQEAQLGDDNNREGRaevirleqDVLTPLAGSGKLYVY 235
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
14-157 |
2.28e-03 |
|
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: 39.18 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 14 AYVLAGGRGSRLAELTDRRAKPAVHFGGKArIIDFALSNALNSGIRRIGVATQYKAHSLIRHLQRGWNFFRTERNESFDI 93
Cdd:cd04198 3 AVILAGGGGSRLYPLTDNIPKALLPVANKP-MIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFPLNLKQKLDEVTI 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494962724 94 lpasqrVSESQWyeGTADAVfQNI-DIIESYApeymVILAGDHVYKMDYELMLQQHVDSGADVTI 157
Cdd:cd04198 82 ------VLDEDM--GTADSL-RHIrKKIKKDF----LVLSCDLITDLPLIELVDLHRSHDASLTV 133
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
14-219 |
2.58e-03 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 39.75 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 14 AYVLAGGRGSRLaelTDRRAKPAVHFGGKArIIDFALSNALNSGiRRIGVATQYKAHSLIRHLQrgwnffrternESFDI 93
Cdd:PRK14357 3 ALVLAAGKGTRM---KSKIPKVLHKISGKP-MINWVIDTAKKVA-QKVGVVLGHEAELVKKLLP-----------EWVKI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 94 LPASQRVsesqwyeGTADAVFQNIDIIESyaPEYMVILAGDhVYKMDYEL---MLQQHVDSGADVTIgcMEVPVKEASGF 170
Cdd:PRK14357 67 FLQEEQL-------GTAHAVMCARDFIEP--GDDLLILYGD-VPLISENTlkrLIEEHNRKGADVTI--LVADLEDPTGY 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494962724 171 GVMHVDEQDVvtAFVEKPKKPPHIpgsPGMALASMGIYVFRTALLIEEL 219
Cdd:PRK14357 135 GRIIRDGGKY--RIVEDKDAPEEE---KKIKEINTGIYVFSGDFLLEVL 178
|
|
| G1P_cytidylyltransferase |
cd02524 |
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ... |
16-42 |
2.69e-03 |
|
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: 39.09 E-value: 2.69e-03
10 20
....*....|....*....|....*..
gi 494962724 16 VLAGGRGSRLAELTDRRAKPAVHFGGK 42
Cdd:cd02524 3 ILAGGLGTRLSEETELKPKPMVEIGGR 29
|
|
| LbH_eIF2B_gamma_C |
cd04652 |
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
352-382 |
2.99e-03 |
|
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.
Pssm-ID: 100057 [Multi-domain] Cd Length: 81 Bit Score: 36.40 E-value: 2.99e-03
10 20 30
....*....|....*....|....*....|.
gi 494962724 352 SSVTESVIMPDCVIGRGARLHKCVLDSGVIV 382
Cdd:cd04652 12 TSIKRSVIGANCKIGKRVKITNCVIMDNVTI 42
|
|
| LbH_eIF2B_gamma_C |
cd04652 |
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
324-385 |
3.79e-03 |
|
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.
Pssm-ID: 100057 [Multi-domain] Cd Length: 81 Bit Score: 36.02 E-value: 3.79e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494962724 324 SLIAGGCIV-SGSSLHRSLLFTGVRTHSFSSVTESVIMPDCVIGRGARLHKCVLDSGVIVPPG 385
Cdd:cd04652 17 SVIGANCKIgKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEAG 79
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
16-221 |
3.86e-03 |
|
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440820 [Multi-domain] Cd Length: 457 Bit Score: 39.24 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 16 VLAGGRGSRLaeltdRRAKPAV-H-FGGKArIIDFALSNALNSGIRRIGVATQYKAHSLIRHLQrgwnffrterneSFDI 93
Cdd:COG1207 7 ILAAGKGTRM-----KSKLPKVlHpLAGKP-MLEHVLDAARALGPDRIVVVVGHGAEQVRAALA------------DLDV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494962724 94 LPASQrvsESQWyeGTADAVFQNIDIIESYApEYMVILAGDhVYKMDYEL---MLQQHVDSGADVTIGCMEVPvkEASGF 170
Cdd:COG1207 69 EFVLQ---EEQL--GTGHAVQQALPALPGDD-GTVLVLYGD-VPLIRAETlkaLLAAHRAAGAAATVLTAELD--DPTGY 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494962724 171 GVMHVDEQDVVTAFVE-KPkkpphipgspgmalASM----------GIYVFRTALLIEELRR 221
Cdd:COG1207 140 GRIVRDEDGRVLRIVEeKD--------------ATEeqraireintGIYAFDAAALREALPK 187
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
16-78 |
4.66e-03 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 38.22 E-value: 4.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494962724 16 VLAGGRGSRLAeltdrRAKPAVHFGGKaRIIDFALSNALNSGIRRIGVATQYKAHSLIRHLQR 78
Cdd:COG2068 8 ILAAGASSRMG-----RPKLLLPLGGK-PLLERAVEAALAAGLDPVVVVLGADAEEVAAALAG 64
|
|
| |
