|
Name |
Accession |
Description |
Interval |
E-value |
| glgC |
PRK05293 |
glucose-1-phosphate adenylyltransferase; Provisional |
3-372 |
0e+00 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 608.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 3 QNKMLAMILAGGRGTRLEGLTKKVAKPAVAFGGKYRIIDFPLSNCANSGIDIVGVLTQYEPVLLNSYVAQSQRWGLDVQG 82
Cdd:PRK05293 1 KKEMLAMILAGGQGTRLGKLTKNIAKPAVPFGGKYRIIDFTLSNCANSGIDTVGVLTQYQPLELNNHIGIGSPWDLDRIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 83 SGIFVLPPSEKIEGFGLYKGTADAITQNIDFIDLHDPEYVLILSGDHIYKMNYDKLLDTHIQNEADATIAVIEVPLKEAS 162
Cdd:PRK05293 81 GGVTILPPYSESEGGKWYKGTAHAIYQNIDYIDQYDPEYVLILSGDHIYKMDYDKMLDYHKEKEADVTIAVIEVPWEEAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 163 RFGIMNTDKDYRIEEFEEKPAKPKSNLASMGIYIFTWKTLRKYLLEDDKLDTSSHDFGHDIIPKYLADGRRLYAHPFRGY 242
Cdd:PRK05293 161 RFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFNWKRLKEYLIEDEKNPNSSHDFGKNVIPLYLEEGEKLYAYPFKGY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 243 WKDVGTVNSLWESNMDLIDHAGDLDLSDASWRIYSEDSGSPAQVIGTSATVRSAYIDKGATIDGLVEHSVISTDAQVQKG 322
Cdd:PRK05293 241 WKDVGTIESLWEANMELLRPENPLNLFDRNWRIYSVNPNLPPQYIAENAKVKNSLVVEGCVVYGTVEHSVLFQGVQVGEG 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2507226545 323 ASVKNSVILPGAIIGEDVDLDYVIVAENIKIADGTKLAGTPDQILLIDKN 372
Cdd:PRK05293 321 SVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVIIGGGKEVITVIGEN 370
|
|
| GlgC |
COG0448 |
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
5-374 |
0e+00 |
|
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];
Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 527.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 5 KMLAMILAGGRGTRLEGLTKKVAKPAVAFGGKYRIIDFPLSNCANSGIDIVGVLTQYEPVLLNSYVAQSQRWGLDVQGSG 84
Cdd:COG0448 1 KVLAIILAGGRGSRLGPLTKDRAKPAVPFGGKYRIIDFPLSNCVNSGIRRVGVLTQYKSHSLNDHIGSGKPWDLDRKRGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 85 IFVLPPSEKIEGFGLYKGTADAITQNIDFIDLHDPEYVLILSGDHIYKMNYDKLLDTHIQNEADATIAVIEVPLKEASRF 164
Cdd:COG0448 81 VFILPPYQQREGEDWYQGTADAVYQNLDFIERSDPDYVLILSGDHIYKMDYRQMLDFHIESGADITVACIEVPREEASRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 165 GIMNTDKDYRIEEFEEKPAKPKSNLASMGIYIFTWKTLRKYLLEDdkLDTSSHDFGHDIIPKYLADGrRLYAHPFRGYWK 244
Cdd:COG0448 161 GVMEVDEDGRITEFEEKPKDPKSALASMGIYVFNKDVLIELLEED--APNSSHDFGKDIIPRLLDRG-KVYAYEFDGYWR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 245 DVGTVNSLWESNMDLIDHAGDLDLSDASWRIYSEDSGSPAQVIGTSATVRSAYIDKGATIDGLVEHSVISTDAQVQKGAS 324
Cdd:COG0448 238 DVGTIDSYYEANMDLLDPEPEFNLYDPEWPIYTKQKDLPPAKFVRGGKVKNSLVSNGCIISGTVENSVLFRGVRVESGAV 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 325 VKNSVILPGAIIGEDVDLDYVIVAENIKIADGTKLAGTPDQ----------ILLIDKNVT 374
Cdd:COG0448 318 VENSVIMPGVVIGEGAVIENAIIDKNVVIPPGVVIGEDPEEdrkrftvssgIVVVGKGAV 377
|
|
| glgC |
TIGR02091 |
glucose-1-phosphate adenylyltransferase; This enzyme, glucose-1-phosphate adenylyltransferase, ... |
8-360 |
1.50e-165 |
|
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: 467.12 E-value: 1.50e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 8 AMILAGGRGTRLEGLTKKVAKPAVAFGGKYRIIDFPLSNCANSGIDIVGVLTQYEPVLLNSYVAQSqrWGLD-VQGSGIF 86
Cdd:TIGR02091 1 AMVLAGGRGSRLSPLTKRRAKPAVPFGGKYRIIDFPLSNCINSGIRRIGVLTQYKSHSLNRHIQRG--WDFDgFIDGFVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 87 VLPPSEKIEGFGLYKGTADAITQNIDFIDLHDPEYVLILSGDHIYKMNYDKLLDTHIQNEADATIAVIEVPLKEASRFGI 166
Cdd:TIGR02091 79 LLPAQQRESGTDWYQGTADAVYQNLDLIEDYDPEYVLILSGDHIYKMDYEKMLDYHIESGADVTIACIPVPRKEASRFGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 167 MNTDKDYRIEEFEEKPAKPKSN-------LASMGIYIFTWKTLRKYLLEDDKLDTSSHDFGHDIIPKYLADGrRLYAHPF 239
Cdd:TIGR02091 159 MQVDEDGRIVDFEEKPANPPSIpgmpdfaLASMGIYIFDKDVLKELLEEDADDPESSHDFGKDIIPRALEEG-SVQAYLF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 240 RGYWKDVGTVNSLWESNMDLIDHAGDLDLSDASWRIYSEDSG-SPAQVIGTSATVRSAYIDKGATIDGL-VEHSVISTDA 317
Cdd:TIGR02091 238 SGYWRDVGTIDSFWEANMDLVSVVPPFDLYDRKWPIYTYNEFlPPAKFVDSDAQVVDSLVSEGCIISGAtVSHSVLGIRV 317
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2507226545 318 QVQKGASVKNSVILPGAIIGEDVDLDYVIVAENIKIADGTKLA 360
Cdd:TIGR02091 318 RIGSGSTVEDSVIMGDVGIGRGAVIRNAIIDKNVRIGEGVVIG 360
|
|
| glgC |
PRK00725 |
glucose-1-phosphate adenylyltransferase; Provisional |
7-357 |
8.57e-145 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234824 [Multi-domain] Cd Length: 425 Bit Score: 416.93 E-value: 8.57e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 7 LAMILAGGRGTRLEGLTKKVAKPAVAFGGKYRIIDFPLSNCANSGIDIVGVLTQYEPVLLNSYVaqsQR-WGLDVQGSGI 85
Cdd:PRK00725 17 LALILAGGRGSRLKELTDKRAKPAVYFGGKFRIIDFALSNCINSGIRRIGVLTQYKAHSLIRHI---QRgWSFFREELGE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 86 FV--LPPSEKIEGFGLYKGTADAITQNIDFIDLHDPEYVLILSGDHIYKMNYDKLLDTHIQNEADATIAVIEVPLKEASR 163
Cdd:PRK00725 94 FVdlLPAQQRVDEENWYRGTADAVYQNLDIIRRYDPKYVVILAGDHIYKMDYSRMLADHVESGADCTVACLEVPREEASA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 164 FGIMNTDKDYRIEEFEEKPA-------KPKSNLASMGIYIFTWKTLRKYLLEDDKLDTSSHDFGHDIIPKYLADGrRLYA 236
Cdd:PRK00725 174 FGVMAVDENDRITAFVEKPAnppampgDPDKSLASMGIYVFNADYLYELLEEDAEDPNSSHDFGKDIIPKIVEEG-KVYA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 237 HPFR-----------GYWKDVGTVNSLWESNMDLIDHAGDLDLSDASWRI--YSEDSgSPAQVI----GTSATVRSAYID 299
Cdd:PRK00725 253 HPFSdscvrsdpeeePYWRDVGTLDAYWQANLDLASVTPELDLYDRNWPIwtYQEQL-PPAKFVfdrsGRRGMAINSLVS 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2507226545 300 KGATIDG-LVEHSVISTDAQVQKGASVKNSVILPGAIIGEDVDLDYVIVAENIKIADGT 357
Cdd:PRK00725 332 GGCIISGaVVRRSVLFSRVRVNSFSNVEDSVLLPDVNVGRSCRLRRCVIDRGCVIPEGM 390
|
|
| glgC |
PRK00844 |
glucose-1-phosphate adenylyltransferase; Provisional |
1-358 |
2.27e-115 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 341.42 E-value: 2.27e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 1 MAQNKMLAMILAGGRGTRLEGLTKKVAKPAVAFGGKYRIIDFPLSNCANSGIDIVGVLTQYEPVLLNSYVaqSQRWGLdv 80
Cdd:PRK00844 1 RAMPKVLAIVLAGGEGKRLMPLTADRAKPAVPFGGSYRLIDFVLSNLVNSGYLRIYVLTQYKSHSLDRHI--SQTWRL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 81 qgSGI---FVLP-PSEKIEGFGLYKGTADAITQNIDFIDLHDPEYVLILSGDHIYKMNYDKLLDTHIQNEADATIAVIEV 156
Cdd:PRK00844 77 --SGLlgnYITPvPAQQRLGKRWYLGSADAIYQSLNLIEDEDPDYVVVFGADHVYRMDPRQMVDFHIESGAGVTVAAIRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 157 PLKEASRFGIMNTDKDYRIEEFEEKPAKPKS-------NLASMGIYIFTWKTLRKYLLEDDKLDTSSHDFGHDIIPKYLA 229
Cdd:PRK00844 155 PREEASAFGVIEVDPDGRIRGFLEKPADPPGlpddpdeALASMGNYVFTTDALVDALRRDAADEDSSHDMGGDIIPRLVE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 230 DGrRLYAHPF------------RGYWKDVGTVNSLWESNMDLIDHAGDLDLSDASWRIYSE-DSGSPAQVIGTSATVRSA 296
Cdd:PRK00844 235 RG-RAYVYDFstnevpgaterdRGYWRDVGTIDAYYDAHMDLLSVHPVFNLYNREWPIYTSsPNLPPAKFVDGGGRVGSA 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2507226545 297 ---YIDKGATIDG-LVEHSVISTDAQVQKGASVKNSVILPGAIIGEDVDLDYVIVAENIKIADGTK 358
Cdd:PRK00844 314 qdsLVSAGSIISGaTVRNSVLSPNVVVESGAEVEDSVLMDGVRIGRGAVVRRAILDKNVVVPPGAT 379
|
|
| glgC |
PRK02862 |
glucose-1-phosphate adenylyltransferase; Provisional |
4-373 |
6.22e-90 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179486 [Multi-domain] Cd Length: 429 Bit Score: 277.15 E-value: 6.22e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 4 NKMLAMILAGGRGTRLEGLTKKVAKPAVAFGGKYRIIDFPLSNCANSGIDIVGVLTQYEPVLLNSYVAQSQRwgLDVQGS 83
Cdd:PRK02862 2 KRVLAIILGGGAGTRLYPLTKLRAKPAVPLAGKYRLIDIPISNCINSGINKIYVLTQFNSASLNRHISQTYN--FDGFSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 84 GiFV--LPPSEKIEGFGLYKGTADAITQNIDFIDLHDPEYVLILSGDHIYKMNYDKLLDTHIQNEADATIAVIEVPLKEA 161
Cdd:PRK02862 80 G-FVevLAAQQTPENPSWFQGTADAVRKYLWHFQEWDVDEYLILSGDQLYRMDYRLFVQHHRETGADITLAVLPVDEKDA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 162 SRFGIMNTDKDYRIEEFEEKP---------------------AKPKSNLASMGIYIFTWKTLRKyLLEDDKldtSSHDFG 220
Cdd:PRK02862 159 SGFGLMKTDDDGRITEFSEKPkgdelkamavdtsrlglspeeAKGKPYLASMGIYVFSRDVLFD-LLNKNP---EYTDFG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 221 HDIIPKyLADGRRLYAHPFRGYWKDVGTVNSLWESNMDL-IDHAGDLDLSDASWRIYSEDSG-SPAQVIGtsATVRSAYI 298
Cdd:PRK02862 235 KEIIPE-AIRDYKVQSYLFDGYWEDIGTIEAFYEANLALtQQPNPPFSFYDEKAPIYTRARYlPPSKLLD--ATITESII 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2507226545 299 DKGATIDGL-VEHSVISTDAQVQKGASVKNSVILpGAIIGEDVDLDYVIVAE---NIKIADGTKLAGTpdqilLIDKNV 373
Cdd:PRK02862 312 AEGCIIKNCsIHHSVLGIRSRIESGCTIEDTLVM-GADFYESSEEREELRKEgkpPLGIGEGTTIKRA-----IIDKNA 384
|
|
| ADP_Glucose_PP |
cd02508 |
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ... |
8-246 |
2.69e-88 |
|
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: 264.79 E-value: 2.69e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 8 AMILAGGRGTRLEGLTKKVAKPAVAFGGKYRIIDFPLSNCANSGIDIVGVLTQYEPVLLNSYVAQSQRWGLDVQGSGIFV 87
Cdd:cd02508 1 AIILAGGEGTRLSPLTKKRAKPAVPFGGRYRLIDFPLSNMVNSGIRNVGVLTQYKSRSLNDHLGSGKEWDLDRKNGGLFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 88 LPPSEKIEGfGLYKGTADAITQNIDFIDLHDPEYVLILSGDHIYKMNYDKLLDTHIQNEADATIAVIevplkeasrfgim 167
Cdd:cd02508 81 LPPQQRKGG-DWYRGTADAIYQNLDYIERSDPEYVLILSGDHIYNMDYREMLDFHIESGADITVVYK------------- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2507226545 168 ntdkdyrieefeekpakpksnlASMGIYIFTWKTLRKYLLEDDKldTSSHDFGHDIIPKYLADGrRLYAHPFRGYWKDV 246
Cdd:cd02508 147 ----------------------ASMGIYIFSKDLLIELLEEDAA--DGSHDFGKDIIPAMLKKL-KIYAYEFNGYWADI 200
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
7-259 |
2.31e-85 |
|
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: 258.72 E-value: 2.31e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 7 LAMILAGGRGTRLEGLTKKVAKPAVAFGGKYRIIDFPLSNCANSGI-DIVGVLTQYEPVLLNSYVAQSQRWGLDVQgsgi 85
Cdd:pfam00483 1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKYPLIDYPLSRLANAGIrEIIVILTQEHRFMLNELLGDGSKFGVQIT---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 86 FVLPPSEKiegfglykGTADAITQNIDFIDLHDPEyVLILSGDHIYKMNYDKLLDTHIQNEADATIAVIEVPLKEASRFG 165
Cdd:pfam00483 77 YALQPEGK--------GTAPAVALAADFLGDEKSD-VLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGIVPVEPPTGYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 166 IMNTDKDYRIEEFEEKPAKPK-SNLASMGIYIFTWKTLrKYLLEDDKLDTSSHDFGHDIIPKYLADGRRLYAHPFRGY-W 243
Cdd:pfam00483 148 VVEFDDNGRVIRFVEKPKLPKaSNYASMGIYIFNSGVL-DFLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYaW 226
|
250
....*....|....*.
gi 2507226545 244 KDVGTVNSLWESNMDL 259
Cdd:pfam00483 227 LDVGTWDSLWEANLFL 242
|
|
| PLN02241 |
PLN02241 |
glucose-1-phosphate adenylyltransferase |
4-373 |
1.75e-83 |
|
glucose-1-phosphate adenylyltransferase
Pssm-ID: 215133 [Multi-domain] Cd Length: 436 Bit Score: 260.56 E-value: 1.75e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 4 NKMLAMILAGGRGTRLEGLTKKVAKPAVAFGGKYRIIDFPLSNCANSGIDIVGVLTQYEPVLLNSYVAQSQRWGLDVQGS 83
Cdd:PLN02241 2 KSVAAIILGGGAGTRLFPLTKRRAKPAVPIGGNYRLIDIPMSNCINSGINKIYVLTQFNSASLNRHLSRAYNFGNGGNFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 84 GIFV--LPPSEKIEGFGLYKGTADAITQNI---DFIDLHDPEYVLILSGDHIYKMNYDKLLDTHIQNEADATIAVIEVPL 158
Cdd:PLN02241 82 DGFVevLAATQTPGEKGWFQGTADAVRQFLwlfEDAKNKNVEEVLILSGDHLYRMDYMDFVQKHRESGADITIACLPVDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 159 KEASRFGIMNTDKDYRIEEFEEKP---------------------AKPKSNLASMGIYIFTWKTLRKyLLEDDKldTSSH 217
Cdd:PLN02241 162 SRASDFGLMKIDDTGRIIEFSEKPkgdelkamqvdttvlglspeeAKEKPYIASMGIYVFKKDVLLK-LLRWRF--PTAN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 218 DFGHDIIPKYLADGRRLYAHPFRGYWKDVGTVNSLWESNMDLIDHAGDLDLSDASWRIY-SEDSGSPAQVIGtsATVRSA 296
Cdd:PLN02241 239 DFGSEIIPGAIKEGYNVQAYLFDGYWEDIGTIKSFYEANLALTKQPPKFSFYDPDAPIYtSPRFLPPSKIED--CRITDS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 297 YIDKGATIDG-LVEHSVISTDAQVQKGASVKNSVILPGAIIGEDVDLDYvIVAEN---IKIADGTKLAGTpdqilLIDKN 372
Cdd:PLN02241 317 IISHGCFLREcKIEHSVVGLRSRIGEGVEIEDTVMMGADYYETEEEIAS-LLAEGkvpIGIGENTKIRNA-----IIDKN 390
|
.
gi 2507226545 373 V 373
Cdd:PLN02241 391 A 391
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
8-247 |
3.32e-52 |
|
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: 172.76 E-value: 3.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 8 AMILAGGRGTRLEGLTKKVAKPAVAFGGKyRIIDFPLSNCANSGIDIVGVLTQYEPVLLNSYVAQSQRWGLDVQgsgiFV 87
Cdd:cd04181 1 AVILAAGKGTRLRPLTDTRPKPLLPIAGK-PILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVNIE----YV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 88 LPPSEKiegfglykGTADAITQNIDFIDlhdPEYVLILSGDHIYKMNYDKLLDTHIQNEADATIAVIEVPlkEASRFGIM 167
Cdd:cd04181 76 VQEEPL--------GTAGAVRNAEDFLG---DDDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVE--DPSRYGVV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 168 NTDKDYRIEEFEEKPAKPKSNLASMGIYIFTwKTLRKYLledDKLDTSSHDFGHDIIPKyLADGRRLYAHPFRGYWKDVG 247
Cdd:cd04181 143 ELDDDGRVTRFVEKPTLPESNLANAGIYIFE-PEILDYI---PEILPRGEDELTDAIPL-LIEEGKVYGYPVDGYWLDIG 217
|
|
| glgD |
TIGR02092 |
glucose-1-phosphate adenylyltransferase, GlgD subunit; This family is GlgD, an apparent ... |
4-371 |
5.51e-51 |
|
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: 174.49 E-value: 5.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 4 NKMLAMILAGGRGTRLEGLTKKVAKPAVAFGGKYRIIDFPLSNCANSGIDIVGVLTQYEPVL-LNSYVAQSQRWGLDVQG 82
Cdd:TIGR02092 1 NKMSAIINLTESSKNLSPLTKVRPLASLPFGGRYRLIDFPLSNMVNAGIRNVFIFFKNKERQsLFDHLGSGREWDLHRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 83 SGIFVLPPSEKIEgfgLYKGTADAITQNIDFIDLHDPEYVLILSGDHIYKMNYDKLLDTHIQNEADATIAVIEV-PLKEA 161
Cdd:TIGR02092 81 DGLFVFPYNDRDD---LSEGGKRYFSQNLEFLKRSTSEYTVVLNSHMVCNIDLKAVLKYHEETGKDITVVYKKVkPADAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 162 SRFGIMNTD-KDYRIEEFEEKPAKPKSNLaSMGIYIFTwKTLRKYLLEDdkldtsSHDFGHDIIPKYL----ADGRRLYA 236
Cdd:TIGR02092 158 EYDTILRFDeSGKVKSIGQNLNPEEEENI-SLDIYIVS-TDLLIELLYE------CIQRGKLTSLEELirenLKELNINA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 237 HPFRGYWKDVGTVNSLWESNMDLIDHAGDLDL-SDASWRIYSEDSGSPAQVIGTSATVRSAYIDKGATIDGLVEHSVIST 315
Cdd:TIGR02092 230 YEYTGYLANINSVKSYYKANMDLLDPQNFQSLfYSSQGPIYTKVKDEPPTYYAENSKVENSLVANGCIIEGKVENSILSR 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2507226545 316 DAQVQKGASVKNSVILPGAIIGEDVDLDYVIVAENIKIADGTKLAGTPDQILLIDK 371
Cdd:TIGR02092 310 GVHVGKDALIKNCIIMQRTVIGEGAHLENVIIDKDVVIEPNVKIAGTSEQPLVISK 365
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
8-259 |
3.51e-50 |
|
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: 168.41 E-value: 3.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 8 AMILAGGRGTRLEGLTKKVAKPAVAFGGKyRIIDFPLSNCANSGIDIVGVLTQYEPVLLNSYVAQSQRWGLDVQGSgifv 87
Cdd:COG1208 2 AVILAGGLGTRLRPLTDTRPKPLLPVGGK-PLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYV---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 88 lppsekIEGFGLykGTADAITQNIDFIDlhdPEYVLILSGDHIYKMNYDKLLDTHIQNEADATIAVIEVPlkEASRFGIM 167
Cdd:COG1208 77 ------DEGEPL--GTGGALKRALPLLG---DEPFLVLNGDILTDLDLAALLAFHREKGADATLALVPVP--DPSRYGVV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 168 NTDKDYRIEEFEEKPAKPKSNLASMGIYIFTWKTLRkYLLEDDKLDTSshdfghDIIPKYLADGrRLYAHPFRGYWKDVG 247
Cdd:COG1208 144 ELDGDGRVTRFVEKPEEPPSNLINAGIYVLEPEIFD-YIPEGEPFDLE------DLLPRLIAEG-RVYGYVHDGYWLDIG 215
|
250
....*....|..
gi 2507226545 248 TVNSLWESNMDL 259
Cdd:COG1208 216 TPEDLLEANALL 227
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
6-256 |
1.76e-33 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 125.97 E-value: 1.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 6 MLAMILAGGRGTRLEGLTKKVAKPAVAFGGKyRIIDFPLSNCANSGI-DIVGVLTQYEPVLLNSYVAQSQRWGLDVQgsg 84
Cdd:COG1209 1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDK-PMIYYPLSTLMLAGIrEILIISTPEDGPQFERLLGDGSQLGIKIS--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 85 iFVLPPSEKiegfglykGTADAITQNIDFIDlhDPEYVLILsGDHIYKMN-YDKLLDTHIQNEADATIAVIEVplKEASR 163
Cdd:COG1209 77 -YAVQPEPL--------GLAHAFIIAEDFIG--GDPVALVL-GDNIFYGDgLSELLREAAARESGATIFGYKV--EDPER 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 164 FGIMNTDKDYRIEEFEEKPAKPKSNLASMGIYIFTwKTLRKYLledDKLDTSSHdfGH----DIIPKYLADGRRLYAHPF 239
Cdd:COG1209 143 YGVVEFDEDGRVVSLEEKPKEPKSNLAVTGLYFYD-NDVVEIA---KNLKPSAR--GEleitDANQAYLERGKLVVELLG 216
|
250
....*....|....*...
gi 2507226545 240 RGY-WKDVGTVNSLWESN 256
Cdd:COG1209 217 RGFaWLDTGTHESLLEAN 234
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
6-262 |
5.24e-32 |
|
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: 120.37 E-value: 5.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 6 MLAMILAGGRGTRLEGLTKKVAKPAVAFGGKyRIIDFPLSNCANSGIDIVGVLTQYEPVLLNSYVAQSQRWGLDVQgsgi 85
Cdd:cd04189 1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGK-PIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFGVRIT---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 86 FVLPPSEkiegfglyKGTADAITQNIDFIDlhDPEYVLILsGDHIYKMNYDKLLDTHIQNEADATIAVIEVPlkEASRFG 165
Cdd:cd04189 76 YILQEEP--------LGLAHAVLAARDFLG--DEPFVVYL-GDNLIQEGISPLVRDFLEEDADASILLAEVE--DPRRFG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 166 IMNTDkDYRIEEFEEKPAKPKSNLASMGIYIFTwktlRKYLLEDDKLDTSSHdfGH----DIIPKYLADGRRLYAHPFRG 241
Cdd:cd04189 143 VAVVD-DGRIVRLVEKPKEPPSNLALVGVYAFT----PAIFDAISRLKPSWR--GEleitDAIQWLIDRGRRVGYSIVTG 215
|
250 260
....*....|....*....|.
gi 2507226545 242 YWKDVGTVNSLWESNMDLIDH 262
Cdd:cd04189 216 WWKDTGTPEDLLEANRLLLDK 236
|
|
| Arch_glmU |
TIGR03992 |
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ... |
6-360 |
4.79e-31 |
|
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.
Pssm-ID: 274908 [Multi-domain] Cd Length: 393 Bit Score: 121.55 E-value: 4.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 6 MLAMILAGGRGTRLEGLTKKVAKPAVAFGGKyRIIDFPLSNCANSGIDIVGVLTQYEPVLLNSYVAQSQRWGLDVQgsgi 85
Cdd:TIGR03992 1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGK-PLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIE---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 86 FVlppsEKIEGfglyKGTADAITQNIDFIDlhdpEYVLILSGDHIYKMNydkLLDTHIQNEADAtIAVIEVPlkEASRFG 165
Cdd:TIGR03992 76 YV----VQEEQ----LGTADALGSAKEYVD----DEFLVLNGDVLLDSD---LLERLIRAEAPA-IAVVEVD--DPSDYG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 166 IMNTDKDyRIEEFEEKPAKPKSNLASMGIYIFTwKTLRKYLledDKLDTSSHdfGH----DIIpKYLADGRRLYAHPFRG 241
Cdd:TIGR03992 138 VVETDGG-RVTGIVEKPENPPSNLINAGIYLFS-PEIFELL---EKTKLSPR--GEyeltDAL-QLLIDEGKVKAVELDG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 242 YWKDVGtvnSLWesnmDLIDhAGDLDLSDASWRIY---SEDSGSPAQV-IGTSATVRS-------AYIDKGATIdG---- 306
Cdd:TIGR03992 210 FWLDVG---RPW----DLLD-ANEALLDNLEPRIEgtvEENVTIKGPVvIGEGAVIRSgtyiegpVYIGKNCDI-Gpnay 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2507226545 307 LVEHSVISTDAQVQKGASVKNSVILPGAIIGEdvdLDYV---IVAENIKIADGTKLA 360
Cdd:TIGR03992 281 IRPYTVIGNNVHIGNAVEIKNSIIMEGTKIPH---LSYVgdsVIGENCNFGAGTKVA 334
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
6-248 |
6.68e-30 |
|
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: 114.62 E-value: 6.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 6 MLAMILAGGRGTRLEGLTKKVAKPAVAFGGKyRIIDFPLSNCANSGIDIVGVLTQYEPVLLNSYV-AQSQRWGLDVQGSg 84
Cdd:cd06425 1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNK-PMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLkEYEKKLGIKITFS- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 85 ifvlppsekIEGFGLykGTADAITQNIDFI-DLHDPEYVliLSGDHIYKMNYDKLLDTHIQNEADATIAVIEVplKEASR 163
Cdd:cd06425 79 ---------IETEPL--GTAGPLALARDLLgDDDEPFFV--LNSDVICDFPLAELLDFHKKHGAEGTILVTKV--EDPSK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 164 FGIMNTDKD-YRIEEFEEKPAKPKSNLASMGIYIFTWKTLRKYLLEddklDTSshdFGHDIIPKYLADGrRLYAHPFRGY 242
Cdd:cd06425 144 YGVVVHDENtGRIERFVEKPKVFVGNKINAGIYILNPSVLDRIPLR----PTS---IEKEIFPKMASEG-QLYAYELPGF 215
|
....*.
gi 2507226545 243 WKDVGT 248
Cdd:cd06425 216 WMDIGQ 221
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
8-247 |
4.27e-28 |
|
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: 109.52 E-value: 4.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 8 AMILAGGRGTRLEGLTKKVAKPAVAFGGKyRIIDFPLSNCANSGIDIVGVLTQYEPVLLNSYVAQSQRWGLDVQgsgiFV 87
Cdd:cd06426 1 VVIMAGGKGTRLRPLTENTPKPMLKVGGK-PILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKFGVNIS----YV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 88 LPPSekiegfglYKGTADAITqnidFIDLHDPEYVLILSGDHIYKMNYDKLLDTHIQNEADATIAVIE----VPlkeasr 163
Cdd:cd06426 76 REDK--------PLGTAGALS----LLPEKPTDPFLVMNGDILTNLNYEHLLDFHKENNADATVCVREyevqVP------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 164 FGIMNTDkDYRIEEFEEKPAkpKSNLASMGIYIFTWKTLrKYLLEDDKLDTSshdfghDIIPKYLADGRRLYAHPFRGYW 243
Cdd:cd06426 138 YGVVETE-GGRITSIEEKPT--HSFLVNAGIYVLEPEVL-DLIPKNEFFDMP------DLIEKLIKEGKKVGVFPIHEYW 207
|
....
gi 2507226545 244 KDVG 247
Cdd:cd06426 208 LDIG 211
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
8-252 |
1.40e-24 |
|
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: 99.93 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 8 AMILAGGRGTRLEGLTKKVAKPAVAFGGKyRIIDFPLSNCANSGIDIVGVLTQYEPVLLNSYVAQSQRWGLDVQGSgifv 87
Cdd:cd06915 1 AVILAGGLGTRLRSVVKDLPKPLAPVAGR-PFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIYYV---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 88 lppsekIEGFGLykGTADAItqnIDFIDLHDPEYVLILSGDHIYKMNYDKLLDTHIQNEADATIAVIEVPlkEASRFGIM 167
Cdd:cd06915 76 ------IEPEPL--GTGGAI---KNALPKLPEDQFLVLNGDTYFDVDLLALLAALRASGADATMALRRVP--DASRYGNV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 168 NTDKDYRIEEFEEKPAKPKSNLASMGIYIFtwktlRKYLLEDDKLDTSShdFGHDIIPKYLADGrRLYAHPFRGYWKDVG 247
Cdd:cd06915 143 TVDGDGRVIAFVEKGPGAAPGLINGGVYLL-----RKEILAEIPADAFS--LEADVLPALVKRG-RLYGFEVDGYFIDIG 214
|
....*
gi 2507226545 248 TVNSL 252
Cdd:cd06915 215 IPEDY 219
|
|
| LbH_G1P_AT_C |
cd04651 |
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ... |
287-375 |
7.88e-19 |
|
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: 80.97 E-value: 7.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 287 IGTSATVRSAYIDKGATI-DGLVEHSVISTDAQVQKGASVKNSVILPGAIIGEDVDLDYVIVAENIKIADGTKLAGTPDQ 365
Cdd:cd04651 4 IGRRGEVKNSLVSEGCIIsGGTVENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIPDGVVIGGDPEE 83
|
90 100
....*....|....*....|.
gi 2507226545 366 -----------ILLIDKNVTK 375
Cdd:cd04651 84 drarfyvtedgIVVVGKGMVI 104
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
8-256 |
8.82e-17 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 79.72 E-value: 8.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 8 AMILAGGRGTRLEGLTKKVAKPAVAFGGKyRIIDFPLSNCANSGI-DIVGVLTQYEPVLLNSYVAQSQRWGLDVQgsgiF 86
Cdd:PRK15480 6 GIILAGGSGTRLYPVTMAVSKQLLPIYDK-PMIYYPLSTLMLAGIrDILIISTPQDTPRFQQLLGDGSQWGLNLQ----Y 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 87 VLPPSEKiegfglykGTADAITQNIDFIDLHDPEYVLilsGDHI-YKMNYDKLLDTHIQNEADATIAVIEVplKEASRFG 165
Cdd:PRK15480 81 KVQPSPD--------GLAQAFIIGEEFIGGDDCALVL---GDNIfYGHDLPKLMEAAVNKESGATVFAYHV--NDPERYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 166 IMNTDKDYRIEEFEEKPAKPKSNLASMGIYIFTWKTLRkyLLEDDKLDTSSHDFGHDIIPKYLADGRRLYAHPFRGY-WK 244
Cdd:PRK15480 148 VVEFDQNGTAISLEEKPLQPKSNYAVTGLYFYDNDVVE--MAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYaWL 225
|
250
....*....|..
gi 2507226545 245 DVGTVNSLWESN 256
Cdd:PRK15480 226 DTGTHQSLIEAS 237
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
6-257 |
1.72e-16 |
|
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: 78.00 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 6 MLAMILAGGRGTRLEGLTKKVAK---PAvafgGKYRIIDFPLSNCANSGI-DIVGVLT-----QYEPVLLNSyvaqSQrW 76
Cdd:cd02538 1 MKGIILAGGSGTRLYPLTKVVSKqllPV----YDKPMIYYPLSTLMLAGIrEILIISTpedlpLFKELLGDG----SD-L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 77 GLDVQgsgiFVLPPSEKiegfglykGTADAITQNIDFIDlhDPEYVLILsGDHI-YKMNYDKLLDTHIQNEADATIAVIE 155
Cdd:cd02538 72 GIRIT----YAVQPKPG--------GLAQAFIIGEEFIG--DDPVCLIL-GDNIfYGQGLSPILQRAAAQKEGATVFGYE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 156 VplKEASRFGIMNTDKDYRIEEFEEKPAKPKSNLASMGIYIFtwktlrkylleddklDTSSHDFGHDIIP---------- 225
Cdd:cd02538 137 V--NDPERYGVVEFDENGRVLSIEEKPKKPKSNYAVTGLYFY---------------DNDVFEIAKQLKPsargeleitd 199
|
250 260 270
....*....|....*....|....*....|....*.
gi 2507226545 226 ---KYLADGRRLYAHPFRGY-WKDVGTVNSLWESNM 257
Cdd:cd02538 200 vnnEYLEKGKLSVELLGRGFaWLDTGTHESLLEASN 235
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
8-248 |
1.15e-14 |
|
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: 72.22 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 8 AMILAGGRGTRLEGLTKKVAKPAVAFGGKyRIIDFPLSNCANSGIDIVGVLTQYEPVLLNSYVaQSQRWGLDVQGSGifv 87
Cdd:cd06422 2 AMILAAGLGTRMRPLTDTRPKPLVPVAGK-PLIDHALDRLAAAGIRRIVVNTHHLADQIEAHL-GDSRFGLRITISD--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 88 lppsekiEGFGLYkGTADAITQNIDFIDlHDPeyVLILSGDHIYKMNYDKLLDTHIQNEADATIAVIEVPLKEASRFGIM 167
Cdd:cd06422 77 -------EPDELL-ETGGGIKKALPLLG-DEP--FLVVNGDILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 168 NTDKDYRIEEFEEKPAKPksnLASMGIYIftwktLRKYLLEDDKLDTSShdfghdIIP---KYLADGrRLYAHPFRGYWK 244
Cdd:cd06422 146 SLDADGRLRRGGGGAVAP---FTFTGIQI-----LSPELFAGIPPGKFS------LNPlwdRAIAAG-RLFGLVYDGLWF 210
|
....
gi 2507226545 245 DVGT 248
Cdd:cd06422 211 DVGT 214
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
8-252 |
2.52e-12 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 66.03 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 8 AMILAGGRGTRLEGLTKKVAKPAVAFGGKyRIIDFPLSNCANSGIDIVGVLTQYEPVLLNSYVaqsQRWGLDVQgsgiFV 87
Cdd:COG1213 2 AVILAAGRGSRLGPLTDDIPKCLVEIGGK-TLLERQLEALAAAGIKDIVVVTGYKAELIEEAL---ARPGPDVT----FV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 88 LPPsekiegfgLYkgtadAITQNI-------DFIDlhdpEYVLILSGDHIYKmnyDKLLDTHIQNEADATIAV---IEVP 157
Cdd:COG1213 74 YNP--------DY-----DETNNIyslwlarEALD----EDFLLLNGDVVFD---PAILKRLLASDGDIVLLVdrkWEKP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 158 LKEASRFGImntDKDYRIEEFEEKPAKPKSNLASMGIYIFTWKTLRKYLLEDDKLDTSSHDFGH--DIIPKYLADGRRLY 235
Cdd:COG1213 134 LDEEVKVRV---DEDGRIVEIGKKLPPEEADGEYIGIFKFSAEGAAALREALEALIDEGGPNLYyeDALQELIDEGGPVK 210
|
250
....*....|....*...
gi 2507226545 236 AHPFRG-YWKDVGTVNSL 252
Cdd:COG1213 211 AVDIGGlPWVEIDTPEDL 228
|
|
| M1P_guanylylT_A_like_N |
cd06428 |
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ... |
8-251 |
4.68e-12 |
|
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: 65.35 E-value: 4.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 8 AMILAGG--RGTRLEGLTKKVAKPAVAFGGKyRIIDFPLSNCAN-SGIDIVGVLTQYEPVLLNSYVAQSQrwgldvQGSG 84
Cdd:cd06428 1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGK-PMIHHHIEACAKvPDLKEVLLIGFYPESVFSDFISDAQ------QEFN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 85 IFVLPPSEkiegfglYK--GTADAITQNIDFIDLHDPEYVLILSGDHIYKMNYDKLLDTHIQNEADATIAVIEVPLKEAS 162
Cdd:cd06428 74 VPIRYLQE-------YKplGTAGGLYHFRDQILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEASREQAS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 163 RFGIMNTD-KDYRIEEFEEKPAKPKSNLASMGIYIFTWKTLR-----------KYLLEDDKLDTSSHDF---GHDIIPKy 227
Cdd:cd06428 147 NYGCIVEDpSTGEVLHYVEKPETFVSDLINCGVYLFSPEIFDtikkafqsrqqEAQLGDDNNREGRAEVirlEQDVLTP- 225
|
250 260
....*....|....*....|....
gi 2507226545 228 LADGRRLYAHPFRGYWKDVGTVNS 251
Cdd:cd06428 226 LAGSGKLYVYKTDDFWSQIKTAGS 249
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
101-259 |
5.64e-10 |
|
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: 59.47 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 101 KGTADAITQNIDFIDlhdPEYVLILSGDHI---YKMNYDKLLDTHiqNEADA-TIAVIEVPLKEASRFGIMNTDKD---- 172
Cdd:cd02541 104 LGLGHAVLCAKPFIG---DEPFAVLLGDDLidsKEPCLKQLIEAY--EKTGAsVIAVEEVPPEDVSKYGIVKGEKIdgdv 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 173 YRIEEFEEKPaKPK---SNLASMGIYIFTWKTLrkylledDKLDTSSHDFGHDIipkYLADG-------RRLYAHPFRGY 242
Cdd:cd02541 179 FKVKGLVEKP-KPEeapSNLAIVGRYVLTPDIF-------DILENTKPGKGGEI---QLTDAiaklleeEPVYAYVFEGK 247
|
170
....*....|....*..
gi 2507226545 243 WKDVGTVNSLWESNMDL 259
Cdd:cd02541 248 RYDCGNKLGYLKATVEF 264
|
|
| G1P_cytidylyltransferase |
cd02524 |
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ... |
8-256 |
2.04e-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: 57.58 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 8 AMILAGGRGTRLEGLTKKVAKPAVAFGGK------------YRIIDFPLsnCANSGIDivgVLTQYepvLLNSYVAQSQr 75
Cdd:cd02524 1 VVILAGGLGTRLSEETELKPKPMVEIGGRpilwhimkiyshYGHNDFIL--CLGYKGH---VIKEY---FLNYFLHNSD- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 76 WGLDVQGSGIFVLppSEKIEGF-------GLYKGTADAITQNIDFIDlhDPEYVLILSGDHIYKMNYDKLLDTHIQNEAD 148
Cdd:cd02524 72 VTIDLGTNRIELH--NSDIEDWkvtlvdtGLNTMTGGRLKRVRRYLG--DDETFMLTYGDGVSDVNINALIEFHRSHGKL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 149 ATIAVIEVPlkeaSRFGIMNTDKDYRIEEFEEKPAKPKSnLASMGIYIFTWKTLrKYLLEDDKldtsshDFGHDIIPKyL 228
Cdd:cd02524 148 ATVTAVHPP----GRFGELDLDDDGQVTSFTEKPQGDGG-WINGGFFVLEPEVF-DYIDGDDT------VFEREPLER-L 214
|
250 260 270
....*....|....*....|....*....|....
gi 2507226545 229 ADGRRLYAHPFRGYW------KDVGTVNSLWESN 256
Cdd:cd02524 215 AKDGELMAYKHTGFWqcmdtlRDKQTLEELWNSG 248
|
|
| GalU |
COG1210 |
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
151-248 |
2.29e-09 |
|
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 57.73 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 151 IAVIEVPLKEASRFGIMNTDKD----YRIEEFEEKPAKPK--SNLASMGIYIFT---WKTLRKylLEDDKLD----Tssh 217
Cdd:COG1210 156 IAVQEVPPEEVSKYGIVDGEEIeggvYRVTGLVEKPAPEEapSNLAIVGRYILTpeiFDILEK--TKPGAGGeiqlT--- 230
|
90 100 110
....*....|....*....|....*....|.
gi 2507226545 218 dfghDIIpKYLADGRRLYAHPFRGYWKDVGT 248
Cdd:COG1210 231 ----DAI-AALAKEEPVYAYEFEGKRYDCGD 256
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
4-341 |
1.02e-08 |
|
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: 56.57 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 4 NKMLAMILAGGRGTRLegltkKVAKPAV--AFGGKYrIIDFPLSNCANSGIDIVGVLT-----QYEPVLLN---SYVAQS 73
Cdd:COG1207 1 SPLAVVILAAGKGTRM-----KSKLPKVlhPLAGKP-MLEHVLDAARALGPDRIVVVVghgaeQVRAALADldvEFVLQE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 74 QRwgldvqgsgifvlppsekiegfglyKGTADAITQNIDFIDLHDpEYVLILSGDH--IYKMNYDKLLDTHIQNEADATI 151
Cdd:COG1207 75 EQ-------------------------LGTGHAVQQALPALPGDD-GTVLVLYGDVplIRAETLKALLAAHRAAGAAATV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 152 AVIEVPlkEASRFGIMNTDKDYRIEEF-EEKPAKP---KSNLASMGIYIFTWKTLRKYLledDKLD----------Tssh 217
Cdd:COG1207 129 LTAELD--DPTGYGRIVRDEDGRVLRIvEEKDATEeqrAIREINTGIYAFDAAALREAL---PKLSndnaqgeyylT--- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 218 dfghDIIPKYLADGRRLYAHPFRGYWKDVGtVNSLWEsnmdlidhagdldLSDASwRIYSE-------DSG----SPAQV 286
Cdd:COG1207 201 ----DVIAIARADGLKVAAVQPEDPWEVLG-VNDRVQ-------------LAEAE-RILQRriaerlmRAGvtiiDPATT 261
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2507226545 287 -IGTSATV-RSAYIDKGATIDGLVE---------HSVIsTDAQVQKGASVKNSVILpGAIIGEDVD 341
Cdd:COG1207 262 yIDGDVEIgRDVVIDPNVILEGKTVigegvvigpNCTL-KDSTIGDGVVIKYSVIE-DAVVGAGAT 325
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
8-206 |
1.37e-08 |
|
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: 54.83 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 8 AMILAGGRGTRLegltkKVAKPAVAF--GGKyRIIDFPLSNCANSGIDIVGVLTQYEPVLLNSYVAqsqrwGLDVQgsgi 85
Cdd:cd02540 1 AVILAAGKGTRM-----KSDLPKVLHplAGK-PMLEHVLDAARALGPDRIVVVVGHGAEQVKKALA-----NPNVE---- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 86 FVLppSEKIegfglyKGTADAITQNIDFIDLHDpEYVLILSGDH--IYKMNYDKLLDTHIQNEADATIAVIEvpLKEASR 163
Cdd:cd02540 66 FVL--QEEQ------LGTGHAVKQALPALKDFE-GDVLVLYGDVplITPETLQRLLEAHREAGADVTVLTAE--LEDPTG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2507226545 164 FGIMNTDKDYRIEEF-EEKPAKP---KSNLASMGIYIFTWKTLRKYL 206
Cdd:cd02540 135 YGRIIRDGNGKVLRIvEEKDATEeekAIREVNAGIYAFDAEFLFEAL 181
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
8-238 |
1.15e-07 |
|
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: 51.85 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 8 AMILAGGRGTRLEGLTKKVAKPAVAFGGKyRIIDFPLSNCANSGIDIVGVLTQYepvlLNSYVAQsqrwgldvqgsgifV 87
Cdd:cd02523 1 AIILAAGRGSRLRPLTEDRPKCLLEINGK-PLLERQIETLKEAGIDDIVIVTGY----KKEQIEE--------------L 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 88 LPPSEKIEgfgLYKGTADAITQNI-------DFIDlhdpEYVLILSGDHIYkmnYDKLLDTHIQNEADATIAVIEVPLKE 160
Cdd:cd02523 62 LKKYPNIK---FVYNPDYAETNNIyslylarDFLD----EDFLLLEGDVVF---DPSILERLLSSPADNAILVDKKTKEW 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 161 ASRFGIMNTDKDYRIEEfEEKPAKPKSNLA-SMGIYIFT---WKTLRKYL--LEDDKLDTSSHDFghdiIPKYLADGRRL 234
Cdd:cd02523 132 EDEYVKDLDDAGVLLGI-ISKAKNLEEIQGeYVGISKFSpedADRLAEALeeLIEAGRVNLYYED----ALQRLISEEGV 206
|
....
gi 2507226545 235 YAHP 238
Cdd:cd02523 207 KVKD 210
|
|
| glmU |
PRK14360 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
6-206 |
6.38e-07 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184646 [Multi-domain] Cd Length: 450 Bit Score: 51.08 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 6 MLAM-ILAGGRGTRLEGLTKKVAKPavaFGGKyRIIDFPLSNCANSGIDIVGVLTQYepvllnsyvaQSQRwgldVQGSg 84
Cdd:PRK14360 1 MLAVaILAAGKGTRMKSSLPKVLHP---LGGK-SLVERVLDSCEELKPDRRLVIVGH----------QAEE----VEQS- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 85 ifvLPPSEKIEgFGLYK---GTADAITQNIDFIDLHDPEyVLILSGD--HIYKMNYDKLLDTHIQNEADATIavIEVPLK 159
Cdd:PRK14360 62 ---LAHLPGLE-FVEQQpqlGTGHAVQQLLPVLKGFEGD-LLVLNGDvpLLRPETLEALLNTHRSSNADVTL--LTARLP 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2507226545 160 EASRFGIMNTDKDYRIEEF-EEK---PAKPKSNLASMGIYIFTWKTLRKYL 206
Cdd:PRK14360 135 NPKGYGRVFCDGNNLVEQIvEDRdctPAQRQNNRINAGIYCFNWPALAEVL 185
|
|
| LbH_eIF2B_gamma_C |
cd04652 |
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
308-359 |
7.44e-07 |
|
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: 46.42 E-value: 7.44e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2507226545 308 VEHSVISTDAQVQKGASVKNSVILPGAIIGEDVDLDYVIVAENIKIADGTKL 359
Cdd:cd04652 14 IKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKL 65
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
6-206 |
1.02e-06 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 50.53 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 6 MLAMILAGGRGTRLEGLTKKVAkpavafggkYRIIDFPLSN----CANSGIDIVGVLTQYEPVLLNSYVAQsqrwglDVQ 81
Cdd:PRK14357 1 MRALVLAAGKGTRMKSKIPKVL---------HKISGKPMINwvidTAKKVAQKVGVVLGHEAELVKKLLPE------WVK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 82 gsgIFVlpPSEKIegfglykGTADAITQNIDFIDLHDPeyVLILSGD--HIYKMNYDKLLDTHIQNEADATIAVIEvpLK 159
Cdd:PRK14357 66 ---IFL--QEEQL-------GTAHAVMCARDFIEPGDD--LLILYGDvpLISENTLKRLIEEHNRKGADVTILVAD--LE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2507226545 160 EASRFG-IMNTDKDYRIEEFEEKPAKPKS-NLASMGIYIFTWKTLRKYL 206
Cdd:PRK14357 130 DPTGYGrIIRDGGKYRIVEDKDAPEEEKKiKEINTGIYVFSGDFLLEVL 178
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
6-153 |
8.34e-06 |
|
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133041 [Multi-domain] Cd Length: 214 Bit Score: 46.11 E-value: 8.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 6 MLAMILAGGRGTRLEGLTKKVAKPAVAFGGKyRIIDFPLSNCANSGI-DIVGVLTQYEPVLLNSYVAQSQrwgLDVQGSG 84
Cdd:cd04198 1 FQAVILAGGGGSRLYPLTDNIPKALLPVANK-PMIWYPLDWLEKAGFeDVIVVVPEEEQAEISTYLRSFP---LNLKQKL 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2507226545 85 IFVLPPSEKiegfglYKGTADAITqnidFIDLHDPEYVLILSGDHIYKMNYDKLLDTHiqNEADATIAV 153
Cdd:cd04198 77 DEVTIVLDE------DMGTADSLR----HIRKKIKKDFLVLSCDLITDLPLIELVDLH--RSHDASLTV 133
|
|
| GT2_BcE_like |
cd04183 |
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ... |
98-197 |
4.43e-05 |
|
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.
Pssm-ID: 133026 [Multi-domain] Cd Length: 231 Bit Score: 44.17 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 98 GLYKGTADAITQNIDFIDLHDPeyVLILSGDHIYKMNYDKLLDTHIQNEADAtiAVIEVPlKEASRFGIMNTDKDYRIEE 177
Cdd:cd04183 79 GETLGAACTVLLAADLIDNDDP--LLIFNCDQIVESDLLAFLAAFRERDLDG--GVLTFF-SSHPRWSYVKLDENGRVIE 153
|
90 100
....*....|....*....|
gi 2507226545 178 FEEKpaKPKSNLASMGIYIF 197
Cdd:cd04183 154 TAEK--EPISDLATAGLYYF 171
|
|
| LbH_G1P_AT_C_like |
cd03356 |
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
286-355 |
1.23e-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: 40.30 E-value: 1.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2507226545 286 VIGTSATVRSAYIDKGATIDglveHSVISTDAQVQKGASVKNSVILPGAIIGEDVDL-DYVIVAENIKIAD 355
Cdd:cd03356 13 IIKNSVIGDNVRIGDGVTIT----NSILMDNVTIGANSVIVDSIIGDNAVIGENVRVvNLCIIGDDVVVED 79
|
|
| LbH_G1P_AT_C_like |
cd03356 |
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
312-373 |
2.42e-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: 39.15 E-value: 2.42e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2507226545 312 VISTDAQVQKGASVKNSVILPGAIIGEDVDLDYVIVAENIKIADGTKLAGTpdqilLIDKNV 373
Cdd:cd03356 1 LIGESTVIGENAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDS-----IIGDNA 57
|
|
| LbH_eIF2B_epsilon |
cd05787 |
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
307-359 |
3.30e-03 |
|
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.
Pssm-ID: 100061 [Multi-domain] Cd Length: 79 Bit Score: 36.02 E-value: 3.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2507226545 307 LVEHSVISTDAQVQKGASVKNSVILPGAIIGEDVDLDYVIVAENIKIADGTKL 359
Cdd:cd05787 13 TIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTI 65
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
102-358 |
3.65e-03 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 39.04 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 102 GTADAITQNIDFIDLHDpEYVLILSGDH--IYKMNYDKLLDTHIQNEADATI--AVIEVPlkeasrFG----IMNTDKDY 173
Cdd:PRK14354 77 GTGHAVMQAEEFLADKE-GTTLVICGDTplITAETLKNLIDFHEEHKAAATIltAIAENP------TGygriIRNENGEV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 174 -RIeeFEEKPAKP---KSNLASMGIYIFTWKTLRKYLledDKLDTSSHDfGH----DIIPKYLADGRRLYAHPFRGYWKD 245
Cdd:PRK14354 150 eKI--VEQKDATEeekQIKEINTGTYCFDNKALFEAL---KKISNDNAQ-GEyyltDVIEILKNEGEKVGAYQTEDFEES 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 246 VGtVNSlwesnmdlidhagDLDLSDAS----WRIYSEDSGSPAQVIGTSATvrsaYIDKGATI--DGLVE---------- 309
Cdd:PRK14354 224 LG-VND-------------RVALAEAEkvmrRRINEKHMVNGVTIIDPEST----YIDADVEIgsDTVIEpgvvikgntv 285
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2507226545 310 ---------HSVIsTDAQVQKGASVKNSVIL-----------------PGAIIGEDVDL-DYVIVaENIKIADGTK 358
Cdd:PRK14354 286 igedcvigpGSRI-VDSTIGDGVTITNSVIEeskvgdnvtvgpfahlrPGSVIGEEVKIgNFVEI-KKSTIGEGTK 359
|
|
| LbH_eIF2B_epsilon |
cd05787 |
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
287-338 |
5.04e-03 |
|
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.
Pssm-ID: 100061 [Multi-domain] Cd Length: 79 Bit Score: 35.63 E-value: 5.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2507226545 287 IGTSATVRSAYIDKGATI-DG-LVEHSVISTDAQVQKGASVKNSVILP-GAIIGE 338
Cdd:cd05787 25 IGKNVVIDNSYIWDDVTIeDGcTIHHSIVADGAVIGKGCTIPPGSLISfGVVIGD 79
|
|
| glmU |
PRK14359 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-206 |
5.82e-03 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237689 [Multi-domain] Cd Length: 430 Bit Score: 38.43 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 4 NKMLAMILAGGRGTRLEGLTKKVAKPAVAFGGKYRIID--FPLSncansgiDIVGVLTQYEPVLLNSYVaqsQRWGLDVq 81
Cdd:PRK14359 1 MKLSIIILAAGKGTRMKSSLPKVLHTICGKPMLFYILKeaFAIS-------DDVHVVLHHQKERIKEAV---LEYFPGV- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 82 gsgIFVLPPSEKiegfglYKGTADAITQ-NIDFidlhdpEYVLILSGDH--IYKMNYDKLLDthiqNEADATIAVIEvpL 158
Cdd:PRK14359 70 ---IFHTQDLEN------YPGTGGALMGiEPKH------ERVLILNGDMplVEKDELEKLLE----NDADIVMSVFH--L 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2507226545 159 KEASRFG--IMNTDKDYRIeeFEEKPAKP---KSNLASMGIYIFTWKTLRKYL 206
Cdd:PRK14359 129 ADPKGYGrvVIENGQVKKI--VEQKDANEeelKIKSVNAGVYLFDRKLLEEYL 179
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
8-153 |
6.33e-03 |
|
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.
Pssm-ID: 463715 [Multi-domain] Cd Length: 159 Bit Score: 37.17 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507226545 8 AMILAGGRGTRLEGltkkvAKPAVAFGGKyRIIDFPLSNCANSGIDIVgVLTQYEPVLlnsyvaqsqrwgLDVQGSGIFV 87
Cdd:pfam12804 1 AVILAGGRSSRMGG-----DKALLPLGGK-PLLERVLERLRPAGDEVV-VVANDEEVL------------AALAGLGVPV 61
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2507226545 88 LPpsEKIEGFGLYKGTADAITQnidfidLHDPEYVLILSGDHIY--KMNYDKLLDTHIQNEADATIAV 153
Cdd:pfam12804 62 VP--DPDPGQGPLAGLLAALRA------APGADAVLVLACDMPFltPELLRRLLAAAEESGADIVVPV 121
|
|
| LbH_G1P_AT_C_like |
cd03356 |
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
297-359 |
6.93e-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: 35.30 E-value: 6.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2507226545 297 YIDKGATI--DGLVEHSVISTDAQVQKGASVKNSVILPGAIIGEDVDLDYVIVAENIKIADGTKL 359
Cdd:cd03356 1 LIGESTVIgeNAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRV 65
|
|
| LbH_eIF2B_gamma_C |
cd04652 |
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
286-358 |
7.35e-03 |
|
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.
Pssm-ID: 100057 [Multi-domain] Cd Length: 81 Bit Score: 35.25 E-value: 7.35e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2507226545 286 VIGTSATvrsayIDKGATIDGlvehSVISTDAQVQKGASVKNSVILPGAIIGEDVDLDYVIVAENIKIADGTK 358
Cdd:cd04652 18 VIGANCK-----IGKRVKITN----CVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEAGTE 81
|
|
| |
