|
Name |
Accession |
Description |
Interval |
E-value |
| glgD |
TIGR02092 |
glucose-1-phosphate adenylyltransferase, GlgD subunit; This family is GlgD, an apparent ... |
4-380 |
0e+00 |
|
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: 556.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 4 EQVSAIINLLEPSDALQSLTAVRPVGMLPFGGRYRLVDFQLSSVINAGIQNVMVTVP-RSGRSVADHLRSGRDWSLNTIR 82
Cdd:TIGR02092 1 NKMSAIINLTESSKNLSPLTKVRPLASLPFGGRYRLIDFPLSNMVNAGIRNVFIFFKnKERQSLFDHLGSGREWDLHRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 83 GGLFLSPYNDLKLVAPEKkaallHHYYDNSIQFLKCSQSEYSVVMSTRNVGNIDLKALLRYHEERNSPVTAVYKRVDPAS 162
Cdd:TIGR02092 81 DGLFVFPYNDRDDLSEGG-----KRYFSQNLEFLKRSTSEYTVVLNSHMVCNIDLKAVLKYHEETGKDITVVYKKVKPAD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 163 LIPENTILQLTAKGEATAVVpmskaKISPKTKQVAKSMAIYLMSTVDLIELLQSANQRGDMISLEELMRQAVIQHNANAF 242
Cdd:TIGR02092 156 ASEYDTILRFDESGKVKSIG-----QNLNPEEEENISLDIYIVSTDLLIELLYECIQRGKLTSLEELIRENLKELNINAY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 243 EYTGFQANIHDINSYFAANMAVLDEANFRALFYSSR-RIYTKVKNEIPTFFATGSQCRDSLCGTGGYIEGQLDHSVIFRD 321
Cdd:TIGR02092 231 EYTGYLANINSVKSYYKANMDLLDPQNFQSLFYSSQgPIYTKVKDEPPTYYAENSKVENSLVANGCIIEGKVENSILSRG 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2046703000 322 VLINRDSQVKNAIIMQGARIGAGCKLENVIIDKDAVIGPNLVLKGTSTTPLVISKGQHV 380
Cdd:TIGR02092 311 VHVGKDALIKNCIIMQRTVIGEGAHLENVIIDKDVVIEPNVKIAGTSEQPLVISKGTVV 369
|
|
| GlgC |
COG0448 |
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
5-379 |
4.93e-112 |
|
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];
Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 332.43 E-value: 4.93e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 5 QVSAIINLLEPSDALQSLTAVRPVGMLPFGGRYRLVDFQLSSVINAGIQNVMVTVPRSGRSVADHLRSGRDWSLNTIRGG 84
Cdd:COG0448 1 KVLAIILAGGRGSRLGPLTKDRAKPAVPFGGKYRIIDFPLSNCVNSGIRRVGVLTQYKSHSLNDHIGSGKPWDLDRKRGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 85 LFLSPYNDLKlVAPEKKAALLHHYYDNsIQFLKCSQSEYSVVMSTRNVGNIDLKALLRYHEERNSPVTAVYKRVdPASLI 164
Cdd:COG0448 81 VFILPPYQQR-EGEDWYQGTADAVYQN-LDFIERSDPDYVLILSGDHIYKMDYRQMLDFHIESGADITVACIEV-PREEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 165 PENTILQLTAKGEATAVVpmskakISPKTKQVAK-SMAIYLMSTVDLIELLQSANQRGDMISLEELMRQAVIQHNANAFE 243
Cdd:COG0448 158 SRFGVMEVDEDGRITEFE------EKPKDPKSALaSMGIYVFNKDVLIELLEEDAPNSSHDFGKDIIPRLLDRGKVYAYE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 244 YTGFQANIHDINSYFAANMAVLDEANFRALFYSSRRIYTKVKNEIPTFFATGSQCRDSLCGTGGYIEGQLDHSVIFRDVL 323
Cdd:COG0448 232 FDGYWRDVGTIDSYYEANMDLLDPEPEFNLYDPEWPIYTKQKDLPPAKFVRGGKVKNSLVSNGCIISGTVENSVLFRGVR 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2046703000 324 INRDSQVKNAIIMQGARIGAGCKLENVIIDKDAVIGPNLVLkGT-----------STTPLVISKGQH 379
Cdd:COG0448 312 VESGAVVENSVIMPGVVIGEGAVIENAIIDKNVVIPPGVVI-GEdpeedrkrftvSSGIVVVGKGAV 377
|
|
| ADP_Glucose_PP |
cd02508 |
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ... |
8-251 |
2.04e-65 |
|
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: 206.62 E-value: 2.04e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 8 AIINLLEPSDALQSLTAVRPVGMLPFGGRYRLVDFQLSSVINAGIQNVMVTVPRSGRSVADHLRSGRDWSLNTIRGGLFL 87
Cdd:cd02508 1 AIILAGGEGTRLSPLTKKRAKPAVPFGGRYRLIDFPLSNMVNSGIRNVGVLTQYKSRSLNDHLGSGKEWDLDRKNGGLFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 88 SPYNDLKlvAPEKKAALLHHYYDNSIQFLKCSQsEYSVVMSTRNVGNIDLKALLRYHEERNSPVTAVYKrvdpaslipen 167
Cdd:cd02508 81 LPPQQRK--GGDWYRGTADAIYQNLDYIERSDP-EYVLILSGDHIYNMDYREMLDFHIESGADITVVYK----------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 168 tilqltakgeatavvpmskakispktkqvaKSMAIYLMSTVDLIELLQSANQRGDMISLEELMRQAVIQHNANAFEYTGF 247
Cdd:cd02508 147 ------------------------------ASMGIYIFSKDLLIELLEEDAADGSHDFGKDIIPAMLKKLKIYAYEFNGY 196
|
....
gi 2046703000 248 QANI 251
Cdd:cd02508 197 WADI 200
|
|
| glgC |
PRK05293 |
glucose-1-phosphate adenylyltransferase; Provisional |
32-380 |
6.37e-42 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 151.17 E-value: 6.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 32 PFGGRYRLVDFQLSSVINAGIQNVMVTVPRSGRSVADHLRSGRDWSLNTIRGGL-FLSPYNDLKLVAPEKKAAllHHYYD 110
Cdd:PRK05293 30 PFGGKYRIIDFTLSNCANSGIDTVGVLTQYQPLELNNHIGIGSPWDLDRINGGVtILPPYSESEGGKWYKGTA--HAIYQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 111 NsIQFLKCSQSEYSVVMSTRNVGNIDLKALLRYHEERNSPVT-AVYK-RVDPASLI------PENTILQLTAKgeatavv 182
Cdd:PRK05293 108 N-IDYIDQYDPEYVLILSGDHIYKMDYDKMLDYHKEKEADVTiAVIEvPWEEASRFgimntdENMRIVEFEEK------- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 183 pmskakisPKT-KQVAKSMAIYLMSTVDLIELLQSANQRG--------DMI--SLEElmrqaviQHNANAFEYTGFQANI 251
Cdd:PRK05293 180 --------PKNpKSNLASMGIYIFNWKRLKEYLIEDEKNPnsshdfgkNVIplYLEE-------GEKLYAYPFKGYWKDV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 252 HDINSYFAANMAVLDEANFRALFYSSRRIYTKVKNEIPTFFATGSQCRDSLCGTGGYIEGQLDHSVIFRDVLINRDSQVK 331
Cdd:PRK05293 245 GTIESLWEANMELLRPENPLNLFDRNWRIYSVNPNLPPQYIAENAKVKNSLVVEGCVVYGTVEHSVLFQGVQVGEGSVVK 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2046703000 332 NAIIMQGARIGAGCKLENVIIDKDAVIGPNLVLKGTSTTPLVISKGQHV 380
Cdd:PRK05293 325 DSVIMPGAKIGENVVIERAIIGENAVIGDGVIIGGGKEVITVIGENEVI 373
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
22-265 |
4.53e-09 |
|
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: 56.49 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 22 LTAVRPVGMLPFGGRYRLVDFQLSSVINAGIQN-VMVTVPRSGRSVADHLRSGRDWSLNTirgglflspyndLKLVAPEK 100
Cdd:pfam00483 16 LTRTLAKPLVPVGGKYPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFGVQI------------TYALQPEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 101 KAALlhhyyDNSIQFLKCSQSEYS--VVMSTRNVGNIDLKALLRYHEERNSPVTAVY--KRVDPAS---LI---PENTIL 170
Cdd:pfam00483 84 KGTA-----PAVALAADFLGDEKSdvLVLGGDHIYRMDLEQAVKFHIEKAADATVTFgiVPVEPPTgygVVefdDNGRVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 171 QLTAKgeatavvPmSKAKISPKTkqvakSMAIYLMST---VDLIELLQSANQRGDMIS------LEELMRQAVIQHNANA 241
Cdd:pfam00483 159 RFVEK-------P-KLPKASNYA-----SMGIYIFNSgvlDFLAKYLEELKRGEDEITdilpkaLEDGKLAYAFIFKGYA 225
|
250 260
....*....|....*....|....
gi 2046703000 242 FEYTGfqanihDINSYFAANMAVL 265
Cdd:pfam00483 226 WLDVG------TWDSLWEANLFLL 243
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| glgD |
TIGR02092 |
glucose-1-phosphate adenylyltransferase, GlgD subunit; This family is GlgD, an apparent ... |
4-380 |
0e+00 |
|
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: 556.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 4 EQVSAIINLLEPSDALQSLTAVRPVGMLPFGGRYRLVDFQLSSVINAGIQNVMVTVP-RSGRSVADHLRSGRDWSLNTIR 82
Cdd:TIGR02092 1 NKMSAIINLTESSKNLSPLTKVRPLASLPFGGRYRLIDFPLSNMVNAGIRNVFIFFKnKERQSLFDHLGSGREWDLHRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 83 GGLFLSPYNDLKLVAPEKkaallHHYYDNSIQFLKCSQSEYSVVMSTRNVGNIDLKALLRYHEERNSPVTAVYKRVDPAS 162
Cdd:TIGR02092 81 DGLFVFPYNDRDDLSEGG-----KRYFSQNLEFLKRSTSEYTVVLNSHMVCNIDLKAVLKYHEETGKDITVVYKKVKPAD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 163 LIPENTILQLTAKGEATAVVpmskaKISPKTKQVAKSMAIYLMSTVDLIELLQSANQRGDMISLEELMRQAVIQHNANAF 242
Cdd:TIGR02092 156 ASEYDTILRFDESGKVKSIG-----QNLNPEEEENISLDIYIVSTDLLIELLYECIQRGKLTSLEELIRENLKELNINAY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 243 EYTGFQANIHDINSYFAANMAVLDEANFRALFYSSR-RIYTKVKNEIPTFFATGSQCRDSLCGTGGYIEGQLDHSVIFRD 321
Cdd:TIGR02092 231 EYTGYLANINSVKSYYKANMDLLDPQNFQSLFYSSQgPIYTKVKDEPPTYYAENSKVENSLVANGCIIEGKVENSILSRG 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2046703000 322 VLINRDSQVKNAIIMQGARIGAGCKLENVIIDKDAVIGPNLVLKGTSTTPLVISKGQHV 380
Cdd:TIGR02092 311 VHVGKDALIKNCIIMQRTVIGEGAHLENVIIDKDVVIEPNVKIAGTSEQPLVISKGTVV 369
|
|
| GlgC |
COG0448 |
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
5-379 |
4.93e-112 |
|
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];
Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 332.43 E-value: 4.93e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 5 QVSAIINLLEPSDALQSLTAVRPVGMLPFGGRYRLVDFQLSSVINAGIQNVMVTVPRSGRSVADHLRSGRDWSLNTIRGG 84
Cdd:COG0448 1 KVLAIILAGGRGSRLGPLTKDRAKPAVPFGGKYRIIDFPLSNCVNSGIRRVGVLTQYKSHSLNDHIGSGKPWDLDRKRGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 85 LFLSPYNDLKlVAPEKKAALLHHYYDNsIQFLKCSQSEYSVVMSTRNVGNIDLKALLRYHEERNSPVTAVYKRVdPASLI 164
Cdd:COG0448 81 VFILPPYQQR-EGEDWYQGTADAVYQN-LDFIERSDPDYVLILSGDHIYKMDYRQMLDFHIESGADITVACIEV-PREEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 165 PENTILQLTAKGEATAVVpmskakISPKTKQVAK-SMAIYLMSTVDLIELLQSANQRGDMISLEELMRQAVIQHNANAFE 243
Cdd:COG0448 158 SRFGVMEVDEDGRITEFE------EKPKDPKSALaSMGIYVFNKDVLIELLEEDAPNSSHDFGKDIIPRLLDRGKVYAYE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 244 YTGFQANIHDINSYFAANMAVLDEANFRALFYSSRRIYTKVKNEIPTFFATGSQCRDSLCGTGGYIEGQLDHSVIFRDVL 323
Cdd:COG0448 232 FDGYWRDVGTIDSYYEANMDLLDPEPEFNLYDPEWPIYTKQKDLPPAKFVRGGKVKNSLVSNGCIISGTVENSVLFRGVR 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2046703000 324 INRDSQVKNAIIMQGARIGAGCKLENVIIDKDAVIGPNLVLkGT-----------STTPLVISKGQH 379
Cdd:COG0448 312 VESGAVVENSVIMPGVVIGEGAVIENAIIDKNVVIPPGVVI-GEdpeedrkrftvSSGIVVVGKGAV 377
|
|
| ADP_Glucose_PP |
cd02508 |
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ... |
8-251 |
2.04e-65 |
|
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: 206.62 E-value: 2.04e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 8 AIINLLEPSDALQSLTAVRPVGMLPFGGRYRLVDFQLSSVINAGIQNVMVTVPRSGRSVADHLRSGRDWSLNTIRGGLFL 87
Cdd:cd02508 1 AIILAGGEGTRLSPLTKKRAKPAVPFGGRYRLIDFPLSNMVNSGIRNVGVLTQYKSRSLNDHLGSGKEWDLDRKNGGLFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 88 SPYNDLKlvAPEKKAALLHHYYDNSIQFLKCSQsEYSVVMSTRNVGNIDLKALLRYHEERNSPVTAVYKrvdpaslipen 167
Cdd:cd02508 81 LPPQQRK--GGDWYRGTADAIYQNLDYIERSDP-EYVLILSGDHIYNMDYREMLDFHIESGADITVVYK----------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 168 tilqltakgeatavvpmskakispktkqvaKSMAIYLMSTVDLIELLQSANQRGDMISLEELMRQAVIQHNANAFEYTGF 247
Cdd:cd02508 147 ------------------------------ASMGIYIFSKDLLIELLEEDAADGSHDFGKDIIPAMLKKLKIYAYEFNGY 196
|
....
gi 2046703000 248 QANI 251
Cdd:cd02508 197 WADI 200
|
|
| glgC |
PRK05293 |
glucose-1-phosphate adenylyltransferase; Provisional |
32-380 |
6.37e-42 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 151.17 E-value: 6.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 32 PFGGRYRLVDFQLSSVINAGIQNVMVTVPRSGRSVADHLRSGRDWSLNTIRGGL-FLSPYNDLKLVAPEKKAAllHHYYD 110
Cdd:PRK05293 30 PFGGKYRIIDFTLSNCANSGIDTVGVLTQYQPLELNNHIGIGSPWDLDRINGGVtILPPYSESEGGKWYKGTA--HAIYQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 111 NsIQFLKCSQSEYSVVMSTRNVGNIDLKALLRYHEERNSPVT-AVYK-RVDPASLI------PENTILQLTAKgeatavv 182
Cdd:PRK05293 108 N-IDYIDQYDPEYVLILSGDHIYKMDYDKMLDYHKEKEADVTiAVIEvPWEEASRFgimntdENMRIVEFEEK------- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 183 pmskakisPKT-KQVAKSMAIYLMSTVDLIELLQSANQRG--------DMI--SLEElmrqaviQHNANAFEYTGFQANI 251
Cdd:PRK05293 180 --------PKNpKSNLASMGIYIFNWKRLKEYLIEDEKNPnsshdfgkNVIplYLEE-------GEKLYAYPFKGYWKDV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 252 HDINSYFAANMAVLDEANFRALFYSSRRIYTKVKNEIPTFFATGSQCRDSLCGTGGYIEGQLDHSVIFRDVLINRDSQVK 331
Cdd:PRK05293 245 GTIESLWEANMELLRPENPLNLFDRNWRIYSVNPNLPPQYIAENAKVKNSLVVEGCVVYGTVEHSVLFQGVQVGEGSVVK 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2046703000 332 NAIIMQGARIGAGCKLENVIIDKDAVIGPNLVLKGTSTTPLVISKGQHV 380
Cdd:PRK05293 325 DSVIMPGAKIGENVVIERAIIGENAVIGDGVIIGGGKEVITVIGENEVI 373
|
|
| glgC |
PRK00844 |
glucose-1-phosphate adenylyltransferase; Provisional |
19-361 |
4.48e-28 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 113.77 E-value: 4.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 19 LQSLTAVRPVGMLPFGGRYRLVDFQLSSVINAGIQNVMVTVPRSGRSVADHLRSGrdWSLNTIRGGlFLSPyndlklVAP 98
Cdd:PRK00844 19 LMPLTADRAKPAVPFGGSYRLIDFVLSNLVNSGYLRIYVLTQYKSHSLDRHISQT--WRLSGLLGN-YITP------VPA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 99 EKKaaLLHHYYDNS-------IQFLKCSQSEYSVVMSTRNVGNIDLKALLRYHEERNSPVTAVYKRVdPASLIPENTILQ 171
Cdd:PRK00844 90 QQR--LGKRWYLGSadaiyqsLNLIEDEDPDYVVVFGADHVYRMDPRQMVDFHIESGAGVTVAAIRV-PREEASAFGVIE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 172 LTAKGEATAVVpmSKAKiSPKT-----KQVAKSMAIYLMSTVDLIELLQ--SANQR------GDMISleelmrQAVIQHN 238
Cdd:PRK00844 167 VDPDGRIRGFL--EKPA-DPPGlpddpDEALASMGNYVFTTDALVDALRrdAADEDsshdmgGDIIP------RLVERGR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 239 ANAFEYT-----GFQANIHD-------INSYFAANMAVLDE-ANFRaLFYSSRRIYTKVKNEIPTFFATGSQCR----DS 301
Cdd:PRK00844 238 AYVYDFStnevpGATERDRGywrdvgtIDAYYDAHMDLLSVhPVFN-LYNREWPIYTSSPNLPPAKFVDGGGRVgsaqDS 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2046703000 302 LCGTGGYIEG-QLDHSVIFRDVLINRDSQVKNAIIMQGARIGAGCKLENVIIDKDAVIGPN 361
Cdd:PRK00844 317 LVSAGSIISGaTVRNSVLSPNVVVESGAEVEDSVLMDGVRIGRGAVVRRAILDKNVVVPPG 377
|
|
| LbH_G1P_AT_C |
cd04651 |
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ... |
289-380 |
8.35e-28 |
|
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: 105.24 E-value: 8.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 289 PTFFATGSQCRDSLCGTGGYIE-GQLDHSVIFRDVLINRDSQVKNAIIMQGARIGAGCKLENVIIDKDAVIGPNLVLKG- 366
Cdd:cd04651 1 PPYIGRRGEVKNSLVSEGCIISgGTVENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIPDGVVIGGd 80
|
90 100
....*....|....*....|....
gi 2046703000 367 ----------TSTTPLVISKGQHV 380
Cdd:cd04651 81 peedrarfyvTEDGIVVVGKGMVI 104
|
|
| PLN02241 |
PLN02241 |
glucose-1-phosphate adenylyltransferase |
6-364 |
3.48e-17 |
|
glucose-1-phosphate adenylyltransferase
Pssm-ID: 215133 [Multi-domain] Cd Length: 436 Bit Score: 82.60 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 6 VSAIINLLEPSDALQSLTAVRPVGMLPFGGRYRLVDFQLSSVINAGIQNVMV-T--------------------VPRSGR 64
Cdd:PLN02241 4 VAAIILGGGAGTRLFPLTKRRAKPAVPIGGNYRLIDIPMSNCINSGINKIYVlTqfnsaslnrhlsraynfgngGNFGDG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 65 SV----ADHLRSGRDWSLNT---IRggLFLSPYNDLKLVAPEkkaallhHYydnsiqflkcsqseysVVMSTRNVGNIDL 137
Cdd:PLN02241 84 FVevlaATQTPGEKGWFQGTadaVR--QFLWLFEDAKNKNVE-------EV----------------LILSGDHLYRMDY 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 138 KALLRYHEERNSPVTAVYKRVD--PAS------LIPENTILQLTAKGEA---------TAVVPMSKAKisPKTKQVAKSM 200
Cdd:PLN02241 139 MDFVQKHRESGADITIACLPVDesRASdfglmkIDDTGRIIEFSEKPKGdelkamqvdTTVLGLSPEE--AKEKPYIASM 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 201 AIYLMSTVDLIELLQS----ANQRGdmislEELMRQAV-IQHNANAFEYTGFQANIHDINSYFAANMAVLDE-ANFRalF 274
Cdd:PLN02241 217 GIYVFKKDVLLKLLRWrfptANDFG-----SEIIPGAIkEGYNVQAYLFDGYWEDIGTIKSFYEANLALTKQpPKFS--F 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 275 Y-SSRRIYTKVKNEIPTFFaTGSQCRDSLCGTGGYIEG-QLDHSVIFRDVLINRDSQVKNAIIMqGAR------------ 340
Cdd:PLN02241 290 YdPDAPIYTSPRFLPPSKI-EDCRITDSIISHGCFLREcKIEHSVVGLRSRIGEGVEIEDTVMM-GADyyeteeeiasll 367
|
410 420 430
....*....|....*....|....*....|..
gi 2046703000 341 --------IGAGCKLENVIIDKDAVIGPNLVL 364
Cdd:PLN02241 368 aegkvpigIGENTKIRNAIIDKNARIGKNVVI 399
|
|
| glgC |
PRK00725 |
glucose-1-phosphate adenylyltransferase; Provisional |
19-363 |
8.48e-17 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234824 [Multi-domain] Cd Length: 425 Bit Score: 81.43 E-value: 8.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 19 LQSLTAVRPVGMLPFGGRYRLVDFQLSSVINAGIQNVMVTVPRSGRSVADHLRSGrdWS-LNTIRGGLFlspyndlKLVA 97
Cdd:PRK00725 29 LKELTDKRAKPAVYFGGKFRIIDFALSNCINSGIRRIGVLTQYKAHSLIRHIQRG--WSfFREELGEFV-------DLLP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 98 PEKKAALLHHY-------YDNsIQFLKCSQSEYSVVMSTRNVGNIDLKALLRYHEERNSPVTAVYKRVDPAslipENT-- 168
Cdd:PRK00725 100 AQQRVDEENWYrgtadavYQN-LDIIRRYDPKYVVILAGDHIYKMDYSRMLADHVESGADCTVACLEVPRE----EASaf 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 169 -ILQLTAKGEATAVV--PMSKAKISPKTKQVAKSMAIYLMSTVDLIELL-QSANQRG-------DMISleelmrQAVIQH 237
Cdd:PRK00725 175 gVMAVDENDRITAFVekPANPPAMPGDPDKSLASMGIYVFNADYLYELLeEDAEDPNsshdfgkDIIP------KIVEEG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 238 NANAFEYTGFQANIHD-----------INSYFAANMAVLDEANFRALFYSSRRIYTKVKNEIPT-FFATGSQCR----DS 301
Cdd:PRK00725 249 KVYAHPFSDSCVRSDPeeepywrdvgtLDAYWQANLDLASVTPELDLYDRNWPIWTYQEQLPPAkFVFDRSGRRgmaiNS 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2046703000 302 LCGTGGYIEG-QLDHSVIFRDVLINRDSQVKNAIIMQGARIGAGCKLENVIIDKDAVIGPNLV 363
Cdd:PRK00725 329 LVSGGCIISGaVVRRSVLFSRVRVNSFSNVEDSVLLPDVNVGRSCRLRRCVIDRGCVIPEGMV 391
|
|
| glgC |
PRK02862 |
glucose-1-phosphate adenylyltransferase; Provisional |
19-366 |
2.33e-16 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179486 [Multi-domain] Cd Length: 429 Bit Score: 80.31 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 19 LQSLTAVRPVGMLPFGGRYRLVDFQLSSVINAGIQNVMVTVPRSGRSVADHLRsgRDWSLNTIRGGlFLSpyndlKLVA- 97
Cdd:PRK02862 17 LYPLTKLRAKPAVPLAGKYRLIDIPISNCINSGINKIYVLTQFNSASLNRHIS--QTYNFDGFSGG-FVE-----VLAAq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 98 --PEKKA-------AL---LHHYYDNSIqflkcsqsEYSVVMSTRNVGNIDLKALLRYHEERNSPVTAVYKRVDPASlIP 165
Cdd:PRK02862 89 qtPENPSwfqgtadAVrkyLWHFQEWDV--------DEYLILSGDQLYRMDYRLFVQHHRETGADITLAVLPVDEKD-AS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 166 ENTILQLTAKGEATAV-------------VPMSKAKISP---KTKQVAKSMAIYLMSTVDLIELLQSANQRGDMisLEEL 229
Cdd:PRK02862 160 GFGLMKTDDDGRITEFsekpkgdelkamaVDTSRLGLSPeeaKGKPYLASMGIYVFSRDVLFDLLNKNPEYTDF--GKEI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 230 MRQAVIQHNANAFEYTGFQANIHDINSYFAANMAVLDEANFRALFYSSRR-IYTKVKNEIPTFFaTGSQCRDSLCGTGGY 308
Cdd:PRK02862 238 IPEAIRDYKVQSYLFDGYWEDIGTIEAFYEANLALTQQPNPPFSFYDEKApIYTRARYLPPSKL-LDATITESIIAEGCI 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2046703000 309 IEG-QLDHSVIFRDVLINRDSQVKNAIIMqGAR--------------------IGAGCKLENVIIDKDAVIGPNLVLKG 366
Cdd:PRK02862 317 IKNcSIHHSVLGIRSRIESGCTIEDTLVM-GADfyesseereelrkegkpplgIGEGTTIKRAIIDKNARIGNNVRIVN 394
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
19-266 |
1.38e-10 |
|
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: 60.94 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 19 LQSLTAVRPVGMLPFGGRyRLVDFQLSSVINAGIQNVMVTVPRSGRSVADHLRSGRDWSLNtIRgglflspyndlklVAP 98
Cdd:COG1208 13 LRPLTDTRPKPLLPVGGK-PLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVR-IT-------------YVD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 99 EKKA-----ALLhhyydNSIQFLKcsqSEYSVVMSTRNVGNIDLKALLRYHEERNSPVTAVYKRVDPASlipENTILQLT 173
Cdd:COG1208 78 EGEPlgtggALK-----RALPLLG---DEPFLVLNGDILTDLDLAALLAFHREKGADATLALVPVPDPS---RYGVVELD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 174 AKGEATAVVPMSKAKISPKTkqvakSMAIYLMSTvDLIELLqsanQRGDMISLEELMRQAVIQHNANAFEYTGFQANIHD 253
Cdd:COG1208 147 GDGRVTRFVEKPEEPPSNLI-----NAGIYVLEP-EIFDYI----PEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGT 216
|
250
....*....|...
gi 2046703000 254 INSYFAANMAVLD 266
Cdd:COG1208 217 PEDLLEANALLLS 229
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
22-265 |
4.53e-09 |
|
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: 56.49 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 22 LTAVRPVGMLPFGGRYRLVDFQLSSVINAGIQN-VMVTVPRSGRSVADHLRSGRDWSLNTirgglflspyndLKLVAPEK 100
Cdd:pfam00483 16 LTRTLAKPLVPVGGKYPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFGVQI------------TYALQPEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 101 KAALlhhyyDNSIQFLKCSQSEYS--VVMSTRNVGNIDLKALLRYHEERNSPVTAVY--KRVDPAS---LI---PENTIL 170
Cdd:pfam00483 84 KGTA-----PAVALAADFLGDEKSdvLVLGGDHIYRMDLEQAVKFHIEKAADATVTFgiVPVEPPTgygVVefdDNGRVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2046703000 171 QLTAKgeatavvPmSKAKISPKTkqvakSMAIYLMST---VDLIELLQSANQRGDMIS------LEELMRQAVIQHNANA 241
Cdd:pfam00483 159 RFVEK-------P-KLPKASNYA-----SMGIYIFNSgvlDFLAKYLEELKRGEDEITdilpkaLEDGKLAYAFIFKGYA 225
|
250 260
....*....|....*....|....
gi 2046703000 242 FEYTGfqanihDINSYFAANMAVL 265
Cdd:pfam00483 226 WLDVG------TWDSLWEANLFLL 243
|
|
| LbH_eIF2B_gamma_C |
cd04652 |
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
315-366 |
1.06e-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: 49.11 E-value: 1.06e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2046703000 315 HSVIFRDVLINRDSQVKNAIIMQGARIGAGCKLENVIIDKDAVIGPNLVLKG 366
Cdd:cd04652 16 RSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKD 67
|
|
| LbH_G1P_AT_C_like |
cd03356 |
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
314-380 |
1.20e-07 |
|
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: 48.78 E-value: 1.20e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2046703000 314 DHSVIFRDVLINRDSQVKNAIIMQGARIGAGCKLENVIIDKDAVIGPNLVLKGTSttplVISKGQHV 380
Cdd:cd03356 15 KNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNLC----IIGDDVVV 77
|
|
| LbH_G1P_AT_C_like |
cd03356 |
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
312-360 |
2.23e-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: 2.23e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2046703000 312 QLDHSVIFRDVLINRDSQVKNAIIMQGARIGAGCKLEN-VIIDKDAVIGP 360
Cdd:cd03356 30 TITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNlCIIGDDVVVED 79
|
|
| LbH_eIF2B_epsilon |
cd05787 |
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ... |
299-365 |
1.87e-05 |
|
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.
Pssm-ID: 100061 [Multi-domain] Cd Length: 79 Bit Score: 42.57 E-value: 1.87e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2046703000 299 RDSLCGTGGYIEgqldHSVIFRDVLINRDSQVKNAIIMQGARIGAGCKLENVIIDKDAVIGPNLVLK 365
Cdd:cd05787 4 RGTSIGEGTTIK----NSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIP 66
|
|
| LbH_G1P_AT_C_like |
cd03356 |
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ... |
317-367 |
7.72e-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: 37.99 E-value: 7.72e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2046703000 317 VIFRDVLINRDSQVKNAIIMQGARIGAGCKLENVIIDKDAVIGPNLVLKGT 367
Cdd:cd03356 1 LIGESTVIGENAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDS 51
|
|
| glmU |
PRK09451 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
311-368 |
6.81e-03 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 181867 [Multi-domain] Cd Length: 456 Bit Score: 38.47 E-value: 6.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2046703000 311 GQLDHSvifRDVLInrDSQVknaiIMQG-------ARIGAGCKLENVIIDKDAVIGPNLVLKGTS 368
Cdd:PRK09451 264 GTLTHG---RDVEI--DTNV----IIEGnvtlgnrVKIGAGCVLKNCVIGDDCEISPYSVVEDAN 319
|
|
| LpxD |
COG1044 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ... |
332-364 |
7.05e-03 |
|
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis
Pssm-ID: 440666 [Multi-domain] Cd Length: 335 Bit Score: 38.07 E-value: 7.05e-03
10 20 30
....*....|....*....|....*....|....
gi 2046703000 332 NAIIMQGARIGAGCKLE-NVIIDKDAVIGPNLVL 364
Cdd:COG1044 120 FAVIGAGVVIGDGVVIGpGVVIGDGVVIGDDCVL 153
|
|
| |
