|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
10-962 |
0e+00 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 1781.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 10 EYSALLSLSCGPI---------TRRRFAVSCRARPPgNLSAQQKKKRGKNIAPKQRSSNAKLLLTTEENGQLPSTSLRTS 80
Cdd:PLN02939 5 ESAALLSHGCGPIrsrapfylpSRRRLAVSCRARRR-GFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 81 MERPQKSTSSEDDTNGAISQIDEKIAAIGNEQQEvlPYWGGHILIS------------AYQDILLLNQARLQAIEDVDKI 148
Cdd:PLN02939 84 MELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQT--NSKDGEQLSDfqledlvgmiqnAEKNILLLNQARLQALEDLEKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 149 LTEKEALQKKVDTLEMNLSKA-----LATKGNINTDIPGDHLEKFTKEILIESALSGGnpahlCESPLFMELTVLKEENM 223
Cdd:PLN02939 162 LTEKEALQGKINILEMRLSETdarikLAAQEKIHVEILEEQLEKLRNELLIRGATEGL-----CVHSLSKELDVLKEENM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 224 LLKADAQFLKAKIVEFAETEEFLFKLEKERSLLDATVRELEARFLVAQTDIWKVVPLQYDVWMEKVENLQHMLGCLKNHV 303
Cdd:PLN02939 237 LLKDDIQFLKAELIEVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 304 EKYAALLDQHDDLHDKIDELEASLKEGKTSEFSPYVVELLQQKLKAAKSHHQAGHQETNTHIQVYQQLTEEFQDNLGKLI 383
Cdd:PLN02939 317 EKAALVLDQNQDLRDKVDKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 384 EESGR--LEHSANSMPSEFWSHILLMIDGWFLERKIPNTDARMLREMAWKRDDRICEAYFACKGAKESDVMETFLKLSLS 461
Cdd:PLN02939 397 EESKKrsLEHPADDMPSEFWSRILLLIDGWLLEKKISNNDAKLLREMVWKRDGRIREAYLSCKGKNEREAVENFLKLTLS 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 462 GNSSGLHIVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCMQLDQITNLKVLDVVIQSYFDGNLFSNNV 541
Cdd:PLN02939 477 GTSSGLHIVHIAAEMAPVAKVGGLADVVSGLGKALQKKGHLVEIVLPKYDCMQYDQIRNLKVLDVVVESYFDGNLFKNKI 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 542 WTGTVEGLPVYFIEPQHPSKFFWRAQYYGEHDDFKRYSYFSRAALELLYQSGKKIDIIHCHDWQTAFVAPLYWDIYATRG 621
Cdd:PLN02939 557 WTGTVEGLPVYFIEPQHPSKFFWRAQYYGEHDDFKRFSYFSRAALELLYQSGKKPDIIHCHDWQTAFVAPLYWDLYAPKG 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 622 FSSARICFTCHNFEYQGTAPAPDLSYCGLDVEQLDRPDRMQDNAHGRINVAKGGIVYSNIVTTVSPTYALEVRSEGGRGL 701
Cdd:PLN02939 637 FNSARICFTCHNFEYQGTAPASDLASCGLDVHQLDRPDRMQDNAHGRINVVKGAIVYSNIVTTVSPTYAQEVRSEGGRGL 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 702 QDTLKMHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATDLQGKAANKAFLRKQLGLYSEDASQPLVACITRLVPQKGLHL 781
Cdd:PLN02939 717 QDTLKFHSKKFVGILNGIDTDTWNPSTDRFLKVQYNANDLQGKAANKAALRKQLGLSSADASQPLVGCITRLVPQKGVHL 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 782 IRHAIYKTAELGGQFVLLGSSPVPHIQREFEGVADQFQKNNNIRLILKYDEALSHCIYAASDMFIIPSMFEPCGLTQMIA 861
Cdd:PLN02939 797 IRHAIYKTAELGGQFVLLGSSPVPHIQREFEGIADQFQSNNNIRLILKYDEALSHSIYAASDMFIIPSMFEPCGLTQMIA 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 862 MRYGSVPIVRQTGGLCDSVFDFDDETIPVELRNGFTFARTDEQDLSSCLERAFSYYSRKPMVWKQLVQKDMQIDFSWDSP 941
Cdd:PLN02939 877 MRYGSVPIVRKTGGLNDSVFDFDDETIPVELRNGFTFLTPDEQGLNSALERAFNYYKRKPEVWKQLVQKDMNIDFSWDSS 956
|
970 980
....*....|....*....|.
gi 262345759 942 ASQYENLYQSAVAQARGAAQT 962
Cdd:PLN02939 957 ASQYEELYQRAVARARAAANR 977
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
467-952 |
0e+00 |
|
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) synthases that use ADP-glucose (EC 2.4.1.21), rather than UDP-glucose (EC 2.4.1.11) as in animals, as the glucose donor. This enzyme is found in bacteria and plants. Whether the name given is glycogen synthase or starch synthase depends on context, and therefore on substrate. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
Pssm-ID: 273969 [Multi-domain] Cd Length: 473 Bit Score: 603.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 467 LHIVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCMQLDQITNLKVLDVVIQSYFDGNLFsNNVWTGTV 546
Cdd:TIGR02095 1 MRVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEVDDQVKVVELVDLSVGPRTLY-VKVFEGVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 547 EGLPVYFIEPQHpskFFWR-AQYYGE--HDDFKRYSYFSRAALELLYQSGKKIDIIHCHDWQTAFVAPLYWDIYatrGFS 623
Cdd:TIGR02095 80 EGVPVYFIDNPS---LFDRpGGIYGDdyPDNAERFAFFSRAAAELLSGLGWQPDVVHAHDWHTALVPALLKAVY---RPN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 624 SARICFTCHNFEYQGTAPAPDLSYCGLDveqldrPDRMQDNA---HGRINVAKGGIVYSNIVTTVSPTYALEVR-SEGGR 699
Cdd:TIGR02095 154 PIKTVFTIHNLAYQGVFPADDFSELGLP------PEYFHMEGlefYGRVNFLKGGIVYADRVTTVSPTYAREILtPEFGY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 700 GLQDTLKMHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATDLQGKAANKAFLRKQLGLySEDASQPLVACITRLVPQKGL 779
Cdd:TIGR02095 228 GLDGVLKARSGKLRGILNGIDTEVWNPATDPYLKANYSADDLAGKAENKEALQEELGL-PVDDDVPLFGVISRLTQQKGV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 780 HLIRHAIYKTAELGGQFVLLGSSPvPHIQREFEGVAdqFQKNNNIRLILKYDEALSHCIYAASDMFIIPSMFEPCGLTQM 859
Cdd:TIGR02095 307 DLLLAALPELLELGGQLVVLGTGD-PELEEALRELA--ERYPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 860 IAMRYGSVPIVRQTGGLCDSVFDFDDETipvELRNGFTFARTDEQDLSSCLERAFSYYSRKPMVWKQLVQKDMQIDFSWD 939
Cdd:TIGR02095 384 YAMRYGTVPIVRRTGGLADTVVDGDPEA---ESGTGFLFEEYDPGALLAALSRALRLYRQDPSLWEALQKNAMSQDFSWD 460
|
490
....*....|...
gi 262345759 940 SPASQYENLYQSA 952
Cdd:TIGR02095 461 KSAKQYVELYRSL 473
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
468-951 |
0e+00 |
|
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.
Pssm-ID: 340822 [Multi-domain] Cd Length: 474 Bit Score: 597.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 468 HIVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCMQLDQITNLKVLDVVIqsYFDGNLFSNNVWTGTVE 547
Cdd:cd03791 1 KVLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRVLGLEV--KVGGRGEEVGVFELPVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 548 GLPVYFIEPQHPSKFFWR--AQYYGEHDDFKRYSYFSRAALELLYQSGKKIDIIHCHDWQTAFVAPLYWDIYATRGFSSA 625
Cdd:cd03791 79 GVDYYFLDNPEFFDRPGLpgPPGYDYPDNAERFAFFSRAALELLRRLGFQPDIIHANDWHTALVPAYLKTRYRGPGFKKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 626 RICFTCHNFEYQGTAPAPDLSYCGLDvEQLDRPDRMQDnaHGRINVAKGGIVYSNIVTTVSPTYALEV-RSEGGRGLQDT 704
Cdd:cd03791 159 KTVFTIHNLAYQGLFPLDTLAELGLP-PELFHIDGLEF--YGQINFLKAGIVYADRVTTVSPTYAKEIlTPEYGEGLDGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 705 LKMHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATDLQGKAANKAFLRKQLGLySEDASQPLVACITRLVPQKGLHLIRH 784
Cdd:cd03791 236 LRARAGKLSGILNGIDYDEWNPATDKLIPANYSANDLEGKAENKAALQKELGL-PVDPDAPLFGFVGRLTEQKGVDLILD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 785 AIYKTAELGGQFVLLGSSPVPHIQREFEgVADQFqkNNNIRLILKYDEALSHCIYAASDMFIIPSMFEPCGLTQMIAMRY 864
Cdd:cd03791 315 ALPELLEEGGQLVVLGSGDPEYEQAFRE-LAERY--PGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYAMRY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 865 GSVPIVRQTGGLCDSVFDFDDETipvELRNGFTFARTDEQDLSSCLERAFSYYsRKPMVWKQLVQKDMQIDFSWDSPASQ 944
Cdd:cd03791 392 GTLPIVRRTGGLADTVFDYDPET---GEGTGFVFEDYDAEALLAALRRALALY-RNPELWRKLQKNAMKQDFSWDKSAKE 467
|
....*..
gi 262345759 945 YENLYQS 951
Cdd:cd03791 468 YLELYRS 474
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
467-952 |
0e+00 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 595.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 467 LHIVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCMqLDQITNLKVLDVvIQSYFDGNLFSNNVWTGTV 546
Cdd:COG0297 1 MKILFVASEAAPFAKTGGLADVVGALPKALAKLGHDVRVVLPGYPSI-DDKLKDLEVVAS-LEVPLGGRTYYARVLEGPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 547 EGLPVYFIEpqHPSkFFWRAQYYGE-----HDDFKRYSYFSRAALELLYQSGKKIDIIHCHDWQTAFVAPLYWDIYATRG 621
Cdd:COG0297 79 DGVPVYFID--NPE-LFDRPGPYGDpdrdyPDNAERFAFFSRAALELLKGLDWKPDIIHCHDWQTGLIPALLKTRYADDP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 622 FSSARICFTCHNFEYQGTAPAPDLSYCGLDvEQLDRPDRMQDnaHGRINVAKGGIVYSNIVTTVSPTYALEVRS-EGGRG 700
Cdd:COG0297 156 FKRIKTVFTIHNLAYQGIFPAEILELLGLP-PELFTPDGLEF--YGQINFLKAGIVYADRVTTVSPTYAREIQTpEFGEG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 701 LQDTLKMHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATDLQGKAANKAFLRKQLGLySEDASQPLVACITRLVPQKGLH 780
Cdd:COG0297 233 LDGLLRARSGKLSGILNGIDYDVWNPATDPYLPANYSADDLEGKAANKAALQEELGL-PVDPDAPLIGMVSRLTEQKGLD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 781 LIRHAIYKTAELGGQFVLLGSSPvPHIQREFEGVADQFqkNNNIRLILKYDEALSHCIYAASDMFIIPSMFEPCGLTQMI 860
Cdd:COG0297 312 LLLEALDELLEEDVQLVVLGSGD-PEYEEAFRELAARY--PGRVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQMY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 861 AMRYGSVPIVRQTGGLCDSVFDFDDETipvELRNGFTFARTDEQDLSSCLERAFSYYsRKPMVWKQLVQKDMQIDFSWDS 940
Cdd:COG0297 389 ALRYGTVPIVRRTGGLADTVIDYNEAT---GEGTGFVFDEYTAEALLAAIRRALALY-RDPEAWRKLQRNAMKQDFSWEK 464
|
490
....*....|..
gi 262345759 941 PASQYENLYQSA 952
Cdd:COG0297 465 SAKEYLELYREL 476
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
469-706 |
1.54e-77 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 253.02 E-value: 1.54e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 469 IVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCMQLDQITNLKVLDVVIQSYFDGNLFSNNVWTGTVEG 548
Cdd:pfam08323 1 ILFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGNIPEERNQLEDVIRLSVAAGVPVRPLTVGVARLELDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 549 LPVYFIEPQHpskFFWRAQYYGE-----HDDFKRYSYFSRAALELLYQSGKKIDIIHCHDWQTAFVAPLYWDIYATRGFS 623
Cdd:pfam08323 81 VDVYFLDNPD---YFDRPGLYGDdgrdyEDNAERFAFFSRAALELAKKLGWIPDIIHCHDWHTALVPAYLKEAYADDPFK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 624 SARICFTCHNFEYQGTAPAPDLSYCGLDVEQLDrPDRMQDnaHGRINVAKGGIVYSNIVTTVSPTYALEVRS-EGGRGLQ 702
Cdd:pfam08323 158 NIKTVFTIHNLAYQGRFPADLLDLLGLPPEDFN-LDGLEF--YGQINFLKAGIVYADAVTTVSPTYAEEIQTpEFGGGLD 234
|
....
gi 262345759 703 DTLK 706
Cdd:pfam08323 235 GLLR 238
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
10-962 |
0e+00 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 1781.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 10 EYSALLSLSCGPI---------TRRRFAVSCRARPPgNLSAQQKKKRGKNIAPKQRSSNAKLLLTTEENGQLPSTSLRTS 80
Cdd:PLN02939 5 ESAALLSHGCGPIrsrapfylpSRRRLAVSCRARRR-GFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 81 MERPQKSTSSEDDTNGAISQIDEKIAAIGNEQQEvlPYWGGHILIS------------AYQDILLLNQARLQAIEDVDKI 148
Cdd:PLN02939 84 MELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQT--NSKDGEQLSDfqledlvgmiqnAEKNILLLNQARLQALEDLEKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 149 LTEKEALQKKVDTLEMNLSKA-----LATKGNINTDIPGDHLEKFTKEILIESALSGGnpahlCESPLFMELTVLKEENM 223
Cdd:PLN02939 162 LTEKEALQGKINILEMRLSETdarikLAAQEKIHVEILEEQLEKLRNELLIRGATEGL-----CVHSLSKELDVLKEENM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 224 LLKADAQFLKAKIVEFAETEEFLFKLEKERSLLDATVRELEARFLVAQTDIWKVVPLQYDVWMEKVENLQHMLGCLKNHV 303
Cdd:PLN02939 237 LLKDDIQFLKAELIEVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 304 EKYAALLDQHDDLHDKIDELEASLKEGKTSEFSPYVVELLQQKLKAAKSHHQAGHQETNTHIQVYQQLTEEFQDNLGKLI 383
Cdd:PLN02939 317 EKAALVLDQNQDLRDKVDKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 384 EESGR--LEHSANSMPSEFWSHILLMIDGWFLERKIPNTDARMLREMAWKRDDRICEAYFACKGAKESDVMETFLKLSLS 461
Cdd:PLN02939 397 EESKKrsLEHPADDMPSEFWSRILLLIDGWLLEKKISNNDAKLLREMVWKRDGRIREAYLSCKGKNEREAVENFLKLTLS 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 462 GNSSGLHIVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCMQLDQITNLKVLDVVIQSYFDGNLFSNNV 541
Cdd:PLN02939 477 GTSSGLHIVHIAAEMAPVAKVGGLADVVSGLGKALQKKGHLVEIVLPKYDCMQYDQIRNLKVLDVVVESYFDGNLFKNKI 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 542 WTGTVEGLPVYFIEPQHPSKFFWRAQYYGEHDDFKRYSYFSRAALELLYQSGKKIDIIHCHDWQTAFVAPLYWDIYATRG 621
Cdd:PLN02939 557 WTGTVEGLPVYFIEPQHPSKFFWRAQYYGEHDDFKRFSYFSRAALELLYQSGKKPDIIHCHDWQTAFVAPLYWDLYAPKG 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 622 FSSARICFTCHNFEYQGTAPAPDLSYCGLDVEQLDRPDRMQDNAHGRINVAKGGIVYSNIVTTVSPTYALEVRSEGGRGL 701
Cdd:PLN02939 637 FNSARICFTCHNFEYQGTAPASDLASCGLDVHQLDRPDRMQDNAHGRINVVKGAIVYSNIVTTVSPTYAQEVRSEGGRGL 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 702 QDTLKMHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATDLQGKAANKAFLRKQLGLYSEDASQPLVACITRLVPQKGLHL 781
Cdd:PLN02939 717 QDTLKFHSKKFVGILNGIDTDTWNPSTDRFLKVQYNANDLQGKAANKAALRKQLGLSSADASQPLVGCITRLVPQKGVHL 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 782 IRHAIYKTAELGGQFVLLGSSPVPHIQREFEGVADQFQKNNNIRLILKYDEALSHCIYAASDMFIIPSMFEPCGLTQMIA 861
Cdd:PLN02939 797 IRHAIYKTAELGGQFVLLGSSPVPHIQREFEGIADQFQSNNNIRLILKYDEALSHSIYAASDMFIIPSMFEPCGLTQMIA 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 862 MRYGSVPIVRQTGGLCDSVFDFDDETIPVELRNGFTFARTDEQDLSSCLERAFSYYSRKPMVWKQLVQKDMQIDFSWDSP 941
Cdd:PLN02939 877 MRYGSVPIVRKTGGLNDSVFDFDDETIPVELRNGFTFLTPDEQGLNSALERAFNYYKRKPEVWKQLVQKDMNIDFSWDSS 956
|
970 980
....*....|....*....|.
gi 262345759 942 ASQYENLYQSAVAQARGAAQT 962
Cdd:PLN02939 957 ASQYEELYQRAVARARAAANR 977
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
467-952 |
0e+00 |
|
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) synthases that use ADP-glucose (EC 2.4.1.21), rather than UDP-glucose (EC 2.4.1.11) as in animals, as the glucose donor. This enzyme is found in bacteria and plants. Whether the name given is glycogen synthase or starch synthase depends on context, and therefore on substrate. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
Pssm-ID: 273969 [Multi-domain] Cd Length: 473 Bit Score: 603.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 467 LHIVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCMQLDQITNLKVLDVVIQSYFDGNLFsNNVWTGTV 546
Cdd:TIGR02095 1 MRVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEVDDQVKVVELVDLSVGPRTLY-VKVFEGVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 547 EGLPVYFIEPQHpskFFWR-AQYYGE--HDDFKRYSYFSRAALELLYQSGKKIDIIHCHDWQTAFVAPLYWDIYatrGFS 623
Cdd:TIGR02095 80 EGVPVYFIDNPS---LFDRpGGIYGDdyPDNAERFAFFSRAAAELLSGLGWQPDVVHAHDWHTALVPALLKAVY---RPN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 624 SARICFTCHNFEYQGTAPAPDLSYCGLDveqldrPDRMQDNA---HGRINVAKGGIVYSNIVTTVSPTYALEVR-SEGGR 699
Cdd:TIGR02095 154 PIKTVFTIHNLAYQGVFPADDFSELGLP------PEYFHMEGlefYGRVNFLKGGIVYADRVTTVSPTYAREILtPEFGY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 700 GLQDTLKMHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATDLQGKAANKAFLRKQLGLySEDASQPLVACITRLVPQKGL 779
Cdd:TIGR02095 228 GLDGVLKARSGKLRGILNGIDTEVWNPATDPYLKANYSADDLAGKAENKEALQEELGL-PVDDDVPLFGVISRLTQQKGV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 780 HLIRHAIYKTAELGGQFVLLGSSPvPHIQREFEGVAdqFQKNNNIRLILKYDEALSHCIYAASDMFIIPSMFEPCGLTQM 859
Cdd:TIGR02095 307 DLLLAALPELLELGGQLVVLGTGD-PELEEALRELA--ERYPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 860 IAMRYGSVPIVRQTGGLCDSVFDFDDETipvELRNGFTFARTDEQDLSSCLERAFSYYSRKPMVWKQLVQKDMQIDFSWD 939
Cdd:TIGR02095 384 YAMRYGTVPIVRRTGGLADTVVDGDPEA---ESGTGFLFEEYDPGALLAALSRALRLYRQDPSLWEALQKNAMSQDFSWD 460
|
490
....*....|...
gi 262345759 940 SPASQYENLYQSA 952
Cdd:TIGR02095 461 KSAKQYVELYRSL 473
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
468-951 |
0e+00 |
|
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.
Pssm-ID: 340822 [Multi-domain] Cd Length: 474 Bit Score: 597.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 468 HIVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCMQLDQITNLKVLDVVIqsYFDGNLFSNNVWTGTVE 547
Cdd:cd03791 1 KVLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRVLGLEV--KVGGRGEEVGVFELPVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 548 GLPVYFIEPQHPSKFFWR--AQYYGEHDDFKRYSYFSRAALELLYQSGKKIDIIHCHDWQTAFVAPLYWDIYATRGFSSA 625
Cdd:cd03791 79 GVDYYFLDNPEFFDRPGLpgPPGYDYPDNAERFAFFSRAALELLRRLGFQPDIIHANDWHTALVPAYLKTRYRGPGFKKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 626 RICFTCHNFEYQGTAPAPDLSYCGLDvEQLDRPDRMQDnaHGRINVAKGGIVYSNIVTTVSPTYALEV-RSEGGRGLQDT 704
Cdd:cd03791 159 KTVFTIHNLAYQGLFPLDTLAELGLP-PELFHIDGLEF--YGQINFLKAGIVYADRVTTVSPTYAKEIlTPEYGEGLDGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 705 LKMHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATDLQGKAANKAFLRKQLGLySEDASQPLVACITRLVPQKGLHLIRH 784
Cdd:cd03791 236 LRARAGKLSGILNGIDYDEWNPATDKLIPANYSANDLEGKAENKAALQKELGL-PVDPDAPLFGFVGRLTEQKGVDLILD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 785 AIYKTAELGGQFVLLGSSPVPHIQREFEgVADQFqkNNNIRLILKYDEALSHCIYAASDMFIIPSMFEPCGLTQMIAMRY 864
Cdd:cd03791 315 ALPELLEEGGQLVVLGSGDPEYEQAFRE-LAERY--PGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYAMRY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 865 GSVPIVRQTGGLCDSVFDFDDETipvELRNGFTFARTDEQDLSSCLERAFSYYsRKPMVWKQLVQKDMQIDFSWDSPASQ 944
Cdd:cd03791 392 GTLPIVRRTGGLADTVFDYDPET---GEGTGFVFEDYDAEALLAALRRALALY-RNPELWRKLQKNAMKQDFSWDKSAKE 467
|
....*..
gi 262345759 945 YENLYQS 951
Cdd:cd03791 468 YLELYRS 474
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
467-952 |
0e+00 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 595.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 467 LHIVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCMqLDQITNLKVLDVvIQSYFDGNLFSNNVWTGTV 546
Cdd:COG0297 1 MKILFVASEAAPFAKTGGLADVVGALPKALAKLGHDVRVVLPGYPSI-DDKLKDLEVVAS-LEVPLGGRTYYARVLEGPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 547 EGLPVYFIEpqHPSkFFWRAQYYGE-----HDDFKRYSYFSRAALELLYQSGKKIDIIHCHDWQTAFVAPLYWDIYATRG 621
Cdd:COG0297 79 DGVPVYFID--NPE-LFDRPGPYGDpdrdyPDNAERFAFFSRAALELLKGLDWKPDIIHCHDWQTGLIPALLKTRYADDP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 622 FSSARICFTCHNFEYQGTAPAPDLSYCGLDvEQLDRPDRMQDnaHGRINVAKGGIVYSNIVTTVSPTYALEVRS-EGGRG 700
Cdd:COG0297 156 FKRIKTVFTIHNLAYQGIFPAEILELLGLP-PELFTPDGLEF--YGQINFLKAGIVYADRVTTVSPTYAREIQTpEFGEG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 701 LQDTLKMHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATDLQGKAANKAFLRKQLGLySEDASQPLVACITRLVPQKGLH 780
Cdd:COG0297 233 LDGLLRARSGKLSGILNGIDYDVWNPATDPYLPANYSADDLEGKAANKAALQEELGL-PVDPDAPLIGMVSRLTEQKGLD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 781 LIRHAIYKTAELGGQFVLLGSSPvPHIQREFEGVADQFqkNNNIRLILKYDEALSHCIYAASDMFIIPSMFEPCGLTQMI 860
Cdd:COG0297 312 LLLEALDELLEEDVQLVVLGSGD-PEYEEAFRELAARY--PGRVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQMY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 861 AMRYGSVPIVRQTGGLCDSVFDFDDETipvELRNGFTFARTDEQDLSSCLERAFSYYsRKPMVWKQLVQKDMQIDFSWDS 940
Cdd:COG0297 389 ALRYGTVPIVRRTGGLADTVIDYNEAT---GEGTGFVFDEYTAEALLAAIRRALALY-RDPEAWRKLQRNAMKQDFSWEK 464
|
490
....*....|..
gi 262345759 941 PASQYENLYQSA 952
Cdd:COG0297 465 SAKEYLELYREL 476
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
467-955 |
0e+00 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 594.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 467 LHIVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCMqLDQITNLKVldvviqsyfDGNLFSNNVWTGTV 546
Cdd:PRK00654 1 MKILFVASECAPLIKTGGLGDVVGALPKALAALGHDVRVLLPGYPAI-REKLRDAQV---------VGRLDLFTVLFGHL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 547 E--GLPVYFIEPQHpskFFWRAQYYGEHDDFKRYSYFSRAALELLYQSGKKIDIIHCHDWQTAFVAPLYWDIYAtRGFSS 624
Cdd:PRK00654 71 EgdGVPVYLIDAPH---LFDRPSGYGYPDNGERFAFFSWAAAEFAEGLDPRPDIVHAHDWHTGLIPALLKEKYW-RGYPD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 625 ARICFTCHNFEYQGTAPAPDLSYCGLDVEQLdRPDRMQDnaHGRINVAKGGIVYSNIVTTVSPTYALEVR-SEGGRGLQD 703
Cdd:PRK00654 147 IKTVFTIHNLAYQGLFPAEILGELGLPAEAF-HLEGLEF--YGQISFLKAGLYYADRVTTVSPTYAREITtPEFGYGLEG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 704 TLKMHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATDLQGKAANKAFLRKQLGLYSEDAsqPLVACITRLVPQKGLHLIR 783
Cdd:PRK00654 224 LLRARSGKLSGILNGIDYDIWNPETDPLLAANYSADDLEGKAENKRALQERFGLPDDDA--PLFAMVSRLTEQKGLDLVL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 784 HAIYKTAELGGQFVLLGSsPVPHIQREFEGVADQFqkNNNIRLILKYDEALSHCIYAASDMFIIPSMFEPCGLTQMIAMR 863
Cdd:PRK00654 302 EALPELLEQGGQLVLLGT-GDPELEEAFRALAARY--PGKVGVQIGYDEALAHRIYAGADMFLMPSRFEPCGLTQLYALR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 864 YGSVPIVRQTGGLCDSVFDFDDETipvELRNGFTFARTDEQDLSSCLERAFSYYSRKPmVWKQLVQKDMQIDFSWDSPAS 943
Cdd:PRK00654 379 YGTLPIVRRTGGLADTVIDYNPED---GEATGFVFDDFNAEDLLRALRRALELYRQPP-LWRALQRQAMAQDFSWDKSAE 454
|
490
....*....|..
gi 262345759 944 QYENLYQSAVAQ 955
Cdd:PRK00654 455 EYLELYRRLLGK 466
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
467-952 |
9.28e-149 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 467.81 E-value: 9.28e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 467 LHIVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCMQLDQITNLKVLdvviQSYFDGNLfSNNVWTGTV 546
Cdd:PLN02316 588 MHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHNVDIILPKYDCLNLSHVKDLHYQ----RSYSWGGT-EIKVWFGKV 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 547 EGLPVYFIEPQhpSKFFWRAQYYGEHDDFKRYSYFSRAALELLYQSGKKIDIIHCHDWQTAFVAPLYWDIYATRGFSSAR 626
Cdd:PLN02316 663 EGLSVYFLEPQ--NGMFWAGCVYGCRNDGERFGFFCHAALEFLLQSGFHPDIIHCHDWSSAPVAWLFKDHYAHYGLSKAR 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 627 ICFTCHNFEYqgtapapdlsycgldveqldrpdrmqdnahGRINVAKGgIVYSNIVTTVSPTYALEVRSEGgrglqdTLK 706
Cdd:PLN02316 741 VVFTIHNLEF------------------------------GANHIGKA-MAYADKATTVSPTYSREVSGNS------AIA 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 707 MHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATD-LQGKAANKAFLRKQLGLYSEDAsqPLVACITRLVPQKGLHLIRHA 785
Cdd:PLN02316 784 PHLYKFHGILNGIDPDIWDPYNDNFIPVPYTSENvVEGKRAAKEALQQRLGLKQADL--PLVGIITRLTHQKGIHLIKHA 861
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 786 IYKTAELGGQFVLLGSSPVPHIQREFEGVADQFQKNNN--IRLILKYDEALSHCIYAASDMFIIPSMFEPCGLTQMIAMR 863
Cdd:PLN02316 862 IWRTLERNGQVVLLGSAPDPRIQNDFVNLANQLHSSHHdrARLCLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLTAMR 941
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 864 YGSVPIVRQTGGLCDSVFDFDDETIPVELR----NGFTFARTDEQDLSSCLERAFS--YYSRKpmvW-KQLVQKDMQIDF 936
Cdd:PLN02316 942 YGSIPVVRKTGGLFDTVFDVDHDKERAQAQglepNGFSFDGADAAGVDYALNRAISawYDGRD---WfNSLCKRVMEQDW 1018
|
490
....*....|....*.
gi 262345759 937 SWDSPASQYENLYQSA 952
Cdd:PLN02316 1019 SWNRPALDYMELYHSA 1034
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
465-957 |
2.03e-86 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 285.84 E-value: 2.03e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 465 SGLHIVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCM--QLDQITNLKVLDvviqSYFDGNlfsNNVW 542
Cdd:PRK14099 2 TPLRVLSVASEIFPLIKTGGLADVAGALPAALKAHGVEVRTLVPGYPAVlaGIEDAEQVHSFP----DLFGGP---ARLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 543 TGTVEGLPVYFIEPQHpskFFWRA--QYYGEH-----DDFKRYSYFSRAALELLYQS--GKKIDIIHCHDWQTAFV-APL 612
Cdd:PRK14099 75 AARAGGLDLFVLDAPH---LYDRPgnPYVGPDgkdwpDNAQRFAALARAAAAIGQGLvpGFVPDIVHAHDWQAGLApAYL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 613 YWDiyatrGFSSARICFTCHNFEYQGTAPAPDLSYCGL-----DVEQLDRpdrmqdnaHGRINVAKGGIVYSNIVTTVSP 687
Cdd:PRK14099 152 HYS-----GRPAPGTVFTIHNLAFQGQFPRELLGALGLppsafSLDGVEY--------YGGIGYLKAGLQLADRITTVSP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 688 TYALEVRS-EGGRGLQDTLKMHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATDLQGKAANKAFLRKQLGLYSEDASqPL 766
Cdd:PRK14099 219 TYALEIQGpEAGMGLDGLLRQRADRLSGILNGIDTAVWNPATDELIAATYDVETLAARAANKAALQARFGLDPDPDA-LL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 767 VACITRLVPQKGLHLIRHAIYKTAELGGQFVLLGSSPvPHIQREFEGVAdqfQKN-NNIRLILKYDEALSHCIYAASDMF 845
Cdd:PRK14099 298 LGVISRLSWQKGLDLLLEALPTLLGEGAQLALLGSGD-AELEARFRAAA---QAYpGQIGVVIGYDEALAHLIQAGADAL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 846 IIPSMFEPCGLTQMIAMRYGSVPIVRQTGGLCDSVFDFDDETIPVELRNGFTFARTDEQDLSSCLERAFSYYSrKPMVWK 925
Cdd:PRK14099 374 LVPSRFEPCGLTQLCALRYGAVPVVARVGGLADTVVDANEMAIATGVATGVQFSPVTADALAAALRKTAALFA-DPVAWR 452
|
490 500 510
....*....|....*....|....*....|..
gi 262345759 926 QLVQKDMQIDFSWDSPASQYENLYQSAVAQAR 957
Cdd:PRK14099 453 RLQRNGMTTDVSWRNPAQHYAALYRSLVAERR 484
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
469-706 |
1.54e-77 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 253.02 E-value: 1.54e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 469 IVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCMQLDQITNLKVLDVVIQSYFDGNLFSNNVWTGTVEG 548
Cdd:pfam08323 1 ILFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGNIPEERNQLEDVIRLSVAAGVPVRPLTVGVARLELDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 549 LPVYFIEPQHpskFFWRAQYYGE-----HDDFKRYSYFSRAALELLYQSGKKIDIIHCHDWQTAFVAPLYWDIYATRGFS 623
Cdd:pfam08323 81 VDVYFLDNPD---YFDRPGLYGDdgrdyEDNAERFAFFSRAALELAKKLGWIPDIIHCHDWHTALVPAYLKEAYADDPFK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 624 SARICFTCHNFEYQGTAPAPDLSYCGLDVEQLDrPDRMQDnaHGRINVAKGGIVYSNIVTTVSPTYALEVRS-EGGRGLQ 702
Cdd:pfam08323 158 NIKTVFTIHNLAYQGRFPADLLDLLGLPPEDFN-LDGLEF--YGQINFLKAGIVYADAVTTVSPTYAEEIQTpEFGGGLD 234
|
....
gi 262345759 703 DTLK 706
Cdd:pfam08323 235 GLLR 238
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
469-950 |
2.27e-68 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 236.55 E-value: 2.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 469 IVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKY-----------DCMQLDQI-TNLK----VLDVV----- 527
Cdd:PRK14098 8 VLYVSGEVSPFVRVSALADFMASFPQALEEEGFEARIMMPKYgtindrkfrlhDVLRLSDIeVPLKektdLLHVKvtalp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 528 ---IQSYFDGN--LFSNNVWtgtveglpvyFIEPQHpskffwraqyygeHDDFK----RYSYFSRAALELLYQSGKKIDI 598
Cdd:PRK14098 88 sskIQTYFLYNekYFKRNGL----------FTDMSL-------------GGDLKgsaeKVIFFNVGVLETLQRLGWKPDI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 599 IHCHDWQTAFVAPLYWDIYATRGF-SSARICFTCHNFEYQGTAPapdlsycgLDVEQLDRPDRMQDNAH---GRINVAKG 674
Cdd:PRK14098 145 IHCHDWYAGLVPLLLKTVYADHEFfKDIKTVLTIHNVYRQGVLP--------FKVFQKLLPEEVCSGLHregDEVNMLYT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 675 GIVYSNIVTTVSPTYALEVRSEGGR--GLQDTLKMHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATDLQGKAANKAFLR 752
Cdd:PRK14098 217 GVEHADLLTTTSPRYAEEIAGDGEEafGLDKVLEERKMRLHGILNGIDTRQWNPSTDKLIKKRYSIERLDGKLENKKALL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 753 KQLGLySEDASQPLVACITRLVPQKGLHLIRHAIYKTAELGGQFVLLGSSpvphiQREFEGVADQFQKNNNIRLILKYD- 831
Cdd:PRK14098 297 EEVGL-PFDEETPLVGVIINFDDFQGAELLAESLEKLVELDIQLVICGSG-----DKEYEKRFQDFAEEHPEQVSVQTEf 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 832 -EALSHCIYAASDMFIIPSMFEPCGLTQMIAMRYGSVPIVRQTGGLCDSVFDFDDetipvELRNGFTFARTDEQDLSSCL 910
Cdd:PRK14098 371 tDAFFHLAIAGLDMLLMPGKIESCGMLQMFAMSYGTIPVAYAGGGIVETIEEVSE-----DKGSGFIFHDYTPEALVAKL 445
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 262345759 911 ERAFSYYSRKPMvWKQLVQKDMQIDFSWDSPASQYENLYQ 950
Cdd:PRK14098 446 GEALALYHDEER-WEELVLEAMERDFSWKNSAEEYAQLYR 484
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
468-950 |
1.80e-17 |
|
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.
Pssm-ID: 340831 [Multi-domain] Cd Length: 366 Bit Score: 85.28 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 468 HIVHIAAEMAPVakVGGLADVVAGLGKALQTKGHLVEIVLPkydcmqldqitnlkvldvviqsyfdgnlfsnnvwtGTVE 547
Cdd:cd03801 1 KILLLSPELPPP--VGGAERHVRELARALAARGHDVTVLTP-----------------------------------ADPG 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 548 GLPVYFIEPQHPSKFFWRAQYYGEHDDFKRYSYFSRAAlellyqsgkKIDIIHCHDWQTAFVAPLYWdiyatrGFSSARI 627
Cdd:cd03801 44 EPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLRLR---------KFDVVHAHGLLAALLAALLA------LLLGAPL 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 628 CFTCHNFEYQGTAPAPDLSYcgldvEQLDRPDRMQDNAHGRInvakggivysnivtTVSPTYALEVRSEGGRglqdtlkm 707
Cdd:cd03801 109 VVTLHGAEPGRLLLLLAAER-----RLLARAEALLRRADAVI--------------AVSEALRDELRALGGI-------- 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 708 HSRKFVGILNGIDTGTWNPstdrflavqysatdlqgkaankaFLRKQLGLyseDASQPLVACITRLVPQKGLHLIRHAIY 787
Cdd:cd03801 162 PPEKIVVIPNGVDLERFSP-----------------------PLRRKLGI---PPDRPVLLFVGRLSPRKGVDLLLEALA 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 788 KTAELGG--QFVLLGSSP--VPHIQREFEGVADqfqknnNIRLILKYDEALSHCIYAASDMFIIPSMFEPCGLTQMIAMR 863
Cdd:cd03801 216 KLLRRGPdvRLVIVGGDGplRAELEELELGLGD------RVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMA 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 864 YGSVPIVRQTGGLCDSVfdfDDETipvelrNGFTFARTDEQDLSSCLERAFSYysrkPMVWKQLVQ---KDMQIDFSWDS 940
Cdd:cd03801 290 AGLPVVATDVGGLPEVV---EDGE------GGLVVPPDDVEALADALLRLLAD----PELRARLGRaarERVAERFSWER 356
|
490
....*....|
gi 262345759 941 PASQYENLYQ 950
Cdd:cd03801 357 VAERLLDLYR 366
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
818-954 |
6.63e-10 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 57.69 E-value: 6.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 818 FQKNNNIRLILkydEALshciYAASDMFIIPSMFEPCGLTQMIAMRYGSVPIVRQTGGLCDSVFDFDdetipvelrNGFT 897
Cdd:COG0438 4 LVPRKGLDLLL---EAL----LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGE---------TGLL 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 898 FARTDEQDLSSCLERAFSYYSRkpmvWKQLVQ---KDMQIDFSWDSPASQYENLYQSAVA 954
Cdd:COG0438 68 VPPGDPEALAEAILRLLEDPEL----RRRLGEaarERAEERFSWEAIAERLLALYEELLA 123
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
751-947 |
7.76e-10 |
|
sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.
Pssm-ID: 340830 [Multi-domain] Cd Length: 398 Bit Score: 61.87 E-value: 7.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 751 LRKQLGLyseDASQPLVACITRLVPQKGLH-LIRhAIYKTAELGGQFVLL---GSSPVPHIQREFEgvADQFQKNNniRL 826
Cdd:cd03800 210 RRARLLL---PPDKPVVLALGRLDPRKGIDtLVR-AFAQLPELRELANLVlvgGPSDDPLSMDREE--LAELAEEL--GL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 827 ILKYD-------EALSHcIYAASDMFIIPSMFEPCGLTQMIAMRYGsVPIV-RQTGGLCDSVfdfddetipVELRNGFTF 898
Cdd:cd03800 282 IDRVRfpgrvsrDDLPE-LYRAADVFVVPSLYEPFGLTAIEAMACG-TPVVaTAVGGLQDIV---------RDGRTGLLV 350
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 262345759 899 ARTDEQDLSSCLERAFsyysRKPMVWKQLvqKDMQID-----FSWDSPASQYEN 947
Cdd:cd03800 351 DPHDPEALAAALRRLL----DDPALWQRL--SRAGLErarahYTWESVADQLLT 398
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
764-920 |
1.96e-09 |
|
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.
Pssm-ID: 425737 [Multi-domain] Cd Length: 158 Bit Score: 57.28 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 764 QPLVACITRLVPQKGLHLIRHAIYKTAELGGQFVLL--GSSPVphiQREFEGVADQFQKNNNIRLIL-KYDEALSHCiYA 840
Cdd:pfam00534 2 KKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLViaGDGEE---EKRLKKLAEKLGLGDNVIFLGfVSDEDLPEL-LK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 841 ASDMFIIPSMFEPCGLTQMIAMRYGSVPIVRQTGGLCDSVFDFDdetipvelrNGFTFARTDEQDLSSCLERA------- 913
Cdd:pfam00534 78 IADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGE---------TGFLVKPNNAEALAEAIDKLledeelr 148
|
....*....
gi 262345759 914 --FSYYSRK 920
Cdd:pfam00534 149 erLGENARK 157
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
765-912 |
1.96e-09 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 56.75 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 765 PLVACITRLVP-QKGLHLIRHAIY--KTAELGGQFVLLGSSPVPHIQREFEGVADqfqknnNIRLiLKYDEALSHcIYAA 841
Cdd:pfam13692 2 PVILFVGRLHPnVKGVDYLLEAVPllRKRDNDVRLVIVGDGPEEELEELAAGLED------RVIF-TGFVEDLAE-LLAA 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 262345759 842 SDMFIIPSMFEPCGLTQMIAMRYGsVPIV-RQTGGLCDSVFDfddetipvelRNGFTFARTDEQDLSSCLER 912
Cdd:pfam13692 74 ADVFVLPSLYEGFGLKLLEAMAAG-LPVVaTDVGGIPELVDG----------ENGLLVPPGDPEALAEAILR 134
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
769-882 |
3.47e-08 |
|
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340816 [Multi-domain] Cd Length: 235 Bit Score: 55.49 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 769 CITRLVPQKGLHLIRHAI--YKTAELGGQFVLLGSSPVPhiQREFEGVADQFQKNNNIRLILKYDEALSHCIYAASDMFI 846
Cdd:cd01635 115 SVGRLVPEKGIDLLLEALalLKARLPDLVLVLVGGGGER--EEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFV 192
|
90 100 110
....*....|....*....|....*....|....*.
gi 262345759 847 IPSMFEPCGLTQMIAMRYGSVPIVRQTGGLCDSVFD 882
Cdd:cd01635 193 LPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVD 228
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
715-951 |
1.02e-05 |
|
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.
Pssm-ID: 340851 [Multi-domain] Cd Length: 364 Bit Score: 48.87 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 715 ILNGIDTGTWNPstdrflavqysatdlqgkaANKAFLRKQLGLySEDAsqPLVACITRLV--PQKGLH-LIR--HAIYKT 789
Cdd:cd03825 166 IPNGIDTEIFAP-------------------VDKAKARKRLGI-PQDK--KVILFGAESVtkPRKGFDeLIEalKLLATK 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 790 AELGGQFV-----LLGSSPVPHIQREFEgvadqfqkNNNIRLILkydealshcIYAASDMFIIPSMFEPCGLTQMIAMRY 864
Cdd:cd03825 224 DDLLLVVFgkndpQIVILPFDIISLGYI--------DDDEQLVD---------IYSAADLFVHPSLADNLPNTLLEAMAC 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 865 GSVPIVRQTGGLCDSVFDfddetipveLRNGFTFARTDEQDLSS----CLERAFSYYSRkpmvwKQLVQKDMQIDFSWDS 940
Cdd:cd03825 287 GTPVVAFDTGGSPEIVQH---------GVTGYLVPPGDVQALAEaiewLLANPKERESL-----GERARALAENHFDQRV 352
|
250
....*....|.
gi 262345759 941 PASQYENLYQS 951
Cdd:cd03825 353 QAQRYLELYKD 363
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
761-949 |
3.70e-05 |
|
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).
Pssm-ID: 340850 [Multi-domain] Cd Length: 357 Bit Score: 46.94 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 761 DASQPLVAC-ITRLVPQKGLHLIRHAIYKTAELGGQFVLLGSSPVpHIQREFEGVAdqfqknnNIRLI--LKYDEALSHc 837
Cdd:cd03823 187 PGTERLRFGyIGRLTEEKGIDLLVEAFKRLPREDIELVIAGHGPL-SDERQIEGGR-------RIAFLgrVPTDDIKDF- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 838 iYAASDMFIIPSMF-EPCGLTQMIAMRYGSVPIVRQTGGLCDSVfdfddetipVELRNGFTFARTDEQDLSSCLERAfsy 916
Cdd:cd03823 258 -YEKIDVLVVPSIWpEPFGLVVREAIAAGLPVIASDLGGIAELI---------QPGVNGLLFAPGDAEDLAAAMRRL--- 324
|
170 180 190
....*....|....*....|....*....|...
gi 262345759 917 ySRKPMVWKQLvQKDMQIDFSWDSPASQYENLY 949
Cdd:cd03823 325 -LTDPALLERL-RAGAEPPRSTESQAEEYLKLY 355
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
683-880 |
7.71e-05 |
|
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.
Pssm-ID: 340842 [Multi-domain] Cd Length: 365 Bit Score: 46.13 E-value: 7.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 683 TTVSPTYALEVRSEGgRGLQDtlkmhsrkfVGILN-GIDTGTWNPStdrflavqysatdlqgkAANKAFLRKQLglyseD 761
Cdd:cd03814 148 TTLVPSPSIARELEG-HGFER---------VRLWPrGVDTELFHPS-----------------RRDAALRRRLG-----P 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 762 ASQPLVACITRLVPQKGLHLIRHAIYK-TAELGGQFVLLGSSPvphiQREfegvADQFQKNNNIRLILKYDEALSHcIYA 840
Cdd:cd03814 196 PGRPLLLYVGRLAPEKNLEALLDADLPlAASPPVRLVVVGDGP----ARA----ELEARGPDVIFTGFLTGEELAR-AYA 266
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 262345759 841 ASDMFIIPSMFEPCGLTQMIAMRYGsVP-IVRQTGGLCDSV 880
Cdd:cd03814 267 SADVFVFPSRTETFGLVVLEAMASG-LPvVAADAGGPRDIV 306
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
483-721 |
3.82e-04 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 42.13 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 483 GGLADVVAGLGKALQTKGHLVEIVLPKYDcmqldqitnlkvldvviqsyfdgNLFSNNVWTGTVEGLPVYFIEPqhpskf 562
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGP-----------------------GPLAEEVVRVVRVPRVPLPLPP------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 563 fwraqyygehdDFKRYSYFSRAALELLyqSGKKIDIIHCHDWqtafvAPLYWDIYATRGFSSARICFTCHNFEYQGTAPA 642
Cdd:pfam13439 52 -----------RLLRSLAFLRRLRRLL--RRERPDVVHAHSP-----FPLGLAALAARLRLGIPLVVTYHGLFPDYKRLG 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 262345759 643 PDLSYCGLDVEQLDRpdRMQDNAHGrinvakggivysniVTTVSPTyaleVRSEggrgLQDTLKMHSRKFVGILNGIDT 721
Cdd:pfam13439 114 ARLSPLRRLLRRLER--RLLRRADR--------------VIAVSEA----VADE----LRRLYGVPPEKIRVIPNGVDL 168
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
681-870 |
8.77e-04 |
|
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.
Pssm-ID: 340826 [Multi-domain] Cd Length: 355 Bit Score: 42.65 E-value: 8.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 681 IVTTvSPTYALEvrSEggrglqdTLKMHSRKFVGILNGIDtgtwnpstdrflAVQYSATDLQGKAANKAFLRKQLGLYse 760
Cdd:cd03795 141 IIAT-SPNYVET--SP-------TLREFKNKVRVIPLGID------------KNVYNIPRVDFENIKREKKGKKIFLF-- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 761 dasqplvacITRLVPQKGLH-LIRHAIYKTAELggqfVLLGSSPvphIQREFEGVADQfQKNNNIRLILKYDEALSHCIY 839
Cdd:cd03795 197 ---------IGRLVYYKGLDyLIEAAQYLNYPI----VIGGEGP---LKPDLEAQIEL-NLLDNVKFLGRVDDEEKVIYL 259
|
170 180 190
....*....|....*....|....*....|...
gi 262345759 840 AASDMFIIPSMF--EPCGLTQMIAMRYGsVPIV 870
Cdd:cd03795 260 HLCDVFVFPSVLrsEAFGIVLLEAMMCG-KPVI 291
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
838-950 |
1.19e-03 |
|
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.
Pssm-ID: 340859 [Multi-domain] Cd Length: 370 Bit Score: 42.34 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 838 IYAASDMFIIPSMFEPCGLTQMIAMRYGSVPIVRQTGGlcdsvfdfddetIPVELRNGFTFARTDEQDLSSCLERAFSYY 917
Cdd:cd04962 266 LLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGG------------IPEVVKHGETGFLSDVGDVDAMAKSALSIL 333
|
90 100 110
....*....|....*....|....*....|....*.
gi 262345759 918 sRKPMVWKQLVQ---KDMQIDFSWDSPASQYENLYQ 950
Cdd:cd04962 334 -EDDELYNRMGRaarKRAAERFDPERIVPQYEAYYR 368
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
142-390 |
2.36e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 142 IEDVDKILTEKEALQKKVDTLEMNLSKALATKGNINTDIP--GDHLEKFTKEIL-IESalsggnpahlcespLFMELTVL 218
Cdd:PRK03918 178 IERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPelREELEKLEKEVKeLEE--------------LKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 219 KEENMLLKADAQFLKAKIVefaETEEFLFKLEKERSLLDATVRELEARFLVAQTDIwKVVPLqYDVWMEKVENLQHMLGC 298
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIR---ELEERIEELKKEIEELEEKVKELKELKEKAEEYI-KLSEF-YEEYLDELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 299 LKNHVEKYAALLDQHDDLHDKIDELEASLKE--GKTSEFSPYvVELLQ---------QKLKAAKSHHQAGhqETNTHIQV 367
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERLEELKKKLKEleKRLEELEER-HELYEeakakkeelERLKKRLTGLTPE--KLEKELEE 395
|
250 260
....*....|....*....|...
gi 262345759 368 YQQLTEEFQDNLGKLIEESGRLE 390
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELK 418
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
682-870 |
5.32e-03 |
|
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.
Pssm-ID: 340836 [Multi-domain] Cd Length: 362 Bit Score: 40.38 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 682 VTTVSPTYALEVRSEGGRglqdtlkmhSRKFVGILNGIDTGTWNPStdrflavqysatdlqgkAANKAFLRKQLGLyseD 761
Cdd:cd03807 137 TVANSSAVAEFHQEQGYA---------KNKIVVIYNGIDLFKLSPD-----------------DASRARARRRLGL---A 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262345759 762 ASQPLVACITRLVPQKGLHLIRHAIYKTAELGGQ--FVLLGSSPV-PHIQREFE--GVADQFqknnnirLILKYDEALSH 836
Cdd:cd03807 188 EDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDlrLLLVGRGPErPNLERLLLelGLEDRV-------HLLGERSDVPA 260
|
170 180 190
....*....|....*....|....*....|....
gi 262345759 837 CiYAASDMFIIPSMFEPCGLTQMIAMRYGsVPIV 870
Cdd:cd03807 261 L-LPAMDIFVLSSRTEGFPNALLEAMACG-LPVV 292
|
|
| |
