|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
10-975 |
0e+00 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 1823.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 10 EYSALLSLSCGPI---------TRRRFAVSCRARPPgNLSAQQKKKRGKNIAPKQRSSNAKLLLTTEENGQLPSTSLRTS 80
Cdd:PLN02939 5 ESAALLSHGCGPIrsrapfylpSRRRLAVSCRARRR-GFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 81 MERPQKSTSSEDDTNGAISQIDEKIAAIGNEQQERSKDKHFESDFQLEDFGEMIQNMEKNILLLNQARLQAIEDVDKILT 160
Cdd:PLN02939 84 MELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 161 EKEALQKKVDTLEMNLSKA-----LATKGNINTDIPGDHLEKFTKEILIESALSGGnpahlCESPLFMELTVLKEENMLL 235
Cdd:PLN02939 164 EKEALQGKINILEMRLSETdarikLAAQEKIHVEILEEQLEKLRNELLIRGATEGL-----CVHSLSKELDVLKEENMLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 236 KADAQFLKAKIVEFAETEEFLFKLEKERSLLDATVRELEARFLVAQTDIWKVVPLQYDVWMEKVENLQHMLGCLKNHVEK 315
Cdd:PLN02939 239 KDDIQFLKAELIEVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 316 YAALLDQHDDLHDKIDELEASLKEGKTSEFSPYVVELLQQKLKAAKSHHQAGHQETNTHIQVYQQLTEEFQDNLGKLIEE 395
Cdd:PLN02939 319 AALVLDQNQDLRDKVDKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 396 SGR--LEHSANSMPSEFWSHILLMIDGWFLERKIPNTDARMLREMAWKRDDRICEAYFACKGAKESDVMETFLKLSLSGN 473
Cdd:PLN02939 399 SKKrsLEHPADDMPSEFWSRILLLIDGWLLEKKISNNDAKLLREMVWKRDGRIREAYLSCKGKNEREAVENFLKLTLSGT 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 474 SqcsSGLHIVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCMQLDQITNLKVLDVVIQSYFDGNLFSNN 553
Cdd:PLN02939 479 S---SGLHIVHIAAEMAPVAKVGGLADVVSGLGKALQKKGHLVEIVLPKYDCMQYDQIRNLKVLDVVVESYFDGNLFKNK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 554 VWTGTVEGLPVYFIEPQHPSKFFWRAQYYGEHDDFKRYSYFSRAALELLYQSGKKIDIIHCHDWQTAFVAPLYWDIYATR 633
Cdd:PLN02939 556 IWTGTVEGLPVYFIEPQHPSKFFWRAQYYGEHDDFKRFSYFSRAALELLYQSGKKPDIIHCHDWQTAFVAPLYWDLYAPK 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 634 GFSSARICFTCHNFEYQGTAPAPDLSYCGLDVEQLDRPDRMQDNAHGRINVAKGGIVYSNIVTTVSPTYALEVRSEGGRG 713
Cdd:PLN02939 636 GFNSARICFTCHNFEYQGTAPASDLASCGLDVHQLDRPDRMQDNAHGRINVVKGAIVYSNIVTTVSPTYAQEVRSEGGRG 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 714 LQDTLKMHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATDLQGKAANKAFLRKQLGLYSEDASQPLVACITRLVPQKGLH 793
Cdd:PLN02939 716 LQDTLKFHSKKFVGILNGIDTDTWNPSTDRFLKVQYNANDLQGKAANKAALRKQLGLSSADASQPLVGCITRLVPQKGVH 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 794 LIRHAIYKTAELGGQFVLLGSSPVPHIQREFEGVADQFQKNNNIRLILKYDEALSHCIYAASDMFIIPSMFEPCGLTQMI 873
Cdd:PLN02939 796 LIRHAIYKTAELGGQFVLLGSSPVPHIQREFEGIADQFQSNNNIRLILKYDEALSHSIYAASDMFIIPSMFEPCGLTQMI 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 874 AMRYGSVPIVRQTGGLCDSVFDFDDETIPVELRNGFTFARTDEQDLSSCLERAFSYYSRKPMVWKQLVQKDMQIDFSWDS 953
Cdd:PLN02939 876 AMRYGSVPIVRKTGGLNDSVFDFDDETIPVELRNGFTFLTPDEQGLNSALERAFNYYKRKPEVWKQLVQKDMNIDFSWDS 955
|
970 980
....*....|....*....|..
gi 1002230293 954 PASQYENLYQSAVAQARGAAQT 975
Cdd:PLN02939 956 SASQYEELYQRAVARARAAANR 977
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
480-965 |
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: 605.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 480 LHIVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCMQLDQITNLKVLDVVIQSYFDGNLFsNNVWTGTV 559
Cdd:TIGR02095 1 MRVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEVDDQVKVVELVDLSVGPRTLY-VKVFEGVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 560 EGLPVYFIEPQHpskFFWR-AQYYGE--HDDFKRYSYFSRAALELLYQSGKKIDIIHCHDWQTAFVAPLYWDIYatrGFS 636
Cdd:TIGR02095 80 EGVPVYFIDNPS---LFDRpGGIYGDdyPDNAERFAFFSRAAAELLSGLGWQPDVVHAHDWHTALVPALLKAVY---RPN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 637 SARICFTCHNFEYQGTAPAPDLSYCGLDveqldrPDRMQDNA---HGRINVAKGGIVYSNIVTTVSPTYALEVR-SEGGR 712
Cdd:TIGR02095 154 PIKTVFTIHNLAYQGVFPADDFSELGLP------PEYFHMEGlefYGRVNFLKGGIVYADRVTTVSPTYAREILtPEFGY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 713 GLQDTLKMHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATDLQGKAANKAFLRKQLGLySEDASQPLVACITRLVPQKGL 792
Cdd:TIGR02095 228 GLDGVLKARSGKLRGILNGIDTEVWNPATDPYLKANYSADDLAGKAENKEALQEELGL-PVDDDVPLFGVISRLTQQKGV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 793 HLIRHAIYKTAELGGQFVLLGSSPvPHIQREFEGVAdqFQKNNNIRLILKYDEALSHCIYAASDMFIIPSMFEPCGLTQM 872
Cdd:TIGR02095 307 DLLLAALPELLELGGQLVVLGTGD-PELEEALRELA--ERYPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 873 IAMRYGSVPIVRQTGGLCDSVFDFDDETipvELRNGFTFARTDEQDLSSCLERAFSYYSRKPMVWKQLVQKDMQIDFSWD 952
Cdd:TIGR02095 384 YAMRYGTVPIVRRTGGLADTVVDGDPEA---ESGTGFLFEEYDPGALLAALSRALRLYRQDPSLWEALQKNAMSQDFSWD 460
|
490
....*....|...
gi 1002230293 953 SPASQYENLYQSA 965
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 ... |
481-964 |
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 1002230293 481 HIVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCMQLDQITNLKVLDVVIqsYFDGNLFSNNVWTGTVE 560
Cdd:cd03791 1 KVLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRVLGLEV--KVGGRGEEVGVFELPVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 561 GLPVYFIEPQHPSKFFWR--AQYYGEHDDFKRYSYFSRAALELLYQSGKKIDIIHCHDWQTAFVAPLYWDIYATRGFSSA 638
Cdd:cd03791 79 GVDYYFLDNPEFFDRPGLpgPPGYDYPDNAERFAFFSRAALELLRRLGFQPDIIHANDWHTALVPAYLKTRYRGPGFKKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 639 RICFTCHNFEYQGTAPAPDLSYCGLDvEQLDRPDRMQDnaHGRINVAKGGIVYSNIVTTVSPTYALEV-RSEGGRGLQDT 717
Cdd:cd03791 159 KTVFTIHNLAYQGLFPLDTLAELGLP-PELFHIDGLEF--YGQINFLKAGIVYADRVTTVSPTYAKEIlTPEYGEGLDGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 718 LKMHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATDLQGKAANKAFLRKQLGLySEDASQPLVACITRLVPQKGLHLIRH 797
Cdd:cd03791 236 LRARAGKLSGILNGIDYDEWNPATDKLIPANYSANDLEGKAENKAALQKELGL-PVDPDAPLFGFVGRLTEQKGVDLILD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 798 AIYKTAELGGQFVLLGSSPVPHIQREFEgVADQFqkNNNIRLILKYDEALSHCIYAASDMFIIPSMFEPCGLTQMIAMRY 877
Cdd:cd03791 315 ALPELLEEGGQLVVLGSGDPEYEQAFRE-LAERY--PGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYAMRY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 878 GSVPIVRQTGGLCDSVFDFDDETipvELRNGFTFARTDEQDLSSCLERAFSYYsRKPMVWKQLVQKDMQIDFSWDSPASQ 957
Cdd:cd03791 392 GTLPIVRRTGGLADTVFDYDPET---GEGTGFVFEDYDAEALLAALRRALALY-RNPELWRKLQKNAMKQDFSWDKSAKE 467
|
....*..
gi 1002230293 958 YENLYQS 964
Cdd:cd03791 468 YLELYRS 474
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
480-965 |
0e+00 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 596.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 480 LHIVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCMqLDQITNLKVLDVvIQSYFDGNLFSNNVWTGTV 559
Cdd:COG0297 1 MKILFVASEAAPFAKTGGLADVVGALPKALAKLGHDVRVVLPGYPSI-DDKLKDLEVVAS-LEVPLGGRTYYARVLEGPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 560 EGLPVYFIEpqHPSkFFWRAQYYGE-----HDDFKRYSYFSRAALELLYQSGKKIDIIHCHDWQTAFVAPLYWDIYATRG 634
Cdd:COG0297 79 DGVPVYFID--NPE-LFDRPGPYGDpdrdyPDNAERFAFFSRAALELLKGLDWKPDIIHCHDWQTGLIPALLKTRYADDP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 635 FSSARICFTCHNFEYQGTAPAPDLSYCGLDvEQLDRPDRMQDnaHGRINVAKGGIVYSNIVTTVSPTYALEVRS-EGGRG 713
Cdd:COG0297 156 FKRIKTVFTIHNLAYQGIFPAEILELLGLP-PELFTPDGLEF--YGQINFLKAGIVYADRVTTVSPTYAREIQTpEFGEG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 714 LQDTLKMHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATDLQGKAANKAFLRKQLGLySEDASQPLVACITRLVPQKGLH 793
Cdd:COG0297 233 LDGLLRARSGKLSGILNGIDYDVWNPATDPYLPANYSADDLEGKAANKAALQEELGL-PVDPDAPLIGMVSRLTEQKGLD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 794 LIRHAIYKTAELGGQFVLLGSSPvPHIQREFEGVADQFqkNNNIRLILKYDEALSHCIYAASDMFIIPSMFEPCGLTQMI 873
Cdd:COG0297 312 LLLEALDELLEEDVQLVVLGSGD-PEYEEAFRELAARY--PGRVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQMY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 874 AMRYGSVPIVRQTGGLCDSVFDFDDETipvELRNGFTFARTDEQDLSSCLERAFSYYsRKPMVWKQLVQKDMQIDFSWDS 953
Cdd:COG0297 389 ALRYGTVPIVRRTGGLADTVIDYNEAT---GEGTGFVFDEYTAEALLAAIRRALALY-RDPEAWRKLQRNAMKQDFSWEK 464
|
490
....*....|..
gi 1002230293 954 PASQYENLYQSA 965
Cdd:COG0297 465 SAKEYLELYREL 476
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
480-968 |
0e+00 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 594.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 480 LHIVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCMqLDQITNLKVldvviqsyfDGNLFSNNVWTGTV 559
Cdd:PRK00654 1 MKILFVASECAPLIKTGGLGDVVGALPKALAALGHDVRVLLPGYPAI-REKLRDAQV---------VGRLDLFTVLFGHL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 560 E--GLPVYFIEPQHpskFFWRAQYYGEHDDFKRYSYFSRAALELLYQSGKKIDIIHCHDWQTAFVAPLYWDIYAtRGFSS 637
Cdd:PRK00654 71 EgdGVPVYLIDAPH---LFDRPSGYGYPDNGERFAFFSWAAAEFAEGLDPRPDIVHAHDWHTGLIPALLKEKYW-RGYPD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 638 ARICFTCHNFEYQGTAPAPDLSYCGLDVEQLdRPDRMQDnaHGRINVAKGGIVYSNIVTTVSPTYALEVR-SEGGRGLQD 716
Cdd:PRK00654 147 IKTVFTIHNLAYQGLFPAEILGELGLPAEAF-HLEGLEF--YGQISFLKAGLYYADRVTTVSPTYAREITtPEFGYGLEG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 717 TLKMHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATDLQGKAANKAFLRKQLGLYSEDAsqPLVACITRLVPQKGLHLIR 796
Cdd:PRK00654 224 LLRARSGKLSGILNGIDYDIWNPETDPLLAANYSADDLEGKAENKRALQERFGLPDDDA--PLFAMVSRLTEQKGLDLVL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 797 HAIYKTAELGGQFVLLGSsPVPHIQREFEGVADQFqkNNNIRLILKYDEALSHCIYAASDMFIIPSMFEPCGLTQMIAMR 876
Cdd:PRK00654 302 EALPELLEQGGQLVLLGT-GDPELEEAFRALAARY--PGKVGVQIGYDEALAHRIYAGADMFLMPSRFEPCGLTQLYALR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 877 YGSVPIVRQTGGLCDSVFDFDDETipvELRNGFTFARTDEQDLSSCLERAFSYYSRKPmVWKQLVQKDMQIDFSWDSPAS 956
Cdd:PRK00654 379 YGTLPIVRRTGGLADTVIDYNPED---GEATGFVFDDFNAEDLLRALRRALELYRQPP-LWRALQRQAMAQDFSWDKSAE 454
|
490
....*....|..
gi 1002230293 957 QYENLYQSAVAQ 968
Cdd:PRK00654 455 EYLELYRRLLGK 466
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
480-965 |
3.16e-148 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 466.65 E-value: 3.16e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 480 LHIVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCMQLDQITNLKVLdvviQSYFDGNLfSNNVWTGTV 559
Cdd:PLN02316 588 MHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHNVDIILPKYDCLNLSHVKDLHYQ----RSYSWGGT-EIKVWFGKV 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 560 EGLPVYFIEPQhpSKFFWRAQYYGEHDDFKRYSYFSRAALELLYQSGKKIDIIHCHDWQTAFVAPLYWDIYATRGFSSAR 639
Cdd:PLN02316 663 EGLSVYFLEPQ--NGMFWAGCVYGCRNDGERFGFFCHAALEFLLQSGFHPDIIHCHDWSSAPVAWLFKDHYAHYGLSKAR 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 640 ICFTCHNFEYqgtapapdlsycgldveqldrpdrmqdnahGRINVAKGgIVYSNIVTTVSPTYALEVRSEGgrglqdTLK 719
Cdd:PLN02316 741 VVFTIHNLEF------------------------------GANHIGKA-MAYADKATTVSPTYSREVSGNS------AIA 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 720 MHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATD-LQGKAANKAFLRKQLGLYSEDAsqPLVACITRLVPQKGLHLIRHA 798
Cdd:PLN02316 784 PHLYKFHGILNGIDPDIWDPYNDNFIPVPYTSENvVEGKRAAKEALQQRLGLKQADL--PLVGIITRLTHQKGIHLIKHA 861
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 799 IYKTAELGGQFVLLGSSPVPHIQREFEGVADQFQKNNN--IRLILKYDEALSHCIYAASDMFIIPSMFEPCGLTQMIAMR 876
Cdd:PLN02316 862 IWRTLERNGQVVLLGSAPDPRIQNDFVNLANQLHSSHHdrARLCLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLTAMR 941
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 877 YGSVPIVRQTGGLCDSVFDFDDETIPVELR----NGFTFARTDEQDLSSCLERAFS--YYSRKpmvW-KQLVQKDMQIDF 949
Cdd:PLN02316 942 YGSIPVVRKTGGLFDTVFDVDHDKERAQAQglepNGFSFDGADAAGVDYALNRAISawYDGRD---WfNSLCKRVMEQDW 1018
|
490
....*....|....*.
gi 1002230293 950 SWDSPASQYENLYQSA 965
Cdd:PLN02316 1019 SWNRPALDYMELYHSA 1034
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
478-970 |
2.47e-86 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 285.84 E-value: 2.47e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 478 SGLHIVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCM--QLDQITNLKVLDvviqSYFDGNlfsNNVW 555
Cdd:PRK14099 2 TPLRVLSVASEIFPLIKTGGLADVAGALPAALKAHGVEVRTLVPGYPAVlaGIEDAEQVHSFP----DLFGGP---ARLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 556 TGTVEGLPVYFIEPQHpskFFWRA--QYYGEH-----DDFKRYSYFSRAALELLYQS--GKKIDIIHCHDWQTAFV-APL 625
Cdd:PRK14099 75 AARAGGLDLFVLDAPH---LYDRPgnPYVGPDgkdwpDNAQRFAALARAAAAIGQGLvpGFVPDIVHAHDWQAGLApAYL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 626 YWDiyatrGFSSARICFTCHNFEYQGTAPAPDLSYCGL-----DVEQLDRpdrmqdnaHGRINVAKGGIVYSNIVTTVSP 700
Cdd:PRK14099 152 HYS-----GRPAPGTVFTIHNLAFQGQFPRELLGALGLppsafSLDGVEY--------YGGIGYLKAGLQLADRITTVSP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 701 TYALEVRS-EGGRGLQDTLKMHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATDLQGKAANKAFLRKQLGLYSEDASqPL 779
Cdd:PRK14099 219 TYALEIQGpEAGMGLDGLLRQRADRLSGILNGIDTAVWNPATDELIAATYDVETLAARAANKAALQARFGLDPDPDA-LL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 780 VACITRLVPQKGLHLIRHAIYKTAELGGQFVLLGSSPvPHIQREFEGVAdqfQKN-NNIRLILKYDEALSHCIYAASDMF 858
Cdd:PRK14099 298 LGVISRLSWQKGLDLLLEALPTLLGEGAQLALLGSGD-AELEARFRAAA---QAYpGQIGVVIGYDEALAHLIQAGADAL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 859 IIPSMFEPCGLTQMIAMRYGSVPIVRQTGGLCDSVFDFDDETIPVELRNGFTFARTDEQDLSSCLERAFSYYSrKPMVWK 938
Cdd:PRK14099 374 LVPSRFEPCGLTQLCALRYGAVPVVARVGGLADTVVDANEMAIATGVATGVQFSPVTADALAAALRKTAALFA-DPVAWR 452
|
490 500 510
....*....|....*....|....*....|..
gi 1002230293 939 QLVQKDMQIDFSWDSPASQYENLYQSAVAQAR 970
Cdd:PRK14099 453 RLQRNGMTTDVSWRNPAQHYAALYRSLVAERR 484
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
482-719 |
1.79e-77 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 253.02 E-value: 1.79e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 482 IVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCMQLDQITNLKVLDVVIQSYFDGNLFSNNVWTGTVEG 561
Cdd:pfam08323 1 ILFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGNIPEERNQLEDVIRLSVAAGVPVRPLTVGVARLELDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 562 LPVYFIEPQHpskFFWRAQYYGE-----HDDFKRYSYFSRAALELLYQSGKKIDIIHCHDWQTAFVAPLYWDIYATRGFS 636
Cdd:pfam08323 81 VDVYFLDNPD---YFDRPGLYGDdgrdyEDNAERFAFFSRAALELAKKLGWIPDIIHCHDWHTALVPAYLKEAYADDPFK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 637 SARICFTCHNFEYQGTAPAPDLSYCGLDVEQLDrPDRMQDnaHGRINVAKGGIVYSNIVTTVSPTYALEVRS-EGGRGLQ 715
Cdd:pfam08323 158 NIKTVFTIHNLAYQGRFPADLLDLLGLPPEDFN-LDGLEF--YGQINFLKAGIVYADAVTTVSPTYAEEIQTpEFGGGLD 234
|
....
gi 1002230293 716 DTLK 719
Cdd:pfam08323 235 GLLR 238
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
482-963 |
3.80e-68 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 236.17 E-value: 3.80e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 482 IVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKY-----------DCMQLDQI-TNLK----VLDVV----- 540
Cdd:PRK14098 8 VLYVSGEVSPFVRVSALADFMASFPQALEEEGFEARIMMPKYgtindrkfrlhDVLRLSDIeVPLKektdLLHVKvtalp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 541 ---IQSYFDGN--LFSNNVWtgtveglpvyFIEPQHpskffwraqyygeHDDFK----RYSYFSRAALELLYQSGKKIDI 611
Cdd:PRK14098 88 sskIQTYFLYNekYFKRNGL----------FTDMSL-------------GGDLKgsaeKVIFFNVGVLETLQRLGWKPDI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 612 IHCHDWQTAFVAPLYWDIYATRGF-SSARICFTCHNFEYQGTAPapdlsycgLDVEQLDRPDRMQDNAH---GRINVAKG 687
Cdd:PRK14098 145 IHCHDWYAGLVPLLLKTVYADHEFfKDIKTVLTIHNVYRQGVLP--------FKVFQKLLPEEVCSGLHregDEVNMLYT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 688 GIVYSNIVTTVSPTYALEVRSEGGR--GLQDTLKMHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATDLQGKAANKAFLR 765
Cdd:PRK14098 217 GVEHADLLTTTSPRYAEEIAGDGEEafGLDKVLEERKMRLHGILNGIDTRQWNPSTDKLIKKRYSIERLDGKLENKKALL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 766 KQLGLySEDASQPLVACITRLVPQKGLHLIRHAIYKTAELGGQFVLLGSSpvphiQREFEGVADQFQKNNNIRLILKYD- 844
Cdd:PRK14098 297 EEVGL-PFDEETPLVGVIINFDDFQGAELLAESLEKLVELDIQLVICGSG-----DKEYEKRFQDFAEEHPEQVSVQTEf 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 845 -EALSHCIYAASDMFIIPSMFEPCGLTQMIAMRYGSVPIVRQTGGLCDSVFDFDDetipvELRNGFTFARTDEQDLSSCL 923
Cdd:PRK14098 371 tDAFFHLAIAGLDMLLMPGKIESCGMLQMFAMSYGTIPVAYAGGGIVETIEEVSE-----DKGSGFIFHDYTPEALVAKL 445
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1002230293 924 ERAFSYYSRKPMvWKQLVQKDMQIDFSWDSPASQYENLYQ 963
Cdd:PRK14098 446 GEALALYHDEER-WEELVLEAMERDFSWKNSAEEYAQLYR 484
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
481-963 |
1.83e-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: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 481 HIVHIAAEMAPVakVGGLADVVAGLGKALQTKGHLVEIVLPkydcmqldqitnlkvldvviqsyfdgnlfsnnvwtGTVE 560
Cdd:cd03801 1 KILLLSPELPPP--VGGAERHVRELARALAARGHDVTVLTP-----------------------------------ADPG 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 561 GLPVYFIEPQHPSKFFWRAQYYGEHDDFKRYSYFSRAAlellyqsgkKIDIIHCHDWQTAFVAPLYWdiyatrGFSSARI 640
Cdd:cd03801 44 EPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLRLR---------KFDVVHAHGLLAALLAALLA------LLLGAPL 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 641 CFTCHNFEYQGTAPAPDLSYcgldvEQLDRPDRMQDNAHGRInvakggivysnivtTVSPTYALEVRSEGGRglqdtlkm 720
Cdd:cd03801 109 VVTLHGAEPGRLLLLLAAER-----RLLARAEALLRRADAVI--------------AVSEALRDELRALGGI-------- 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 721 HSRKFVGILNGIDTGTWNPstdrflavqysatdlqgkaankaFLRKQLGLyseDASQPLVACITRLVPQKGLHLIRHAIY 800
Cdd:cd03801 162 PPEKIVVIPNGVDLERFSP-----------------------PLRRKLGI---PPDRPVLLFVGRLSPRKGVDLLLEALA 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 801 KTAELGG--QFVLLGSSP--VPHIQREFEGVADqfqknnNIRLILKYDEALSHCIYAASDMFIIPSMFEPCGLTQMIAMR 876
Cdd:cd03801 216 KLLRRGPdvRLVIVGGDGplRAELEELELGLGD------RVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMA 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 877 YGSVPIVRQTGGLCDSVfdfDDETipvelrNGFTFARTDEQDLSSCLERAFSYysrkPMVWKQLVQ---KDMQIDFSWDS 953
Cdd:cd03801 290 AGLPVVATDVGGLPEVV---EDGE------GGLVVPPDDVEALADALLRLLAD----PELRARLGRaarERVAERFSWER 356
|
490
....*....|
gi 1002230293 954 PASQYENLYQ 963
Cdd:cd03801 357 VAERLLDLYR 366
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
831-967 |
5.59e-10 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 58.08 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 831 FQKNNNIRLILkydEALshciYAASDMFIIPSMFEPCGLTQMIAMRYGSVPIVRQTGGLCDSVFDFDdetipvelrNGFT 910
Cdd:COG0438 4 LVPRKGLDLLL---EAL----LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGE---------TGLL 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 911 FARTDEQDLSSCLERAFSYYSRkpmvWKQLVQ---KDMQIDFSWDSPASQYENLYQSAVA 967
Cdd:COG0438 68 VPPGDPEALAEAILRLLEDPEL----RRRLGEaarERAEERFSWEAIAERLLALYEELLA 123
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
764-960 |
7.89e-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: 7.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 764 LRKQLGLyseDASQPLVACITRLVPQKGLH-LIRhAIYKTAELGGQFVLL---GSSPVPHIQREFEgvADQFQKNNniRL 839
Cdd:cd03800 210 RRARLLL---PPDKPVVLALGRLDPRKGIDtLVR-AFAQLPELRELANLVlvgGPSDDPLSMDREE--LAELAEEL--GL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 840 ILKYD-------EALSHcIYAASDMFIIPSMFEPCGLTQMIAMRYGsVPIV-RQTGGLCDSVfdfddetipVELRNGFTF 911
Cdd:cd03800 282 IDRVRfpgrvsrDDLPE-LYRAADVFVVPSLYEPFGLTAIEAMACG-TPVVaTAVGGLQDIV---------RDGRTGLLV 350
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002230293 912 ARTDEQDLSSCLERAFsyysRKPMVWKQLvqKDMQID-----FSWDSPASQYEN 960
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 ... |
777-933 |
1.84e-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: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 777 QPLVACITRLVPQKGLHLIRHAIYKTAELGGQFVLL--GSSPVphiQREFEGVADQFQKNNNIRLIL-KYDEALSHCiYA 853
Cdd:pfam00534 2 KKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLViaGDGEE---EKRLKKLAEKLGLGDNVIFLGfVSDEDLPEL-LK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 854 ASDMFIIPSMFEPCGLTQMIAMRYGSVPIVRQTGGLCDSVFDFDdetipvelrNGFTFARTDEQDLSSCLERA------- 926
Cdd:pfam00534 78 IADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGE---------TGFLVKPNNAEALAEAIDKLledeelr 148
|
....*....
gi 1002230293 927 --FSYYSRK 933
Cdd:pfam00534 149 erLGENARK 157
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
778-925 |
1.99e-09 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 56.75 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 778 PLVACITRLVP-QKGLHLIRHAIY--KTAELGGQFVLLGSSPVPHIQREFEGVADqfqknnNIRLiLKYDEALSHcIYAA 854
Cdd:pfam13692 2 PVILFVGRLHPnVKGVDYLLEAVPllRKRDNDVRLVIVGDGPEEELEELAAGLED------RVIF-TGFVEDLAE-LLAA 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002230293 855 SDMFIIPSMFEPCGLTQMIAMRYGsVPIV-RQTGGLCDSVFDfddetipvelRNGFTFARTDEQDLSSCLER 925
Cdd:pfam13692 74 ADVFVLPSLYEGFGLKLLEAMAAG-LPVVaTDVGGIPELVDG----------ENGLLVPPGDPEALAEAILR 134
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
782-895 |
3.53e-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: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 782 CITRLVPQKGLHLIRHAI--YKTAELGGQFVLLGSSPVPhiQREFEGVADQFQKNNNIRLILKYDEALSHCIYAASDMFI 859
Cdd:cd01635 115 SVGRLVPEKGIDLLLEALalLKARLPDLVLVLVGGGGER--EEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFV 192
|
90 100 110
....*....|....*....|....*....|....*.
gi 1002230293 860 IPSMFEPCGLTQMIAMRYGSVPIVRQTGGLCDSVFD 895
Cdd:cd01635 193 LPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVD 228
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
728-964 |
1.04e-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: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 728 ILNGIDTGTWNPstdrflavqysatdlqgkaANKAFLRKQLGLySEDAsqPLVACITRLV--PQKGLH-LIR--HAIYKT 802
Cdd:cd03825 166 IPNGIDTEIFAP-------------------VDKAKARKRLGI-PQDK--KVILFGAESVtkPRKGFDeLIEalKLLATK 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 803 AELGGQFV-----LLGSSPVPHIQREFEgvadqfqkNNNIRLILkydealshcIYAASDMFIIPSMFEPCGLTQMIAMRY 877
Cdd:cd03825 224 DDLLLVVFgkndpQIVILPFDIISLGYI--------DDDEQLVD---------IYSAADLFVHPSLADNLPNTLLEAMAC 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 878 GSVPIVRQTGGLCDSVFDfddetipveLRNGFTFARTDEQDLSS----CLERAFSYYSRkpmvwKQLVQKDMQIDFSWDS 953
Cdd:cd03825 287 GTPVVAFDTGGSPEIVQH---------GVTGYLVPPGDVQALAEaiewLLANPKERESL-----GERARALAENHFDQRV 352
|
250
....*....|.
gi 1002230293 954 PASQYENLYQS 964
Cdd:cd03825 353 QAQRYLELYKD 363
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
774-962 |
3.76e-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: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 774 DASQPLVAC-ITRLVPQKGLHLIRHAIYKTAELGGQFVLLGSSPVpHIQREFEGVAdqfqknnNIRLI--LKYDEALSHc 850
Cdd:cd03823 187 PGTERLRFGyIGRLTEEKGIDLLVEAFKRLPREDIELVIAGHGPL-SDERQIEGGR-------RIAFLgrVPTDDIKDF- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 851 iYAASDMFIIPSMF-EPCGLTQMIAMRYGSVPIVRQTGGLCDSVfdfddetipVELRNGFTFARTDEQDLSSCLERAfsy 929
Cdd:cd03823 258 -YEKIDVLVVPSIWpEPFGLVVREAIAAGLPVIASDLGGIAELI---------QPGVNGLLFAPGDAEDLAAAMRRL--- 324
|
170 180 190
....*....|....*....|....*....|...
gi 1002230293 930 ySRKPMVWKQLvQKDMQIDFSWDSPASQYENLY 962
Cdd:cd03823 325 -LTDPALLERL-RAGAEPPRSTESQAEEYLKLY 355
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
696-893 |
7.84e-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: 7.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 696 TTVSPTYALEVRSEGgRGLQDtlkmhsrkfVGILN-GIDTGTWNPStdrflavqysatdlqgkAANKAFLRKQLglyseD 774
Cdd:cd03814 148 TTLVPSPSIARELEG-HGFER---------VRLWPrGVDTELFHPS-----------------RRDAALRRRLG-----P 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 775 ASQPLVACITRLVPQKGLHLIRHAIYK-TAELGGQFVLLGSSPvphiQREfegvADQFQKNNNIRLILKYDEALSHcIYA 853
Cdd:cd03814 196 PGRPLLLYVGRLAPEKNLEALLDADLPlAASPPVRLVVVGDGP----ARA----ELEARGPDVIFTGFLTGEELAR-AYA 266
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1002230293 854 ASDMFIIPSMFEPCGLTQMIAMRYGsVP-IVRQTGGLCDSV 893
Cdd:cd03814 267 SADVFVFPSRTETFGLVVLEAMASG-LPvVAADAGGPRDIV 306
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
54-339 |
3.01e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 54 KQRSSNAKLLLTTEENGQLPSTS-LRTSMERpQKSTSSEDDTNG---AISQIDEKIAAIgNEQQERSKDKHFESDFQLED 129
Cdd:PRK02224 168 RERASDARLGVERVLSDQRGSLDqLKAQIEE-KEEKDLHERLNGlesELAELDEEIERY-EEQREQARETRDEADEVLEE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 130 FGEMIQNMEKnillLNQARLQAIEDVDKILTEKEALQKKV-------DTLEMNLSKALATKGNINTDIPG--DHLEKFTK 200
Cdd:PRK02224 246 HEERREELET----LEAEIEDLRETIAETEREREELAEEVrdlrerlEELEEERDDLLAEAGLDDADAEAveARREELED 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 201 EI------LIESALSGGNPAHLCESpLFMELTVLKEENMLLKADAQFLKAKIvefAETEEFLFKLEKERSLLDATVRELE 274
Cdd:PRK02224 322 RDeelrdrLEECRVAAQAHNEEAES-LREDADDLEERAEELREEAAELESEL---EEAREAVEDRREEIEELEEEIEELR 397
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002230293 275 ARFLVAQTDiwkvvplqydvwmekvenlqhmLGCLKNHVEkyaALLDQHDDLHDKIDELEASLKE 339
Cdd:PRK02224 398 ERFGDAPVD----------------------LGNAEDFLE---ELREERDELREREAELEATLRT 437
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
496-734 |
3.88e-04 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 42.13 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 496 GGLADVVAGLGKALQTKGHLVEIVLPKYDcmqldqitnlkvldvviqsyfdgNLFSNNVWTGTVEGLPVYFIEPqhpskf 575
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGP-----------------------GPLAEEVVRVVRVPRVPLPLPP------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 576 fwraqyygehdDFKRYSYFSRAALELLyqSGKKIDIIHCHDWqtafvAPLYWDIYATRGFSSARICFTCHNFEYQGTAPA 655
Cdd:pfam13439 52 -----------RLLRSLAFLRRLRRLL--RRERPDVVHAHSP-----FPLGLAALAARLRLGIPLVVTYHGLFPDYKRLG 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002230293 656 PDLSYCGLDVEQLDRpdRMQDNAHGrinvakggivysniVTTVSPTyaleVRSEggrgLQDTLKMHSRKFVGILNGIDT 734
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 ... |
694-883 |
8.91e-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: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 694 IVTTvSPTYALEvrSEggrglqdTLKMHSRKFVGILNGIDtgtwnpstdrflAVQYSATDLQGKAANKAFLRKQLGLYse 773
Cdd:cd03795 141 IIAT-SPNYVET--SP-------TLREFKNKVRVIPLGID------------KNVYNIPRVDFENIKREKKGKKIFLF-- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 774 dasqplvacITRLVPQKGLH-LIRHAIYKTAELggqfVLLGSSPvphIQREFEGVADQfQKNNNIRLILKYDEALSHCIY 852
Cdd:cd03795 197 ---------IGRLVYYKGLDyLIEAAQYLNYPI----VIGGEGP---LKPDLEAQIEL-NLLDNVKFLGRVDDEEKVIYL 259
|
170 180 190
....*....|....*....|....*....|...
gi 1002230293 853 AASDMFIIPSMF--EPCGLTQMIAMRYGsVPIV 883
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 ... |
851-963 |
1.21e-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: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 851 IYAASDMFIIPSMFEPCGLTQMIAMRYGSVPIVRQTGGlcdsvfdfddetIPVELRNGFTFARTDEQDLSSCLERAFSYY 930
Cdd:cd04962 266 LLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGG------------IPEVVKHGETGFLSDVGDVDAMAKSALSIL 333
|
90 100 110
....*....|....*....|....*....|....*.
gi 1002230293 931 sRKPMVWKQLVQ---KDMQIDFSWDSPASQYENLYQ 963
Cdd:cd04962 334 -EDDELYNRMGRaarKRAAERFDPERIVPQYEAYYR 368
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
126-400 |
1.73e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 126 QLEDFGEMIQNMEKNILLLNqARLQAIEdvdKILTEKEALQKKVDTLEMNLSKALATKGNINTDIP--GDHLEKFTKEIL 203
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIK-RRIERLE---KFIKRTENIEELIKEKEKELEEVLREINEISSELPelREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 204 -IESalsggnpahlcespLFMELTVLKEENMLLKADAQFLKAKIVefaETEEFLFKLEKERSLLDATVRELEARFLVAQT 282
Cdd:PRK03918 232 eLEE--------------LKEEIEELEKELESLEGSKRKLEEKIR---ELEERIEELKKEIEELEEKVKELKELKEKAEE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 283 DIwKVVPLqYDVWMEKVENLQHMLGCLKNHVEKYAALLDQHDDLHDKIDELEASLKE--GKTSEFSPYvVELLQ------ 354
Cdd:PRK03918 295 YI-KLSEF-YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKEleKRLEELEER-HELYEeakakk 371
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1002230293 355 ---QKLKAAKSHHQAGhqETNTHIQVYQQLTEEFQDNLGKLIEESGRLE 400
Cdd:PRK03918 372 eelERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELK 418
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
87-339 |
2.48e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 87 STSSEDDTNGAISQIDEKIAAIgNEQQERSKDKHFESDFQLEDFGEMIQNMEKNILLLNQARLQAIEDVDKILTEKEALQ 166
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAEL-EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 167 KKVDTLEMNLSKALATkgnintdipgdhLEKFTKEILIESALSGGNPAHlcespLFMELTVLKEENMLLKADAQFLKAKI 246
Cdd:COG4942 97 AELEAQKEELAELLRA------------LYRLGRQPPLALLLSPEDFLD-----AVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 247 VEFAETEEflfKLEKERSLLDATVRELEA--RFLVAQTDiwkvvplqydvwmEKVENLQHMLGCLKNHVEKYAALLDQHD 324
Cdd:COG4942 160 AELAALRA---ELEAERAELEALLAELEEerAALEALKA-------------ERQKLLARLEKELAELAAELAELQQEAE 223
|
250
....*....|....*
gi 1002230293 325 DLHDKIDELEASLKE 339
Cdd:COG4942 224 ELEALIARLEAEAAA 238
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
131-362 |
4.69e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 131 GEMIQNMEKNILLLNQARLQAIEDVDKILTEKEALQKKVDTLEMNLSKALATKGN-------INTDIPGDHLEKFTKEIL 203
Cdd:PRK03918 383 GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreLTEEHRKELLEEYTAELK 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 204 ----------------------IESALSGgnpahlcESPLFMELTVLKE----ENMLLKADAQFLKAKIVEFAETEEFLF 257
Cdd:PRK03918 463 riekelkeieekerklrkelreLEKVLKK-------ESELIKLKELAEQlkelEEKLKKYNLEELEKKAEEYEKLKEKLI 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 258 KLEKERSLLDATVRELEARflvaqtdIWKVVPLQydvwmEKVENLQHMLGCLKNHVEKYAalLDQHDDLHDKIDELEASL 337
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEEL-------KKKLAELE-----KKLDELEEELAELLKELEELG--FESVEELEERLKELEPFY 601
|
250 260
....*....|....*....|....*
gi 1002230293 338 KEGKTSEFSPYVVELLQQKLKAAKS 362
Cdd:PRK03918 602 NEYLELKDAEKELEREEKELKKLEE 626
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
695-883 |
5.41e-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: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 695 VTTVSPTYALEVRSEGGRglqdtlkmhSRKFVGILNGIDTGTWNPStdrflavqysatdlqgkAANKAFLRKQLGLyseD 774
Cdd:cd03807 137 TVANSSAVAEFHQEQGYA---------KNKIVVIYNGIDLFKLSPD-----------------DASRARARRRLGL---A 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 775 ASQPLVACITRLVPQKGLHLIRHAIYKTAELGGQ--FVLLGSSPV-PHIQREFE--GVADQFqknnnirLILKYDEALSH 849
Cdd:cd03807 188 EDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDlrLLLVGRGPErPNLERLLLelGLEDRV-------HLLGERSDVPA 260
|
170 180 190
....*....|....*....|....*....|....
gi 1002230293 850 CiYAASDMFIIPSMFEPCGLTQMIAMRYGsVPIV 883
Cdd:cd03807 261 L-LPAMDIFVLSSRTEGFPNALLEAMACG-LPVV 292
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
92-277 |
5.85e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.59 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 92 DDTNGAISQIDEKIAAiGNEQQERSKDKHFEsdFQLEDFGEMIQNMEKniLLLNQARLQAIEDVDKILTEK-EALQKKVD 170
Cdd:pfam12128 304 DELNGELSAADAAVAK-DRSELEALEDQHGA--FLDADIETAAADQEQ--LPSWQSELENLEERLKALTGKhQDVTAKYN 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002230293 171 TLEMNLSKALATK-GNINTDIPGDHLEKFTKEILIESALSGgnpahlCESPLFMEL----TVLKEENMLLKADAQFLKAK 245
Cdd:pfam12128 379 RRRSKIKEQNNRDiAGIKDKLAKIREARDRQLAVAEDDLQA------LESELREQLeagkLEFNEEEYRLKSRLGELKLR 452
|
170 180 190
....*....|....*....|....*....|..
gi 1002230293 246 IVEFAETEEFLFKLEKERSLLDATVRELEARF 277
Cdd:pfam12128 453 LNQATATPELLLQLENFDERIERAREEQEAAN 484
|
|
| |
