|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
10-972 |
0e+00 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 1828.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 10 EYSALLSLSCGPI---------TRRRFAVSCRARPPgNLSAQQKKKRGKNIAPKQRSSNAKLLLTTEENGQLPSTSLRTS 80
Cdd:PLN02939 5 ESAALLSHGCGPIrsrapfylpSRRRLAVSCRARRR-GFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 81 MERPQKSTSSEDDTNGAISQIDEKIAAIGNEQQERSKDKHFESDFQLEDFGEMIQNMEKNILLLNQARLQAIEDVDKILT 160
Cdd:PLN02939 84 MELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 161 EKEALQKKVDTLEMNLSKA-----LATKGNINTDIPGDHLEKFTKEILIESALSGGnpahlCESPLFMELTVLKEENMLL 235
Cdd:PLN02939 164 EKEALQGKINILEMRLSETdarikLAAQEKIHVEILEEQLEKLRNELLIRGATEGL-----CVHSLSKELDVLKEENMLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 236 KADAQFLKAKIVEFAETEEFLFKLEKERSLLDATVRELEARFLVAQTDIWKVVPLQYDVWMEKVENLQHMLGCLKNHVEK 315
Cdd:PLN02939 239 KDDIQFLKAELIEVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 316 YAALLDQHDDLHDKIDELEASLKEGKTSEFSPYVVELLQQKLKAAKSHHQAGHQETNTHIQVYQQLTEEFQDNLGKLIEE 395
Cdd:PLN02939 319 AALVLDQNQDLRDKVDKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 396 SGR--LEHSANSMPSEFWSHILLMIDGWFLERKIPNTDARMLREMAWKRDDRICEAYFACKGAKESDVMETFLKLSLSGN 473
Cdd:PLN02939 399 SKKrsLEHPADDMPSEFWSRILLLIDGWLLEKKISNNDAKLLREMVWKRDGRIREAYLSCKGKNEREAVENFLKLTLSGT 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 474 SSGLHIVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCMQLDQITNLKVLDVVIQSYFDGNLFSNNVWT 553
Cdd:PLN02939 479 SSGLHIVHIAAEMAPVAKVGGLADVVSGLGKALQKKGHLVEIVLPKYDCMQYDQIRNLKVLDVVVESYFDGNLFKNKIWT 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 554 GTVEGLPVYFIEPQHPSKFFWRAQYYGEHDDFKRYSYFSRAALELLYQSGKKIDIIHCHDWQTAFVAPLYWDIYATRGFS 633
Cdd:PLN02939 559 GTVEGLPVYFIEPQHPSKFFWRAQYYGEHDDFKRFSYFSRAALELLYQSGKKPDIIHCHDWQTAFVAPLYWDLYAPKGFN 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 634 SARICFTCHNFEYQGTAPAPDLSYCGLDVEQLDRPDRMQDNAHGRINVAKGGIVYSNIVTTVSPTYALEVRSEGGRGLQD 713
Cdd:PLN02939 639 SARICFTCHNFEYQGTAPASDLASCGLDVHQLDRPDRMQDNAHGRINVVKGAIVYSNIVTTVSPTYAQEVRSEGGRGLQD 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 714 TLKMHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATDLQGKAANKAFLRKQLGLYSEDASQPLVACITRLVPQKGLHLIR 793
Cdd:PLN02939 719 TLKFHSKKFVGILNGIDTDTWNPSTDRFLKVQYNANDLQGKAANKAALRKQLGLSSADASQPLVGCITRLVPQKGVHLIR 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 794 HAIYKTAELGGQFVLLGSSPVPHIQREFEGVADQFQKNNNIRLILKYDEALSHCIYAASDMFIIPSMFEPCGLTQMIAMR 873
Cdd:PLN02939 799 HAIYKTAELGGQFVLLGSSPVPHIQREFEGIADQFQSNNNIRLILKYDEALSHSIYAASDMFIIPSMFEPCGLTQMIAMR 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 874 YGSVPIVRQTGGLCDSVFDFDDETIPVELRNGFTFARTDEQDLSSCLERAFSYYSRKPMVWKQLVQKDMQIDFSWDSPAS 953
Cdd:PLN02939 879 YGSVPIVRKTGGLNDSVFDFDDETIPVELRNGFTFLTPDEQGLNSALERAFNYYKRKPEVWKQLVQKDMNIDFSWDSSAS 958
|
970
....*....|....*....
gi 34809050 954 QYENLYQSAVAQARGAAQT 972
Cdd:PLN02939 959 QYEELYQRAVARARAAANR 977
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
477-962 |
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: 605.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 477 LHIVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCMQLDQITNLKVLDVVIQSYFDGNLFsNNVWTGTV 556
Cdd:TIGR02095 1 MRVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEVDDQVKVVELVDLSVGPRTLY-VKVFEGVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 557 EGLPVYFIEPQHpskFFWR-AQYYGE--HDDFKRYSYFSRAALELLYQSGKKIDIIHCHDWQTAFVAPLYWDIYatrGFS 633
Cdd:TIGR02095 80 EGVPVYFIDNPS---LFDRpGGIYGDdyPDNAERFAFFSRAAAELLSGLGWQPDVVHAHDWHTALVPALLKAVY---RPN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 634 SARICFTCHNFEYQGTAPAPDLSYCGLDveqldrPDRMQDNA---HGRINVAKGGIVYSNIVTTVSPTYALEVR-SEGGR 709
Cdd:TIGR02095 154 PIKTVFTIHNLAYQGVFPADDFSELGLP------PEYFHMEGlefYGRVNFLKGGIVYADRVTTVSPTYAREILtPEFGY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 710 GLQDTLKMHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATDLQGKAANKAFLRKQLGLySEDASQPLVACITRLVPQKGL 789
Cdd:TIGR02095 228 GLDGVLKARSGKLRGILNGIDTEVWNPATDPYLKANYSADDLAGKAENKEALQEELGL-PVDDDVPLFGVISRLTQQKGV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 790 HLIRHAIYKTAELGGQFVLLGSSPvPHIQREFEGVAdqFQKNNNIRLILKYDEALSHCIYAASDMFIIPSMFEPCGLTQM 869
Cdd:TIGR02095 307 DLLLAALPELLELGGQLVVLGTGD-PELEEALRELA--ERYPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 870 IAMRYGSVPIVRQTGGLCDSVFDFDDETipvELRNGFTFARTDEQDLSSCLERAFSYYSRKPMVWKQLVQKDMQIDFSWD 949
Cdd:TIGR02095 384 YAMRYGTVPIVRRTGGLADTVVDGDPEA---ESGTGFLFEEYDPGALLAALSRALRLYRQDPSLWEALQKNAMSQDFSWD 460
|
490
....*....|...
gi 34809050 950 SPASQYENLYQSA 962
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 ... |
478-961 |
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 34809050 478 HIVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCMQLDQITNLKVLDVVIqsYFDGNLFSNNVWTGTVE 557
Cdd:cd03791 1 KVLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRVLGLEV--KVGGRGEEVGVFELPVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 558 GLPVYFIEPQHPSKFFWR--AQYYGEHDDFKRYSYFSRAALELLYQSGKKIDIIHCHDWQTAFVAPLYWDIYATRGFSSA 635
Cdd:cd03791 79 GVDYYFLDNPEFFDRPGLpgPPGYDYPDNAERFAFFSRAALELLRRLGFQPDIIHANDWHTALVPAYLKTRYRGPGFKKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 636 RICFTCHNFEYQGTAPAPDLSYCGLDvEQLDRPDRMQDnaHGRINVAKGGIVYSNIVTTVSPTYALEV-RSEGGRGLQDT 714
Cdd:cd03791 159 KTVFTIHNLAYQGLFPLDTLAELGLP-PELFHIDGLEF--YGQINFLKAGIVYADRVTTVSPTYAKEIlTPEYGEGLDGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 715 LKMHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATDLQGKAANKAFLRKQLGLySEDASQPLVACITRLVPQKGLHLIRH 794
Cdd:cd03791 236 LRARAGKLSGILNGIDYDEWNPATDKLIPANYSANDLEGKAENKAALQKELGL-PVDPDAPLFGFVGRLTEQKGVDLILD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 795 AIYKTAELGGQFVLLGSSPVPHIQREFEgVADQFqkNNNIRLILKYDEALSHCIYAASDMFIIPSMFEPCGLTQMIAMRY 874
Cdd:cd03791 315 ALPELLEEGGQLVVLGSGDPEYEQAFRE-LAERY--PGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYAMRY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 875 GSVPIVRQTGGLCDSVFDFDDETipvELRNGFTFARTDEQDLSSCLERAFSYYsRKPMVWKQLVQKDMQIDFSWDSPASQ 954
Cdd:cd03791 392 GTLPIVRRTGGLADTVFDYDPET---GEGTGFVFEDYDAEALLAALRRALALY-RNPELWRKLQKNAMKQDFSWDKSAKE 467
|
....*..
gi 34809050 955 YENLYQS 961
Cdd:cd03791 468 YLELYRS 474
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
477-962 |
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 34809050 477 LHIVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCMqLDQITNLKVLDVvIQSYFDGNLFSNNVWTGTV 556
Cdd:COG0297 1 MKILFVASEAAPFAKTGGLADVVGALPKALAKLGHDVRVVLPGYPSI-DDKLKDLEVVAS-LEVPLGGRTYYARVLEGPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 557 EGLPVYFIEpqHPSkFFWRAQYYGE-----HDDFKRYSYFSRAALELLYQSGKKIDIIHCHDWQTAFVAPLYWDIYATRG 631
Cdd:COG0297 79 DGVPVYFID--NPE-LFDRPGPYGDpdrdyPDNAERFAFFSRAALELLKGLDWKPDIIHCHDWQTGLIPALLKTRYADDP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 632 FSSARICFTCHNFEYQGTAPAPDLSYCGLDvEQLDRPDRMQDnaHGRINVAKGGIVYSNIVTTVSPTYALEVRS-EGGRG 710
Cdd:COG0297 156 FKRIKTVFTIHNLAYQGIFPAEILELLGLP-PELFTPDGLEF--YGQINFLKAGIVYADRVTTVSPTYAREIQTpEFGEG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 711 LQDTLKMHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATDLQGKAANKAFLRKQLGLySEDASQPLVACITRLVPQKGLH 790
Cdd:COG0297 233 LDGLLRARSGKLSGILNGIDYDVWNPATDPYLPANYSADDLEGKAANKAALQEELGL-PVDPDAPLIGMVSRLTEQKGLD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 791 LIRHAIYKTAELGGQFVLLGSSPvPHIQREFEGVADQFqkNNNIRLILKYDEALSHCIYAASDMFIIPSMFEPCGLTQMI 870
Cdd:COG0297 312 LLLEALDELLEEDVQLVVLGSGD-PEYEEAFRELAARY--PGRVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQMY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 871 AMRYGSVPIVRQTGGLCDSVFDFDDETipvELRNGFTFARTDEQDLSSCLERAFSYYsRKPMVWKQLVQKDMQIDFSWDS 950
Cdd:COG0297 389 ALRYGTVPIVRRTGGLADTVIDYNEAT---GEGTGFVFDEYTAEALLAAIRRALALY-RDPEAWRKLQRNAMKQDFSWEK 464
|
490
....*....|..
gi 34809050 951 PASQYENLYQSA 962
Cdd:COG0297 465 SAKEYLELYREL 476
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
477-965 |
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 34809050 477 LHIVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCMqLDQITNLKVldvviqsyfDGNLFSNNVWTGTV 556
Cdd:PRK00654 1 MKILFVASECAPLIKTGGLGDVVGALPKALAALGHDVRVLLPGYPAI-REKLRDAQV---------VGRLDLFTVLFGHL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 557 E--GLPVYFIEPQHpskFFWRAQYYGEHDDFKRYSYFSRAALELLYQSGKKIDIIHCHDWQTAFVAPLYWDIYAtRGFSS 634
Cdd:PRK00654 71 EgdGVPVYLIDAPH---LFDRPSGYGYPDNGERFAFFSWAAAEFAEGLDPRPDIVHAHDWHTGLIPALLKEKYW-RGYPD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 635 ARICFTCHNFEYQGTAPAPDLSYCGLDVEQLdRPDRMQDnaHGRINVAKGGIVYSNIVTTVSPTYALEVR-SEGGRGLQD 713
Cdd:PRK00654 147 IKTVFTIHNLAYQGLFPAEILGELGLPAEAF-HLEGLEF--YGQISFLKAGLYYADRVTTVSPTYAREITtPEFGYGLEG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 714 TLKMHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATDLQGKAANKAFLRKQLGLYSEDAsqPLVACITRLVPQKGLHLIR 793
Cdd:PRK00654 224 LLRARSGKLSGILNGIDYDIWNPETDPLLAANYSADDLEGKAENKRALQERFGLPDDDA--PLFAMVSRLTEQKGLDLVL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 794 HAIYKTAELGGQFVLLGSsPVPHIQREFEGVADQFqkNNNIRLILKYDEALSHCIYAASDMFIIPSMFEPCGLTQMIAMR 873
Cdd:PRK00654 302 EALPELLEQGGQLVLLGT-GDPELEEAFRALAARY--PGKVGVQIGYDEALAHRIYAGADMFLMPSRFEPCGLTQLYALR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 874 YGSVPIVRQTGGLCDSVFDFDDETipvELRNGFTFARTDEQDLSSCLERAFSYYSRKPmVWKQLVQKDMQIDFSWDSPAS 953
Cdd:PRK00654 379 YGTLPIVRRTGGLADTVIDYNPED---GEATGFVFDDFNAEDLLRALRRALELYRQPP-LWRALQRQAMAQDFSWDKSAE 454
|
490
....*....|..
gi 34809050 954 QYENLYQSAVAQ 965
Cdd:PRK00654 455 EYLELYRRLLGK 466
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
477-962 |
4.69e-148 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 466.27 E-value: 4.69e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 477 LHIVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCMQLDQITNLKVLdvviQSYFDGNLfSNNVWTGTV 556
Cdd:PLN02316 588 MHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHNVDIILPKYDCLNLSHVKDLHYQ----RSYSWGGT-EIKVWFGKV 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 557 EGLPVYFIEPQhpSKFFWRAQYYGEHDDFKRYSYFSRAALELLYQSGKKIDIIHCHDWQTAFVAPLYWDIYATRGFSSAR 636
Cdd:PLN02316 663 EGLSVYFLEPQ--NGMFWAGCVYGCRNDGERFGFFCHAALEFLLQSGFHPDIIHCHDWSSAPVAWLFKDHYAHYGLSKAR 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 637 ICFTCHNFEYqgtapapdlsycgldveqldrpdrmqdnahGRINVAKGgIVYSNIVTTVSPTYALEVRSEGgrglqdTLK 716
Cdd:PLN02316 741 VVFTIHNLEF------------------------------GANHIGKA-MAYADKATTVSPTYSREVSGNS------AIA 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 717 MHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATD-LQGKAANKAFLRKQLGLYSEDAsqPLVACITRLVPQKGLHLIRHA 795
Cdd:PLN02316 784 PHLYKFHGILNGIDPDIWDPYNDNFIPVPYTSENvVEGKRAAKEALQQRLGLKQADL--PLVGIITRLTHQKGIHLIKHA 861
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 796 IYKTAELGGQFVLLGSSPVPHIQREFEGVADQFQKNNN--IRLILKYDEALSHCIYAASDMFIIPSMFEPCGLTQMIAMR 873
Cdd:PLN02316 862 IWRTLERNGQVVLLGSAPDPRIQNDFVNLANQLHSSHHdrARLCLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLTAMR 941
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 874 YGSVPIVRQTGGLCDSVFDFDDETIPVELR----NGFTFARTDEQDLSSCLERAFS--YYSRKpmvW-KQLVQKDMQIDF 946
Cdd:PLN02316 942 YGSIPVVRKTGGLFDTVFDVDHDKERAQAQglepNGFSFDGADAAGVDYALNRAISawYDGRD---WfNSLCKRVMEQDW 1018
|
490
....*....|....*.
gi 34809050 947 SWDSPASQYENLYQSA 962
Cdd:PLN02316 1019 SWNRPALDYMELYHSA 1034
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
475-967 |
2.36e-86 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 285.84 E-value: 2.36e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 475 SGLHIVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCM--QLDQITNLKVLDvviqSYFDGNlfsNNVW 552
Cdd:PRK14099 2 TPLRVLSVASEIFPLIKTGGLADVAGALPAALKAHGVEVRTLVPGYPAVlaGIEDAEQVHSFP----DLFGGP---ARLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 553 TGTVEGLPVYFIEPQHpskFFWRA--QYYGEH-----DDFKRYSYFSRAALELLYQS--GKKIDIIHCHDWQTAFV-APL 622
Cdd:PRK14099 75 AARAGGLDLFVLDAPH---LYDRPgnPYVGPDgkdwpDNAQRFAALARAAAAIGQGLvpGFVPDIVHAHDWQAGLApAYL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 623 YWDiyatrGFSSARICFTCHNFEYQGTAPAPDLSYCGL-----DVEQLDRpdrmqdnaHGRINVAKGGIVYSNIVTTVSP 697
Cdd:PRK14099 152 HYS-----GRPAPGTVFTIHNLAFQGQFPRELLGALGLppsafSLDGVEY--------YGGIGYLKAGLQLADRITTVSP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 698 TYALEVRS-EGGRGLQDTLKMHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATDLQGKAANKAFLRKQLGLYSEDASqPL 776
Cdd:PRK14099 219 TYALEIQGpEAGMGLDGLLRQRADRLSGILNGIDTAVWNPATDELIAATYDVETLAARAANKAALQARFGLDPDPDA-LL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 777 VACITRLVPQKGLHLIRHAIYKTAELGGQFVLLGSSPvPHIQREFEGVAdqfQKN-NNIRLILKYDEALSHCIYAASDMF 855
Cdd:PRK14099 298 LGVISRLSWQKGLDLLLEALPTLLGEGAQLALLGSGD-AELEARFRAAA---QAYpGQIGVVIGYDEALAHLIQAGADAL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 856 IIPSMFEPCGLTQMIAMRYGSVPIVRQTGGLCDSVFDFDDETIPVELRNGFTFARTDEQDLSSCLERAFSYYSrKPMVWK 935
Cdd:PRK14099 374 LVPSRFEPCGLTQLCALRYGAVPVVARVGGLADTVVDANEMAIATGVATGVQFSPVTADALAAALRKTAALFA-DPVAWR 452
|
490 500 510
....*....|....*....|....*....|..
gi 34809050 936 QLVQKDMQIDFSWDSPASQYENLYQSAVAQAR 967
Cdd:PRK14099 453 RLQRNGMTTDVSWRNPAQHYAALYRSLVAERR 484
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
479-716 |
1.73e-77 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 253.02 E-value: 1.73e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 479 IVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKYDCMQLDQITNLKVLDVVIQSYFDGNLFSNNVWTGTVEG 558
Cdd:pfam08323 1 ILFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGNIPEERNQLEDVIRLSVAAGVPVRPLTVGVARLELDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 559 LPVYFIEPQHpskFFWRAQYYGE-----HDDFKRYSYFSRAALELLYQSGKKIDIIHCHDWQTAFVAPLYWDIYATRGFS 633
Cdd:pfam08323 81 VDVYFLDNPD---YFDRPGLYGDdgrdyEDNAERFAFFSRAALELAKKLGWIPDIIHCHDWHTALVPAYLKEAYADDPFK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 634 SARICFTCHNFEYQGTAPAPDLSYCGLDVEQLDrPDRMQDnaHGRINVAKGGIVYSNIVTTVSPTYALEVRS-EGGRGLQ 712
Cdd:pfam08323 158 NIKTVFTIHNLAYQGRFPADLLDLLGLPPEDFN-LDGLEF--YGQINFLKAGIVYADAVTTVSPTYAEEIQTpEFGGGLD 234
|
....
gi 34809050 713 DTLK 716
Cdd:pfam08323 235 GLLR 238
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
479-960 |
4.42e-68 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 235.78 E-value: 4.42e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 479 IVHIAAEMAPVAKVGGLADVVAGLGKALQTKGHLVEIVLPKY-----------DCMQLDQI-TNLK----VLDVV----- 537
Cdd:PRK14098 8 VLYVSGEVSPFVRVSALADFMASFPQALEEEGFEARIMMPKYgtindrkfrlhDVLRLSDIeVPLKektdLLHVKvtalp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 538 ---IQSYFDGN--LFSNNVWtgtveglpvyFIEPQHpskffwraqyygeHDDFK----RYSYFSRAALELLYQSGKKIDI 608
Cdd:PRK14098 88 sskIQTYFLYNekYFKRNGL----------FTDMSL-------------GGDLKgsaeKVIFFNVGVLETLQRLGWKPDI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 609 IHCHDWQTAFVAPLYWDIYATRGF-SSARICFTCHNFEYQGTAPapdlsycgLDVEQLDRPDRMQDNAH---GRINVAKG 684
Cdd:PRK14098 145 IHCHDWYAGLVPLLLKTVYADHEFfKDIKTVLTIHNVYRQGVLP--------FKVFQKLLPEEVCSGLHregDEVNMLYT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 685 GIVYSNIVTTVSPTYALEVRSEGGR--GLQDTLKMHSRKFVGILNGIDTGTWNPSTDRFLAVQYSATDLQGKAANKAFLR 762
Cdd:PRK14098 217 GVEHADLLTTTSPRYAEEIAGDGEEafGLDKVLEERKMRLHGILNGIDTRQWNPSTDKLIKKRYSIERLDGKLENKKALL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 763 KQLGLySEDASQPLVACITRLVPQKGLHLIRHAIYKTAELGGQFVLLGSSpvphiQREFEGVADQFQKNNNIRLILKYD- 841
Cdd:PRK14098 297 EEVGL-PFDEETPLVGVIINFDDFQGAELLAESLEKLVELDIQLVICGSG-----DKEYEKRFQDFAEEHPEQVSVQTEf 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 842 -EALSHCIYAASDMFIIPSMFEPCGLTQMIAMRYGSVPIVRQTGGLCDSVFDFDDetipvELRNGFTFARTDEQDLSSCL 920
Cdd:PRK14098 371 tDAFFHLAIAGLDMLLMPGKIESCGMLQMFAMSYGTIPVAYAGGGIVETIEEVSE-----DKGSGFIFHDYTPEALVAKL 445
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 34809050 921 ERAFSYYSRKPMvWKQLVQKDMQIDFSWDSPASQYENLYQ 960
Cdd:PRK14098 446 GEALALYHDEER-WEELVLEAMERDFSWKNSAEEYAQLYR 484
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
478-960 |
1.82e-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: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 478 HIVHIAAEMAPVakVGGLADVVAGLGKALQTKGHLVEIVLPkydcmqldqitnlkvldvviqsyfdgnlfsnnvwtGTVE 557
Cdd:cd03801 1 KILLLSPELPPP--VGGAERHVRELARALAARGHDVTVLTP-----------------------------------ADPG 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 558 GLPVYFIEPQHPSKFFWRAQYYGEHDDFKRYSYFSRAAlellyqsgkKIDIIHCHDWQTAFVAPLYWdiyatrGFSSARI 637
Cdd:cd03801 44 EPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLRLR---------KFDVVHAHGLLAALLAALLA------LLLGAPL 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 638 CFTCHNFEYQGTAPAPDLSYcgldvEQLDRPDRMQDNAHGRInvakggivysnivtTVSPTYALEVRSEGGRglqdtlkm 717
Cdd:cd03801 109 VVTLHGAEPGRLLLLLAAER-----RLLARAEALLRRADAVI--------------AVSEALRDELRALGGI-------- 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 718 HSRKFVGILNGIDTGTWNPstdrflavqysatdlqgkaankaFLRKQLGLyseDASQPLVACITRLVPQKGLHLIRHAIY 797
Cdd:cd03801 162 PPEKIVVIPNGVDLERFSP-----------------------PLRRKLGI---PPDRPVLLFVGRLSPRKGVDLLLEALA 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 798 KTAELGG--QFVLLGSSP--VPHIQREFEGVADqfqknnNIRLILKYDEALSHCIYAASDMFIIPSMFEPCGLTQMIAMR 873
Cdd:cd03801 216 KLLRRGPdvRLVIVGGDGplRAELEELELGLGD------RVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMA 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 874 YGSVPIVRQTGGLCDSVfdfDDETipvelrNGFTFARTDEQDLSSCLERAFSYysrkPMVWKQLVQ---KDMQIDFSWDS 950
Cdd:cd03801 290 AGLPVVATDVGGLPEVV---EDGE------GGLVVPPDDVEALADALLRLLAD----PELRARLGRaarERVAERFSWER 356
|
490
....*....|
gi 34809050 951 PASQYENLYQ 960
Cdd:cd03801 357 VAERLLDLYR 366
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
828-964 |
5.91e-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: 5.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 828 FQKNNNIRLILkydEALshciYAASDMFIIPSMFEPCGLTQMIAMRYGSVPIVRQTGGLCDSVFDFDdetipvelrNGFT 907
Cdd:COG0438 4 LVPRKGLDLLL---EAL----LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGE---------TGLL 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 908 FARTDEQDLSSCLERAFSYYSRkpmvWKQLVQ---KDMQIDFSWDSPASQYENLYQSAVA 964
Cdd:COG0438 68 VPPGDPEALAEAILRLLEDPEL----RRRLGEaarERAEERFSWEAIAERLLALYEELLA 123
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
761-957 |
7.86e-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: 7.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 761 LRKQLGLyseDASQPLVACITRLVPQKGLH-LIRhAIYKTAELGGQFVLL---GSSPVPHIQREFEgvADQFQKNNniRL 836
Cdd:cd03800 210 RRARLLL---PPDKPVVLALGRLDPRKGIDtLVR-AFAQLPELRELANLVlvgGPSDDPLSMDREE--LAELAEEL--GL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 837 ILKYD-------EALSHcIYAASDMFIIPSMFEPCGLTQMIAMRYGsVPIV-RQTGGLCDSVfdfddetipVELRNGFTF 908
Cdd:cd03800 282 IDRVRfpgrvsrDDLPE-LYRAADVFVVPSLYEPFGLTAIEAMACG-TPVVaTAVGGLQDIV---------RDGRTGLLV 350
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 34809050 909 ARTDEQDLSSCLERAFsyysRKPMVWKQLvqKDMQID-----FSWDSPASQYEN 957
Cdd:cd03800 351 DPHDPEALAAALRRLL----DDPALWQRL--SRAGLErarahYTWESVADQLLT 398
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
775-922 |
1.98e-09 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 56.75 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 775 PLVACITRLVP-QKGLHLIRHAIY--KTAELGGQFVLLGSSPVPHIQREFEGVADqfqknnNIRLiLKYDEALSHcIYAA 851
Cdd:pfam13692 2 PVILFVGRLHPnVKGVDYLLEAVPllRKRDNDVRLVIVGDGPEEELEELAAGLED------RVIF-TGFVEDLAE-LLAA 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34809050 852 SDMFIIPSMFEPCGLTQMIAMRYGsVPIV-RQTGGLCDSVFDfddetipvelRNGFTFARTDEQDLSSCLER 922
Cdd:pfam13692 74 ADVFVLPSLYEGFGLKLLEAMAAG-LPVVaTDVGGIPELVDG----------ENGLLVPPGDPEALAEAILR 134
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
774-930 |
2.12e-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: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 774 QPLVACITRLVPQKGLHLIRHAIYKTAELGGQFVLL--GSSPVphiQREFEGVADQFQKNNNIRLIL-KYDEALSHCiYA 850
Cdd:pfam00534 2 KKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLViaGDGEE---EKRLKKLAEKLGLGDNVIFLGfVSDEDLPEL-LK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 851 ASDMFIIPSMFEPCGLTQMIAMRYGSVPIVRQTGGLCDSVFDFDdetipvelrNGFTFARTDEQDLSSCLERA------- 923
Cdd:pfam00534 78 IADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGE---------TGFLVKPNNAEALAEAIDKLledeelr 148
|
....*....
gi 34809050 924 --FSYYSRK 930
Cdd:pfam00534 149 erLGENARK 157
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
779-892 |
3.51e-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: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 779 CITRLVPQKGLHLIRHAI--YKTAELGGQFVLLGSSPVPhiQREFEGVADQFQKNNNIRLILKYDEALSHCIYAASDMFI 856
Cdd:cd01635 115 SVGRLVPEKGIDLLLEALalLKARLPDLVLVLVGGGGER--EEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFV 192
|
90 100 110
....*....|....*....|....*....|....*.
gi 34809050 857 IPSMFEPCGLTQMIAMRYGSVPIVRQTGGLCDSVFD 892
Cdd:cd01635 193 LPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVD 228
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
725-961 |
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 34809050 725 ILNGIDTGTWNPstdrflavqysatdlqgkaANKAFLRKQLGLySEDAsqPLVACITRLV--PQKGLH-LIR--HAIYKT 799
Cdd:cd03825 166 IPNGIDTEIFAP-------------------VDKAKARKRLGI-PQDK--KVILFGAESVtkPRKGFDeLIEalKLLATK 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 800 AELGGQFV-----LLGSSPVPHIQREFEgvadqfqkNNNIRLILkydealshcIYAASDMFIIPSMFEPCGLTQMIAMRY 874
Cdd:cd03825 224 DDLLLVVFgkndpQIVILPFDIISLGYI--------DDDEQLVD---------IYSAADLFVHPSLADNLPNTLLEAMAC 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 875 GSVPIVRQTGGLCDSVFDfddetipveLRNGFTFARTDEQDLSS----CLERAFSYYSRkpmvwKQLVQKDMQIDFSWDS 950
Cdd:cd03825 287 GTPVVAFDTGGSPEIVQH---------GVTGYLVPPGDVQALAEaiewLLANPKERESL-----GERARALAENHFDQRV 352
|
250
....*....|.
gi 34809050 951 PASQYENLYQS 961
Cdd:cd03825 353 QAQRYLELYKD 363
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
771-959 |
3.74e-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: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 771 DASQPLVAC-ITRLVPQKGLHLIRHAIYKTAELGGQFVLLGSSPVpHIQREFEGVAdqfqknnNIRLI--LKYDEALSHc 847
Cdd:cd03823 187 PGTERLRFGyIGRLTEEKGIDLLVEAFKRLPREDIELVIAGHGPL-SDERQIEGGR-------RIAFLgrVPTDDIKDF- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 848 iYAASDMFIIPSMF-EPCGLTQMIAMRYGSVPIVRQTGGLCDSVfdfddetipVELRNGFTFARTDEQDLSSCLERAfsy 926
Cdd:cd03823 258 -YEKIDVLVVPSIWpEPFGLVVREAIAAGLPVIASDLGGIAELI---------QPGVNGLLFAPGDAEDLAAAMRRL--- 324
|
170 180 190
....*....|....*....|....*....|...
gi 34809050 927 ySRKPMVWKQLvQKDMQIDFSWDSPASQYENLY 959
Cdd:cd03823 325 -LTDPALLERL-RAGAEPPRSTESQAEEYLKLY 355
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
693-890 |
7.81e-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: 7.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 693 TTVSPTYALEVRSEGgRGLQDtlkmhsrkfVGILN-GIDTGTWNPStdrflavqysatdlqgkAANKAFLRKQLglyseD 771
Cdd:cd03814 148 TTLVPSPSIARELEG-HGFER---------VRLWPrGVDTELFHPS-----------------RRDAALRRRLG-----P 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 772 ASQPLVACITRLVPQKGLHLIRHAIYK-TAELGGQFVLLGSSPvphiQREfegvADQFQKNNNIRLILKYDEALSHcIYA 850
Cdd:cd03814 196 PGRPLLLYVGRLAPEKNLEALLDADLPlAASPPVRLVVVGDGP----ARA----ELEARGPDVIFTGFLTGEELAR-AYA 266
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 34809050 851 ASDMFIIPSMFEPCGLTQMIAMRYGsVP-IVRQTGGLCDSV 890
Cdd:cd03814 267 SADVFVFPSRTETFGLVVLEAMASG-LPvVAADAGGPRDIV 306
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
54-339 |
3.10e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 54 KQRSSNAKLLLTTEENGQLPSTS-LRTSMERpQKSTSSEDDTNG---AISQIDEKIAAIgNEQQERSKDKHFESDFQLED 129
Cdd:PRK02224 168 RERASDARLGVERVLSDQRGSLDqLKAQIEE-KEEKDLHERLNGlesELAELDEEIERY-EEQREQARETRDEADEVLEE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 130 FGEMIQNMEKnillLNQARLQAIEDVDKILTEKEALQKKV-------DTLEMNLSKALATKGNINTDIPG--DHLEKFTK 200
Cdd:PRK02224 246 HEERREELET----LEAEIEDLRETIAETEREREELAEEVrdlrerlEELEEERDDLLAEAGLDDADAEAveARREELED 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 201 EI------LIESALSGGNPAHLCESpLFMELTVLKEENMLLKADAQFLKAKIvefAETEEFLFKLEKERSLLDATVRELE 274
Cdd:PRK02224 322 RDeelrdrLEECRVAAQAHNEEAES-LREDADDLEERAEELREEAAELESEL---EEAREAVEDRREEIEELEEEIEELR 397
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34809050 275 ARFLVAQTDiwkvvplqydvwmekvenlqhmLGCLKNHVEkyaALLDQHDDLHDKIDELEASLKE 339
Cdd:PRK02224 398 ERFGDAPVD----------------------LGNAEDFLE---ELREERDELREREAELEATLRT 437
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
493-731 |
3.87e-04 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 42.13 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 493 GGLADVVAGLGKALQTKGHLVEIVLPKYDcmqldqitnlkvldvviqsyfdgNLFSNNVWTGTVEGLPVYFIEPqhpskf 572
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGP-----------------------GPLAEEVVRVVRVPRVPLPLPP------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 573 fwraqyygehdDFKRYSYFSRAALELLyqSGKKIDIIHCHDWqtafvAPLYWDIYATRGFSSARICFTCHNFEYQGTAPA 652
Cdd:pfam13439 52 -----------RLLRSLAFLRRLRRLL--RRERPDVVHAHSP-----FPLGLAALAARLRLGIPLVVTYHGLFPDYKRLG 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34809050 653 PDLSYCGLDVEQLDRpdRMQDNAHGrinvakggivysniVTTVSPTyaleVRSEggrgLQDTLKMHSRKFVGILNGIDT 731
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 ... |
691-880 |
8.87e-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: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 691 IVTTvSPTYALEvrSEggrglqdTLKMHSRKFVGILNGIDtgtwnpstdrflAVQYSATDLQGKAANKAFLRKQLGLYse 770
Cdd:cd03795 141 IIAT-SPNYVET--SP-------TLREFKNKVRVIPLGID------------KNVYNIPRVDFENIKREKKGKKIFLF-- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 771 dasqplvacITRLVPQKGLH-LIRHAIYKTAELggqfVLLGSSPvphIQREFEGVADQfQKNNNIRLILKYDEALSHCIY 849
Cdd:cd03795 197 ---------IGRLVYYKGLDyLIEAAQYLNYPI----VIGGEGP---LKPDLEAQIEL-NLLDNVKFLGRVDDEEKVIYL 259
|
170 180 190
....*....|....*....|....*....|...
gi 34809050 850 AASDMFIIPSMF--EPCGLTQMIAMRYGsVPIV 880
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 ... |
848-960 |
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 34809050 848 IYAASDMFIIPSMFEPCGLTQMIAMRYGSVPIVRQTGGlcdsvfdfddetIPVELRNGFTFARTDEQDLSSCLERAFSYY 927
Cdd:cd04962 266 LLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGG------------IPEVVKHGETGFLSDVGDVDAMAKSALSIL 333
|
90 100 110
....*....|....*....|....*....|....*.
gi 34809050 928 sRKPMVWKQLVQ---KDMQIDFSWDSPASQYENLYQ 960
Cdd:cd04962 334 -EDDELYNRMGRaarKRAAERFDPERIVPQYEAYYR 368
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
126-400 |
2.05e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 126 QLEDFGEMIQNMEKNILLLNqARLQAIEdvdKILTEKEALQKKVDTLEMNLSKALATKGNINTDIP--GDHLEKFTKEIL 203
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIK-RRIERLE---KFIKRTENIEELIKEKEKELEEVLREINEISSELPelREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 204 -IESalsggnpahlcespLFMELTVLKEENMLLKADAQFLKAKIVefaETEEFLFKLEKERSLLDATVRELE-------- 274
Cdd:PRK03918 232 eLEE--------------LKEEIEELEKELESLEGSKRKLEEKIR---ELEERIEELKKEIEELEEKVKELKelkekaee 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 275 ----ARFLVAQTDIWKVVPLQYDVWMEKVENLQHMLGCLKNHVEKYAALLDQHDDLHDKIDELEASLK------------ 338
Cdd:PRK03918 295 yiklSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHElyeeakakkeel 374
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34809050 339 EGKTSEFSPYVVELLQQKLKAAKSHHqaghqetnthiqvyqqltEEFQDNLGKLIEESGRLE 400
Cdd:PRK03918 375 ERLKKRLTGLTPEKLEKELEELEKAK------------------EEIEEEISKITARIGELK 418
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
87-339 |
2.72e-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: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 87 STSSEDDTNGAISQIDEKIAAIgNEQQERSKDKHFESDFQLEDFGEMIQNMEKNILLLNQARLQAIEDVDKILTEKEALQ 166
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAEL-EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 167 KKVDTLEMNLSKALATkgnintdipgdhLEKFTKEILIESALSGGNPAHlcespLFMELTVLKEENMLLKADAQFLKAKI 246
Cdd:COG4942 97 AELEAQKEELAELLRA------------LYRLGRQPPLALLLSPEDFLD-----AVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 247 VEFAETEEflfKLEKERSLLDATVRELEARFLVAQTDIwkvvplqydvwMEKVENLQHMLGCLKNHVEKYAALLDQHDDL 326
Cdd:COG4942 160 AELAALRA---ELEAERAELEALLAELEEERAALEALK-----------AERQKLLARLEKELAELAAELAELQQEAEEL 225
|
250
....*....|...
gi 34809050 327 HDKIDELEASLKE 339
Cdd:COG4942 226 EALIARLEAEAAA 238
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
131-362 |
5.00e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 131 GEMIQNMEKNILLLNQARLQAIEDVDKILTEKEALQKKVDTLEMNLSKALATKGN-------INTDIPGDHLEKFTKEIL 203
Cdd:PRK03918 383 GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreLTEEHRKELLEEYTAELK 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 204 ----------------------IESALSGgnpahlcESPLFMELTVLKE----ENMLLKADAQFLKAKIVEFAETEEFLF 257
Cdd:PRK03918 463 riekelkeieekerklrkelreLEKVLKK-------ESELIKLKELAEQlkelEEKLKKYNLEELEKKAEEYEKLKEKLI 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 258 KLEKERSLLDATVRELEARflvaqtdIWKVVPLQydvwmEKVENLQHMLGCLKNHVEKYAalLDQHDDLHDKIDELEASL 337
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEEL-------KKKLAELE-----KKLDELEEELAELLKELEELG--FESVEELEERLKELEPFY 601
|
250 260
....*....|....*....|....*
gi 34809050 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 ... |
692-880 |
5.39e-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: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 692 VTTVSPTYALEVRSEGGRglqdtlkmhSRKFVGILNGIDTGTWNPStdrflavqysatdlqgkAANKAFLRKQLGLyseD 771
Cdd:cd03807 137 TVANSSAVAEFHQEQGYA---------KNKIVVIYNGIDLFKLSPD-----------------DASRARARRRLGL---A 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 772 ASQPLVACITRLVPQKGLHLIRHAIYKTAELGGQ--FVLLGSSPV-PHIQREFE--GVADQFqknnnirLILKYDEALSH 846
Cdd:cd03807 188 EDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDlrLLLVGRGPErPNLERLLLelGLEDRV-------HLLGERSDVPA 260
|
170 180 190
....*....|....*....|....*....|....
gi 34809050 847 CiYAASDMFIIPSMFEPCGLTQMIAMRYGsVPIV 880
Cdd:cd03807 261 L-LPAMDIFVLSSRTEGFPNALLEAMACG-LPVV 292
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
92-277 |
5.98e-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: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 92 DDTNGAISQIDEKIAAiGNEQQERSKDKHFEsdFQLEDFGEMIQNMEKniLLLNQARLQAIEDVDKILTEK-EALQKKVD 170
Cdd:pfam12128 304 DELNGELSAADAAVAK-DRSELEALEDQHGA--FLDADIETAAADQEQ--LPSWQSELENLEERLKALTGKhQDVTAKYN 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34809050 171 TLEMNLSKALATK-GNINTDIPGDHLEKFTKEILIESALSGgnpahlCESPLFMEL----TVLKEENMLLKADAQFLKAK 245
Cdd:pfam12128 379 RRRSKIKEQNNRDiAGIKDKLAKIREARDRQLAVAEDDLQA------LESELREQLeagkLEFNEEEYRLKSRLGELKLR 452
|
170 180 190
....*....|....*....|....*....|..
gi 34809050 246 IVEFAETEEFLFKLEKERSLLDATVRELEARF 277
Cdd:pfam12128 453 LNQATATPELLLQLENFDERIERAREEQEAAN 484
|
|
| |
