|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02316 |
PLN02316 |
synthase/transferase |
875-1787 |
0e+00 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 1779.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 875 QELRRMLQELADQNCSMGNKLFVFPEAVKANSTIDVYLNRNLSALANEPDVHIKGAFNSWRWRPFTERLHKSELSGDWWS 954
Cdd:PLN02316 123 NLRKREIEELAEENFSRGNKLFVYPQVVKPDSDIEVYLNRSLSTLANEPDVLIMGAFNGWRWKSFTERLEKTELGGDWWS 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 955 CKLHIPKEAYRLDFVFFNGRLVYDNNDSNDFVLQVESTMDEDSFEEFLVEEKKRELERVATEEAERRRHAEEQQRMGEQR 1034
Cdd:PLN02316 203 CKLHIPKEAYKMDFVFFNGQNVYDNNDHKDFCVEIEGGMDEHSFEDFLLEEKRRELEKLAKEEAERERQAEEQRRREEEK 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1035 AAEQAAREQAKKEIELKKNKLQNLLSSARTHVDNLWHIEPSTYRQGDTVRLYYNRNSRPLMHSTEIWMHGGCNSWTDGLS 1114
Cdd:PLN02316 283 AAMEADRAQAKAEVEKRREKLQNLLKKASRSADNVWYIEPSEFKAGDTVKLYYNRSSGPLAHSTEIWIHGGYNNWIDGLS 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1115 IVERLVECDDENGDWWYANVHIPEKAFVLDWVFADGPPGNARNYDNNGRQDFHAILPNAMTNEEYWVEEENCIYTRLLHE 1194
Cdd:PLN02316 363 IVEKLVKSEEKDGDWWYAEVVVPERALVLDWVFADGPPGNARNYDNNGRQDFHAIVPNNIPEELYWVEEEHQIYRKLQEE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1195 IREREEAIKIKVEKRAKMKSEMKEKTMRMFLLSQKHIVYTEPLEIRAGTTVDVLYNPSNTVLNGKPEVWFRWSFNRWMHP 1274
Cdd:PLN02316 443 RRLREEAIRAKAEKTARMKAEMKEKTLKMFLLSQKHIVYTEPLEVQAGTTVTVLYNPANTVLNGKPEVWFRGSFNRWTHR 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1275 SGVLPPKKMVKTEDGCHLKATVSVPSDAYMMDFVFSESEEGGIYDNRNGTDYHIPVSGSNAKEPPIHIVHIAVEMAPIAK 1354
Cdd:PLN02316 523 LGPLPPQKMVPADNGSHLKATVKVPLDAYMMDFVFSEKEEGGIFDNRNGLDYHIPVFGGIAKEPPMHIVHIAVEMAPIAK 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1355 VGGLADVVTSLSRAIQELGHHVEVILPKYNFMNQSNVKNLHVRQSFSLGGTEIKVWFGLVEDLSVYFLEPQNGMFGGGWV 1434
Cdd:PLN02316 603 VGGLGDVVTSLSRAVQDLNHNVDIILPKYDCLNLSHVKDLHYQRSYSWGGTEIKVWFGKVEGLSVYFLEPQNGMFWAGCV 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1435 YGG-NDAGRFGLFCQSALEFLLQSGSSPHIIHCHDWSSAPVAWLYKEHYAESRLATARIIFTIHNLEFGAHFIGKAMTYC 1513
Cdd:PLN02316 683 YGCrNDGERFGFFCHAALEFLLQSGFHPDIIHCHDWSSAPVAWLFKDHYAHYGLSKARVVFTIHNLEFGANHIGKAMAYA 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1514 DKATTVSHTYSKEVAGHGAIAPHRGKFYGILNGIDPDIWDPYTDNFIPMHYTSENVVEGKNAAKRALQQRFGLQQTDVPI 1593
Cdd:PLN02316 763 DKATTVSPTYSREVSGNSAIAPHLYKFHGILNGIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEALQQRLGLKQADLPL 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1594 VGIITRLTAQKGIHLIKHALHRTLERNGQVVLLGSAPDPRIQSDFCRLADSLHGENHGRVRLCLTYDEPLSHLIYAGSDF 1673
Cdd:PLN02316 843 VGIITRLTHQKGIHLIKHAIWRTLERNGQVVLLGSAPDPRIQNDFVNLANQLHSSHHDRARLCLTYDEPLSHLIYAGADF 922
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1674 ILVPSIFEPCGLTQLVAMRYGSIPIVRKTGGLYDTVFDVDHDKDRARVLGLEPNGFSFDGADCNGVDYALNRAISSWFEA 1753
Cdd:PLN02316 923 ILVPSIFEPCGLTQLTAMRYGSIPVVRKTGGLFDTVFDVDHDKERAQAQGLEPNGFSFDGADAAGVDYALNRAISAWYDG 1002
|
890 900 910
....*....|....*....|....*....|....
gi 1002292629 1754 RGWFHSLCKRVMEQDWSWNRPALDYIELYHSAHK 1787
Cdd:PLN02316 1003 RDWFNSLCKRVMEQDWSWNRPALDYMELYHSARK 1036
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
1341-1784 |
4.67e-174 |
|
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: 534.84 E-value: 4.67e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1341 HIVHIAVEMAPIAKVGGLADVVTSLSRAIQELGHHVEVILPKYNFMNQSNVKNLHVRQS---FSLGGTEIKVWFGLVEDL 1417
Cdd:cd03791 1 KVLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRVLGLevkVGGRGEEVGVFELPVDGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1418 SVYFLEPQNgMFGGGWVYGGN------DAGRFGLFCQSALEFLLQSGSSPHIIHCHDWSSAPVAWLYKEHYAESRLATAR 1491
Cdd:cd03791 81 DYYFLDNPE-FFDRPGLPGPPgydypdNAERFAFFSRAALELLRRLGFQPDIIHANDWHTALVPAYLKTRYRGPGFKKIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1492 IIFTIHNLEF----------------------GAHFIGK------AMTYCDKATTVSHTYSKEVA-------GHGAIAPH 1536
Cdd:cd03791 160 TVFTIHNLAYqglfpldtlaelglppelfhidGLEFYGQinflkaGIVYADRVTTVSPTYAKEILtpeygegLDGVLRAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1537 RGKFYGILNGIDPDIWDPYTDNFIPMHYtSENVVEGKNAAKRALQQRFGLQQ-TDVPIVGIITRLTAQKGIHLIKHALHR 1615
Cdd:cd03791 240 AGKLSGILNGIDYDEWNPATDKLIPANY-SANDLEGKAENKAALQKELGLPVdPDAPLFGFVGRLTEQKGVDLILDALPE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1616 TLERNGQVVLLGSApDPRIQSDFCRLADslhgENHGRVRLCLTYDEPLSHLIYAGSDFILVPSIFEPCGLTQLVAMRYGS 1695
Cdd:cd03791 319 LLEEGGQLVVLGSG-DPEYEQAFRELAE----RYPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYAMRYGT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1696 IPIVRKTGGLYDTVFDVDHDKDrarvlglEPNGFSFDGADCNGVDYALNRAISSWFEaRGWFHSLCKRVMEQDWSWNRPA 1775
Cdd:cd03791 394 LPIVRRTGGLADTVFDYDPETG-------EGTGFVFEDYDAEALLAALRRALALYRN-PELWRKLQKNAMKQDFSWDKSA 465
|
....*....
gi 1002292629 1776 LDYIELYHS 1784
Cdd:cd03791 466 KEYLELYRS 474
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
1341-1785 |
3.24e-166 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 513.87 E-value: 3.24e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1341 HIVHIAVEMAPIAKVGGLADVVTSLSRAIQELGHHVEVILPKYNFMNQsNVKNLHVRQSFS--LGGTEIK--VWFGLVED 1416
Cdd:COG0297 2 KILFVASEAAPFAKTGGLADVVGALPKALAKLGHDVRVVLPGYPSIDD-KLKDLEVVASLEvpLGGRTYYarVLEGPDDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1417 LSVYFLEpQNGMFGGGWVYGGN------DAGRFGLFCQSALEFLLQSGSSPHIIHCHDWSSAPVAWLYKEHYAESRLATA 1490
Cdd:COG0297 81 VPVYFID-NPELFDRPGPYGDPdrdypdNAERFAFFSRAALELLKGLDWKPDIIHCHDWQTGLIPALLKTRYADDPFKRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1491 RIIFTIHNLEF----------------------GAHFIGK------AMTYCDKATTVSHTYSKEV------AG-HGAIAP 1535
Cdd:COG0297 160 KTVFTIHNLAYqgifpaeilellglppelftpdGLEFYGQinflkaGIVYADRVTTVSPTYAREIqtpefgEGlDGLLRA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1536 HRGKFYGILNGIDPDIWDPYTDNFIPMHYTSENVvEGKNAAKRALQQRFGLQQT-DVPIVGIITRLTAQKGIHLIKHALH 1614
Cdd:COG0297 240 RSGKLSGILNGIDYDVWNPATDPYLPANYSADDL-EGKAANKAALQEELGLPVDpDAPLIGMVSRLTEQKGLDLLLEALD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1615 RTLERNGQVVLLGSApDPRIQSDFCRLADslhgENHGRVRLCLTYDEPLSHLIYAGSDFILVPSIFEPCGLTQLVAMRYG 1694
Cdd:COG0297 319 ELLEEDVQLVVLGSG-DPEYEEAFRELAA----RYPGRVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQMYALRYG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1695 SIPIVRKTGGLYDTVFDVDHDKDRArvlglepNGFSFDGADCNGVDYALNRAISSWFEARGWfHSLCKRVMEQDWSWNRP 1774
Cdd:COG0297 394 TVPIVRRTGGLADTVIDYNEATGEG-------TGFVFDEYTAEALLAAIRRALALYRDPEAW-RKLQRNAMKQDFSWEKS 465
|
490
....*....|.
gi 1002292629 1775 ALDYIELYHSA 1785
Cdd:COG0297 466 AKEYLELYREL 476
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
1340-1785 |
2.46e-150 |
|
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: 470.98 E-value: 2.46e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1340 IHIVHIAVEMAPIAKVGGLADVVTSLSRAIQELGHHVEVILPKYNFMNQSNVKNLHV--RQSFSLGGT--EIKVWFGLVE 1415
Cdd:TIGR02095 1 MRVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEVDDQVKVveLVDLSVGPRtlYVKVFEGVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1416 DLSVYFLEPQNGMFGGGWVYGGN---DAGRFGLFCQSALEFLLQSGSSPHIIHCHDWSSAPVAWLYKEHYAESRlatARI 1492
Cdd:TIGR02095 81 GVPVYFIDNPSLFDRPGGIYGDDypdNAERFAFFSRAAAELLSGLGWQPDVVHAHDWHTALVPALLKAVYRPNP---IKT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1493 IFTIHNLEF----------------------GAHFIGK------AMTYCDKATTVSHTYSKEV----AG---HGAIAPHR 1537
Cdd:TIGR02095 158 VFTIHNLAYqgvfpaddfselglppeyfhmeGLEFYGRvnflkgGIVYADRVTTVSPTYAREIltpeFGyglDGVLKARS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1538 GKFYGILNGIDPDIWDPYTDNFIPMHYTSENVvEGKNAAKRALQQRFGLQQ-TDVPIVGIITRLTAQKGIHLIKHALHRT 1616
Cdd:TIGR02095 238 GKLRGILNGIDTEVWNPATDPYLKANYSADDL-AGKAENKEALQEELGLPVdDDVPLFGVISRLTQQKGVDLLLAALPEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1617 LERNGQVVLLGSApDPRIQSDFCRLAdslhGENHGRVRLCLTYDEPLSHLIYAGSDFILVPSIFEPCGLTQLVAMRYGSI 1696
Cdd:TIGR02095 317 LELGGQLVVLGTG-DPELEEALRELA----ERYPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQLYAMRYGTV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1697 PIVRKTGGLYDTVFDVDHDKDRArvlglepNGFSFDGADCNGVDYALNRAISSWFEARGWFHSLCKRVMEQDWSWNRPAL 1776
Cdd:TIGR02095 392 PIVRRTGGLADTVVDGDPEAESG-------TGFLFEEYDPGALLAALSRALRLYRQDPSLWEALQKNAMSQDFSWDKSAK 464
|
....*....
gi 1002292629 1777 DYIELYHSA 1785
Cdd:TIGR02095 465 QYVELYRSL 473
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
1342-1527 |
2.45e-56 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 196.01 E-value: 2.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1342 IVHIAVEMAPIAKVGGLADVVTSLSRAIQELGHHVEVILPKYNFMNQS-----NVKNLHVRQSFSLGGTEIKVWFGLVED 1416
Cdd:pfam08323 1 ILFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGNIPEErnqleDVIRLSVAAGVPVRPLTVGVARLELDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1417 LSVYFLEPQNgMFGGGWVYGG------NDAGRFGLFCQSALEFLLQSGSSPHIIHCHDWSSAPVAWLYKEHYAESRLATA 1490
Cdd:pfam08323 81 VDVYFLDNPD-YFDRPGLYGDdgrdyeDNAERFAFFSRAALELAKKLGWIPDIIHCHDWHTALVPAYLKEAYADDPFKNI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002292629 1491 RIIFTIHNLEFGAHFIGK----------------------------AMTYCDKATTVSHTYSKEV 1527
Cdd:pfam08323 160 KTVFTIHNLAYQGRFPADlldllglppedfnldglefygqinflkaGIVYADAVTTVSPTYAEEI 224
|
|
| CBM_25 |
smart01066 |
Carbohydrate binding domain; |
1242-1331 |
1.65e-16 |
|
Carbohydrate binding domain;
Pssm-ID: 198134 [Multi-domain] Cd Length: 83 Bit Score: 75.86 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1242 GTTVDVLYNPSNTVlNGKPEVWFRWSF--NRWMHPSGVlppkKMVKTEDGcHLKATVsVPSDAYMMDFVFSEseEGGIYD 1319
Cdd:smart01066 1 GNTVTVYYNGLLAT-SGAKNVYLHYGFgeNNWTDVPDV----RMEKTGEG-WVKATI-PVKEAYKLNFCFKD--GAGNWD 71
|
90
....*....|..
gi 1002292629 1320 NRNGTDYHIPVS 1331
Cdd:smart01066 72 NNGGANYHFEIG 83
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
72-182 |
1.91e-04 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 46.40 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 72 VASSRGYAPRIAAESSIQEREHINSDEETFDTYNRLLRNESTEW--KKLDTTEVDLSQDVSSSSMRKVDATDEAkLDILE 149
Cdd:PLN02316 8 GSAPRGFAPRTTVESSQKRIQQNNGDKEDSSTSTSSLSVSAVEKtsNAKEEIQVDFQHNSESAVEEVEAEDEIE-VEQNQ 86
|
90 100 110
....*....|....*....|....*....|...
gi 1002292629 150 DDLPRNLLNGVTMGEvdMLDEAGAEDDVFEVDL 182
Cdd:PLN02316 87 SDVLKSSSIVKEESI--STDMDGIDDDSLDRKL 117
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02316 |
PLN02316 |
synthase/transferase |
875-1787 |
0e+00 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 1779.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 875 QELRRMLQELADQNCSMGNKLFVFPEAVKANSTIDVYLNRNLSALANEPDVHIKGAFNSWRWRPFTERLHKSELSGDWWS 954
Cdd:PLN02316 123 NLRKREIEELAEENFSRGNKLFVYPQVVKPDSDIEVYLNRSLSTLANEPDVLIMGAFNGWRWKSFTERLEKTELGGDWWS 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 955 CKLHIPKEAYRLDFVFFNGRLVYDNNDSNDFVLQVESTMDEDSFEEFLVEEKKRELERVATEEAERRRHAEEQQRMGEQR 1034
Cdd:PLN02316 203 CKLHIPKEAYKMDFVFFNGQNVYDNNDHKDFCVEIEGGMDEHSFEDFLLEEKRRELEKLAKEEAERERQAEEQRRREEEK 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1035 AAEQAAREQAKKEIELKKNKLQNLLSSARTHVDNLWHIEPSTYRQGDTVRLYYNRNSRPLMHSTEIWMHGGCNSWTDGLS 1114
Cdd:PLN02316 283 AAMEADRAQAKAEVEKRREKLQNLLKKASRSADNVWYIEPSEFKAGDTVKLYYNRSSGPLAHSTEIWIHGGYNNWIDGLS 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1115 IVERLVECDDENGDWWYANVHIPEKAFVLDWVFADGPPGNARNYDNNGRQDFHAILPNAMTNEEYWVEEENCIYTRLLHE 1194
Cdd:PLN02316 363 IVEKLVKSEEKDGDWWYAEVVVPERALVLDWVFADGPPGNARNYDNNGRQDFHAIVPNNIPEELYWVEEEHQIYRKLQEE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1195 IREREEAIKIKVEKRAKMKSEMKEKTMRMFLLSQKHIVYTEPLEIRAGTTVDVLYNPSNTVLNGKPEVWFRWSFNRWMHP 1274
Cdd:PLN02316 443 RRLREEAIRAKAEKTARMKAEMKEKTLKMFLLSQKHIVYTEPLEVQAGTTVTVLYNPANTVLNGKPEVWFRGSFNRWTHR 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1275 SGVLPPKKMVKTEDGCHLKATVSVPSDAYMMDFVFSESEEGGIYDNRNGTDYHIPVSGSNAKEPPIHIVHIAVEMAPIAK 1354
Cdd:PLN02316 523 LGPLPPQKMVPADNGSHLKATVKVPLDAYMMDFVFSEKEEGGIFDNRNGLDYHIPVFGGIAKEPPMHIVHIAVEMAPIAK 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1355 VGGLADVVTSLSRAIQELGHHVEVILPKYNFMNQSNVKNLHVRQSFSLGGTEIKVWFGLVEDLSVYFLEPQNGMFGGGWV 1434
Cdd:PLN02316 603 VGGLGDVVTSLSRAVQDLNHNVDIILPKYDCLNLSHVKDLHYQRSYSWGGTEIKVWFGKVEGLSVYFLEPQNGMFWAGCV 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1435 YGG-NDAGRFGLFCQSALEFLLQSGSSPHIIHCHDWSSAPVAWLYKEHYAESRLATARIIFTIHNLEFGAHFIGKAMTYC 1513
Cdd:PLN02316 683 YGCrNDGERFGFFCHAALEFLLQSGFHPDIIHCHDWSSAPVAWLFKDHYAHYGLSKARVVFTIHNLEFGANHIGKAMAYA 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1514 DKATTVSHTYSKEVAGHGAIAPHRGKFYGILNGIDPDIWDPYTDNFIPMHYTSENVVEGKNAAKRALQQRFGLQQTDVPI 1593
Cdd:PLN02316 763 DKATTVSPTYSREVSGNSAIAPHLYKFHGILNGIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEALQQRLGLKQADLPL 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1594 VGIITRLTAQKGIHLIKHALHRTLERNGQVVLLGSAPDPRIQSDFCRLADSLHGENHGRVRLCLTYDEPLSHLIYAGSDF 1673
Cdd:PLN02316 843 VGIITRLTHQKGIHLIKHAIWRTLERNGQVVLLGSAPDPRIQNDFVNLANQLHSSHHDRARLCLTYDEPLSHLIYAGADF 922
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1674 ILVPSIFEPCGLTQLVAMRYGSIPIVRKTGGLYDTVFDVDHDKDRARVLGLEPNGFSFDGADCNGVDYALNRAISSWFEA 1753
Cdd:PLN02316 923 ILVPSIFEPCGLTQLTAMRYGSIPVVRKTGGLFDTVFDVDHDKERAQAQGLEPNGFSFDGADAAGVDYALNRAISAWYDG 1002
|
890 900 910
....*....|....*....|....*....|....
gi 1002292629 1754 RGWFHSLCKRVMEQDWSWNRPALDYIELYHSAHK 1787
Cdd:PLN02316 1003 RDWFNSLCKRVMEQDWSWNRPALDYMELYHSARK 1036
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
1341-1784 |
4.67e-174 |
|
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: 534.84 E-value: 4.67e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1341 HIVHIAVEMAPIAKVGGLADVVTSLSRAIQELGHHVEVILPKYNFMNQSNVKNLHVRQS---FSLGGTEIKVWFGLVEDL 1417
Cdd:cd03791 1 KVLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRVLGLevkVGGRGEEVGVFELPVDGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1418 SVYFLEPQNgMFGGGWVYGGN------DAGRFGLFCQSALEFLLQSGSSPHIIHCHDWSSAPVAWLYKEHYAESRLATAR 1491
Cdd:cd03791 81 DYYFLDNPE-FFDRPGLPGPPgydypdNAERFAFFSRAALELLRRLGFQPDIIHANDWHTALVPAYLKTRYRGPGFKKIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1492 IIFTIHNLEF----------------------GAHFIGK------AMTYCDKATTVSHTYSKEVA-------GHGAIAPH 1536
Cdd:cd03791 160 TVFTIHNLAYqglfpldtlaelglppelfhidGLEFYGQinflkaGIVYADRVTTVSPTYAKEILtpeygegLDGVLRAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1537 RGKFYGILNGIDPDIWDPYTDNFIPMHYtSENVVEGKNAAKRALQQRFGLQQ-TDVPIVGIITRLTAQKGIHLIKHALHR 1615
Cdd:cd03791 240 AGKLSGILNGIDYDEWNPATDKLIPANY-SANDLEGKAENKAALQKELGLPVdPDAPLFGFVGRLTEQKGVDLILDALPE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1616 TLERNGQVVLLGSApDPRIQSDFCRLADslhgENHGRVRLCLTYDEPLSHLIYAGSDFILVPSIFEPCGLTQLVAMRYGS 1695
Cdd:cd03791 319 LLEEGGQLVVLGSG-DPEYEQAFRELAE----RYPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYAMRYGT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1696 IPIVRKTGGLYDTVFDVDHDKDrarvlglEPNGFSFDGADCNGVDYALNRAISSWFEaRGWFHSLCKRVMEQDWSWNRPA 1775
Cdd:cd03791 394 LPIVRRTGGLADTVFDYDPETG-------EGTGFVFEDYDAEALLAALRRALALYRN-PELWRKLQKNAMKQDFSWDKSA 465
|
....*....
gi 1002292629 1776 LDYIELYHS 1784
Cdd:cd03791 466 KEYLELYRS 474
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
1341-1785 |
3.24e-166 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 513.87 E-value: 3.24e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1341 HIVHIAVEMAPIAKVGGLADVVTSLSRAIQELGHHVEVILPKYNFMNQsNVKNLHVRQSFS--LGGTEIK--VWFGLVED 1416
Cdd:COG0297 2 KILFVASEAAPFAKTGGLADVVGALPKALAKLGHDVRVVLPGYPSIDD-KLKDLEVVASLEvpLGGRTYYarVLEGPDDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1417 LSVYFLEpQNGMFGGGWVYGGN------DAGRFGLFCQSALEFLLQSGSSPHIIHCHDWSSAPVAWLYKEHYAESRLATA 1490
Cdd:COG0297 81 VPVYFID-NPELFDRPGPYGDPdrdypdNAERFAFFSRAALELLKGLDWKPDIIHCHDWQTGLIPALLKTRYADDPFKRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1491 RIIFTIHNLEF----------------------GAHFIGK------AMTYCDKATTVSHTYSKEV------AG-HGAIAP 1535
Cdd:COG0297 160 KTVFTIHNLAYqgifpaeilellglppelftpdGLEFYGQinflkaGIVYADRVTTVSPTYAREIqtpefgEGlDGLLRA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1536 HRGKFYGILNGIDPDIWDPYTDNFIPMHYTSENVvEGKNAAKRALQQRFGLQQT-DVPIVGIITRLTAQKGIHLIKHALH 1614
Cdd:COG0297 240 RSGKLSGILNGIDYDVWNPATDPYLPANYSADDL-EGKAANKAALQEELGLPVDpDAPLIGMVSRLTEQKGLDLLLEALD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1615 RTLERNGQVVLLGSApDPRIQSDFCRLADslhgENHGRVRLCLTYDEPLSHLIYAGSDFILVPSIFEPCGLTQLVAMRYG 1694
Cdd:COG0297 319 ELLEEDVQLVVLGSG-DPEYEEAFRELAA----RYPGRVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQMYALRYG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1695 SIPIVRKTGGLYDTVFDVDHDKDRArvlglepNGFSFDGADCNGVDYALNRAISSWFEARGWfHSLCKRVMEQDWSWNRP 1774
Cdd:COG0297 394 TVPIVRRTGGLADTVIDYNEATGEG-------TGFVFDEYTAEALLAAIRRALALYRDPEAW-RKLQRNAMKQDFSWEKS 465
|
490
....*....|.
gi 1002292629 1775 ALDYIELYHSA 1785
Cdd:COG0297 466 AKEYLELYREL 476
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
1341-1785 |
1.43e-161 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 500.80 E-value: 1.43e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1341 HIVHIAVEMAPIAKVGGLADVVTSLSRAIQELGHHVEVILPKYNFMNQSNVKNLHVRQSFSLggteiKVWFGLVE--DLS 1418
Cdd:PRK00654 2 KILFVASECAPLIKTGGLGDVVGALPKALAALGHDVRVLLPGYPAIREKLRDAQVVGRLDLF-----TVLFGHLEgdGVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1419 VYFLEPQNgMFGGGWVYGGND-AGRFGLFCQSALEFLLQSGSSPHIIHCHDWSSAPVAWLYKEHYAeSRLATARIIFTIH 1497
Cdd:PRK00654 77 VYLIDAPH-LFDRPSGYGYPDnGERFAFFSWAAAEFAEGLDPRPDIVHAHDWHTGLIPALLKEKYW-RGYPDIKTVFTIH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1498 NLEF----------------------GAHFIGK------AMTYCDKATTVSHTYSKEV----AGHG---AIAPHRGKFYG 1542
Cdd:PRK00654 155 NLAYqglfpaeilgelglpaeafhleGLEFYGQisflkaGLYYADRVTTVSPTYAREIttpeFGYGlegLLRARSGKLSG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1543 ILNGIDPDIWDPYTDNFIPMHYTSENVvEGKNAAKRALQQRFGLQQTDVPIVGIITRLTAQKGIHLIKHALHRTLERNGQ 1622
Cdd:PRK00654 235 ILNGIDYDIWNPETDPLLAANYSADDL-EGKAENKRALQERFGLPDDDAPLFAMVSRLTEQKGLDLVLEALPELLEQGGQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1623 VVLLGSaPDPRIQSDFCRLADSLHGenhgRVRLCLTYDEPLSHLIYAGSDFILVPSIFEPCGLTQLVAMRYGSIPIVRKT 1702
Cdd:PRK00654 314 LVLLGT-GDPELEEAFRALAARYPG----KVGVQIGYDEALAHRIYAGADMFLMPSRFEPCGLTQLYALRYGTLPIVRRT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1703 GGLYDTVFDVDHDKDRArvlglepNGFSFDGADCNGVDYALNRAISSWFEARGWfHSLCKRVMEQDWSWNRPALDYIELY 1782
Cdd:PRK00654 389 GGLADTVIDYNPEDGEA-------TGFVFDDFNAEDLLRALRRALELYRQPPLW-RALQRQAMAQDFSWDKSAEEYLELY 460
|
...
gi 1002292629 1783 HSA 1785
Cdd:PRK00654 461 RRL 463
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
1340-1785 |
2.46e-150 |
|
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: 470.98 E-value: 2.46e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1340 IHIVHIAVEMAPIAKVGGLADVVTSLSRAIQELGHHVEVILPKYNFMNQSNVKNLHV--RQSFSLGGT--EIKVWFGLVE 1415
Cdd:TIGR02095 1 MRVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEVDDQVKVveLVDLSVGPRtlYVKVFEGVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1416 DLSVYFLEPQNGMFGGGWVYGGN---DAGRFGLFCQSALEFLLQSGSSPHIIHCHDWSSAPVAWLYKEHYAESRlatARI 1492
Cdd:TIGR02095 81 GVPVYFIDNPSLFDRPGGIYGDDypdNAERFAFFSRAAAELLSGLGWQPDVVHAHDWHTALVPALLKAVYRPNP---IKT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1493 IFTIHNLEF----------------------GAHFIGK------AMTYCDKATTVSHTYSKEV----AG---HGAIAPHR 1537
Cdd:TIGR02095 158 VFTIHNLAYqgvfpaddfselglppeyfhmeGLEFYGRvnflkgGIVYADRVTTVSPTYAREIltpeFGyglDGVLKARS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1538 GKFYGILNGIDPDIWDPYTDNFIPMHYTSENVvEGKNAAKRALQQRFGLQQ-TDVPIVGIITRLTAQKGIHLIKHALHRT 1616
Cdd:TIGR02095 238 GKLRGILNGIDTEVWNPATDPYLKANYSADDL-AGKAENKEALQEELGLPVdDDVPLFGVISRLTQQKGVDLLLAALPEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1617 LERNGQVVLLGSApDPRIQSDFCRLAdslhGENHGRVRLCLTYDEPLSHLIYAGSDFILVPSIFEPCGLTQLVAMRYGSI 1696
Cdd:TIGR02095 317 LELGGQLVVLGTG-DPELEEALRELA----ERYPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQLYAMRYGTV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1697 PIVRKTGGLYDTVFDVDHDKDRArvlglepNGFSFDGADCNGVDYALNRAISSWFEARGWFHSLCKRVMEQDWSWNRPAL 1776
Cdd:TIGR02095 392 PIVRRTGGLADTVVDGDPEAESG-------TGFLFEEYDPGALLAALSRALRLYRQDPSLWEALQKNAMSQDFSWDKSAK 464
|
....*....
gi 1002292629 1777 DYIELYHSA 1785
Cdd:TIGR02095 465 QYVELYRSL 473
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1340-1785 |
2.98e-138 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 455.52 E-value: 2.98e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1340 IHIVHIAVEMAPIAKVGGLADVVTSLSRAIQELGHHVEVILPKYNFMNQSNVKNLH----VRQSFSLGGT-EIKVWFGLV 1414
Cdd:PLN02939 482 LHIVHIAAEMAPVAKVGGLADVVSGLGKALQKKGHLVEIVLPKYDCMQYDQIRNLKvldvVVESYFDGNLfKNKIWTGTV 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1415 EDLSVYFLEPQN--GMFGGGWVYG-GNDAGRFGLFCQSALEFLLQSGSSPHIIHCHDWSSAPVAWLYKEHYAESRLATAR 1491
Cdd:PLN02939 562 EGLPVYFIEPQHpsKFFWRAQYYGeHDDFKRFSYFSRAALELLYQSGKKPDIIHCHDWQTAFVAPLYWDLYAPKGFNSAR 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1492 IIFTIHNLEFGAHFIGKAMTYC--------------DKA-----------------TTVSHTYSKEVAGHG------AIA 1534
Cdd:PLN02939 642 ICFTCHNFEYQGTAPASDLASCgldvhqldrpdrmqDNAhgrinvvkgaivysnivTTVSPTYAQEVRSEGgrglqdTLK 721
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1535 PHRGKFYGILNGIDPDIWDPYTDNFIPMHYtSENVVEGKNAAKRALQQRFGLQQTDV--PIVGIITRLTAQKGIHLIKHA 1612
Cdd:PLN02939 722 FHSKKFVGILNGIDTDTWNPSTDRFLKVQY-NANDLQGKAANKAALRKQLGLSSADAsqPLVGCITRLVPQKGVHLIRHA 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1613 LHRTLERNGQVVLLGSAPDPRIQSDFCRLADslHGENHGRVRLCLTYDEPLSHLIYAGSDFILVPSIFEPCGLTQLVAMR 1692
Cdd:PLN02939 801 IYKTAELGGQFVLLGSSPVPHIQREFEGIAD--QFQSNNNIRLILKYDEALSHSIYAASDMFIIPSMFEPCGLTQMIAMR 878
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1693 YGSIPIVRKTGGLYDTVFDVDHDkdrarVLGLE-PNGFSFDGADCNGVDYALNRAISSWFEARGWFHSLCKRVMEQDWSW 1771
Cdd:PLN02939 879 YGSVPIVRKTGGLNDSVFDFDDE-----TIPVElRNGFTFLTPDEQGLNSALERAFNYYKRKPEVWKQLVQKDMNIDFSW 953
|
490
....*....|....
gi 1002292629 1772 NRPALDYIELYHSA 1785
Cdd:PLN02939 954 DSSASQYEELYQRA 967
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
1339-1784 |
4.02e-75 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 259.27 E-value: 4.02e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1339 PIHIVHIAVEMAPIAKVGGLADVVTSLSRAIQELGHHVEVILPKY-NFMNQ-SNVKNLHVRQSFsLGGTEiKVWFGLVED 1416
Cdd:PRK14099 3 PLRVLSVASEIFPLIKTGGLADVAGALPAALKAHGVEVRTLVPGYpAVLAGiEDAEQVHSFPDL-FGGPA-RLLAARAGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1417 LSVYFLE-------PQNGMFGGGWVYGGNDAGRFGLFCQ--SALEFLLQSGSSPHIIHCHDWSSAPV-AWLykeHYaeSR 1486
Cdd:PRK14099 81 LDLFVLDaphlydrPGNPYVGPDGKDWPDNAQRFAALARaaAAIGQGLVPGFVPDIVHAHDWQAGLApAYL---HY--SG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1487 LATARIIFTIHNL----EFGAHFIG-----------------------KA-MTYCDKATTVSHTYSKEVAG-------HG 1531
Cdd:PRK14099 156 RPAPGTVFTIHNLafqgQFPRELLGalglppsafsldgveyyggigylKAgLQLADRITTVSPTYALEIQGpeagmglDG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1532 AIAPHRGKFYGILNGIDPDIWDPYTDNFIPMHYTSENVvEGKNAAKRALQQRFGLQ-QTDVPIVGIITRLTAQKGIHLIK 1610
Cdd:PRK14099 236 LLRQRADRLSGILNGIDTAVWNPATDELIAATYDVETL-AARAANKAALQARFGLDpDPDALLLGVISRLSWQKGLDLLL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1611 HALHrTLERNG-QVVLLGSApDPRIQSDFCRLADSlhgeNHGRVRLCLTYDEPLSHLIYAGSDFILVPSIFEPCGLTQLV 1689
Cdd:PRK14099 315 EALP-TLLGEGaQLALLGSG-DAELEARFRAAAQA----YPGQIGVVIGYDEALAHLIQAGADALLVPSRFEPCGLTQLC 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1690 AMRYGSIPIVRKTGGLYDTVFDVDhdkDRARVLGLePNGFSFDGADCNGVDYALNRAISSWFEARGWfHSLCKRVMEQDW 1769
Cdd:PRK14099 389 ALRYGAVPVVARVGGLADTVVDAN---EMAIATGV-ATGVQFSPVTADALAAALRKTAALFADPVAW-RRLQRNGMTTDV 463
|
490
....*....|....*
gi 1002292629 1770 SWNRPALDYIELYHS 1784
Cdd:PRK14099 464 SWRNPAQHYAALYRS 478
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
1342-1527 |
2.45e-56 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 196.01 E-value: 2.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1342 IVHIAVEMAPIAKVGGLADVVTSLSRAIQELGHHVEVILPKYNFMNQS-----NVKNLHVRQSFSLGGTEIKVWFGLVED 1416
Cdd:pfam08323 1 ILFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGNIPEErnqleDVIRLSVAAGVPVRPLTVGVARLELDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1417 LSVYFLEPQNgMFGGGWVYGG------NDAGRFGLFCQSALEFLLQSGSSPHIIHCHDWSSAPVAWLYKEHYAESRLATA 1490
Cdd:pfam08323 81 VDVYFLDNPD-YFDRPGLYGDdgrdyeDNAERFAFFSRAALELAKKLGWIPDIIHCHDWHTALVPAYLKEAYADDPFKNI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002292629 1491 RIIFTIHNLEFGAHFIGK----------------------------AMTYCDKATTVSHTYSKEV 1527
Cdd:pfam08323 160 KTVFTIHNLAYQGRFPADlldllglppedfnldglefygqinflkaGIVYADAVTTVSPTYAEEI 224
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
1342-1782 |
1.37e-54 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 199.58 E-value: 1.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1342 IVHIAVEMAPIAKVGGLADVVTSLSRAIQELGHHVEVILPKYNFMN-------------------QSNVKNLHVRQSfSL 1402
Cdd:PRK14098 8 VLYVSGEVSPFVRVSALADFMASFPQALEEEGFEARIMMPKYGTINdrkfrlhdvlrlsdievplKEKTDLLHVKVT-AL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1403 GGTEIKVWFGLVEDlsvYFlePQNGMFGGgwVYGGND----AGRFGLFCQSALEFLLQSGSSPHIIHCHDWSSAPVAWLY 1478
Cdd:PRK14098 87 PSSKIQTYFLYNEK---YF--KRNGLFTD--MSLGGDlkgsAEKVIFFNVGVLETLQRLGWKPDIIHCHDWYAGLVPLLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1479 KEHYAESRL-ATARIIFTIHN------LEF-------------GAHFIGK-------AMTYCDKATTVSHTYSKEVAGHG 1531
Cdd:PRK14098 160 KTVYADHEFfKDIKTVLTIHNvyrqgvLPFkvfqkllpeevcsGLHREGDevnmlytGVEHADLLTTTSPRYAEEIAGDG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1532 --------AIAPHRGKFYGILNGIDPDIWDPYTDNFIPMHYTSENVvEGKNAAKRALQQRFGLQQTD-VPIVGIITRLTA 1602
Cdd:PRK14098 240 eeafgldkVLEERKMRLHGILNGIDTRQWNPSTDKLIKKRYSIERL-DGKLENKKALLEEVGLPFDEeTPLVGVIINFDD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1603 QKGIHLIKHALHRTLERNGQVVLLGSApDPRIQSDFCRLADslhgENHGRVRLCLTYDEPLSHLIYAGSDFILVPSIFEP 1682
Cdd:PRK14098 319 FQGAELLAESLEKLVELDIQLVICGSG-DKEYEKRFQDFAE----EHPEQVSVQTEFTDAFFHLAIAGLDMLLMPGKIES 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1683 CGLTQLVAMRYGSIPIVRKTGGLYDTVFDVDHDKDrarvlglepNGFSFDgadcngvDYALNRAISSWFEARGWFH---- 1758
Cdd:PRK14098 394 CGMLQMFAMSYGTIPVAYAGGGIVETIEEVSEDKG---------SGFIFH-------DYTPEALVAKLGEALALYHdeer 457
|
490 500
....*....|....*....|....*.
gi 1002292629 1759 --SLCKRVMEQDWSWNRPALDYIELY 1782
Cdd:PRK14098 458 weELVLEAMERDFSWKNSAEEYAQLY 483
|
|
| CBM53 |
pfam16760 |
Starch/carbohydrate-binding module (family 53); |
1247-1329 |
1.91e-21 |
|
Starch/carbohydrate-binding module (family 53);
Pssm-ID: 465261 [Multi-domain] Cd Length: 76 Bit Score: 89.66 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1247 VLYNPSNtvlngKPEVWFRWSFNRWMHPSGVlPPKKMVKTEDGCHLKATVSVPSDAYMMDFVFSESeeGGIYDNRNGTDY 1326
Cdd:pfam16760 2 IYYNGSL-----AKEVYIHGGFNGWKNVQDV-PMEKLPPTGGGDWFSATVPVPEDAYVLDFVFKDG--AGNWDNNNGQNY 73
|
...
gi 1002292629 1327 HIP 1329
Cdd:pfam16760 74 HIP 76
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
1341-1783 |
6.43e-21 |
|
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: 96.84 E-value: 6.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1341 HIVHIAVEMAPiaKVGGLADVVTSLSRAIQELGHHVEVILPkYNFMNQSNVKNLHVRQSFSLGGTEIKVWFGLVEDLSVY 1420
Cdd:cd03801 1 KILLLSPELPP--PVGGAERHVRELARALAARGHDVTVLTP-ADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1421 FLEPQngmfgggwvyggndagrfglfcqsalefllqsgssPHIIHCHDWSSAPVAWLYKehyaesRLATARIIFTIHNLE 1500
Cdd:cd03801 78 LRLRK-----------------------------------FDVVHAHGLLAALLAALLA------LLLGAPLVVTLHGAE 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1501 FGAHF------------IGKAMTYCDKATTVSHTYSKEVAGHGAIAPHRGKFygILNGIDPDIWDPytdnfipmhytsen 1568
Cdd:cd03801 117 PGRLLlllaaerrllarAEALLRRADAVIAVSEALRDELRALGGIPPEKIVV--IPNGVDLERFSP-------------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1569 vvegknaakrALQQRFGLQQtDVPIVGIITRLTAQKGIHLIKHALHRTLERNGQVVLL--GSAPD--PRIQSDFCRLADS 1644
Cdd:cd03801 181 ----------PLRRKLGIPP-DRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVivGGDGPlrAELEELELGLGDR 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1645 LHgeNHGRVrlcltYDEPLSHLiYAGSDFILVPSIFEPCGLTQLVAMRYGsIPIVrktgglydtVFDVDHDKDrarVLGL 1724
Cdd:cd03801 250 VR--FLGFV-----PDEELPAL-YAAADVFVLPSRYEGFGLVVLEAMAAG-LPVV---------ATDVGGLPE---VVED 308
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002292629 1725 EPNGFSFDGADCNGVDYALNRAISSwFEARGWFHSLCKRVMEQDWSWNRPALDYIELYH 1783
Cdd:cd03801 309 GEGGLVVPPDDVEALADALLRLLAD-PELRARLGRAARERVAERFSWERVAERLLDLYR 366
|
|
| CBM53 |
pfam16760 |
Starch/carbohydrate-binding module (family 53); |
1084-1169 |
6.60e-20 |
|
Starch/carbohydrate-binding module (family 53);
Pssm-ID: 465261 [Multi-domain] Cd Length: 76 Bit Score: 85.42 E-value: 6.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1084 RLYYNRNSRPlmhstEIWMHGGCNSWTDGLSI-VERLveCDDENGDWWYANVHIPEKAFVLDWVFADGppgnARNYDNNG 1162
Cdd:pfam16760 1 NIYYNGSLAK-----EVYIHGGFNGWKNVQDVpMEKL--PPTGGGDWFSATVPVPEDAYVLDFVFKDG----AGNWDNNN 69
|
....*..
gi 1002292629 1163 RQDFHAI 1169
Cdd:pfam16760 70 GQNYHIP 76
|
|
| CBM53 |
pfam16760 |
Starch/carbohydrate-binding module (family 53); |
910-988 |
3.65e-18 |
|
Starch/carbohydrate-binding module (family 53);
Pssm-ID: 465261 [Multi-domain] Cd Length: 76 Bit Score: 80.41 E-value: 3.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 910 VYLNRNLSalanePDVHIKGAFNSWRWRPFTERLH-KSELSGDWWSCKLHIPKEAYRLDFVFFNGRLVYDNNDSNDFVLQ 988
Cdd:pfam16760 2 IYYNGSLA-----KEVYIHGGFNGWKNVQDVPMEKlPPTGGGDWFSATVPVPEDAYVLDFVFKDGAGNWDNNNGQNYHIP 76
|
|
| CBM_25 |
smart01066 |
Carbohydrate binding domain; |
1242-1331 |
1.65e-16 |
|
Carbohydrate binding domain;
Pssm-ID: 198134 [Multi-domain] Cd Length: 83 Bit Score: 75.86 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1242 GTTVDVLYNPSNTVlNGKPEVWFRWSF--NRWMHPSGVlppkKMVKTEDGcHLKATVsVPSDAYMMDFVFSEseEGGIYD 1319
Cdd:smart01066 1 GNTVTVYYNGLLAT-SGAKNVYLHYGFgeNNWTDVPDV----RMEKTGEG-WVKATI-PVKEAYKLNFCFKD--GAGNWD 71
|
90
....*....|..
gi 1002292629 1320 NRNGTDYHIPVS 1331
Cdd:smart01066 72 NNGGANYHFEIG 83
|
|
| CBM_25 |
smart01066 |
Carbohydrate binding domain; |
907-989 |
2.19e-14 |
|
Carbohydrate binding domain;
Pssm-ID: 198134 [Multi-domain] Cd Length: 83 Bit Score: 70.08 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 907 TIDVYLNRNLSALANEPdVHIKGAFNSWRWRPFTERLHKSELSGdWWSCKLHIpKEAYRLDFVFFNGRLVYDNNDSNDFV 986
Cdd:smart01066 3 TVTVYYNGLLATSGAKN-VYLHYGFGENNWTDVPDVRMEKTGEG-WVKATIPV-KEAYKLNFCFKDGAGNWDNNGGANYH 79
|
...
gi 1002292629 987 LQV 989
Cdd:smart01066 80 FEI 82
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
1461-1709 |
3.14e-14 |
|
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.
Pssm-ID: 340846 [Multi-domain] Cd Length: 345 Bit Score: 76.24 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1461 PHIIHCHDWSSAPVAWLYkehyaeSRLATARIIFTIHNLEFgAHFIGKA-----MTYCDKATTVSH-TYSKEVAGHGAIa 1534
Cdd:cd03819 77 IDLIHAHSRAPAWLGWLA------SRLTGVPLVTTVHGSYL-ATYHPKDfalavRARGDRVIAVSElVRDHLIEALGVD- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1535 phRGKFYGILNGIDPDIWDPytdnfipmhytsenvvegknAAKRALQQRFGLQqTDVPIVGIITRLTAQKGIHLIKHALH 1614
Cdd:cd03819 149 --PERIRVIPNGVDTDRFPP--------------------EAEAEERAQLGLP-EGKPVVGYVGRLSPEKGWLLLVDAAA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1615 RtLERNGQVVLL--GSAPdpriQSDFCRLADSLHGENhGRVRLcLTYDEPLSHLiYAGSDFILVPSIFEPCGLTQLVAMR 1692
Cdd:cd03819 206 E-LKDEPDFRLLvaGDGP----ERDEIRRLVERLGLR-DRVTF-TGFREDVPAA-LAASDVVVLPSLHEEFGRVALEAMA 277
|
250
....*....|....*..
gi 1002292629 1693 YGSIPIVRKTGGLYDTV 1709
Cdd:cd03819 278 CGTPVVATDVGGAREIV 294
|
|
| CBM_25 |
smart01066 |
Carbohydrate binding domain; |
1080-1168 |
1.80e-12 |
|
Carbohydrate binding domain;
Pssm-ID: 198134 [Multi-domain] Cd Length: 83 Bit Score: 64.68 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1080 GDTVRLYYNRNSRPLmHSTEIWMHGG--CNSWTDglsIVERLVECDDEngDWWYANVHIpEKAFVLDWVFADGppgnARN 1157
Cdd:smart01066 1 GNTVTVYYNGLLATS-GAKNVYLHYGfgENNWTD---VPDVRMEKTGE--GWVKATIPV-KEAYKLNFCFKDG----AGN 69
|
90
....*....|.
gi 1002292629 1158 YDNNGRQDFHA 1168
Cdd:smart01066 70 WDNNGGANYHF 80
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
1446-1778 |
7.88e-09 |
|
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: 59.95 E-value: 7.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1446 FCQSALEFLLQSGSSPHIIHCHDWSSAPVAWLykehyAESRLATArIIFTIHNL--------------EFGAHFIGK--A 1509
Cdd:cd03800 87 FADGLLRFIAREGGRYDLIHSHYWDSGLVGAL-----LARRLGVP-LVHTFHSLgrvkyrhlgaqdtyHPSLRITAEeqI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1510 MTYCDK--ATTvshtySKEVAGHGA-IAPHRGKFYGILNGIDPDIWDPYTDnfipmhytsenvvegknaaKRALQQRFGL 1586
Cdd:cd03800 161 LEAADRviAST-----PQEADELISlYGADPSRINVVPPGVDLERFFPVDR-------------------AEARRARLLL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1587 QQtDVPIVGIITRLTAQKGIHLIKHALHRTLERNGQVVLL---GSAPDPRIQSDFCR--LADSLHGEnhGRVRLCLTYDE 1661
Cdd:cd03800 217 PP-DKPVVLALGRLDPRKGIDTLVRAFAQLPELRELANLVlvgGPSDDPLSMDREELaeLAEELGLI--DRVRFPGRVSR 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1662 PLSHLIYAGSDFILVPSIFEPCGLTQLVAMRYGsIPIV-RKTGGLYDTVFDvdhdkdrarvlglEPNGFSFDGADCNgvd 1740
Cdd:cd03800 294 DDLPELYRAADVFVVPSLYEPFGLTAIEAMACG-TPVVaTAVGGLQDIVRD-------------GRTGLLVDPHDPE--- 356
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1002292629 1741 yALNRAISSWFEARGWFHSLCKRVME---QDWSWNRPALDY 1778
Cdd:cd03800 357 -ALAAALRRLLDDPALWQRLSRAGLErarAHYTWESVADQL 396
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
1665-1785 |
8.61e-08 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 52.30 E-value: 8.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1665 HLIYAGSDFILVPSIFEPCGLTQLVAMRYGSIPIVRKTGGLYDTVFDvdhdkdrarvlglEPNGFSFDGADCNGVDYALN 1744
Cdd:COG0438 15 EALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIED-------------GETGLLVPPGDPEALAEAIL 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1002292629 1745 RAISSwFEARGWFHSLCKRVMEQDWSWNRPALDYIELYHSA 1785
Cdd:COG0438 82 RLLED-PELRRRLGEAARERAEERFSWEAIAERLLALYEEL 121
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
1590-1709 |
2.03e-07 |
|
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: 52.28 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1590 DVPIVGIITRLTAQKGIHLIKHALHRTLERNGQVVLL--GSAPDpriQSDFCRLADSLHGENHGRVRLCLTYDEPlsHLI 1667
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLViaGDGEE---EKRLKKLAEKLGLGDNVIFLGFVSDEDL--PEL 75
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1002292629 1668 YAGSDFILVPSIFEPCGLTQLVAMRYGSIPIVRKTGGLYDTV 1709
Cdd:pfam00534 76 LKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVV 117
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
1576-1711 |
2.60e-06 |
|
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: 50.48 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1576 AKRALQQRFGLQQTDVPIVGiitRLTAQKGIHLIKHALHRTLER--NGQVVLLGSAPDPriQSDFCRLADSLHGENHGRV 1653
Cdd:cd01635 98 LLALARLLVSLPLADKVSVG---RLVPEKGIDLLLEALALLKARlpDLVLVLVGGGGER--EEEEALAAALGLLERVVII 172
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002292629 1654 RLCltYDEPLSHLIYAGSDFILVPSIFEPCGLTQLVAMRYGSIPIVRKTGGLYDTVFD 1711
Cdd:cd01635 173 GGL--VDDEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVD 228
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
1356-1550 |
3.56e-06 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 49.07 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1356 GGLADVVTSLSRAIQELGHHVEVILPKYNFMNQSNVKNLHVrqsfslggteikvwfglvedlsvyflepqngmfGGGWVY 1435
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVR---------------------------------VPRVPL 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1436 GGNDAGRFGLFCQSALEFLLQSGSsPHIIHCHDWSSAPVAWLykehyAESRLATARIIFTIHNLEFGAHFIG-------- 1507
Cdd:pfam13439 48 PLPPRLLRSLAFLRRLRRLLRRER-PDVVHAHSPFPLGLAAL-----AARLRLGIPLVVTYHGLFPDYKRLGarlsplrr 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1508 -------KAMTYCDKATTVSHTYSKEVAGHGAIAPHRGKFygILNGIDPD 1550
Cdd:pfam13439 122 llrrlerRLLRRADRVIAVSEAVADELRRLYGVPPEKIRV--IPNGVDLE 169
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
1460-1699 |
1.01e-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: 49.63 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1460 SPHIIHCHDWSSAPVawlykEHYAESRLATARIIFTIHNLEFGAHFIGKAMTYCDKATTVSHTYSKEVAGHGAIAPhrgK 1539
Cdd:cd03823 96 RPDVVHTHNLSGLGA-----SLLDAARDLGIPVVHTLHDYWLLCPRQFLFKKGGDAVLAPSRFTANLHEANGLFSA---R 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1540 FYGILNGIDPDIWDPytdnfipmhytsenvVEGKNAAKRAlqqRFGLqqtdvpivgiITRLTAQKGIHLIKHALHRTLER 1619
Cdd:cd03823 168 ISVIPNAVEPDLAPP---------------PRRRPGTERL---RFGY----------IGRLTEEKGIDLLVEAFKRLPRE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1620 NGQVVLLGSAPD--PRIQSDFCRLAdslhgeNHGRVrlclTYDEPLSHliYAGSDFILVPSIF-EPCGLTQLVAMRYGsI 1696
Cdd:cd03823 220 DIELVIAGHGPLsdERQIEGGRRIA------FLGRV----PTDDIKDF--YEKIDVLVVPSIWpEPFGLVVREAIAAG-L 286
|
...
gi 1002292629 1697 PIV 1699
Cdd:cd03823 287 PVI 289
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
1434-1709 |
1.06e-05 |
|
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.
Pssm-ID: 340828 [Multi-domain] Cd Length: 376 Bit Score: 49.69 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1434 VYGGNDAGRFGLFCQSALEFLLQS-GSSPHIIHCH-DWSSAPVAWLYKehyaesRLATARIIFTIHNLEFGAH------- 1504
Cdd:cd03798 68 PLKPRLRLLAPLRAPSLAKLLKRRrRGPPDLIHAHfAYPAGFAAALLA------RLYGVPYVVTEHGSDINVFpprsllr 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1505 -FIGKAMTYCDKATTVSHTYSKEVAGHGAIaphRGKFYGILNGIDPDIWDPytdnfipmhytsenvvegknaakraLQQR 1583
Cdd:cd03798 142 kLLRWALRRAARVIAVSKALAEELVALGVP---RDRVDVIPNGVDPARFQP-------------------------EDRG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1584 FGLQqTDVPIVGIITRLTAQKGIHLIKHALHRTLERNGQVVLL--GSAPD-PRIQsdfcRLADSLHGEN----HGRvrlc 1656
Cdd:cd03798 194 LGLP-LDAFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLivGDGPLrEALR----ALAEDLGLGDrvtfTGR---- 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1002292629 1657 LTYDEPLSHliYAGSDFILVPSIFEPCGLTQLVAMRYGsIPIV-RKTGGLYDTV 1709
Cdd:cd03798 265 LPHEQVPAY--YRACDVFVLPSRHEGFGLVLLEAMACG-LPVVaTDVGGIPEVV 315
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
1592-1713 |
2.14e-05 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 45.97 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1592 PIVGIITRLTA-QKGIHLIKHALHRTLERNGQVVLL--GSAPDPRIQSDFCRLADSLHgeNHGRVrlcltydEPLSHLiY 1668
Cdd:pfam13692 2 PVILFVGRLHPnVKGVDYLLEAVPLLRKRDNDVRLVivGDGPEEELEELAAGLEDRVI--FTGFV-------EDLAEL-L 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1002292629 1669 AGSDFILVPSIFEPCGLTQLVAMRYGsIPIV-RKTGGLYDTVFDVD 1713
Cdd:pfam13692 72 AAADVFVLPSLYEGFGLKLLEAMAAG-LPVVaTDVGGIPELVDGEN 116
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
72-182 |
1.91e-04 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 46.40 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 72 VASSRGYAPRIAAESSIQEREHINSDEETFDTYNRLLRNESTEW--KKLDTTEVDLSQDVSSSSMRKVDATDEAkLDILE 149
Cdd:PLN02316 8 GSAPRGFAPRTTVESSQKRIQQNNGDKEDSSTSTSSLSVSAVEKtsNAKEEIQVDFQHNSESAVEEVEAEDEIE-VEQNQ 86
|
90 100 110
....*....|....*....|....*....|...
gi 1002292629 150 DDLPRNLLNGVTMGEvdMLDEAGAEDDVFEVDL 182
Cdd:PLN02316 87 SDVLKSSSIVKEESI--STDMDGIDDDSLDRKL 117
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
1491-1699 |
3.30e-04 |
|
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.
Pssm-ID: 340839 [Multi-domain] Cd Length: 351 Bit Score: 45.04 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1491 RIIFTIHN-------LEFGAHFIGKAMTYCDKATTVSHTYSKEVAGHGAIAPHRGKFygILNGIDPDiwdpytdnfipmh 1563
Cdd:cd03811 107 KVIAWIHSslsklyyLKKKLLLKLKLYKKADKIVCVSKGIKEDLIRLGPSPPEKIEV--IYNPIDID------------- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1564 ytsenvvegknAAKRALQQRFGLQQTDVPIVGIITRLTAQKGIHLIKHALHRTLERNGQV--VLLGSAPD-PRIQsdfcR 1640
Cdd:cd03811 172 -----------RIRALAKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVklVILGDGPLrEELE----K 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002292629 1641 LADSLHGENhgRVRLCLTYDEPLShlIYAGSDFILVPSIFEPCGLTQLVAMRYGsIPIV 1699
Cdd:cd03811 237 LAKELGLAE--RVIFLGFQSNPYP--YLKKADLFVLSSRYEGFPNVLLEAMALG-TPVV 290
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
1490-1699 |
2.10e-03 |
|
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.
Pssm-ID: 340838 [Multi-domain] Cd Length: 362 Bit Score: 42.35 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1490 ARIIFTIHNL------------EFGAHFIGKAMT--YCDKATTVSHtYSK-EVAGHGAIAPHrgKFYGILNGIDPDIwdp 1554
Cdd:cd03809 102 CPQVVTIHDLiplrypeffpkrFRLYYRLLLPISlrRADAIITVSE-ATRdDIIKFYGVPPE--KIVVIPLGVDPSF--- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292629 1555 ytdnfipmhytSENVVEGKNAAKRALQQRFGLqqtdvpIVGiitRLTAQKGIH-LIK-HALHRTLERNGQVVLLGSAPDP 1632
Cdd:cd03809 176 -----------FPPESAAVLIAKYLLPEPYFL------YVG---TLEPRKNHErLLKaFALLKKQGGDLKLVIVGGKGWE 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002292629 1633 RiqSDFCRLADslHGENHGRVRLcLTY--DEPLSHLiYAGSDFILVPSIFEPCGLTQLVAMRYGsIPIV 1699
Cdd:cd03809 236 D--EELLDLVK--KLGLGGRVRF-LGYvsDEDLPAL-YRGARAFVFPSLYEGFGLPVLEAMACG-TPVI 297
|
|
| |
