|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_ALG11-like |
cd03806 |
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ... |
63-480 |
0e+00 |
|
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG11 in yeast is involved in adding the final 1,2-linked Man to the Man5GlcNAc2-PP-Dol synthesized on the cytosolic face of the ER. The deletion analysis of ALG11 was shown to block the early steps of core biosynthesis that takes place on the cytoplasmic face of the ER and lead to a defect in the assembly of lipid-linked oligosaccharides.
Pssm-ID: 340835 [Multi-domain] Cd Length: 419 Bit Score: 714.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 63 MVIAFFHPYCNAGGGGERVLWCALRALQKKYPEAVYVVYTGDVNVNGQQILEGAFRRFNIRLIHPVQFVF-LRKRYLVED 141
Cdd:cd03806 1 ITVGFFHPYCNAGGGGERVLWCAVKATQKAYPNNICVIYTGDTDSSPEEILEKVESRFNIDLDSPRIVFFlLKYRKLVEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 142 SLYPHFTLLGQSLGSIFLGWEALMQCVPDVYIDSMGYAFTLPLFKYIGGCQVGSYVHYPTISTDMLSVVKNQNIGFNNAA 221
Cdd:cd03806 81 KTYPRFTLLGQALGSMILGFEALLKLVPDVFIDTMGYPFTYPLVRLLGGCPVVAYVHYPTISTDMLNKVRSREASYNNDS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 222 FITRNPFLSKVKLIYYYLFAFIYGLVGSCSDVVMVNSSWTLNHILSLWKVGNCTNIVYPPCDVQTFLDIPLHEKKMTpgH 301
Cdd:cd03806 161 TIARSSVLSIAKLLYYRLFAFLYGLAGSFADVVMVNSTWTYNHIRQLWKRNIKPSIVYPPCDTEELTKLPIDEKTRE--N 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 302 LLVSVGQFRPEKNHPLQIRAFAKLLNKKMVESPPSLKLVLIGGCRNKDDELRVNQLRRLSEDLGVQEYVEFKINIPFDEL 381
Cdd:cd03806 239 QILSIAQFRPEKNHPLQLRAFAELLKRLPESIRSNPKLVLIGSCRNEEDKERVEALKLLAKELILEDSVEFVVDAPYEEL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 382 KNYLSEATIGLHTMWNEHFGIGVVECMAAGTIILAHNSGGPKLDIVVPHEGDITGFLAESEEDYAETIAHILSMSAEKRL 461
Cdd:cd03806 319 KELLSTASIGLHTMWNEHFGIGVVEYMAAGLIPLAHASAGPLLDIVVPWDGGPTGFLASTPEEYAEAIEKILTLSEEERL 398
|
410
....*....|....*....
gi 304434672 462 QIRKSARASVSRFSDQEFE 480
Cdd:cd03806 399 QRREAARSSAERFSDEEFE 417
|
|
| PLN02949 |
PLN02949 |
transferase, transferring glycosyl groups |
31-491 |
0e+00 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215511 [Multi-domain] Cd Length: 463 Bit Score: 552.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 31 LCVCLVIVLwgirLLLQRKKKLVSTSKNGKNqmVIAFFHPYCNAGGGGERVLWCALRALQKKYPEAVYVVYTGDVNVNGQ 110
Cdd:PLN02949 8 YHLLTSIVL----LLVAIALSVLRARRSRKR--AVGFFHPYTNDGGGGERVLWCAVRAIQEENPDLDCVIYTGDHDASPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 111 QILEGAFRRFNIRLIHPVQFVFLRKRYLVEDSLYPHFTLLGQSLGSIFLGWEALMQCVPDVYIDSMGYAFTLPLFKyIGG 190
Cdd:PLN02949 82 SLAARARDRFGVELLSPPKVVHLRKRKWIEEETYPRFTMIGQSLGSVYLAWEALCKFTPLYFFDTSGYAFTYPLAR-LFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 191 CQVGSYVHYPTISTDMLSVVKNQNIGFNNAAFITRNPFLSKVKLIYYYLFAFIYGLVGSCSDVVMVNSSWTLNHILSLWK 270
Cdd:PLN02949 161 CKVVCYTHYPTISSDMISRVRDRSSMYNNDASIARSFWLSTCKILYYRAFAWMYGLVGRCAHLAMVNSSWTKSHIEALWR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 271 VGNCTNIVYPPCDVQTFLDIPLHEKKMTPghLLVSVGQFRPEKNHPLQIRAFAKLLnKKMVESPPSLKLVLIGGCRNKDD 350
Cdd:PLN02949 241 IPERIKRVYPPCDTSGLQALPLERSEDPP--YIISVAQFRPEKAHALQLEAFALAL-EKLDADVPRPKLQFVGSCRNKED 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 351 ELRVNQLRRLSEDLGVQEYVEFKINIPFDELKNYLSEATIGLHTMWNEHFGIGVVECMAAGTIILAHNSGGPKLDIVVPH 430
Cdd:PLN02949 318 EERLQKLKDRAKELGLDGDVEFHKNVSYRDLVRLLGGAVAGLHSMIDEHFGISVVEYMAAGAVPIAHNSAGPKMDIVLDE 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 304434672 431 EGDITGFLAESEEDYAETIAHILSMSAEKRLQIRKSARASVSRFSDQEFEVTFLSSVEKLF 491
Cdd:PLN02949 398 DGQQTGFLATTVEEYADAILEVLRMRETERLEIAAAARKRANRFSEQRFNEDFKDAIRPIL 458
|
|
| ALG11_N |
pfam15924 |
ALG11 mannosyltransferase N-terminus; |
63-269 |
6.60e-146 |
|
ALG11 mannosyltransferase N-terminus;
Pssm-ID: 464944 Cd Length: 209 Bit Score: 416.10 E-value: 6.60e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 63 MVIAFFHPYCNAGGGGERVLWCALRALQKKYPEAVYVVYTGDVNVNGQQILEGAFRRFNIRLIH-PVQFVFLRKRYLVED 141
Cdd:pfam15924 2 GIVGFFHPYCNAGGGGERVLWCAVRATQRRYPNAICVVYTGDIDASKEEILAKVKSRFNIELDPsRIVFVYLRKRKLVEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 142 SLYPHFTLLGQSLGSIFLGWEALMQCVPDVYIDSMGYAFTLPLFKYIGGCQVGSYVHYPTISTDMLSVVKNQNIGFNNAA 221
Cdd:pfam15924 82 STYPRFTLLGQSLGSIILAWEALSKLVPDVFIDTMGYAFTYPLVRLLGGCPVGAYVHYPTISTDMLSRVSSREAGYNNDS 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 304434672 222 FITRNPFLSKVKLIYYYLFAFIYGLVGSCSDVVMVNSSWTLNHILSLW 269
Cdd:pfam15924 162 AIASSGLLSKAKLIYYRLFALLYGLVGSFADVVMVNSSWTQNHIRSLW 209
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
142-479 |
8.96e-35 |
|
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.
Pssm-ID: 340834 [Multi-domain] Cd Length: 392 Bit Score: 134.25 E-value: 8.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 142 SLYPHFTLLGQSLGSIFLGWEALMQCV--PDVYI-DSMgyAFTLPLFKYIGGCQVGSYVHYPtistDMLSVVKNqnigfn 218
Cdd:cd03805 66 SIFGRFHALCAYLRMLYLALYLLLFSGekYDVFIvDQV--SACVPLLKLFRPSKILFYCHFP----DQLLAQRK------ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 219 naafitrnpflSKVKLIYYYLFAFIYGLVGSCSDVVMVNSSWTLNHIL----SLWKVGNctNIVYPPCDVQTF-----LD 289
Cdd:cd03805 134 -----------SLLKRLYRKPFDWLEEFTTGMADQIVVNSNFTAGVFKktfpSLAKNPP--EVLYPCVDTDSFdstseDP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 290 IPLHEKKMTPGHLLVSVGQFRPEKNHPLQIRAFAKLlnKKMVESPPSLKLVLIGGcrnKDDELRVN-----QLRRLSEDL 364
Cdd:cd03805 201 DPGDLIAKSNKKFFLSINRFERKKNIALAIEAFAKL--KQKLPEFENVRLVIAGG---YDPRVAENveyleELQRLAEEL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 365 -GVQEYVEFKINIPfDELKNYL-SEATIGLHTMWNEHFGIGVVECMAAGTIILAHNSGGPKLDIVVphegDITGFLAESE 442
Cdd:cd03805 276 lNVEDQVLFLRSIS-DSQKEQLlSSALALLYTPSNEHFGIVPLEAMYAGKPVIACNSGGPLETVVE----GVTGFLCEPT 350
|
330 340 350
....*....|....*....|....*....|....*....
gi 304434672 443 -EDYAETIAHILSMSAEKRlQIRKSARASVS-RFSDQEF 479
Cdd:cd03805 351 pEAFAEAMLKLANDPDLAD-RMGAAGRKRVKeKFSREAF 388
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
302-468 |
7.21e-28 |
|
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: 108.90 E-value: 7.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 302 LLVSVGQFRPEKNHPLQIRAFAKLLNKKmvespPSLKLVLIGgcrnkdDELRVNQLRRLSEDLGVQEYVEFKINIPFDEL 381
Cdd:pfam00534 4 IILFVGRLEPEKGLDLLIKAFALLKEKN-----PNLKLVIAG------DGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 382 KNYLSEATIGLHTMWNEHFGIGVVECMAAGTIILAHNSGGPKlDIVVPHEgdiTGFLAE--SEEDYAETIAHILSMSaEK 459
Cdd:pfam00534 73 PELLKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPP-EVVKDGE---TGFLVKpnNAEALAEAIDKLLEDE-EL 147
|
....*....
gi 304434672 460 RLQIRKSAR 468
Cdd:pfam00534 148 RERLGENAR 156
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
252-475 |
5.15e-25 |
|
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: 106.08 E-value: 5.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 252 DVVMVNSSWTLNHILSLWKVGNCTNIV-YPPCDVQTFLDIPLHEKKMTPGH-LLVSVGQFRPEKNHPLQIRAFAKLLNKk 329
Cdd:cd03801 142 DAVIAVSEALRDELRALGGIPPEKIVViPNGVDLERFSPPLRRKLGIPPDRpVLLFVGRLSPRKGVDLLLEALAKLLRR- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 330 mvesPPSLKLVLIGGcrnkDDELRvNQLRRLseDLGVQEYVEFKINIPFDELKNYLSEATIGLHTMWNEHFGIGVVECMA 409
Cdd:cd03801 221 ----GPDVRLVIVGG----DGPLR-AELEEL--ELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMA 289
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 304434672 410 AGTIILAHNSGGPKlDIVVPHEGditGFLAESE--EDYAETIAHILSmSAEKRLQIRKSARASVS-RFS 475
Cdd:cd03801 290 AGLPVVATDVGGLP-EVVEDGEG---GLVVPPDdvEALADALLRLLA-DPELRARLGRAARERVAeRFS 353
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
76-475 |
3.21e-18 |
|
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: 85.88 E-value: 3.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 76 GGGERVLWCALRALQKKYPEAVYVVytgdvnVNGQQILEGAFRRFNIRLIHPVQFVFLRKRYLvedslyphftllgqslG 155
Cdd:cd03809 14 TGIGRYTRELLKALAKNDPDESVLA------VPPLPGELLRLLREYPELSLGVIKIKLWRELA----------------L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 156 SIFLGWEALMQCVPDVYIdsmGYAFTLPLFKYigGCQVGSYVHyptistDMLsvvknqnigfnnaAFITRNPFLSKVKLI 235
Cdd:cd03809 72 LRWLQILLPKKDKPDLLH---SPHNTAPLLLK--GCPQVVTIH------DLI-------------PLRYPEFFPKRFRLY 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 236 YYYLFAfiygLVGSCSDVVMVNSSWTLNHILSLWKVgNCTNIVYPPCDVQTFLDIPLHEKKMTPGHLL-----VSVGQFR 310
Cdd:cd03809 128 YRLLLP----ISLRRADAIITVSEATRDDIIKFYGV-PPEKIVVIPLGVDPSFFPPESAAVLIAKYLLpepyfLYVGTLE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 311 PEKNHPLQIRAFAKLLNKKmvespPSLKLVLIGGCRNKDDElrvnqLRRLSEDLGVQEYVEFKINIPFDELKNYLSEATI 390
Cdd:cd03809 203 PRKNHERLLKAFALLKKQG-----GDLKLVIVGGKGWEDEE-----LLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARA 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 391 GLHTMWNEHFGIGVVECMAAGTIILAhnSGGPKLDIVVPheGDITGFLAESEEDYAETIAHILSMSAEkRLQIRKSARAS 470
Cdd:cd03809 273 FVFPSLYEGFGLPVLEAMACGTPVIA--SNISVLPEVAG--DAALYFDPLDPESIADAILRLLEDPSL-REELIRKGLER 347
|
....*
gi 304434672 471 VSRFS 475
Cdd:cd03809 348 AKKFS 352
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
246-454 |
6.92e-18 |
|
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: 85.37 E-value: 6.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 246 LVGSCSDVVMVNSSWTLNHILSLWKV-GNCTNIVYPPCDVQTFLDIPLHEKKMTP------GHLLVSVGQFRPEKNHPLQ 318
Cdd:cd03800 159 QILEAADRVIASTPQEADELISLYGAdPSRINVVPPGVDLERFFPVDRAEARRARlllppdKPVVLALGRLDPRKGIDTL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 319 IRAFAKLLnkkmvESPPSLKLVLIGGCRNKDDELRVNQLRRLSEDLGVQEYVEFKINIPFDELKNYLSEATIGLHTMWNE 398
Cdd:cd03800 239 VRAFAQLP-----ELRELANLVLVGGPSDDPLSMDREELAELAEELGLIDRVRFPGRVSRDDLPELYRAADVFVVPSLYE 313
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 304434672 399 HFGIGVVECMAAGTIILAHNSGGPKlDIVVPhegDITGFLAE--SEEDYAETIAHILS 454
Cdd:cd03800 314 PFGLTAIEAMACGTPVVATAVGGLQ-DIVRD---GRTGLLVDphDPEALAAALRRLLD 367
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
302-475 |
1.67e-16 |
|
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: 80.82 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 302 LLVSVGQFRPEKNHPLQIRAFAKLlnkkmVESPPSLKLVLIGgcrnkdDELRVNQLRRLSEDLGVQEYVEFKINIPfdEL 381
Cdd:cd03807 192 VIGIVGRLHPVKDHSDLLRAAALL-----VETHPDLRLLLVG------RGPERPNLERLLLELGLEDRVHLLGERS--DV 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 382 KNYLSEATIGLHTMWNEHFGIGVVECMAAGTIILAHNSGGpKLDIVvpheGDITGFL--AESEEDYAETIAHILSMsAEK 459
Cdd:cd03807 259 PALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGG-AAELV----DDGTGFLvpAGDPQALADAIRALLED-PEK 332
|
170
....*....|....*..
gi 304434672 460 RLQIRKSARASV-SRFS 475
Cdd:cd03807 333 RARLGRAARERIaNEFS 349
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
302-490 |
1.30e-15 |
|
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.
Pssm-ID: 340844 [Multi-domain] Cd Length: 372 Bit Score: 78.09 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 302 LLVSVGQFRPEKNHPLQIRAFAKLLNKkmvespPSLKLVLIGGcrNKDDElrvnQLRRLSEDLGVQEYVEFKINIPFDEL 381
Cdd:cd03817 203 ILLYVGRLAKEKNIDFLLRAFAELKKE------PNIKLVIVGD--GPERE----ELKELARELGLADKVIFTGFVPREEL 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 382 KNYLSEATIGLHTMWNEHFGIGVVECMAAGT-IILAHNSGGPklDIVvpHEGDiTGFLAESEEDYAET-IAHILSMsAEK 459
Cdd:cd03817 271 PEYYKAADLFVFASTTETQGLVYLEAMAAGLpVVAAKDPAAS--ELV--EDGE-NGFLFEPNDETLAEkLLHLREN-LEL 344
|
170 180 190
....*....|....*....|....*....|.
gi 304434672 460 RLQIRKSARASVSRFSdqefevtFLSSVEKL 490
Cdd:cd03817 345 LRKLSKNAEISAREFA-------FAKSVEKL 368
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
302-479 |
1.23e-14 |
|
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: 75.49 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 302 LLVSVGQFRPEKNHPLQIRAFAKLlNKKMvespPSLKLVLIGgcrnkDDELRVnQLRRLSEDLGVQEYVEFKINIPFDEL 381
Cdd:cd03798 202 VILFVGRLIPRKGIDLLLEAFARL-AKAR----PDVVLLIVG-----DGPLRE-ALRALAEDLGLGDRVTFTGRLPHEQV 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 382 KNYLSEATIGLHTMWNEHFGIGVVECMAAGTIILAHNSGGPKlDIVvphEGDITGFLAE--SEEDYAETIAHILsMSAEK 459
Cdd:cd03798 271 PAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIP-EVV---GDPETGLLVPpgDADALAAALRRAL-AEPYL 345
|
170 180
....*....|....*....|
gi 304434672 460 RLQIRKSARASVSRFSDQEF 479
Cdd:cd03798 346 RELGEAARARVAERFSWVKA 365
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
233-434 |
1.86e-14 |
|
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: 72.82 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 233 KLIYYYLFAFIYGLVGSCsDVVMVNS--SWTLNHILSLWKVGN----CTNIVYPPCDVQTFLDIPLHEKKMTPGHLLVSV 306
Cdd:cd01635 38 LLLLALRRILKKLLELKP-DVVHAHSphAAALAALLAARLLGIpivvTVHGPDSLESTRSELLALARLLVSLPLADKVSV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 307 GQFRPEKNHPLQIRAFAKLlnkkmVESPPSLKLVLIGGCRNKDDELRVNQLRRLSEDlgvqeyVEFKINIPFDELKNYLS 386
Cdd:cd01635 117 GRLVPEKGIDLLLEALALL-----KARLPDLVLVLVGGGGEREEEEALAAALGLLER------VVIIGGLVDDEVLELLL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 304434672 387 E-ATIGLHTMWNEHFGIGVVECMAAGTIILAHNSGGPKLDIVVPHEGDI 434
Cdd:cd01635 186 AaADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLL 234
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
299-477 |
9.18e-14 |
|
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.
Pssm-ID: 340832 [Multi-domain] Cd Length: 333 Bit Score: 72.32 E-value: 9.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 299 PGHLLVsVGQFRPEKNHPLQIRAfAKLLNkkmvesppsLKLVLIGGCRNKDDELRVNQLRrlsedlgVQEYVEFKINIPF 378
Cdd:cd03802 169 EDYLAF-LGRIAPEKGLEDAIRV-ARRAG---------LPLKIAGKVRDEDYFYYLQEPL-------PGPRIEFIGEVGH 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 379 DELKNYLSEATIGLHT-MWNEHFGIGVVECMAAGTIILAHNSGGPkLDIVVPHEgdiTGFLAESEEDYAETIAHILSMSa 457
Cdd:cd03802 231 DEKQELLGGARALLFPiNWDEPFGLVMIEAMACGTPVIAYRRGGL-PEVIQHGE---TGFLVDSVEEMAEAIANIDRID- 305
|
170 180
....*....|....*....|..
gi 304434672 458 ekRLQIRKSA--RASVSRFSDQ 477
Cdd:cd03802 306 --RAACRRYAedRFSAARMADR 325
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
252-483 |
3.83e-13 |
|
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.
Pssm-ID: 340833 [Multi-domain] Cd Length: 356 Bit Score: 70.78 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 252 DVVMVNSSWTLNHIlslWKV-GNCTNIVYPPCDVQTFLdiPLHEKkmtpGHLLVSVGQFRPEKNHPLQIRAFAKLlnkkm 330
Cdd:cd03804 159 DLFIANSQFVARRI---KKFyGRESTVIYPPVDTDAFA--PAADK----EDYYLTASRLVPYKRIDLAVEAFNEL----- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 331 vesppSLKLVLIGgcrnkDDElrvnQLRRLsEDLGvQEYVEFKINIPFDELKNYLSEATiGLHTMWNEHFGIGVVECMAA 410
Cdd:cd03804 225 -----PKRLVVIG-----DGP----DLDRL-RAMA-SPNVEFLGYQPDEVLKELLSKAR-AFVFAAEEDFGIVPVEAQAC 287
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 304434672 411 GTIILAHNSGGpKLDIVVPHEgdiTGFLaeseedYAE-TIAHILS-MSAEKRLQIR---KSARASVSRFSDQEFEVTF 483
Cdd:cd03804 288 GTPVIAFGKGG-ALETVRPGP---TGIL------FGEqTVESLKAaVEEFEQNFDRfkpQAIRANAERFSRARFRQEI 355
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
220-480 |
1.42e-12 |
|
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: 68.92 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 220 AAFITRNPFLSKVKLIY---------YYLFAFIYGLVGSC--SDVVMVNSSWTLNHILSL-WKVGNCTNIVYPPCDVQTF 287
Cdd:cd03811 94 ATYIVAKLAAARSKVIAwihsslsklYYLKKKLLLKLKLYkkADKIVCVSKGIKEDLIRLgPSPPEKIEVIYNPIDIDRI 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 288 LDIPLHEKKMTPGH--LLVSVGQFRPEKNHPLQIRAFAKLLNKKmvespPSLKLVLIGgcrnkDDELRvNQLRRLSEDLG 365
Cdd:cd03811 174 RALAKEPILNEPEDgpVILAVGRLDPQKGHDLLIEAFAKLRKKY-----PDVKLVILG-----DGPLR-EELEKLAKELG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 366 VQEYVEF---KINIPfdelkNYLSEATIGLHTMWNEHFGIGVVECMAAGTIILAHNSGGPKlDIVVPHEgdiTGFLAESE 442
Cdd:cd03811 243 LAERVIFlgfQSNPY-----PYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPR-EILDDGE---NGLLVPDG 313
|
250 260 270
....*....|....*....|....*....|....*...
gi 304434672 443 EDYAETIAHILSMSAEKRLQIRKSARASVSRFSDQEFE 480
Cdd:cd03811 314 DAAALAGILAALLQKKLDAALRERLAKAQEAVFREYTI 351
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
300-454 |
2.26e-12 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 64.45 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 300 GHLLVSVGQFRPE-KNHPLQIRAFAKLLNKkmvesPPSLKLVLIGgcrnkDDELRvnQLRRLSEdlGVQEYVEFkinIPF 378
Cdd:pfam13692 1 RPVILFVGRLHPNvKGVDYLLEAVPLLRKR-----DNDVRLVIVG-----DGPEE--ELEELAA--GLEDRVIF---TGF 63
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 304434672 379 -DELKNYLSEATIGLHTMWNEHFGIGVVECMAAGTIILAHNSGGPKlDIVvphEGDiTGFLAESE--EDYAETIAHILS 454
Cdd:pfam13692 64 vEDLAELLAAADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIP-ELV---DGE-NGLLVPPGdpEALAEAILRLLE 137
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
251-475 |
6.20e-12 |
|
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: 66.99 E-value: 6.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 251 SDVVMVNSSWTLNHILSLWKVGNCTNIVYPPCDVQTFLDIP---LHEKKMTP--GHLLVSVGQFRPEKNHPLQIRAFAKL 325
Cdd:cd04962 142 SDRVTAVSSSLRQETYELFDVDKDIEVIHNFIDEDVFKRKPagaLKRRLLAPpdEKVVIHVSNFRPVKRIDDVVRVFARV 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 326 LNKKmvespPSlKLVLIGgcrnkDDELRVNqLRRLSEDLGVQEYVEFKINipFDELKNYLSEATIGLHTMWNEHFGIGVV 405
Cdd:cd04962 222 RRKI-----PA-KLLLVG-----DGPERVP-AEELARELGVEDRVLFLGK--QDDVEELLSIADLFLLPSEKESFGLAAL 287
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 304434672 406 ECMAAGTIILAHNSGGpkLDIVVPHegDITGFL-----AESEEDYAETIAHilsmSAEKRLQIRKSARA-SVSRFS 475
Cdd:cd04962 288 EAMACGVPVVSSNAGG--IPEVVKH--GETGFLsdvgdVDAMAKSALSILE----DDELYNRMGRAARKrAAERFD 355
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
381-475 |
1.26e-10 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 58.85 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 381 LKNYLSEATIGLHTMWNEHFGIGVVECMAAGTIILAHNSGGPKlDIVVPHEgdiTGFLAESE--EDYAETIAHILSmSAE 458
Cdd:COG0438 14 LEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLP-EVIEDGE---TGLLVPPGdpEALAEAILRLLE-DPE 88
|
90
....*....|....*...
gi 304434672 459 KRLQIRKSARASV-SRFS 475
Cdd:COG0438 89 LRRRLGEAARERAeERFS 106
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
302-475 |
1.70e-10 |
|
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after WbdM in Escherichia coli. In general 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 in bacteria.
Pssm-ID: 340857 [Multi-domain] Cd Length: 360 Bit Score: 62.46 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 302 LLVSVGQFRPEKNHPLQIRAFakllnKKMVESPPSLKLVLIGgcrnkDDELRvNQLRRLSEDLGVQEYVEFKINIpfDEL 381
Cdd:cd04951 190 VILNVGRLTEAKDYPNLLLAI-----SELILSKNDFKLLIAG-----DGPLR-NELERLICNLNLVDRVILLGQI--SNI 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 382 KNYLSEATIG-LHTMWnEHFGIGVVECMAAGTIILAHNSGGPKlDIVVPHEGDITgfLAESEEdYAETIAHILSMSAEKR 460
Cdd:cd04951 257 SEYYNAADLFvLSSEW-EGFGLVVAEAMACERPVVATDAGGVA-EVVGDHNYVVP--VSDPQL-LAEKIKEIFDMSDEER 331
|
170
....*....|....*
gi 304434672 461 LQIRKSARASVSRFS 475
Cdd:cd04951 332 DILGNKNEYIAKNFS 346
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
306-474 |
4.46e-10 |
|
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: 61.22 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 306 VGQFRPEKNHPLQIRAFAKLlnKKMvespPSLKLVLIGgcrnkDDELRvNQLRRLSEDLGVQEYVEFKINIpfDELKNYL 385
Cdd:cd03819 188 VGRLSPEKGWLLLVDAAAEL--KDE----PDFRLLVAG-----DGPER-DEIRRLVERLGLRDRVTFTGFR--EDVPAAL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 386 SEATIGLHTMWNEHFGIGVVECMAAGTIILAHNSGGPkLDIVVPHE-------GDITGfLAESEEDYAETIahilsmSAE 458
Cdd:cd03819 254 AASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGA-REIVVHGRtgllvppGDAEA-LADAIRAAKLLP------EAR 325
|
170
....*....|....*.
gi 304434672 459 KRLQIRKSARASVSRF 474
Cdd:cd03819 326 EKLQAAAALTEAVREL 341
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
196-475 |
2.23e-09 |
|
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.
Pssm-ID: 340847 [Multi-domain] Cd Length: 351 Bit Score: 58.79 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 196 YVHYPTISTDMLSVVKNQN----IGFNNAAFITRNPFLSKVKLIYYYLFAFIYGLVGS-----------CSDVVMVNSSW 260
Cdd:cd03820 69 LLKYFKKVRRLRKYLKNNKpdvvISFRTSLLTFLALIGLKSKLIVWEHNNYEAYNKGLrrlllrrllykRADKIVVLTEA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 261 TLNHILSLWKvgncTNIVYPPcdvqTFLDIPLHEKKMTP-GHLLVSVGQFRPEKNHPLQIRAFAKLLNKkmvesPPSLKL 339
Cdd:cd03820 149 DKLKKYKQPN----SNVVVIP----NPLSFPSEEPSTNLkSKRILAVGRLTYQKGFDLLIEAWALIAKK-----HPDWKL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 340 VLIGgcrnkDDELRvNQLRRLSEDLGVQEYVEFKINIpfDELKNYLSEATIGLHTMWNEHFGIGVVECMAAGTIILAHNS 419
Cdd:cd03820 216 RIYG-----DGPER-EELEKLIDKLGLEDRVKLLGPT--KNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDC 287
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 304434672 420 -GGPKlDIVVPHEgdiTGFLAESE--EDYAETIAHILSmSAEKRLQIRKSARASVSRFS 475
Cdd:cd03820 288 pTGPS-EIIEDGE---NGLLVPNGdvDALAEALLRLME-DEELRKKMGKNARKNAERFS 341
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
306-480 |
2.40e-09 |
|
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: 58.88 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 306 VGQFRPEKNHPLQIRAFAKLlnkkmveSPPSLKLVLIGGCRNkddelrvNQLRRLSEDlgvqEYVEFKINIPFDELKNYL 385
Cdd:cd03823 197 IGRLTEEKGIDLLVEAFKRL-------PREDIELVIAGHGPL-------SDERQIEGG----RRIAFLGRVPTDDIKDFY 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 386 SEATIGL-HTMWNEHFGIGVVECMAAGTIILAHNSGGPKlDIVVPHEGDITgFLAESEEDYAETIAHILSMSAekrLQIR 464
Cdd:cd03823 259 EKIDVLVvPSIWPEPFGLVVREAIAAGLPVIASDLGGIA-ELIQPGVNGLL-FAPGDAEDLAAAMRRLLTDPA---LLER 333
|
170
....*....|....*.
gi 304434672 465 KSARASVSRFSDQEFE 480
Cdd:cd03823 334 LRAGAEPPRSTESQAE 349
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
275-492 |
2.77e-09 |
|
glycosyltransferase family 4 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, while some of them are also found in Archaea and eukaryotes.
Pssm-ID: 340841 [Multi-domain] Cd Length: 474 Bit Score: 59.27 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 275 TNIVYPPCDVQTFLDIPLHEKKMTPGHLlVSVGQFRPEKNHPLQIRAFaKLLNKKMvespPSLKLVLIGGcrNKDDELRV 354
Cdd:cd03813 269 TRVIPNGIDIQRFAPAREERPEKEPPVV-GLVGRVVPIKDVKTFIRAF-KLVRRAM----PDAEGWLIGP--EDEDPEYA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 355 NQLRRLSEDLGVQEYVEFkinIPFDELKNYLSEATIGLHTMWNEHFGIGVVECMAAGTIILAHNSG------GPKLD--- 425
Cdd:cd03813 341 QECKRLVASLGLENKVKF---LGFQNIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVGscreliYGADDalg 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 426 ---IVVPhegditgflAESEEDYAETIAHILSmSAEKRLQIRKSARASVSRFSDQEfevTFLSSVEKLFK 492
Cdd:cd03813 418 qagLVVP---------PADPEALAEALIKLLR-DPELRQAFGEAGRKRVEKYYTLE---GMIDSYRKLYL 474
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
301-476 |
7.99e-09 |
|
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general 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 in bacteria.
Pssm-ID: 340855 [Multi-domain] Cd Length: 328 Bit Score: 56.93 E-value: 7.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 301 HLLVSVGQFRPEKNHPLQIRAFAKLlnkkmVESPPSLKLVLIGgcRNKDDElrvnQLRRLSEDLGVQEYVEFK--INIPF 378
Cdd:cd04949 161 NKIITISRLAPEKQLDHLIEAVAKA-----VKKVPEITLDIYG--YGEERE----KLKKLIEELHLEDNVFLKgyHSNLD 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 379 DELKNYlsEATIGLHTMwnEHFGIGVVECMAAGTIILAHNSG-GPKlDIVVPHEgdiTGFLAESE--EDYAETIAHILSm 455
Cdd:cd04949 230 QEYQDA--YLSLLTSQM--EGFGLTLMEAIGHGLPVVSYDVKyGPS-ELIEDGE---NGYLIEKNniDALADKIIELLN- 300
|
170 180
....*....|....*....|.
gi 304434672 456 SAEKRLQIRKSARASVSRFSD 476
Cdd:cd04949 301 DPEKLQQFSEESYKIAEKYST 321
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
302-479 |
1.68e-08 |
|
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: 56.15 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 302 LLVSVGQFRPEKNHPLQIRAFAKLlnkkmvESPPSLKLVLIGGCRNKDdELRvnqlRRLSEdlgvqeyVEFKINIPFDEL 381
Cdd:cd03814 200 LLLYVGRLAPEKNLEALLDADLPL------AASPPVRLVVVGDGPARA-ELE----ARGPD-------VIFTGFLTGEEL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 382 KNYLSEATIGLHTMWNEHFGIGVVECMAAGTIILAHNSGGPKlDIVVPHEgdiTGFLAES--EEDYAETIAHiLSMSAEK 459
Cdd:cd03814 262 ARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPR-DIVRPGG---TGALVEPgdAAAFAAALRA-LLEDPEL 336
|
170 180
....*....|....*....|
gi 304434672 460 RLQIRKSARASVSRFSDQEF 479
Cdd:cd03814 337 RRRMAARARAEAERYSWEAF 356
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
276-473 |
9.03e-07 |
|
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly catalyzes trehalose synthesis and degradation from alpha-glucose-1-phosphate (alpha-Glc-1-P) and glucose. The catalyzing activity includes the phosphorolysis of trehalose, which produce alpha-Glc-1-P and glucose, and the subsequent synthesis of trehalose. This family is most closely related to the GT4 family of glycosyltransferases.
Pssm-ID: 340823 [Multi-domain] Cd Length: 378 Bit Score: 51.17 E-value: 9.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 276 NIVYPPCDVQTFL----DIPLHEKkmtpghLLVSVGQFRPEKNHPLQIRAFAKLlnKKMVESPpslKLVLIGGCRNKDDE 351
Cdd:cd03792 175 NKDLSPADIRYYLekpfVIDPERP------YILQVARFDPSKDPLGVIDAYKLF--KRRAEEP---QLVICGHGAVDDPE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 352 LRV--NQLRRLSEDlgvQEYVEFKINIPFDELKN-YLSEATIGLHTMWNEHFGIGVVECMAAGTIILAHNSGGPKLDIvv 428
Cdd:cd03792 244 GSVvyEEVMEYAGD---DHDIHVLRLPPSDQEINaLQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQV-- 318
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 304434672 429 phEGDITGFLAESEEDYAETIAHILSmSAEKRLQIRKSARASVSR 473
Cdd:cd03792 319 --IDGETGFLVNSVEGAAVRILRLLT-DPELRRKMGLAAREHVRD 360
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
319-475 |
1.89e-06 |
|
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.
Pssm-ID: 340825 [Multi-domain] Cd Length: 391 Bit Score: 50.03 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 319 IRAFAKLLNKkmvespPSLKLVLIGGCRNKDdelrvnQLRRLSEDLGVQEyVEFKINIPFDELKNYLSEATIGLHTMWNE 398
Cdd:cd03794 236 LEAAERLKRR------PDIRFLFVGDGDEKE------RLKELAKARGLDN-VTFLGRVPKEEVPELLSAADVGLVPLKDN 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 399 HFGIGVV-----ECMAAGTIILAHNSGGPKLDIVVphegDITGFLAESE--EDYAETIAHiLSMSAEKRLQIRKSARASV 471
Cdd:cd03794 303 PANRGSSpsklfEYMAAGKPILASDDGGSDLAVEI----NGCGLVVEPGdpEALADAILE-LLDDPELRRAMGENGRELA 377
|
....*
gi 304434672 472 -SRFS 475
Cdd:cd03794 378 eEKFS 382
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
302-449 |
3.52e-05 |
|
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1).
Pssm-ID: 340840 [Multi-domain] Cd Length: 357 Bit Score: 45.74 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 302 LLVSVGQFRPEKNHPLQIRAFAKLLNKKmvespPSLKLVLIGgcrnkDDELRvNQLRRLSEDLGVQEYVEF---KINIPf 378
Cdd:cd03812 193 VLGHVGRFNEQKNHSFLIDIFEELKKKN-----PNVKLVLVG-----EGELK-EKIKEKVKELGLEDKVIFlgfRNDVS- 260
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 304434672 379 delkNYLSEATIGLHTMWNEHFGIGVVECMAAGTIILAHNSGGPKLDIvvpheGDITGF--LAESEEDYAETI 449
Cdd:cd03812 261 ----EILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITKECDI-----TNNVEFlpLNETPSTWAEKI 324
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
233-478 |
4.66e-05 |
|
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.
Pssm-ID: 340848 [Multi-domain] Cd Length: 377 Bit Score: 45.44 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 233 KLIYYYLfafIYGLVGSCSDVVMVNSSWTLNHILSLwkvgnctNIVYPPCDVQTFLDIP-------LHEKKMTPGH--LL 303
Cdd:cd03821 138 KRIALHL---IERRNLNNAALVHFTSEQEADELRRF-------GLEPPIAVIPNGVDIPefdpglrDRRKHNGLEDrrII 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 304 VSVGQFRPEKNHPLQIRAFAKLLNKKMVesppsLKLVLIGgcrnkDDELRVNQLRRLSEDLGVQEYVEFKINIPFDELKN 383
Cdd:cd03821 208 LFLGRIHPKKGLDLLIRAARKLAEQGRD-----WHLVIAG-----PDDGAYPAFLQLQSSLGLGDRVTFTGPLYGEAKWA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 384 YLSEATIGLHTMWNEHFGIGVVECMAAGT-IILAHNSGGPKLdivvpHEGDITGFLAESEEDYAETIAHILSMSAEkrlq 462
Cdd:cd03821 278 LYASADLFVLPSYSENFGNVVAEALACGLpVVITDKCGLSEL-----VEAGCGVVVDPNVSSLAEALAEALRDPAD---- 348
|
250
....*....|....*.
gi 304434672 463 iRKSARASVSRFSDQE 478
Cdd:cd03821 349 -RKRLGEMARRARQVE 363
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
295-475 |
1.21e-04 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 44.32 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 295 KKMTPGH----LLVSVGQFRPEKNhplqirafAKLLnKKMVESPPSLKLVLIGgcrnkDDELRvNQLRRLSEDLGVQeyv 370
Cdd:PLN02871 254 ARLSGGEpekpLIVYVGRLGAEKN--------LDFL-KRVMERLPGARLAFVG-----DGPYR-EELEKMFAGTPTV--- 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 371 eFKINIPFDELKNYLSEATIGLHTMWNEHFGIGVVECMAAGTIILAHNSGGPKlDIVVPHEGDITGFLAESeEDYAETIA 450
Cdd:PLN02871 316 -FTGMLQGDELSQAYASGDVFVMPSESETLGFVVLEAMASGVPVVAARAGGIP-DIIPPDQEGKTGFLYTP-GDVDDCVE 392
|
170 180
....*....|....*....|....*..
gi 304434672 451 HI--LSMSAEKRLQIRKSARASVSRFS 475
Cdd:PLN02871 393 KLetLLADPELRERMGAAAREEVEKWD 419
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
255-477 |
1.83e-04 |
|
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: 43.86 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 255 MVNSSwtlnhilSLWKVGNCTNIVYPpCDVQTFLdiPLHEKKM-----TPGH----LLVSVGQFRPEKNHPLQIRAFAKL 325
Cdd:cd03825 151 MVRRS-------PLLKGLPVVVIPNG-IDTEIFA--PVDKAKArkrlgIPQDkkviLFGAESVTKPRKGFDELIEALKLL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 326 lnkkmvESPPSLKLVLIGGC--RNKDDELRVNQLRRLSEDLgvqeyvefkinipfdELKNYLSEATIGLHTMWNEHFGIG 403
Cdd:cd03825 221 ------ATKDDLLLVVFGKNdpQIVILPFDIISLGYIDDDE---------------QLVDIYSAADLFVHPSLADNLPNT 279
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 304434672 404 VVECMAAGTIILAHNSGGPkLDIVVPHEgdiTGFLA--ESEEDYAETIAHILsMSAEKRLQIRKSARASVSRFSDQ 477
Cdd:cd03825 280 LLEAMACGTPVVAFDTGGS-PEIVQHGV---TGYLVppGDVQALAEAIEWLL-ANPKERESLGERARALAENHFDQ 350
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
303-453 |
1.16e-03 |
|
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.
Pssm-ID: 340829 [Multi-domain] Cd Length: 350 Bit Score: 41.28 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 303 LVSVGQFRPEKNHPLQIRAFAKLLNKKmvespPSLKLVLIGgcrnkDDELRvNQLRRLSEDLGVQEYVEFKINIPFDELK 382
Cdd:cd03799 177 ILTVGRLTEKKGLEYAIEAVAKLAQKY-----PNIEYQIIG-----DGDLK-EQLQQLIQELNIGDCVKLLGWKPQEEII 245
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 304434672 383 NYLSEATIGLHTMWN----EHFGIGVV--ECMAAG-TIILAHNSGGPKLdivvpHEGDITGFLAeSEEDyAETIAHIL 453
Cdd:cd03799 246 EILDEADIFIAPSVTaadgDQDGPPNTlkEAMAMGlPVISTEHGGIPEL-----VEDGVSGFLV-PERD-AEAIAEKL 316
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
288-480 |
1.26e-03 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 40.93 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 288 LDIPLHEKkmtpghLLVSVGQFRPEKNHPLQIRAFakllnKKMVESPPSLKLVLIGGCRNK---DDELRVNQLRRLSEDL 364
Cdd:PRK15484 187 LNISPDET------VLLYAGRISPDKGILLLMQAF-----EKLATAHSNLKLVVVGDPTASskgEKAAYQKKVLEAAKRI 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434672 365 GVQEYVEFkiNIPFDELKNYLSEAT-IGLHTMWNEHFGIGVVECMAAGTIILAHNSGGpkldIVVPHEGDITGF-LAE-- 440
Cdd:PRK15484 256 GDRCIMLG--GQPPEKMHNYYPLADlVVVPSQVEEAFCMVAVEAMAAGKPVLASTKGG----ITEFVLEGITGYhLAEpm 329
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 304434672 441 SEEDYAETIAHILsmSAEKRLQIRKSARASV-SRFS----DQEFE 480
Cdd:PRK15484 330 TSDSIISDINRTL--ADPELTQIAEQAKDFVfSKYSwegvTQRFE 372
|
|
| |
