|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00142 |
PLN00142 |
sucrose synthase |
1-802 |
0e+00 |
|
sucrose synthase
Pssm-ID: 215073 [Multi-domain] Cd Length: 815 Bit Score: 1578.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 1 MEMTSGSLGNGIPEAMGQNRGNIKRCLEKYIENGRRVMKLNELMDEMEIVINDVTQRRRVMEGDLGKILCFTQEAVVIPP 80
Cdd:PLN00142 6 VLTRSHSIRERVPDALSQHRNELKALLSRYVAQGKGILQPHQLIDELEAVIDDDEERKKLLDGPFGDILRSTQEAIVLPP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 81 NVAFAVRGTPGNWQYVKVNSSNLSVEALSSTQYLKLKEFLFDENWaNDENALEVDFGALDFTLPWLSLSSSIGNGLSFVS 160
Cdd:PLN00142 86 FVALAVRPRPGVWEYVRVNVSELSVEELTVSEYLKFKEELVDGSW-NDNFVLELDFEPFNASFPRPTLSSSIGNGVQFLN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 161 SKLGGRLN---DNPQSLVDYLLSLEHQGEKLMMNETLNTARKLEMSLILADVFLSELPKDTPFQAFELRFKECGFEKGWG 237
Cdd:PLN00142 165 RHLSSKLFrdkESLEPLLDFLRAHNHKGETLMLNDRIQTLSKLQSALRKAEEYLSKLPKDTPYSEFEHRFQELGLEKGWG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 238 ESAGRVKETMRILSEILQAPDPQNIDRFFARVPRIFNVVIFSVHGYFGQTDVLGLPDTGGQVVYILDQVKALEDELLQRI 317
Cdd:PLN00142 245 DTAERVLETIHLLLDLLQAPDPSTLEKFLGRIPMVFNVVIFSPHGYFGQANVLGLPDTGGQVVYILDQVRALENEMLLRI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 318 NSQGLNFKPQILVVTRLIPDAKKTKCNQELEPIFGTKYSNILRIPFVTENGILRRWVSRFDIYPYLERFTKDATTKILDI 397
Cdd:PLN00142 325 KQQGLDIKPQILIVTRLIPDAKGTTCNQRLEKVSGTEHSHILRVPFRTEKGILRKWISRFDVWPYLETFAEDAASEILAE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 398 LEGKPDLIIGNYTDGNLVASLMANKLGITQATIAHALEKTKYEDSDIKWKEFDPKYHFSSQFTADLISMNSADFIIASTY 477
Cdd:PLN00142 405 LQGKPDLIIGNYSDGNLVASLLAHKLGVTQCTIAHALEKTKYPDSDIYWKKFDDKYHFSCQFTADLIAMNHADFIITSTY 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 478 QEIAGSKERAGQYESHMSFTVPGLYRVVSGINVFDPRFNIAAPGADDSIYFPFTAQDRRFTKFYTSIDELLYSQSENDEH 557
Cdd:PLN00142 485 QEIAGSKDTVGQYESHTAFTLPGLYRVVHGIDVFDPKFNIVSPGADMSIYFPYTEKQKRLTSLHPSIEELLYSPEQNDEH 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 558 IGYLVDKKKPIIFSMARLDVVKNLTGLTEWYAKNKRLRDLVNLVIVGGFFDASKSKDREEISEIKKMHSLIEKYQLKGQF 637
Cdd:PLN00142 565 IGYLKDRKKPIIFSMARLDRVKNLTGLVEWYGKNKRLRELVNLVVVGGFIDPSKSKDREEIAEIKKMHSLIEKYNLKGQF 644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 638 RWITAQTDRTRNGELYRSIADTRGAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSD 717
Cdd:PLN00142 645 RWIAAQTNRVRNGELYRYIADTKGAFVQPALYEAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFHIDPYHGDEAAN 724
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 718 KIADFFEKSGMDPDYWNMFSNEGLQRINECYTWKIYANKVINMGSTYSYWRHLNKDQKLAKQRYIHSFYNLQYRNLVKTI 797
Cdd:PLN00142 725 KIADFFEKCKEDPSYWNKISDAGLQRIYECYTWKIYAERLLTLGGVYGFWKYVSKLERRETRRYLEMFYNLKFRELAKTV 804
|
....*
gi 1039022228 798 PILSD 802
Cdd:PLN00142 805 PLAVD 809
|
|
| sucr_synth |
TIGR02470 |
sucrose synthase; This model represents sucrose synthase, an enzyme that, despite its name, ... |
20-798 |
0e+00 |
|
sucrose synthase; This model represents sucrose synthase, an enzyme that, despite its name, generally uses rather produces sucrose. Sucrose plus UDP (or ADP) becomes D-fructose plus UDP-glucose (or ADP-glucose), which is then available for cell wall (or starch) biosynthesis. The enzyme is homologous to sucrose phosphate synthase, which catalyzes the penultimate step in sucrose synthesis. Sucrose synthase is found, so far, exclusively in plants and cyanobacteria. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
Pssm-ID: 274149 [Multi-domain] Cd Length: 784 Bit Score: 1209.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 20 RGNIKRCLEKYIENGRRVMKLNELMDEMEIVINDVTQRRRVMEGDLGKILCFTQEAVVIPPNVAFAVRGTPGNWQYVKVN 99
Cdd:TIGR02470 1 RAELRQLLSRYVSQGKRYLLRHQLLDEFEQYCSDADKEKKLSESPLGKLIFSTQEAIVLPPWVALAVRPRIGVWEYVRVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 100 SSNLSVEALSSTQYLKLKEFLFDEnWANDENALEVDFGALDFTLPWLSLSSSIGNGLSFVSSKLGGRLNDNPQS---LVD 176
Cdd:TIGR02470 81 VEELSVEELTISEYLDFKEQLVNG-HANDPNVLELDFEPFNASFPRPSDSKSIGNGVQFLNRHLSSKLFQDPESmepLLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 177 YLLSLEHQGEKLMMNETLNTARKLEMSLILADVFLSELPKDTPFQAFELRFKECGFEKGWGESAGRVKETMRILSEILQA 256
Cdd:TIGR02470 160 FLRVHNYNGIQLMINDRIQSVSHLQSQLRKAEEFLSALPPDTPYSEFEFELQELGFEPGWGDTAQRVLETLHLLDDLLEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 257 PDPQNIDRFFARVPRIFNVVIFSVHGYFGQTDVLGLPDTGGQVVYILDQVKALEDELLQRINSQGLNFKPQILVVTRLIP 336
Cdd:TIGR02470 240 PDPSVLEAFLGRIPMVFNVVILSPHGYFGQENVLGLPDTGGQVVYILDQVRALENEMLQRIKLQGLEITPKILIVTRLIP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 337 DAKKTKCNQELEPIFGTKYSNILRIPFVTENGI-LRRWVSRFDIYPYLERFTKDATTKILDILEGKPDLIIGNYTDGNLV 415
Cdd:TIGR02470 320 DAEGTTCNQRLEKVYGTEHAWILRVPFRTENGIiLRNWISRFEIWPYLETFAEDAEKEILAELQGKPDLIIGNYSDGNLV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 416 ASLMANKLGITQATIAHALEKTKYEDSDIKWKEFDPKYHFSSQFTADLISMNSADFIIASTYQEIAGSKERAGQYESHMS 495
Cdd:TIGR02470 400 ASLLARKLGVTQCTIAHALEKTKYPDSDIYWQEFEDKYHFSCQFTADLIAMNAADFIITSTYQEIAGTKDSVGQYESHQA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 496 FTVPGLYRVVSGINVFDPRFNIAAPGADDSIYFPFTAQDRRFTKFYTSIDELLYSQSENDEHIGYLVDKKKPIIFSMARL 575
Cdd:TIGR02470 480 FTMPGLYRVVHGIDVFDPKFNIVSPGADESIYFPYSDKEKRLTNLHPEIEELLFSLEDNDEHYGYLKDPNKPIIFSMARL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 576 DVVKNLTGLTEWYAKNKRLRDLVNLVIVGGFFDASKSKDREEISEIKKMHSLIEKYQLKGQFRWITAQTDRTRNGELYRS 655
Cdd:TIGR02470 560 DRVKNLTGLVECYGRSPKLRELVNLVVVAGKLDAKESKDREEQAEIEKMHNLIDQYQLHGQIRWIGAQLNRVRNGELYRY 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 656 IADTRGAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSDKIADFFEKSGMDPDYWNM 735
Cdd:TIGR02470 640 IADTKGIFVQPALYEAFGLTVLEAMTCGLPTFATRFGGPLEIIQDGVSGFHIDPYHGEEAAEKIVDFFEKCDEDPSYWQK 719
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039022228 736 FSNEGLQRINECYTWKIYANKVINMGSTYSYWRHLNKDQKLAKQRYIHSFYNLQYRNLVKTIP 798
Cdd:TIGR02470 720 ISQGGLQRIYEKYTWKIYSERLLTLAGIYGFWKFVSKLEREETRRYLEMFYHLKYRPLAEAVP 782
|
|
| Sucrose_synth |
pfam00862 |
Sucrose synthase; Sucrose synthases catalyze the synthesis of sucrose from UDP-glucose and ... |
12-549 |
0e+00 |
|
Sucrose synthase; Sucrose synthases catalyze the synthesis of sucrose from UDP-glucose and fructose. This family includes the bulk of the sucrose synthase protein. However the carboxyl terminal region of the sucrose synthases belongs to the glycosyl transferase family pfam00534.
Pssm-ID: 395692 Cd Length: 540 Bit Score: 1025.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 12 IPEAMGQNRGNIKRCLEKYIENGRRVMKLNELMDEMEIVINDVTQRRRVMEGDLGKILCFTQEAVVIPPNVAFAVRGTPG 91
Cdd:pfam00862 1 VPDALSQSRNELKRLLSRYVAQGKRLMKRHELLDEFEKVIEDKKERSKLMEGLLGKILHSTQEAIVLPPWVAFAVRPRPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 92 NWQYVKVNSSNLSVEALSSTQYLKLKEFLFDENWaNDENALEVDFGALDFTLPWLSLSSSIGNGLSFVSSKLGGRLNDNP 171
Cdd:pfam00862 81 VWEYVRVNADELSVEELTVSEYLKFKERLVDESW-NDENALELDFGPFNASFPRLTLPSSIGNGVQFLNRHLSSKLFRDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 172 QS---LVDYLLSLEHQGEKLMMNETLNTARKLEMSLILADVFLSELPKDTPFQAFELRFKECGFEKGWGESAGRVKETMR 248
Cdd:pfam00862 160 ESlepLLDFLRSHNYDGESLMINDRINSVSKLQSALIKAEEFLSKLPKDTPYEEFEYRLQELGFEKGWGDTAERVKETMH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 249 ILSEILQAPDPQNIDRFFARVPRIFNVVIFSVHGYFGQTDVLGLPDTGGQVVYILDQVKALEDELLQRINSQGLNFKPQI 328
Cdd:pfam00862 240 LLSELLQAPDPSTLEKFLGRIPMVFNVVILSPHGYFGQANVLGLPDTGGQVVYILDQVRALENELLLRIKQQGLDIKPQI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 329 LVVTRLIPDAKKTKCNQELEPIFGTKYSNILRIPFVTENGILRRWVSRFDIYPYLERFTKDATTKILDILEGKPDLIIGN 408
Cdd:pfam00862 320 LVVTRLIPEARGTTCNQELEKISGTKHSHILRVPFRTENGILRQWISRFDIWPYLERFTQDAAKEILAELEGKPDLIIGN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 409 YTDGNLVASLMANKLGITQATIAHALEKTKYEDSDIKWKEFDPKYHFSSQFTADLISMNSADFIIASTYQEIAGSKERAG 488
Cdd:pfam00862 400 YSDGNLVASLLAHKLGVTQCTIAHALEKTKYEDSDIYWKELEPKYHFSCQFTADLIAMNAADFIITSTYQEIAGSKDRVG 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039022228 489 QYESHMSFTVPGLYRVVSGINVFDPRFNIAAPGADDSIYFPFTAQDRRFTKFYTSIDELLY 549
Cdd:pfam00862 480 QYESHTAFTLPGLYRVVSGIDVFDPKFNIVSPGADQSIYFPYTEKERRLTSLHPSIEELLY 540
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
274-754 |
3.68e-128 |
|
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: 389.68 E-value: 3.68e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 274 NVVIFSVHGYFGQtdVLGLPDTGGQVVYILDQVKALedelLQRInsqglnfkPQILVVTRLIPDAKktkcnqeLEPIFGT 353
Cdd:cd03800 1 RIALISVHGSPLA--QPGGADTGGQNVYVLELARAL----AELG--------YQVDIFTRRISPAD-------PEVVEIA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 354 KYSNILRIPFVTENGILRRWVsrfdiYPYLERFTKDATTKILDILeGKPDLIIGNYTDGNLVASLMANKLGITQATIAHA 433
Cdd:cd03800 60 PGARVIRVPAGPPEYLPKEEL-----WPYLEEFADGLLRFIAREG-GRYDLIHSHYWDSGLVGALLARRLGVPLVHTFHS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 434 LEKTKYEDSDIKWKefdpkYHFSSQFTADLISMNSADFIIASTYQEIAGSKERAGQYESHMsftvpglyRVVSginvfdp 513
Cdd:cd03800 134 LGRVKYRHLGAQDT-----YHPSLRITAEEQILEAADRVIASTPQEADELISLYGADPSRI--------NVVP------- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 514 rfniaaPGADDSIYFPFTAQDRRFTKFytsidellysqsendehigyLVDKKKPIIFSMARLDVVKNLTGLTEWYAKNKR 593
Cdd:cd03800 194 ------PGVDLERFFPVDRAEARRARL--------------------LLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPE 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 594 LRDLVNLVIVGGFFDASKSKDREEISEIKKMHSLIEKYQLKGQFRwitaqtdRTRNGELYRSiadtRGAFVQPAHYEAFG 673
Cdd:cd03800 248 LRELANLVLVGGPSDDPLSMDREELAELAEELGLIDRVRFPGRVS-------RDDLPELYRA----ADVFVVPSLYEPFG 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 674 LTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSDKIADFFEksgmDPDYWNMFSNEGLQRINECYTWKIY 753
Cdd:cd03800 317 LTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLD----DPALWQRLSRAGLERARAHYTWESV 392
|
.
gi 1039022228 754 A 754
Cdd:cd03800 393 A 393
|
|
| sucrsPsyn_pln |
TIGR02468 |
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ... |
249-767 |
4.38e-35 |
|
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.
Pssm-ID: 274147 [Multi-domain] Cd Length: 1050 Bit Score: 144.15 E-value: 4.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 249 ILSEILQAPDPqniDRFFARVPRIFN-----------------VVIFSVHGYF-GQTDVLGL-PDTGGQVVYILDQVKAL 309
Cdd:TIGR02468 132 VAGDISVAGGE---PSTKGRLPRISSnlemetwsdqqkekklyIVLISLHGLVrGENMELGRdSDTGGQVKYVVELARAL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 310 E--------DELLQRINSQGLNF---KPQILVVTRlipdakKTKCNQELEPIFGTKYsnILRIPFvtenGILRRWVSRFD 378
Cdd:TIGR02468 209 GsmpgvyrvDLLTRQVSSPDVDWsygEPTEMLTPR------SSENDGDEMGESSGAY--IIRIPF----GPRDKYIPKEE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 379 IYPYLERFTKDATTKILD--------ILEGK---PDLIIGNYTDGNLVASLMANKLGITQATIAHALEKTKYED----SD 443
Cdd:TIGR02468 277 LWPYIPEFVDGALSHIVNmskvlgeqIGSGHpvwPYVIHGHYADAGDSAALLSGALNVPMVLTGHSLGRDKLEQllkqGR 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 444 IKWKEFDPKYHFSSQFTADLISMNSADFIIASTYQEIagsKERAGQYEShmsFTvPGLYRV--------VSGINVFDPRF 515
Cdd:TIGR02468 357 MSKEEINSTYKIMRRIEAEELSLDASEIVITSTRQEI---EEQWGLYDG---FD-VILERKlrararrgVSCYGRFMPRM 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 516 NIAAPGADdsiyfpFTAQDRRFTKFYTSIDELLYSQSEND-----EHIGYLVDKKKPIIFSMARLDVVKNLTGLTEWYAK 590
Cdd:TIGR02468 430 AVIPPGME------FSHIVPHDGDMDGETEGNEEHPAKPDppiwsEIMRFFTNPRKPMILALARPDPKKNITTLVKAFGE 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 591 NKRLRDLVNLVIVGGffdaskskDREEISEIKKMHS--------LIEKYQLKGQFRWIT--AQTDRTrngELYRSIADTR 660
Cdd:TIGR02468 504 CRPLRELANLTLIMG--------NRDDIDEMSSGSSsvltsvlkLIDKYDLYGQVAYPKhhKQSDVP---DIYRLAAKTK 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 661 GAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPsngeESSDKIADFFEKSGMDPDYWNMFSNEG 740
Cdd:TIGR02468 573 GVFINPAFIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDP----HDQQAIADALLKLVADKQLWAECRQNG 648
|
570 580 590
....*....|....*....|....*....|.
gi 1039022228 741 LQRINEcYTW----KIYANKVINMGSTYSYW 767
Cdd:TIGR02468 649 LKNIHL-FSWpehcKTYLSRIASCRPRHPQW 678
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
565-743 |
1.42e-31 |
|
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: 120.84 E-value: 1.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 565 KKPIIFSMARLDVVKNLTGLTEWYAKNKRLRDLVNLVIVGgffdaskskdreEISEIKKMHSLIEKYQLKGQFRWITAQt 644
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAG------------DGEEEKRLKKLAEKLGLGDNVIFLGFV- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 645 DRTRNGELYRsIADtrgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSDKIADFFE 724
Cdd:pfam00534 68 SDEDLPELLK-IAD---VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLE 143
|
170
....*....|....*....
gi 1039022228 725 ksgmDPDYWNMFSNEGLQR 743
Cdd:pfam00534 144 ----DEELRERLGENARKR 158
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
534-760 |
4.35e-23 |
|
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: 101.85 E-value: 4.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 534 DRRFTKFYTSIDELLYSQSENDEhigYLVDKKKPIIFSMARLDVVKNLTGLTEWYAKNKRLRDLVNLVIVGGffdasksk 613
Cdd:cd03801 163 PEKIVVIPNGVDLERFSPPLRRK---LGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGG-------- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 614 DREEISEIKKMhslieKYQLKGQFRWITAQTDRTRNgELYRSiADtrgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGG 693
Cdd:cd03801 232 DGPLRAELEEL-----ELGLGDRVRFLGFVPDEELP-ALYAA-AD---VFVLPSRYEGFGLVVLEAMAAGLPVVATDVGG 301
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039022228 694 PAEIIVDGVSGFHIDPSNGEESSDKIADFFEksgmDPDYWNMFSNEGLQRINECYTWKIYANKVINM 760
Cdd:cd03801 302 LPEVVEDGEGGLVVPPDDVEALADALLRLLA----DPELRARLGRAARERVAERFSWERVAERLLDL 364
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
652-760 |
4.94e-21 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 89.28 E-value: 4.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 652 LYRSiADtrgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSDKIADFFEksgmDPD 731
Cdd:COG0438 17 LLAA-AD---VFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLE----DPE 88
|
90 100
....*....|....*....|....*....
gi 1039022228 732 YWNMFSNEGLQRINECYTWKIYANKVINM 760
Cdd:COG0438 89 LRRRLGEAARERAEERFSWEAIAERLLAL 117
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
564-749 |
2.82e-16 |
|
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.
Pssm-ID: 340837 [Multi-domain] Cd Length: 358 Bit Score: 81.49 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 564 KKKPIIFSMARLDVVKNLTGLTEwYAKNKRLRDL-VNLVIVGGFfdaskskDREEISEIkkmhsLIEKYQLKGQFRWita 642
Cdd:cd03808 187 SEKVVFLFVARLLKDKGIDELIE-AAKILKKKGPnVRFLLVGDG-------ELENPSEI-----LIEKLGLEGRIEF--- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 643 qTDRTRNGELYRSIADtrgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSDKIADF 722
Cdd:cd03808 251 -LGFRSDVPELLAESD---VFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVPPGDVEALADAIEKL 326
|
170 180
....*....|....*....|....*..
gi 1039022228 723 FEksgmDPDYWNMFSNEGLQRINECYT 749
Cdd:cd03808 327 IE----DPELRKEMGEAARKRVEEKFD 349
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
530-759 |
1.32e-15 |
|
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: 79.33 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 530 FTAQD---------RRFTKFYTSIDELLYSQSENDEHIGYLVDKKkPIIFSMARLDVVKNLTGLTEWYAKNKRLRDLVNL 600
Cdd:cd03809 148 ATRDDiikfygvppEKIVVIPLGVDPSFFPPESAAVLIAKYLLPE-PYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 601 VIVGGffdasKSKDREEIseikkmHSLIEKYQLKGQFRWitaqTDRTRNGEL---YRSiADtrgAFVQPAHYEAFGLTVI 677
Cdd:cd03809 227 VIVGG-----KGWEDEEL------LDLVKKLGLGGRVRF----LGYVSDEDLpalYRG-AR---AFVFPSLYEGFGLPVL 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 678 EAMSCGLVTFATNqgGPA--EIIvdGVSGFHIDPSNGEEssdkIADFFEKSGMDPDYWNMFSNEGLQRInECYTWKIYAN 755
Cdd:cd03809 288 EAMACGTPVIASN--ISVlpEVA--GDAALYFDPLDPES----IADAILRLLEDPSLREELIRKGLERA-KKFSWEKTAE 358
|
....
gi 1039022228 756 KVIN 759
Cdd:cd03809 359 KTLE 362
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
563-725 |
6.14e-15 |
|
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: 77.01 E-value: 6.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 563 DKKKPIIFSMARLDVVKNLTGLTEWYAKNKRLRDLVNLVIVGgffdasKSKDREEIseikkmHSLIEKYQLKGQFRWITA 642
Cdd:cd03811 185 PEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILG------DGPLREEL------EKLAKELGLAERVIFLGF 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 643 QTDrtrngeLYRSIADTRgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSDKIADF 722
Cdd:cd03811 253 QSN------PYPYLKKAD-LFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAAALAGILAAL 325
|
...
gi 1039022228 723 FEK 725
Cdd:cd03811 326 LQK 328
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
620-746 |
3.85e-13 |
|
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: 72.00 E-value: 3.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 620 EIKKMHSLIEKYQLKGQFRWITAQTDRtrngELYRSIADTrgaFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIV 699
Cdd:cd04962 237 ERVPAEELARELGVEDRVLFLGKQDDV----EELLSIADL---FLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVK 309
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1039022228 700 DGVSGFHIDPSNGEESSDKIADFFEksgmDPDYWNMFSNEGLQRINE 746
Cdd:cd04962 310 HGETGFLSDVGDVDAMAKSALSILE----DDELYNRMGRAARKRAAE 352
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
543-758 |
1.29e-12 |
|
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: 70.49 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 543 SIDELLYSQSENDEHIGylvdKKKPIIFSMARLDVVKNLTGLTEWYAK-NKRLRDLVnLVIVGGFfdaskskdreeiSEI 621
Cdd:cd03798 181 GVDPARFQPEDRGLGLP----LDAFVILFVGRLIPRKGIDLLLEAFARlAKARPDVV-LLIVGDG------------PLR 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 622 KKMHSLIEKYQLKGQFRwITAQTDRTRNGELYRSiADtrgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDG 701
Cdd:cd03798 244 EALRALAEDLGLGDRVT-FTGRLPHEQVPAYYRA-CD---VFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDP 318
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039022228 702 VSGFHIDPSNGEESSDKIADFfeksgMDPDYWNMFSNEGLQRINECYTWKIYANKVI 758
Cdd:cd03798 319 ETGLLVPPGDADALAAALRRA-----LAEPYLRELGEAARARVAERFSWVKAADRIA 370
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
566-724 |
1.79e-12 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 65.23 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 566 KPIIFSMARLDV-VKNLtgltEWYAKN-KRLR---DLVNLVIVGgffdaskSKDREEISEIKKmhsliekyQLKGQFRWI 640
Cdd:pfam13692 1 RPVILFVGRLHPnVKGV----DYLLEAvPLLRkrdNDVRLVIVG-------DGPEEELEELAA--------GLEDRVIFT 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 641 TAQTDRtrnGELYRSiADtrgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIvDGVSGFHIDPSNGEESSDKIA 720
Cdd:pfam13692 62 GFVEDL---AELLAA-AD---VFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPPGDPEALAEAIL 133
|
....
gi 1039022228 721 DFFE 724
Cdd:pfam13692 134 RLLE 137
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
562-746 |
1.18e-11 |
|
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: 67.34 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 562 VDKKKPIIFSMARLDVVKNLTGLTEWYAK-NKRLRDLVnLVIVGgffdasKSKDREEISEIKKMHSLIEKYQLKGQfrwi 640
Cdd:cd03807 186 LAEDRRVIGIVGRLHPVKDHSDLLRAAALlVETHPDLR-LLLVG------RGPERPNLERLLLELGLEDRVHLLGE---- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 641 taqtdRTRNGELYRsIADtrgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGvSGFHIDPsngeESSDKIA 720
Cdd:cd03807 255 -----RSDVPALLP-AMD---IFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDDG-TGFLVPA----GDPQALA 320
|
170 180
....*....|....*....|....*.
gi 1039022228 721 DFFEKSGMDPDYWNMFSNEGLQRINE 746
Cdd:cd03807 321 DAIRALLEDPEKRARLGRAARERIAN 346
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
618-730 |
2.04e-11 |
|
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: 66.58 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 618 ISEIKKMHSLIEKYQLKGQFRWITAQTDRTRNGELYRSIADTR----GAFVQ---PAHY-------------EAFGLTVI 677
Cdd:cd03823 200 LTEEKGIDLLVEAFKRLPREDIELVIAGHGPLSDERQIEGGRRiaflGRVPTddiKDFYekidvlvvpsiwpEPFGLVVR 279
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1039022228 678 EAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSDKIADFFEKSGMDP 730
Cdd:cd03823 280 EAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLE 332
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
415-751 |
5.08e-11 |
|
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: 64.95 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 415 VASLMANKLG-----ITQATIAHALEKTKYE-DSDIKWKE--------FDPKYHFSSQFTA--DLISMNSADFIIAS--- 475
Cdd:cd03820 18 VAINLANHLAkkgydVTIISLDSAEKPPFYElDDNIKIKNlgdrkyshFKLLLKYFKKVRRlrKYLKNNKPDVVISFrts 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 476 --TYQEIAGSKERAGQYEsHMSftvpglYRVVSGINVFDPRFNIAAPGADDsiyfpFTAQdrrftkfyTSIDELLYSQSE 553
Cdd:cd03820 98 llTFLALIGLKSKLIVWE-HNN------YEAYNKGLRRLLLRRLLYKRADK-----IVVL--------TEADKLKKYKQP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 554 N-----------DEHIGYLVDKKKPIIFSMARLDVVKNLTGLTEWYAKNKRLRDLVNLVIVGgffdaskskDREEISEIK 622
Cdd:cd03820 158 NsnvvvipnplsFPSEEPSTNLKSKRILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYG---------DGPEREELE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 623 KmhsLIEKYQLKGQFRWITaqtdRTRN-GELYRSIAdtrgAFVQPAHYEAFGLTVIEAMSCGL--VTFATNqGGPAEIIV 699
Cdd:cd03820 229 K---LIDKLGLEDRVKLLG----PTKNiAEEYANSS----IFVLSSRYEGFPMVLLEAMAYGLpiISFDCP-TGPSEIIE 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1039022228 700 DGVSGFHIDPSNGEESSDKIADFFEksgmDPDYWNMFSNEGLQRInECYTWK 751
Cdd:cd03820 297 DGENGLLVPNGDVDALAEALLRLME----DEELRKKMGKNARKNA-ERFSIE 343
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
530-746 |
1.01e-10 |
|
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: 64.53 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 530 FTAQ--DRRFTKFYTSIDELLY---------SQSENDEHIGYLVDKKKPIIFSMARLDVVKNLTGLTEWYAK---NKRLR 595
Cdd:cd03805 164 FTAGvfKKTFPSLAKNPPEVLYpcvdtdsfdSTSEDPDPGDLIAKSNKKFFLSINRFERKKNIALAIEAFAKlkqKLPEF 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 596 DLVNLVIVGGFfDASKSKDREEISEIKkmhSLIEKYQ-LKGQFRWITAQTDRTRNgELYRSiadTRGAFVQPAHyEAFGL 674
Cdd:cd03805 244 ENVRLVIAGGY-DPRVAENVEYLEELQ---RLAEELLnVEDQVLFLRSISDSQKE-QLLSS---ALALLYTPSN-EHFGI 314
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039022228 675 TVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPsNGEESSDKIADFFEksgmDPDYWNMFSNEGLQRINE 746
Cdd:cd03805 315 VPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEP-TPEAFAEAMLKLAN----DPDLADRMGAAGRKRVKE 381
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
571-707 |
1.14e-10 |
|
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: 62.42 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 571 SMARLDVVKNLTGLTEWYAKNKRLRDLVNLVIVGGffdaskSKDREEISEikkmhsLIEKYQLKGQFRWITAQTDRTRNg 650
Cdd:cd01635 115 SVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGG------GGEREEEEA------LAAALGLLERVVIIGGLVDDEVL- 181
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039022228 651 ELYRSIADtrgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHI 707
Cdd:cd01635 182 ELLLAAAD---VFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
563-743 |
4.12e-10 |
|
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: 62.30 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 563 DKKKPIIFSMARLDVVKNLTGLTEWYAKNKRLRDlVNLVIVGgffdasKSKDREEISEIKKMHSLIEKYQLKGqfrWIta 642
Cdd:cd03817 198 PPDEPILLYVGRLAKEKNIDFLLRAFAELKKEPN-IKLVIVG------DGPEREELKELARELGLADKVIFTG---FV-- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 643 qtDRTRNGELYRsIADtrgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEessdkIADF 722
Cdd:cd03817 266 --PREELPEYYK-AAD---LFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPNDET-----LAEK 334
|
170 180
....*....|....*....|.
gi 1039022228 723 FEKSGMDPDYWNMFSNEGLQR 743
Cdd:cd03817 335 LLHLRENLELLRKLSKNAEIS 355
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
669-709 |
1.18e-09 |
|
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: 60.76 E-value: 1.18e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1039022228 669 YEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDP 709
Cdd:cd03802 250 DEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVDS 290
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
561-724 |
4.60e-09 |
|
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: 59.23 E-value: 4.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 561 LVDKKKPIIFSMARLDVVKNLTGLTEWYAKNKRLRDlVNLVIVGGffdaskSKDREEISEIK-KMHSLIEKyqlkgqfrw 639
Cdd:cd03814 193 LGPPGRPLLLYVGRLAPEKNLEALLDADLPLAASPP-VRLVVVGD------GPARAELEARGpDVIFTGFL--------- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 640 itaqtDRTRNGELYRSiADtrgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSDKI 719
Cdd:cd03814 257 -----TGEELARAYAS-AD---VFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAAL 327
|
....*
gi 1039022228 720 ADFFE 724
Cdd:cd03814 328 RALLE 332
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
551-719 |
1.13e-08 |
|
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: 57.75 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 551 QSENDEHIGYLVDKKKPIIFSMARLDVVKNLTGLTEWYAKNKRLRDLVnLVIVGgffDASkskDREEiseikkMHSLIEK 630
Cdd:cd03819 167 EAEAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDEPDFR-LLVAG---DGP---ERDE------IRRLVER 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 631 YQLKGQFRwITAQTDRTRNgelYRSIADTrgaFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPS 710
Cdd:cd03819 234 LGLRDRVT-FTGFREDVPA---ALAASDV---VVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPG 306
|
....*....
gi 1039022228 711 NGEESSDKI 719
Cdd:cd03819 307 DAEALADAI 315
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
562-756 |
2.20e-08 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 57.11 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 562 VDKKKPIIFSMARLDVVKNLTGLTEWYAKNKRLRDLVNLVIVGGFFDASKSkdrEEISEIKKMHSLIEkyQLKGQFRWIT 641
Cdd:PRK15484 189 ISPDETVLLYAGRISPDKGILLLMQAFEKLATAHSNLKLVVVGDPTASSKG---EKAAYQKKVLEAAK--RIGDRCIMLG 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 642 AQT-DRTRNgelYRSIADTrgaFVQPAHY-EAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHI-DPSngeeSSDK 718
Cdd:PRK15484 264 GQPpEKMHN---YYPLADL---VVVPSQVeEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGYHLaEPM----TSDS 333
|
170 180 190
....*....|....*....|....*....|....*...
gi 1039022228 719 IADFFEKSGMDPDYWNMfSNEGLQRINECYTWKIYANK 756
Cdd:PRK15484 334 IISDINRTLADPELTQI-AEQAKDFVFSKYSWEGVTQR 370
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
651-759 |
2.27e-08 |
|
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: 56.96 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 651 ELYRSiADtrgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSDKIADFFeksgMDP 730
Cdd:cd03825 259 DIYSA-AD---LFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLL----ANP 330
|
90 100
....*....|....*....|....*....
gi 1039022228 731 DYWNMFSNEGLQRINECYTWKIYANKVIN 759
Cdd:cd03825 331 KERESLGERARALAENHFDQRVQAQRYLE 359
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
568-738 |
2.60e-08 |
|
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: 56.68 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 568 IIFSMARLDVVKNLTGLTEWYAKNKRLRDLVNLVIVGgffdasKSKDREEISEIKKMHSLIEKYQLKGQFRwitaqtdrt 647
Cdd:cd04951 190 VILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAG------DGPLRNELERLICNLNLVDRVILLGQIS--------- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 648 rNGELYRSIADTrgaFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDgvSGFHIDPSNGEESSDKIADFFEksg 727
Cdd:cd04951 255 -NISEYYNAADL---FVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGD--HNYVVPVSDPQLLAEKIKEIFD--- 325
|
170
....*....|.
gi 1039022228 728 MDPDYWNMFSN 738
Cdd:cd04951 326 MSDEERDILGN 336
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
543-749 |
8.41e-08 |
|
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.
Pssm-ID: 340826 [Multi-domain] Cd Length: 355 Bit Score: 54.97 E-value: 8.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 543 SIDELLYSQSENDEHIGYLVDKKKPIIFSMARLDVVKNLTGLTEWYAKNKrlrdlVNLVIVGgffdaskskdreEISEIK 622
Cdd:cd03795 168 GIDKNVYNIPRVDFENIKREKKGKKIFLFIGRLVYYKGLDYLIEAAQYLN-----YPIVIGG------------EGPLKP 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 623 KMHSLIEKyQLKGQFRWITAQTDRTRNgeLYRSIADtrgAFVQPAHY--EAFGLTVIEAMSCGLVTFATNQGGPAEIIV- 699
Cdd:cd03795 231 DLEAQIEL-NLLDNVKFLGRVDDEEKV--IYLHLCD---VFVFPSVLrsEAFGIVLLEAMMCGKPVISTNIGTGVPYVNn 304
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1039022228 700 DGVSGFHIDPSNGEESSDKIaDFFEKsgmDPDYWNMFSNEGLQRINECYT 749
Cdd:cd03795 305 NGETGLVVPPKDPDALAEAI-DKLLS---DEELRESYGENAKKRFEELFT 350
|
|
| GT4_GtfA-like |
cd04949 |
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ... |
530-739 |
1.02e-07 |
|
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: 54.61 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 530 FTAQDRRFTKFYTSIDELLYSQSENDehigylvdKKKPIIFSMARLDVVKNLTGLTEWYAKNKRLRDLVNLVIVGgfFDA 609
Cdd:cd04949 132 FNKYPPIFTIPVGYVDQLDTAESNHE--------RKSNKIITISRLAPEKQLDHLIEAVAKAVKKVPEITLDIYG--YGE 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 610 SKSKDREEISEIKkmhslIEKY-QLKGQfrwitaqtdrTRNgelYRSIADTRGAFVQPAHYEAFGLTVIEAMS--CGLVT 686
Cdd:cd04949 202 EREKLKKLIEELH-----LEDNvFLKGY----------HSN---LDQEYQDAYLSLLTSQMEGFGLTLMEAIGhgLPVVS 263
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039022228 687 FATNQgGPAEIIVDGVSGFHIDPSNGEESSDKIADFFEksgmDPDYWNMFSNE 739
Cdd:cd04949 264 YDVKY-GPSELIEDGENGYLIEKNNIDALADKIIELLN----DPEKLQQFSEE 311
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
566-759 |
1.30e-07 |
|
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: 54.68 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 566 KPIIFSMARLDVVKNLTGLTEWYAKNKRLRDLVNLVIVGgffdaskskdREEISEIKKMHsLIEKYQLKGQFRWITAQTD 645
Cdd:cd03821 204 RRIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAG----------PDDGAYPAFLQ-LQSSLGLGDRVTFTGPLYG 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 646 RTRnGELYRSiADtrgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGvSGFHIDPsNGEESSDKIADFFEK 725
Cdd:cd03821 273 EAK-WALYAS-AD---LFVLPSYSENFGNVVAEALACGLPVVITDKCGLSELVEAG-CGVVVDP-NVSSLAEALAEALRD 345
|
170 180 190
....*....|....*....|....*....|....
gi 1039022228 726 SGmDPDYWNMfSNEGLQRINECYTWKIYANKVIN 759
Cdd:cd03821 346 PA-DRKRLGE-MARRARQVEENFSWEAVAGQLGE 377
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
666-758 |
3.64e-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: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 666 PAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEEssdkIADFFEKSGMDPDYWNMFSNEGLQRIN 745
Cdd:cd03794 303 PANRGSSPSKLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEA----LADAILELLDDPELRRAMGENGRELAE 378
|
90
....*....|...
gi 1039022228 746 ECYTWKIYANKVI 758
Cdd:cd03794 379 EKFSREKLADRLL 391
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
670-749 |
4.53e-06 |
|
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: 50.03 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 670 EAFGLTVIEAMSCGLVTFATNQGGPAEIIVD-----GVSGFHIDPSNGEessdKIADFFEKSGMDPDYWNMFSNEGLQRI 744
Cdd:cd03813 381 EGQPLVILEAMASGVPVVATDVGSCRELIYGaddalGQAGLVVPPADPE----ALAEALIKLLRDPELRQAFGEAGRKRV 456
|
....*
gi 1039022228 745 NECYT 749
Cdd:cd03813 457 EKYYT 461
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
662-726 |
5.25e-06 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 49.32 E-value: 5.25e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039022228 662 AFVQPAHYEAFGLTVIEAMSCGLVTFATN-QGGPAEIIVDGVSGFHIDPSNGEESSDKIADFFEKS 726
Cdd:PRK09922 260 ALLLTSKFEGFPMTLLEAMSYGIPCISSDcMSGPRDIIKPGLNGELYTPGNIDEFVGKLNKVISGE 325
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
598-750 |
2.25e-04 |
|
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.
Pssm-ID: 340827 [Multi-domain] Cd Length: 398 Bit Score: 44.54 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 598 VNLVIVGgffDASKSKDREEIseikkmhslIEKYQLKGQFRWITA-QTDRTRN----GELYRSIADTrgafvqpahyEAF 672
Cdd:cd03796 225 VRFIIGG---DGPKRIELEEM---------REKYQLQDRVELLGAvPHEEVRDvlvqGHIFLNTSLT----------EAF 282
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039022228 673 GLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGF-HIDPSNGEESSDKIADFFEKSGMDPdyWNMFsneglQRINECYTW 750
Cdd:cd03796 283 CIAIVEAASCGLLVVSTRVGGIPEVLPPDMILLaEPDPEDIVRKLEEAISILRTGKHDP--WSFH-----NRVKKMYSW 354
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
566-778 |
2.83e-04 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 44.32 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 566 KPIIFSMARLDVVKNLTGLTEWYAKNKRlrdlVNLVIVGgffdaskskDREEISEIKKMhsliekyqLKGQFRWITAQTD 645
Cdd:PLN02871 263 KPLIVYVGRLGAEKNLDFLKRVMERLPG----ARLAFVG---------DGPYREELEKM--------FAGTPTVFTGMLQ 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 646 RTRNGELYRSiADTrgaFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVD---GVSGFHIDPSNGEESSDKIADF 722
Cdd:PLN02871 322 GDELSQAYAS-GDV---FVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIPPdqeGKTGFLYTPGDVDDCVEKLETL 397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039022228 723 FEksgmdpdywnmfSNEGLQRIN-------ECYTWKIYANKVINMGSTYSYWRHLNKDQKLAK 778
Cdd:PLN02871 398 LA------------DPELRERMGaaareevEKWDWRAATRKLRNEQYSAAIWFWRKKRAQLLG 448
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
544-793 |
8.19e-04 |
|
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: 42.66 E-value: 8.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 544 IDELLYSQSENDEHIGYLVDKKKPIIFSMARLDVVKNLTGLTEWYAKNKRLRDLVNLVIVGgffdasKSKDREEISEIKK 623
Cdd:cd03812 169 IEKYKFNKEKRRKRRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVG------EGELKEKIKEKVK 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 624 MHSLIEKYQLKGQfrwitaqtdRTRNGELYrSIADTrgaFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVS 703
Cdd:cd03812 243 ELGLEDKVIFLGF---------RNDVSEIL-SAMDV---FLFPSLYEGLPLVAVEAQASGLPCLLSDTITKECDITNNVE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039022228 704 GFHIDPSngeessdkiadffeksgmdPDYWnmfsneglqrinecytwkiyANKVINMgstYSYWRHLNKDQKLAKQRYIH 783
Cdd:cd03812 310 FLPLNET-------------------PSTW--------------------AEKILKL---IKRKRRINKEINKEKKELGY 347
|
250
....*....|
gi 1039022228 784 SFYNLQYRNL 793
Cdd:cd03812 348 DDESLELTLL 357
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
662-725 |
8.20e-04 |
|
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: 42.66 E-value: 8.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039022228 662 AFVQPAHyEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNgEESSDKIADFFEK 725
Cdd:cd03804 268 AFVFAAE-EDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQT-VESLKAAVEEFEQ 329
|
|
| GT4_ALG11-like |
cd03806 |
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ... |
668-724 |
8.58e-04 |
|
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: 42.60 E-value: 8.58e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039022228 668 HYEAFGLTVIEAMSCGLVTFATNQGGPAEIIV----DGVSGFHidPSNGEESSDKIADFFE 724
Cdd:cd03806 333 WNEHFGIGVVEYMAAGLIPLAHASAGPLLDIVvpwdGGPTGFL--ASTPEEYAEAIEKILT 391
|
|
| |
