|
Name |
Accession |
Description |
Interval |
E-value |
| glgA |
PRK00654 |
glycogen synthase GlgA; |
1-476 |
0e+00 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 747.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 1 MQVLHVCSEMFPLLKTGGLADVIGALPAAQIADGVDARVLLPAFPDIRRGVTDAQVVSRRDTFaghiTLLFGHYNGVGI- 79
Cdd:PRK00654 1 MKILFVASECAPLIKTGGLGDVVGALPKALAALGHDVRVLLPGYPAIREKLRDAQVVGRLDLF----TVLFGHLEGDGVp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 80 -YLIDAPHLYDRPGspyhdtnLFAYTDNVLRFALLGWVGAEMASGLDpfWRPDVVHAHDWHAGLAPAYLA---ARGRP-A 154
Cdd:PRK00654 77 vYLIDAPHLFDRPS-------GYGYPDNGERFAFFSWAAAEFAEGLD--PRPDIVHAHDWHTGLIPALLKekyWRGYPdI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 155 KSVFTVHNLAYQGMFYAHHMNDIQLPWSFFNIHGLEFNGQISFLKAGLYYADHITAVSPTYAREITEPQFAYGMEGLLQQ 234
Cdd:PRK00654 148 KTVFTIHNLAYQGLFPAEILGELGLPAEAFHLEGLEFYGQISFLKAGLYYADRVTTVSPTYAREITTPEFGYGLEGLLRA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 235 RHreGRLSGVLNGVDEKIWSPETDLLLASRYTRDTLEDKAENKRQLQIAMGLKVDDkVPLFAVVSRLTSQKGLDLVLEAL 314
Cdd:PRK00654 228 RS--GKLSGILNGIDYDIWNPETDPLLAANYSADDLEGKAENKRALQERFGLPDDD-APLFAMVSRLTEQKGLDLVLEAL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 315 PGLLEQGGQLALLGAGDPVLQEGFLAAAAEYPGQVGVQIGYHEAFSHRIMGGADVILVPSRFAPCGLTQLYGLKYGTLPL 394
Cdd:PRK00654 305 PELLEQGGQLVLLGTGDPELEEAFRALAARYPGKVGVQIGYDEALAHRIYAGADMFLMPSRFEPCGLTQLYALRYGTLPI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 395 VRRTGGLADTVSDCsleNLADGVASGFVFEDSNAWSLLRAIRRAFVLWSRPSLWRFVQRQAMAMDFSWQVAAKSYRELYY 474
Cdd:PRK00654 385 VRRTGGLADTVIDY---NPEDGEATGFVFDDFNAEDLLRALRRALELYRQPPLWRALQRQAMAQDFSWDKSAEEYLELYR 461
|
..
3COP_A 475 RL 476
Cdd:PRK00654 462 RL 463
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
1-476 |
0e+00 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 703.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 1 MQVLHVCSEMFPLLKTGGLADVIGALPAAQIADGVDARVLLPAFPDIRRGVTDAQVVSRRDTFAG----HITLLFGHYNG 76
Cdd:COG0297 1 MKILFVASEAAPFAKTGGLADVVGALPKALAKLGHDVRVVLPGYPSIDDKLKDLEVVASLEVPLGgrtyYARVLEGPDDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 77 VGIYLIDAPHLYDRPGsPYHDTNlFAYTDNVLRFALLGWVGAEMASGLDpfWRPDVVHAHDWHAGLAPAYLAARGR---- 152
Cdd:COG0297 81 VPVYFIDNPELFDRPG-PYGDPD-RDYPDNAERFAFFSRAALELLKGLD--WKPDIIHCHDWQTGLIPALLKTRYAddpf 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 153 -PAKSVFTVHNLAYQGMFYAHHMNDIQLPWSFFNIHGLEFNGQISFLKAGLYYADHITAVSPTYAREITEPQFAYGMEGL 231
Cdd:COG0297 157 kRIKTVFTIHNLAYQGIFPAEILELLGLPPELFTPDGLEFYGQINFLKAGIVYADRVTTVSPTYAREIQTPEFGEGLDGL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 232 LqqRHREGRLSGVLNGVDEKIWSPETDLLLASRYTRDTLEDKAENKRQLQIAMGLKVDDKVPLFAVVSRLTSQKGLDLVL 311
Cdd:COG0297 237 L--RARSGKLSGILNGIDYDVWNPATDPYLPANYSADDLEGKAANKAALQEELGLPVDPDAPLIGMVSRLTEQKGLDLLL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 312 EALPGLLEQGGQLALLGAGDPVLQEGFLAAAAEYPGQVGVQIGYHEAFSHRIMGGADVILVPSRFAPCGLTQLYGLKYGT 391
Cdd:COG0297 315 EALDELLEEDVQLVVLGSGDPEYEEAFRELAARYPGRVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQMYALRYGT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 392 LPLVRRTGGLADTVSDCsleNLADGVASGFVFEDSNAWSLLRAIRRAFVLWSRPSLWRFVQRQAMAMDFSWQVAAKSYRE 471
Cdd:COG0297 395 VPIVRRTGGLADTVIDY---NEATGEGTGFVFDEYTAEALLAAIRRALALYRDPEAWRKLQRNAMKQDFSWEKSAKEYLE 471
|
....*
3COP_A 472 LYYRL 476
Cdd:COG0297 472 LYREL 476
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
1-476 |
0e+00 |
|
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) synthases that use ADP-glucose (EC 2.4.1.21), rather than UDP-glucose (EC 2.4.1.11) as in animals, as the glucose donor. This enzyme is found in bacteria and plants. Whether the name given is glycogen synthase or starch synthase depends on context, and therefore on substrate. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
Pssm-ID: 273969 [Multi-domain] Cd Length: 473 Bit Score: 661.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 1 MQVLHVCSEMFPLLKTGGLADVIGALPAAQIADGVDARVLLPAFPDIRRGVTD-AQVVSRRDTFAGHITLLF----GHYN 75
Cdd:TIGR02095 1 MRVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEVDDqVKVVELVDLSVGPRTLYVkvfeGVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 76 GVGIYLIDAPHLYDRPGSPYHDtnlfAYTDNVLRFALLGWVGAEMASGLDpfWRPDVVHAHDWHAGLAPAYLAARGRP-- 153
Cdd:TIGR02095 81 GVPVYFIDNPSLFDRPGGIYGD----DYPDNAERFAFFSRAAAELLSGLG--WQPDVVHAHDWHTALVPALLKAVYRPnp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 154 AKSVFTVHNLAYQGMFYAHHMNDIQLPWSFFNIHGLEFNGQISFLKAGLYYADHITAVSPTYAREITEPQFAYGMEGLLQ 233
Cdd:TIGR02095 155 IKTVFTIHNLAYQGVFPADDFSELGLPPEYFHMEGLEFYGRVNFLKGGIVYADRVTTVSPTYAREILTPEFGYGLDGVLK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 234 QRhrEGRLSGVLNGVDEKIWSPETDLLLASRYTRDTLEDKAENKRQLQIAMGLKVDDKVPLFAVVSRLTSQKGLDLVLEA 313
Cdd:TIGR02095 235 AR--SGKLRGILNGIDTEVWNPATDPYLKANYSADDLAGKAENKEALQEELGLPVDDDVPLFGVISRLTQQKGVDLLLAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 314 LPGLLEQGGQLALLGAGDPVLQEGFLAAAAEYPGQVGVQIGYHEAFSHRIMGGADVILVPSRFAPCGLTQLYGLKYGTLP 393
Cdd:TIGR02095 313 LPELLELGGQLVVLGTGDPELEEALRELAERYPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQLYAMRYGTVP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 394 LVRRTGGLADTVSDCSLENladGVASGFVFEDSNAWSLLRAIRRAFVLW-SRPSLWRFVQRQAMAMDFSWQVAAKSYREL 472
Cdd:TIGR02095 393 IVRRTGGLADTVVDGDPEA---ESGTGFLFEEYDPGALLAALSRALRLYrQDPSLWEALQKNAMSQDFSWDKSAKQYVEL 469
|
....
3COP_A 473 YYRL 476
Cdd:TIGR02095 470 YRSL 473
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
2-475 |
0e+00 |
|
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.
Pssm-ID: 340822 [Multi-domain] Cd Length: 474 Bit Score: 647.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 2 QVLHVCSEMFPLLKTGGLADVIGALPAAQIADGVDARVLLPAFPDIRRGVTDAQVVSRRDTFAGH----ITLLFGHYNGV 77
Cdd:cd03791 1 KVLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRVLGLEVKVGGrgeeVGVFELPVDGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 78 GIYLIDAPHLYDRPGSPYhdTNLFAYTDNVLRFALLGWVGAEMASGLDpfWRPDVVHAHDWHAGLAPAYLAARGRP---- 153
Cdd:cd03791 81 DYYFLDNPEFFDRPGLPG--PPGYDYPDNAERFAFFSRAALELLRRLG--FQPDIIHANDWHTALVPAYLKTRYRGpgfk 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 154 -AKSVFTVHNLAYQGMFYAHHMNDIQLPWSFFNIHGLEFNGQISFLKAGLYYADHITAVSPTYAREITEPQFAYGMEGLL 232
Cdd:cd03791 157 kIKTVFTIHNLAYQGLFPLDTLAELGLPPELFHIDGLEFYGQINFLKAGIVYADRVTTVSPTYAKEILTPEYGEGLDGVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 233 qqRHREGRLSGVLNGVDEKIWSPETDLLLASRYTRDTLEDKAENKRQLQIAMGLKVDDKVPLFAVVSRLTSQKGLDLVLE 312
Cdd:cd03791 237 --RARAGKLSGILNGIDYDEWNPATDKLIPANYSANDLEGKAENKAALQKELGLPVDPDAPLFGFVGRLTEQKGVDLILD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 313 ALPGLLEQGGQLALLGAGDPVLQEGFLAAAAEYPGQVGVQIGYHEAFSHRIMGGADVILVPSRFAPCGLTQLYGLKYGTL 392
Cdd:cd03791 315 ALPELLEEGGQLVVLGSGDPEYEQAFRELAERYPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYAMRYGTL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 393 PLVRRTGGLADTVSDcslENLADGVASGFVFEDSNAWSLLRAIRRAFVLWSRPSLWRFVQRQAMAMDFSWQVAAKSYREL 472
Cdd:cd03791 395 PIVRRTGGLADTVFD---YDPETGEGTGFVFEDYDAEALLAALRRALALYRNPELWRKLQKNAMKQDFSWDKSAKEYLEL 471
|
...
3COP_A 473 YYR 475
Cdd:cd03791 472 YRS 474
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
1-476 |
0e+00 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 555.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 1 MQVLHVCSEMFPLLKTGGLADVIGALPAAQIADGVDARVLLPAFPDIRRGVTDAQVVSR-RDTFAGHITLLFGHYNGVGI 79
Cdd:PRK14099 4 LRVLSVASEIFPLIKTGGLADVAGALPAALKAHGVEVRTLVPGYPAVLAGIEDAEQVHSfPDLFGGPARLLAARAGGLDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 80 YLIDAPHLYDRPGSPYHDTNLFAYTDNVLRFALLGWVGAEMASGLDPFWRPDVVHAHDWHAGLAPAYLAARGRPA-KSVF 158
Cdd:PRK14099 84 FVLDAPHLYDRPGNPYVGPDGKDWPDNAQRFAALARAAAAIGQGLVPGFVPDIVHAHDWQAGLAPAYLHYSGRPApGTVF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 159 TVHNLAYQGMFYAHHMNDIQLPWSFFNIHGLEFNGQISFLKAGLYYADHITAVSPTYAREITEPQFAYGMEGLLQQRhrE 238
Cdd:PRK14099 164 TIHNLAFQGQFPRELLGALGLPPSAFSLDGVEYYGGIGYLKAGLQLADRITTVSPTYALEIQGPEAGMGLDGLLRQR--A 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 239 GRLSGVLNGVDEKIWSPETDLLLASRYTRDTLEDKAENKRQLQIAMGLKVDDKVPLFAVVSRLTSQKGLDLVLEALPGLL 318
Cdd:PRK14099 242 DRLSGILNGIDTAVWNPATDELIAATYDVETLAARAANKAALQARFGLDPDPDALLLGVISRLSWQKGLDLLLEALPTLL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 319 EQGGQLALLGAGDPVLQEGFLAAAAEYPGQVGVQIGYHEAFSHRIMGGADVILVPSRFAPCGLTQLYGLKYGTLPLVRRT 398
Cdd:PRK14099 322 GEGAQLALLGSGDAELEARFRAAAQAYPGQIGVVIGYDEALAHLIQAGADALLVPSRFEPCGLTQLCALRYGAVPVVARV 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3COP_A 399 GGLADTVSDCSLENLADGVASGFVFEDSNAWSLLRAIRRAFVLWSRPSLWRFVQRQAMAMDFSWQVAAKSYRELYYRL 476
Cdd:PRK14099 402 GGLADTVVDANEMAIATGVATGVQFSPVTADALAAALRKTAALFADPVAWRRLQRNGMTTDVSWRNPAQHYAALYRSL 479
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
3-234 |
5.93e-98 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 294.62 E-value: 5.93e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 3 VLHVCSEMFPLLKTGGLADVIGALPAAQIADGVDARVLLPAFPDIRRGVTDAQVVSRRDTFAG------HITLLFGHYNG 76
Cdd:pfam08323 1 ILFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGNIPEERNQLEDVIRLSVAAGvpvrplTVGVARLELDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 77 VGIYLIDAPHLYDRPGsPYHDTNlFAYTDNVLRFALLGWVGAEMASGLDpfWRPDVVHAHDWHAGLAPAYLAARGRP--- 153
Cdd:pfam08323 81 VDVYFLDNPDYFDRPG-LYGDDG-RDYEDNAERFAFFSRAALELAKKLG--WIPDIIHCHDWHTALVPAYLKEAYADdpf 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 154 --AKSVFTVHNLAYQGMFYAHHMNDIQLPWSFFNIHGLEFNGQISFLKAGLYYADHITAVSPTYAREITEPQFAYGMEGL 231
Cdd:pfam08323 157 knIKTVFTIHNLAYQGRFPADLLDLLGLPPEDFNLDGLEFYGQINFLKAGIVYADAVTTVSPTYAEEIQTPEFGGGLDGL 236
|
...
3COP_A 232 LQQ 234
Cdd:pfam08323 237 LRE 239
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
2-476 |
3.61e-81 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 260.05 E-value: 3.61e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 2 QVLHVCSEMFPLLKTGGLADVIGALPAAQIADGVDARVLLPAFP----------DIRRgVTDAQVVSRRDTFAGHITLLF 71
Cdd:PRK14098 7 KVLYVSGEVSPFVRVSALADFMASFPQALEEEGFEARIMMPKYGtindrkfrlhDVLR-LSDIEVPLKEKTDLLHVKVTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 72 GHYNGVGIYLIDAPHLYDRPG---SPYHDTNLFAYTDNVLRFAllgwVGAeMASGLDPFWRPDVVHAHDWHAGLAPAYLA 148
Cdd:PRK14098 86 LPSSKIQTYFLYNEKYFKRNGlftDMSLGGDLKGSAEKVIFFN----VGV-LETLQRLGWKPDIIHCHDWYAGLVPLLLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 149 ARG------RPAKSVFTVHNLAYQGMFYAHHMNDIqLPWSFFNihGLEF-NGQISFLKAGLYYADHITAVSPTYAREIT- 220
Cdd:PRK14098 161 TVYadheffKDIKTVLTIHNVYRQGVLPFKVFQKL-LPEEVCS--GLHReGDEVNMLYTGVEHADLLTTTSPRYAEEIAg 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 221 EPQFAYGMEGLLQQRhrEGRLSGVLNGVDEKIWSPETDLLLASRYTRDTLEDKAENKRQLQIAMGLKVDDKVPLFAVVSR 300
Cdd:PRK14098 238 DGEEAFGLDKVLEER--KMRLHGILNGIDTRQWNPSTDKLIKKRYSIERLDGKLENKKALLEEVGLPFDEETPLVGVIIN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 301 LTSQKGLDLVLEALPGLLEQGGQLALLGAGDPVLQEGFLAAAAEYPGQVGVQIGYHEAFSHRIMGGADVILVPSRFAPCG 380
Cdd:PRK14098 316 FDDFQGAELLAESLEKLVELDIQLVICGSGDKEYEKRFQDFAEEHPEQVSVQTEFTDAFFHLAIAGLDMLLMPGKIESCG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 381 LTQLYGLKYGTLPLVRRTGGLADTVsdcslENLADGVASGFVFEDSNAWSLLRAIRRAFVLWSRPSLWRFVQRQAMAMDF 460
Cdd:PRK14098 396 MLQMFAMSYGTIPVAYAGGGIVETI-----EEVSEDKGSGFIFHDYTPEALVAKLGEALALYHDEERWEELVLEAMERDF 470
|
490
....*....|....*.
3COP_A 461 SWQVAAKSYRELYYRL 476
Cdd:PRK14098 471 SWKNSAEEYAQLYREL 486
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1-475 |
7.83e-75 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 253.67 E-value: 7.83e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 1 MQVLHVCSEMFPLLKTGGLADVIGALPAAQIADGVDARVLLPAFP--------DIRrgVTDAQVVSRRD--TFAGHITLl 70
Cdd:PLN02939 482 LHIVHIAAEMAPVAKVGGLADVVSGLGKALQKKGHLVEIVLPKYDcmqydqirNLK--VLDVVVESYFDgnLFKNKIWT- 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 71 fGHYNGVGIYLIDAPHlydrPGSPYHDTNLFAYTDNVLRFALLGWVGAEM--ASGLdpfwRPDVVHAHDWH-AGLAPAY- 146
Cdd:PLN02939 559 -GTVEGLPVYFIEPQH----PSKFFWRAQYYGEHDDFKRFSYFSRAALELlyQSGK----KPDIIHCHDWQtAFVAPLYw 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 147 --LAARG-RPAKSVFTVHNLAYQGMFYAHHMNDIQLpwsffNIHGLE--------FNGQISFLKAGLYYADHITAVSPTY 215
Cdd:PLN02939 630 dlYAPKGfNSARICFTCHNFEYQGTAPASDLASCGL-----DVHQLDrpdrmqdnAHGRINVVKGAIVYSNIVTTVSPTY 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 216 AREItEPQFAYGMEGLLQQRHRegRLSGVLNGVDEKIWSPETDLLLASRYTRDTLEDKAENKRQLQIAMGL-KVDDKVPL 294
Cdd:PLN02939 705 AQEV-RSEGGRGLQDTLKFHSK--KFVGILNGIDTDTWNPSTDRFLKVQYNANDLQGKAANKAALRKQLGLsSADASQPL 781
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 295 FAVVSRLTSQKGLDLVLEALPGLLEQGGQLALLGAgDPV--LQEGFLAAAAEYPGQVGVQI--GYHEAFSHRIMGGADVI 370
Cdd:PLN02939 782 VGCITRLVPQKGVHLIRHAIYKTAELGGQFVLLGS-SPVphIQREFEGIADQFQSNNNIRLilKYDEALSHSIYAASDMF 860
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 371 LVPSRFAPCGLTQLYGLKYGTLPLVRRTGGLADTVSDCSLENLADGVASGFVFEDSNAWSLLRAIRRAFVLWSR-PSLWR 449
Cdd:PLN02939 861 IIPSMFEPCGLTQMIAMRYGSVPIVRKTGGLNDSVFDFDDETIPVELRNGFTFLTPDEQGLNSALERAFNYYKRkPEVWK 940
|
490 500
....*....|....*....|....*.
3COP_A 450 FVQRQAMAMDFSWQVAAKSYRELYYR 475
Cdd:PLN02939 941 QLVQKDMNIDFSWDSSASQYEELYQR 966
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1-474 |
1.56e-66 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 231.30 E-value: 1.56e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 1 MQVLHVCSEMFPLLKTGGLADVIGALPAAQIADGVDARVLLPAFPDIR-RGVTDAQvVSRRDTFAG-HITLLFGHYNGVG 78
Cdd:PLN02316 588 MHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHNVDIILPKYDCLNlSHVKDLH-YQRSYSWGGtEIKVWFGKVEGLS 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 79 IYLIDAPHLYDRPGSPY---HDTNLFA-YTDNVLRFALlgwvgaemASGldpfWRPDVVHAHDWHAglAPA-------YL 147
Cdd:PLN02316 667 VYFLEPQNGMFWAGCVYgcrNDGERFGfFCHAALEFLL--------QSG----FHPDIIHCHDWSS--APVawlfkdhYA 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 148 AARGRPAKSVFTVHNLAyqgmFYAHHMNdiqlpwsffnihglefngqisflKAgLYYADHITAVSPTYAREITepqfayG 227
Cdd:PLN02316 733 HYGLSKARVVFTIHNLE----FGANHIG-----------------------KA-MAYADKATTVSPTYSREVS------G 778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 228 MEGLLQQRHregRLSGVLNGVDEKIWSPETDLLLASRYTRD-TLEDKAENKRQLQIAMGLKVDDKvPLFAVVSRLTSQKG 306
Cdd:PLN02316 779 NSAIAPHLY---KFHGILNGIDPDIWDPYNDNFIPVPYTSEnVVEGKRAAKEALQQRLGLKQADL-PLVGIITRLTHQKG 854
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 307 LDLVLEALPGLLEQGGQLALLG-AGDPVLQEGFLAAA----AEYPGQVGVQIGYHEAFSHRIMGGADVILVPSRFAPCGL 381
Cdd:PLN02316 855 IHLIKHAIWRTLERNGQVVLLGsAPDPRIQNDFVNLAnqlhSSHHDRARLCLTYDEPLSHLIYAGADFILVPSIFEPCGL 934
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 382 TQLYGLKYGTLPLVRRTGGLADTVSDCSLEN---LADGV-ASGFVFEDSNAWSLLRAIRRAFVLWSRPSLW-RFVQRQAM 456
Cdd:PLN02316 935 TQLTAMRYGSIPVVRKTGGLFDTVFDVDHDKeraQAQGLePNGFSFDGADAAGVDYALNRAISAWYDGRDWfNSLCKRVM 1014
|
490
....*....|....*...
3COP_A 457 AMDFSWQVAAKSYRELYY 474
Cdd:PLN02316 1015 EQDWSWNRPALDYMELYH 1032
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
127-473 |
6.95e-22 |
|
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.
Pssm-ID: 340831 [Multi-domain] Cd Length: 366 Bit Score: 96.84 E-value: 6.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 127 FWRPDVVHAHDWHAGLApAYLAARGRPAKSVFTVHNLAYQGMFYAHHmndIQLPWsffnihglefngqISFLKAGLYYAD 206
Cdd:cd03801 80 LRKFDVVHAHGLLAALL-AALLALLLGAPLVVTLHGAEPGRLLLLLA---AERRL-------------LARAEALLRRAD 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 207 HITAVSPTYAREITEpqfAYGMEgllqqrhrEGRLSGVLNGVDEKIWSPETDLllasrytrdtledkaenkrqlqiamGL 286
Cdd:cd03801 143 AVIAVSEALRDELRA---LGGIP--------PEKIVVIPNGVDLERFSPPLRR-------------------------KL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 287 KVDDKVPLFAVVSRLTSQKGLDLVLEALPGLLEQGGQLALL--GAGDPVLQEgflAAAAEYPGQVGVQIGYHEAFS--HR 362
Cdd:cd03801 187 GIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVivGGDGPLRAE---LEELELGLGDRVRFLGFVPDEelPA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 363 IMGGADVILVPSRFAPCGLTQLYGLKYGTLPLVRRTGGLADTVSDcslenladgVASGFVFEDSNAWSLLRAIRRAfvLW 442
Cdd:cd03801 264 LYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVED---------GEGGLVVPPDDVEALADALLRL--LA 332
|
330 340 350
....*....|....*....|....*....|...
3COP_A 443 SRPSLWRFVQ--RQAMAMDFSWQVAAKSYRELY 473
Cdd:cd03801 333 DPELRARLGRaaRERVAERFSWERVAERLLDLY 365
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
291-438 |
1.07e-13 |
|
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: 68.45 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 291 KVPLFAVVSRLTSQKGLDLVLEALPGLLEQGGQLALLGAGDPVLQEGF--LAAAAEYPGQVGV--QIGYHEAfsHRIMGG 366
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLkkLAEKLGLGDNVIFlgFVSDEDL--PELLKI 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3COP_A 367 ADVILVPSRFAPCGLTQLYGLKYGTLPLVRRTGGLADTVsdcslenlADGVAsGFVFEDSNAWSLLRAIRRA 438
Cdd:pfam00534 79 ADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVV--------KDGET-GFLVKPNNAEALAEAIDKL 141
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
88-475 |
2.68e-13 |
|
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: 70.85 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 88 YDRPGSPYHDTNLFAYTDNVLRFALLGWVgaemasgldpfWRPDVVHAHDWHAGLApAYLAARGRPAKSVFTVHNLAYQG 167
Cdd:cd03819 46 QIGIGLPGLKVPLLRALLGNVRLARLIRR-----------ERIDLIHAHSRAPAWL-GWLASRLTGVPLVTTVHGSYLAT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 168 MFYAHHMNDIQlpwsffnihglefngqisflkaglYYADHITAVSPtYAREITEPQFAYGmegllqqrhrEGRLSGVLNG 247
Cdd:cd03819 114 YHPKDFALAVR------------------------ARGDRVIAVSE-LVRDHLIEALGVD----------PERIRVIPNG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 248 VDEKIWSPETdlllasrytrdtledKAENKRQLqiamglKVDDKVPLFAVVSRLTSQKGLDLVLEALPGLLEQGGQLALL 327
Cdd:cd03819 159 VDTDRFPPEA---------------EAEERAQL------GLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDEPDFRLLV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 328 gAGDPvLQEGFLAAAAEYPG---QVGVqIGYHEAfSHRIMGGADVILVPSRFAPCGLTQLYGLKYGTLPLVRRTGGLADT 404
Cdd:cd03819 218 -AGDG-PERDEIRRLVERLGlrdRVTF-TGFRED-VPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREI 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3COP_A 405 VSdcslenladGVASGFVFEDSNAWSLLRAIRRAFVLwsrPSLWRFVQRQAMamdfswqvAAKSYRELYYR 475
Cdd:cd03819 294 VV---------HGRTGLLVPPGDAEALADAIRAAKLL---PEAREKLQAAAA--------LTEAVRELLLR 344
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
363-476 |
1.26e-09 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 56.15 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 363 IMGGADVILVPSRFAPCGLTQLYGLKYGTLPLVRRTGGLADTVsdcslenlADGVAsGFVFEDSNAWSLLRAIRRafvLW 442
Cdd:COG0438 17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVI--------EDGET-GLLVPPGDPEALAEAILR---LL 84
|
90 100 110
....*....|....*....|....*....|....*..
3COP_A 443 SRPSLWRFVQ---RQAMAMDFSWQVAAKSYRELYYRL 476
Cdd:COG0438 85 EDPELRRRLGeaaRERAEERFSWEAIAERLLALYEEL 121
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
129-469 |
1.88e-09 |
|
sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.
Pssm-ID: 340830 [Multi-domain] Cd Length: 398 Bit Score: 59.56 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 129 RPDVVHAHDWHAGLApAYLAARGRPAKSVFTVHNLA---YQgmfyahHMNDIqlpWSFFnihgleFNGQISFLKAGLYYA 205
Cdd:cd03800 101 RYDLIHSHYWDSGLV-GALLARRLGVPLVHTFHSLGrvkYR------HLGAQ---DTYH------PSLRITAEEQILEAA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 206 DHITAvsptyareiTEPQFAYGMEGLLQQRhrEGRLSGVLNGVDEKIWSPEtdlllasrytrdtleDKAENKRqlqIAMG 285
Cdd:cd03800 165 DRVIA---------STPQEADELISLYGAD--PSRINVVPPGVDLERFFPV---------------DRAEARR---ARLL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 286 LKVDDKVPLFavVSRLTSQKGLDLVLEALpGLLEQGGQLALL----GAGDPVLQEGFLAAAA-----------EYPGQVG 350
Cdd:cd03800 216 LPPDKPVVLA--LGRLDPRKGIDTLVRAF-AQLPELRELANLvlvgGPSDDPLSMDREELAElaeelglidrvRFPGRVS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 351 vQIGYHEAFShrimgGADVILVPSRFAPCGLTQLYGLKYGTLPLVRRTGGLADTVSDCSlenladgvaSGFVFEDSNAWS 430
Cdd:cd03800 293 -RDDLPELYR-----AADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGR---------TGLLVDPHDPEA 357
|
330 340 350 360
....*....|....*....|....*....|....*....|..
3COP_A 431 LLRAIRRAFvlwSRPSLWRFVQRQAM---AMDFSWQVAAKSY 469
Cdd:cd03800 358 LAAALRRLL---DDPALWQRLSRAGLeraRAHYTWESVADQL 396
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
258-473 |
4.41e-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: 58.11 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 258 DLLLA-SRYTRDTLEDK-AENKRQLQIAMGLKVDDKVPL----------FAVVSRLTSQKGLDLVLEALPGLLEQGGQLA 325
Cdd:cd03823 145 DAVLApSRFTANLHEANgLFSARISVIPNAVEPDLAPPPrrrpgterlrFGYIGRLTEEKGIDLLVEAFKRLPREDIELV 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 326 LLGAGdPVLQEGFLAAaaeypgqvGVQIGYHEAFSH----RIMGGADVILVPSRFA-PCGLTQLYGLKYGTLPLVRRTGG 400
Cdd:cd03823 225 IAGHG-PLSDERQIEG--------GRRIAFLGRVPTddikDFYEKIDVLVVPSIWPePFGLVVREAIAAGLPVIASDLGG 295
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3COP_A 401 LADTVSDcslenladgVASGFVFEDSNAWSLLRAIRRafvLWSRPSLWRFVQRQAMAMDFSWQVAAKsYRELY 473
Cdd:cd03823 296 IAELIQP---------GVNGLLFAPGDAEDLAAAMRR---LLTDPALLERLRAGAEPPRSTESQAEE-YLKLY 355
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
128-476 |
6.62e-09 |
|
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: 57.77 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 128 WRPDVVHAH-DWHAGLAPAYLAAR-GRPAksVFTVHNlayqgmfyahhmNDIQ-LPWSffnihglefNGQISFLKAGLYY 204
Cdd:cd03798 94 GPPDLIHAHfAYPAGFAAALLARLyGVPY--VVTEHG------------SDINvFPPR---------SLLRKLLRWALRR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 205 ADHITAVSptyaREITEPQFAYGMegllqqrhREGRLSGVLNGVDEKIWSPETDlllasrytrdtledkaenkrqlqiam 284
Cdd:cd03798 151 AARVIAVS----KALAEELVALGV--------PRDRVDVIPNGVDPARFQPEDR-------------------------- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 285 GLKVDDKVPLFAVVSRLTSQKGLDLVLEALPGLLEQGGQLALLGAGDPVLQEgFLAAAAEYPGqVGVQIGYHEAFSH--- 361
Cdd:cd03798 193 GLGLPLDAFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVGDGPLRE-ALRALAEDLG-LGDRVTFTGRLPHeqv 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 362 -RIMGGADVILVPSRFAPCGLTQLYGLKYGTLPLVRRTGGLADTVsdcslenlaDGVASGFVFEDSNAWSLLRAIRRAFV 440
Cdd:cd03798 271 pAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVV---------GDPETGLLVPPGDADALAAALRRALA 341
|
330 340 350
....*....|....*....|....*....|....*.
3COP_A 441 LWSRPSLWRfVQRQAMAMDFSWQVAAKSYRELYYRL 476
Cdd:cd03798 342 EPYLRELGE-AARARVAERFSWVKAADRIAAAYRDV 376
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
297-407 |
1.65e-08 |
|
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340816 [Multi-domain] Cd Length: 235 Bit Score: 55.10 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 297 VVSRLTSQKGLDLVLEALPGLLEQGG--QLALLGAGDPVLQEGFLAAAAEYPGQVGVQIGY-HEAFSHRIMGGADVILVP 373
Cdd:cd01635 115 SVGRLVPEKGIDLLLEALALLKARLPdlVLVLVGGGGEREEEEALAAALGLLERVVIIGGLvDDEVLELLLAAADVFVLP 194
|
90 100 110
....*....|....*....|....*....|....
3COP_A 374 SRFAPCGLTQLYGLKYGTLPLVRRTGGLADTVSD 407
Cdd:cd01635 195 SRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVD 228
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
128-249 |
2.51e-08 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 53.31 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 128 WRPDVVHAHDWHAGLAPAYLAARGRPAKSVFTVHNLAYQGMFYAHHMNDIQLPWsffnihglefngqISFLKAGLYYADH 207
Cdd:pfam13439 70 ERPDVVHAHSPFPLGLAALAARLRLGIPLVVTYHGLFPDYKRLGARLSPLRRLL-------------RRLERRLLRRADR 136
|
90 100 110 120
....*....|....*....|....*....|....*....|..
3COP_A 208 ITAVSPTYAREITEpqfAYGMegllqqrhREGRLSGVLNGVD 249
Cdd:pfam13439 137 VIAVSEAVADELRR---LYGV--------PPEKIRVIPNGVD 167
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
127-330 |
4.77e-08 |
|
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: 54.98 E-value: 4.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 127 FWRPDVVHAHD-WHAGLApAYLAARGRPAKSVFTVHNLAYQgmfYAHHMNdiqLPWSFFNIHGlefngqISFLKAGLYYA 205
Cdd:cd03817 82 ELGPDIIHTHTpFSLGKL-GLRIARKLKIPIVHTYHTMYED---YLHYIP---KGKLLVKAVV------RKLVRRFYNHT 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 206 DHITAVSPTYAREitepqfaygmeglLQQRHREGRLSGVLNGVDEKIWSPetdlllasrytrdtlEDKAENKRQLQIamg 285
Cdd:cd03817 149 DAVIAPSEKIKDT-------------LREYGVKGPIEVIPNGIDLDKFEK---------------PLNTEERRKLGL--- 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
3COP_A 286 lkvDDKVPLFAVVSRLTSQKGLDLVLEALPGLL-EQGGQLALLGAG 330
Cdd:cd03817 198 ---PPDEPILLYVGRLAKEKNIDFLLRAFAELKkEPNIKLVIVGDG 240
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
17-221 |
6.52e-07 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 48.94 E-value: 6.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 17 GGLADVIGALPAAQIADGVDARVLLPAFPDIRRGVTDAqvvsrrdtfaghitllfghynGVGIYLIDAPHLYDRPGSPYH 96
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPELVGD---------------------GVRVHRLPVPPRPSPLADLAA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 97 dtnlfaytdnvlRFALLGWVGAemasgldpfWRPDVVHAHDWHAGLApAYLAARGRPAKSVFTVHNLAYQGmfyahhmnd 176
Cdd:pfam13579 60 ------------LRRLRRLLRA---------ERPDVVHAHSPTAGLA-ARLARRRRGVPLVVTVHGLALDY--------- 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
3COP_A 177 iQLPWSFFNIHGLEfngqisflKAGLYYADHITAVSPTYAREITE 221
Cdd:pfam13579 109 -GSGWKRRLARALE--------RRLLRRADAVVVVSEAEAELLRA 144
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
74-469 |
4.99e-05 |
|
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: 45.41 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 74 YNGVGIYLIDAPhlydrpgsPYHDTNLFAYTDNVLRFALLGWvgaemASGLDPFWRPDVVHAHDWHAGLA-PAYLAARGR 152
Cdd:cd03794 56 KDGIRVIRVKLG--------PIKKNGLIRRLLNYLSFALAAL-----LKLLVREERPDVIIAYSPPITLGlAALLLKKLR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 153 PAKSVFTVHNLAYQGMFyahHMNDIQLPWSFFNIHGLEfngqisflKAGLYYADHITAVSPTYAREItepqfaygmeglL 232
Cdd:cd03794 123 GAPFILDVRDLWPESLI---ALGVLKKGSLLKLLKKLE--------RKLYRLADAIIVLSPGLKEYL------------L 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 233 QQRHREGRLSGVLNGVDEKIWSPetdlllasrytrdtledkaeNKRQLQIAMGLKVDDKVPLFAVVsrLTSQKGLDLVLE 312
Cdd:cd03794 180 RKGVPKEKIIVIPNWADLEEFKP--------------------PPKDELRKKLGLDDKFVVVYAGN--IGKAQGLETLLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 313 ALPGLLEQGG-QLALLGAGDPVLQEGFLAAAAEYPGqvgvqIGYHEAFSHR----IMGGADVILVPSRFAPCGL----TQ 383
Cdd:cd03794 238 AAERLKRRPDiRFLFVGDGDEKERLKELAKARGLDN-----VTFLGRVPKEevpeLLSAADVGLVPLKDNPANRgsspSK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 384 LYG-LKYGtLPLVrrtgGLADTVSDcslENLADGVAsGFVFEDSNAWSLLRAIRRAfvLWSRpslwrfVQRQAMAM---- 458
Cdd:cd03794 313 LFEyMAAG-KPIL----ASDDGGSD---LAVEINGC-GLVVEPGDPEALADAILEL--LDDP------ELRRAMGEngre 375
|
410
....*....|....*
3COP_A 459 ----DFSWQVAAKSY 469
Cdd:cd03794 376 laeeKFSREKLADRL 390
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
293-437 |
9.84e-05 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 42.11 E-value: 9.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 293 PLFAVVSRLTS-QKGLDLVLEALPGLLEQGGQLALLGAGDPVLQEgFLAAAAEYPGQVgVQIGYHEAFsHRIMGGADVIL 371
Cdd:pfam13692 2 PVILFVGRLHPnVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEE-LEELAAGLEDRV-IFTGFVEDL-AELLAAADVFV 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
3COP_A 372 VPSRFAPCGLTQLYGLKYGtLPLV-RRTGGLADTVsdcslenlaDGVAsGFVFEDSNAWSLLRAIRR 437
Cdd:pfam13692 79 LPSLYEGFGLKLLEAMAAG-LPVVaTDVGGIPELV---------DGEN-GLLVPPGDPEALAEAILR 134
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
3-471 |
7.05e-04 |
|
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: 41.97 E-value: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 3 VLHVCSEMFPllKTGGLADVIGALPAAQIADGVDARVLLPAfPDIRRGVTDAQVVSRRDTFAGHITLLFGHYNGVGIYli 82
Cdd:cd03821 2 ILHVTPSISP--KAGGPVKVVLRLAAALAALGHEVTIVSTG-DGYESLVVEENGRYIPPQDGFASIPLLRQGAGRTDF-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 83 daphlydrpgspyhdtnlfaytdnvlRFALLGWVGAEMAsgldpfwRPDVVHAHD-WHAGLAPAYLAARGRPAKSVFTVH 161
Cdd:cd03821 77 --------------------------SPGLPNWLRRNLR-------EYDVVHIHGvWTYTSLAACKLARRRGIPYVVSPH 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 162 nlayqGMFyahhmndiqLPWSFFNIHGLEFNGQISFLKAGLYYADHITAVSPTYAREITEPQFaygmegllqqrhrEGRL 241
Cdd:cd03821 124 -----GML---------DPWALQQKHWKKRIALHLIERRNLNNAALVHFTSEQEADELRRFGL-------------EPPI 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 242 SGVLNGVDEKIWSPEtdllLASRYTRDTLEDKaenkrqlqiamglkvddKVPLFavVSRLTSQKGLDLVLEALPGLLEQG 321
Cdd:cd03821 177 AVIPNGVDIPEFDPG----LRDRRKHNGLEDR-----------------RIILF--LGRIHPKKGLDLLIRAARKLAEQG 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 322 GQLALLGAG-DPVLQEGFLAAAAEYPGQVGVQIG---YHEAFShRIMGGADVILVPSRFAPCGLTQLYGLKYGtLPLVrr 397
Cdd:cd03821 234 RDWHLVIAGpDDGAYPAFLQLQSSLGLGDRVTFTgplYGEAKW-ALYASADLFVLPSYSENFGNVVAEALACG-LPVV-- 309
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
3COP_A 398 tggladTVSDCSLENLADGVASGFVfeDSNAWSLLRAIRRAFVLWSRPSLWRFVQRQAMAMD--FSWQVAAKSYRE 471
Cdd:cd03821 310 ------ITDKCGLSELVEAGCGVVV--DPNVSSLAEALAEALRDPADRKRLGEMARRARQVEenFSWEAVAGQLGE 377
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
293-476 |
7.46e-04 |
|
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: 41.90 E-value: 7.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 293 PLFAVVSRLTSQKGLDLVLEA-LPGLLEQGGQLALLGAG--DPVLQEGFLAAaaeypgqvgVQIGYH--EAFShRIMGGA 367
Cdd:cd03814 199 PLLLYVGRLAPEKNLEALLDAdLPLAASPPVRLVVVGDGpaRAELEARGPDV---------IFTGFLtgEELA-RAYASA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 368 DVILVPSRFAPCGLTQLYGLKYGtLPLV-RRTGGLADTVSDCslenladgvASGFVFEDSNAWSLLRAIRRafvLWSRPS 446
Cdd:cd03814 269 DVFVFPSRTETFGLVVLEAMASG-LPVVaADAGGPRDIVRPG---------GTGALVEPGDAAAFAAALRA---LLEDPE 335
|
170 180 190
....*....|....*....|....*....|
3COP_A 447 LwrfvqRQAMAMDFSWQVAAKSYRELYYRL 476
Cdd:cd03814 336 L-----RRRMAARARAEAERYSWEAFLDNL 360
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
246-476 |
3.22e-03 |
|
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: 39.62 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 246 NGVDEKIWSPEtdlllasrytrdtleDKAENKRQLqiamGLKVDDKVPLFAVVSRLTSQKGLDLVLEALPGLL-EQGGQL 324
Cdd:cd03825 168 NGIDTEIFAPV---------------DKAKARKRL----GIPQDKKVILFGAESVTKPRKGFDELIEALKLLAtKDDLLL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 325 ALLGAGDPVLQEGflaaaaeyPGQVgVQIGY--HEAFSHRIMGGADVILVPSRFAPCGLTQLYGLKYGTLPLVRRTGGLA 402
Cdd:cd03825 229 VVFGKNDPQIVIL--------PFDI-ISLGYidDDEQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSP 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3COP_A 403 DTVSdcslenlaDGVAsGFVF--EDSNAwsLLRAIRRafVLWSRPSLWRFVQRQ-AMAM-DFSWQVAAKSYRELYYRL 476
Cdd:cd03825 300 EIVQ--------HGVT-GYLVppGDVQA--LAEAIEW--LLANPKERESLGERArALAEnHFDQRVQAQRYLELYKDL 364
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
271-407 |
3.64e-03 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 39.77 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 271 EDKAENKRQlqiAMGLKVDDKVPLFAvvSRLTSQKGLDLVLEALPGLLEQGGQLALLGAGDPVLQEGflAAAAEYPGQV- 349
Cdd:PRK15484 177 SNPQPNLRQ---QLNISPDETVLLYA--GRISPDKGILLLMQAFEKLATAHSNLKLVVVGDPTASSK--GEKAAYQKKVl 249
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3COP_A 350 --GVQIGyheafSHRIMGG-------------ADVILVPSRFA-PCGLTQLYGLKYGTLPLVRRTGGLADTVSD 407
Cdd:PRK15484 250 eaAKRIG-----DRCIMLGgqppekmhnyyplADLVVVPSQVEeAFCMVAVEAMAAGKPVLASTKGGITEFVLE 318
|
|
| GT3_GSY2-like |
cd03793 |
glycogen synthase GSY2 and similar proteins; Glycogen synthase, which is most closely related ... |
92-161 |
7.63e-03 |
|
glycogen synthase GSY2 and similar proteins; Glycogen synthase, which is most closely related to the GT3 family of glycosyltransferases, catalyzes the transfer of a glucose molecule from UDP-glucose to a terminal branch of a glycogen molecule, a rate-limit step of glycogen biosynthesis. GSY2, the member of this family in S. cerevisiae, has been shown to possess glycogen synthase activity.
Pssm-ID: 340824 [Multi-domain] Cd Length: 590 Bit Score: 38.89 E-value: 7.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3COP_A 92 GSPYHD--TNlfaytDNVLRFALLGWVGAEMASGLDPfwRPDVV-HAHDWHAGLAPAYLAARGRPAKSVFTVH 161
Cdd:cd03793 115 GIPWNDreTN-----DAIVFGYLVAWFLGEFAAQFDP--QPAVVaHFHEWQAGVGLILCRKRKVDVATIFTTH 180
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
286-474 |
7.92e-03 |
|
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.
Pssm-ID: 340836 [Multi-domain] Cd Length: 362 Bit Score: 38.45 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 286 LKVDDKVPLFAVVSRLTSQKGLDLVLEALPGLLEQGGQLALLGAGD--------PVLQEGFLAAAAEYPGQVGVQIGYHE 357
Cdd:cd03807 184 LGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGRgperpnleRLLLELGLEDRVHLLGERSDVPALLP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 358 AFshrimggaDVILVPSRFAPCGLTQLYGLKYGTLPLVRRTGGLADTVSdcslenlaDGVASGFVFEDSNAwsLLRAIRR 437
Cdd:cd03807 264 AM--------DIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVD--------DGTGFLVPAGDPQA--LADAIRA 325
|
170 180 190
....*....|....*....|....*....|....*..
3COP_A 438 AFVLWSRPSLWRFVQRQAMAMDFSWQVAAKSYRELYY 474
Cdd:cd03807 326 LLEDPEKRARLGRAARERIANEFSIDAMVRRYETLYY 362
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
293-380 |
8.56e-03 |
|
glycosyltransferase family 4 proteins; 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 glycosyltransferase family 4 (GT4). 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.
Pssm-ID: 340860 [Multi-domain] Cd Length: 365 Bit Score: 38.20 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3COP_A 293 PLFAVVSRLTSQKGLDLVLEALPGLLEQGGQLALLGAGDPVLQeGFLAAAAEYPGQVGVQIGYHEAFSHRIMGGADVILV 372
Cdd:cd05844 190 PTILFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIAGDGPLR-PALQALAAALGRVRFLGALPHAEVQDWMRRAEIFCL 268
|
....*...
3COP_A 373 PSRFAPCG 380
Cdd:cd05844 269 PSVTAASG 276
|
|
| |
