|
Name |
Accession |
Description |
Interval |
E-value |
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
6-482 |
0e+00 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 659.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 6 LKVLFVASEVEGLVKTGGLADVAKALPQHLAREGHDVRIILPFYQTLKRR-DEARLLAsrWLPTPQGRDDISYRIYQLEL 84
Cdd:COG0297 1 MKILFVASEAAPFAKTGGLADVVGALPKALAKLGHDVRVVLPGYPSIDDKlKDLEVVA--SLEVPLGGRTYYARVLEGPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 85 DGICVYLLDCPAYFERPQLYAENNQAYPDNGERFAFLAAAALHACEQLNFAPDIVHCNDWHTGLLPLLLKTRHAHNPFfQ 164
Cdd:COG0297 79 DGVPVYFIDNPELFDRPGPYGDPDRDYPDNAERFAFFSRAALELLKGLDWKPDIIHCHDWQTGLIPALLKTRYADDPF-K 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 165 RTRSVISIHNAAFQGVFDRQQFWA--VPEIQDYEQRINYdYGHINLLKCGVLYADKINAVSPNYASELLTHLGAHGMASV 242
Cdd:COG0297 158 RIKTVFTIHNLAYQGIFPAEILELlgLPPELFTPDGLEF-YGQINFLKAGIVYADRVTTVSPTYAREIQTPEFGEGLDGL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 243 FQQRASDLRGILNGCDYQDWDPAFDPLLPATYDADHLAGKHTCKRALQQETGLPVG-NLPIYGMVCRLTEQKGVHLLIPA 321
Cdd:COG0297 237 LRARSGKLSGILNGIDYDVWNPATDPYLPANYSADDLEGKAANKAALQEELGLPVDpDAPLIGMVSRLTEQKGLDLLLEA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 322 LDKFLQHQVQVVIVGSGDPSLAAQLQTIAQQHPDRFAFINAYDDRLAHLVEAGADFFLMPSLFEPCGLNQMYSLAYGTLP 401
Cdd:COG0297 317 LDELLEEDVQLVVLGSGDPEYEEAFRELAARYPGRVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQMYALRYGTVP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 402 LVRAVGGLKDTVVDWDADPARATGFCFNDPTASTLLDAMRRSLLHYlQEPERFARVQQNAMHTRFDWADSIPLYEQMYQD 481
Cdd:COG0297 397 IVRRTGGLADTVIDYNEATGEGTGFVFDEYTAEALLAAIRRALALY-RDPEAWRKLQRNAMKQDFSWEKSAKEYLELYRE 475
|
.
gi 752533439 482 A 482
Cdd:COG0297 476 L 476
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
6-484 |
0e+00 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 651.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 6 LKVLFVASEVEGLVKTGGLADVAKALPQHLAREGHDVRIILPFYQTLKRRDEARLLASRWlptpqgrDDISYRIYQLELD 85
Cdd:PRK00654 1 MKILFVASECAPLIKTGGLGDVVGALPKALAALGHDVRVLLPGYPAIREKLRDAQVVGRL-------DLFTVLFGHLEGD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 86 GICVYLLDCPAYFERPQLYAennqaYPDNGERFAFLAAAALHACEQLNFAPDIVHCNDWHTGLLPLLLKTRHAHnpFFQR 165
Cdd:PRK00654 74 GVPVYLIDAPHLFDRPSGYG-----YPDNGERFAFFSWAAAEFAEGLDPRPDIVHAHDWHTGLIPALLKEKYWR--GYPD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 166 TRSVISIHNAAFQGVFDRQQFWA--VPEIQDYEQRINYdYGHINLLKCGVLYADKINAVSPNYASELLTHLGAHGMASVF 243
Cdd:PRK00654 147 IKTVFTIHNLAYQGLFPAEILGElgLPAEAFHLEGLEF-YGQISFLKAGLYYADRVTTVSPTYAREITTPEFGYGLEGLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 244 QQRASDLRGILNGCDYQDWDPAFDPLLPATYDADHLAGKHTCKRALQQETGLPVGNLPIYGMVCRLTEQKGVHLLIPALD 323
Cdd:PRK00654 226 RARSGKLSGILNGIDYDIWNPETDPLLAANYSADDLEGKAENKRALQERFGLPDDDAPLFAMVSRLTEQKGLDLVLEALP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 324 KFLQHQVQVVIVGSGDPSLAAQLQTIAQQHPDRFAFINAYDDRLAHLVEAGADFFLMPSLFEPCGLNQMYSLAYGTLPLV 403
Cdd:PRK00654 306 ELLEQGGQLVLLGTGDPELEEAFRALAARYPGKVGVQIGYDEALAHRIYAGADMFLMPSRFEPCGLTQLYALRYGTLPIV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 404 RAVGGLKDTVVDWDADPARATGFCFNDPTASTLLDAMRRSLLHYLQEPErFARVQQNAMHTRFDWADSIPLYEQMYQDAL 483
Cdd:PRK00654 386 RRTGGLADTVIDYNPEDGEATGFVFDDFNAEDLLRALRRALELYRQPPL-WRALQRQAMAQDFSWDKSAEEYLELYRRLL 464
|
.
gi 752533439 484 A 484
Cdd:PRK00654 465 G 465
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
7-481 |
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: 593.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 7 KVLFVASEVEGLVKTGGLADVAKALPQHLAREGHDVRIILPFYQTLKRRDEARLLASRWLPTPQGRDdISYRIYQLELDG 86
Cdd:cd03791 1 KVLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRVLGLEVKVGGRG-EEVGVFELPVDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 87 ICVYLLDCPAYFERPQLYAENNQAYPDNGERFAFLAAAALHACEQLNFAPDIVHCNDWHTGLLPLLLKTrHAHNPFFQRT 166
Cdd:cd03791 80 VDYYFLDNPEFFDRPGLPGPPGYDYPDNAERFAFFSRAALELLRRLGFQPDIIHANDWHTALVPAYLKT-RYRGPGFKKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 167 RSVISIHNAAFQGVFDRQQFWAVPEIQDYEQRINYD-YGHINLLKCGVLYADKINAVSPNYASELLTHLGAHGMASVFQQ 245
Cdd:cd03791 159 KTVFTIHNLAYQGLFPLDTLAELGLPPELFHIDGLEfYGQINFLKAGIVYADRVTTVSPTYAKEILTPEYGEGLDGVLRA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 246 RASDLRGILNGCDYQDWDPAFDPLLPATYDADHLAGKHTCKRALQQETGLPV-GNLPIYGMVCRLTEQKGVHLLIPALDK 324
Cdd:cd03791 239 RAGKLSGILNGIDYDEWNPATDKLIPANYSANDLEGKAENKAALQKELGLPVdPDAPLFGFVGRLTEQKGVDLILDALPE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 325 FLQHQVQVVIVGSGDPSLAAQLQTIAQQHPDRFAFINAYDDRLAHLVEAGADFFLMPSLFEPCGLNQMYSLAYGTLPLVR 404
Cdd:cd03791 319 LLEEGGQLVVLGSGDPEYEQAFRELAERYPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYAMRYGTLPIVR 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752533439 405 AVGGLKDTVVDWDADPARATGFCFNDPTASTLLDAMRRSLLHYlQEPERFARVQQNAMHTRFDWADSIPLYEQMYQD 481
Cdd:cd03791 399 RTGGLADTVFDYDPETGEGTGFVFEDYDAEALLAALRRALALY-RNPELWRKLQKNAMKQDFSWDKSAKEYLELYRS 474
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
6-480 |
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: 537.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 6 LKVLFVASEVEGLVKTGGLADVAKALPQHLAREGHDVRIILPFYQTLKRRDEARLLASRWLPTPQGRDDISYRIYQLELD 85
Cdd:TIGR02095 1 MRVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEVDDQVKVVELVDLSVGPRTLYVKVFEGVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 86 GICVYLLDCPAYFERP-QLYAENnqaYPDNGERFAFLAAAALHACEQLNFAPDIVHCNDWHTGLLPLLLKTRHAHNPffq 164
Cdd:TIGR02095 81 GVPVYFIDNPSLFDRPgGIYGDD---YPDNAERFAFFSRAAAELLSGLGWQPDVVHAHDWHTALVPALLKAVYRPNP--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 165 rTRSVISIHNAAFQGVFDRQQFWAVPEIQDY-EQRINYDYGHINLLKCGVLYADKINAVSPNYASELLTHLGAHGMASVF 243
Cdd:TIGR02095 155 -IKTVFTIHNLAYQGVFPADDFSELGLPPEYfHMEGLEFYGRVNFLKGGIVYADRVTTVSPTYAREILTPEFGYGLDGVL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 244 QQRASDLRGILNGCDYQDWDPAFDPLLPATYDADHLAGKHTCKRALQQETGLPVGN-LPIYGMVCRLTEQKGVHLLIPAL 322
Cdd:TIGR02095 234 KARSGKLRGILNGIDTEVWNPATDPYLKANYSADDLAGKAENKEALQEELGLPVDDdVPLFGVISRLTQQKGVDLLLAAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 323 DKFLQHQVQVVIVGSGDPSLAAQLQTIAQQHPDRFAFINAYDDRLAHLVEAGADFFLMPSLFEPCGLNQMYSLAYGTLPL 402
Cdd:TIGR02095 314 PELLELGGQLVVLGTGDPELEEALRELAERYPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQLYAMRYGTVPI 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 752533439 403 VRAVGGLKDTVVDWDADPARATGFCFNDPTASTLLDAMRRSLLHYLQEPERFARVQQNAMHTRFDWADSIPLYEQMYQ 480
Cdd:TIGR02095 394 VRRTGGLADTVVDGDPEAESGTGFLFEEYDPGALLAALSRALRLYRQDPSLWEALQKNAMSQDFSWDKSAKQYVELYR 471
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
5-484 |
1.22e-112 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 341.31 E-value: 1.22e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 5 PLKVLFVASEVEGLVKTGGLADVAKALPQHLAREGHDVRIILPFYQTLKRRDEARLLASRWLPTPQGrddiSYRIYQLEL 84
Cdd:PRK14099 3 PLRVLSVASEIFPLIKTGGLADVAGALPAALKAHGVEVRTLVPGYPAVLAGIEDAEQVHSFPDLFGG----PARLLAARA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 85 DGICVYLLDCPAYFERP--QLYAENNQAYPDNGERFAFLAAAALHACEQL--NFAPDIVHCNDWHTGLLPLLLktRHAHN 160
Cdd:PRK14099 79 GGLDLFVLDAPHLYDRPgnPYVGPDGKDWPDNAQRFAALARAAAAIGQGLvpGFVPDIVHAHDWQAGLAPAYL--HYSGR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 161 PffqRTRSVISIHNAAFQGVFDRQQFWAV--PEIQDYEQRINYdYGHINLLKCGVLYADKINAVSPNYASELLTHLGAHG 238
Cdd:PRK14099 157 P---APGTVFTIHNLAFQGQFPRELLGALglPPSAFSLDGVEY-YGGIGYLKAGLQLADRITTVSPTYALEIQGPEAGMG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 239 MASVFQQRASDLRGILNGCDYQDWDPAFDPLLPATYDADHLAGKHTCKRALQQETGL-PVGNLPIYGMVCRLTEQKGVHL 317
Cdd:PRK14099 233 LDGLLRQRADRLSGILNGIDTAVWNPATDELIAATYDVETLAARAANKAALQARFGLdPDPDALLLGVISRLSWQKGLDL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 318 LIPALDKFLQHQVQVVIVGSGDPSLAAQLQTIAQQHPDRFAFINAYDDRLAHLVEAGADFFLMPSLFEPCGLNQMYSLAY 397
Cdd:PRK14099 313 LLEALPTLLGEGAQLALLGSGDAELEARFRAAAQAYPGQIGVVIGYDEALAHLIQAGADALLVPSRFEPCGLTQLCALRY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 398 GTLPLVRAVGGLKDTVVdwDADPA-----RATGFCFNDPTASTLLDAMRRSLLHYlQEPERFARVQQNAMHTRFDWADSI 472
Cdd:PRK14099 393 GAVPVVARVGGLADTVV--DANEMaiatgVATGVQFSPVTADALAAALRKTAALF-ADPVAWRRLQRNGMTTDVSWRNPA 469
|
490
....*....|..
gi 752533439 473 PLYEQMYQDALA 484
Cdd:PRK14099 470 QHYAALYRSLVA 481
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
1-485 |
2.75e-98 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 304.35 E-value: 2.75e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 1 MAINPLKVLFVASEVEGLVKTGGLADVAKALPQHLAREGHDVRIILPFYQTLKRRdEARL-----LASRWLPTPQGRDDI 75
Cdd:PRK14098 1 MSRRNFKVLYVSGEVSPFVRVSALADFMASFPQALEEEGFEARIMMPKYGTINDR-KFRLhdvlrLSDIEVPLKEKTDLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 76 SYRIYQLELDGICVYLLDCPAYFERPQLYAE--NNQAYPDNGERFAFLAAAALHACEQLNFAPDIVHCNDWHTGLLPLLL 153
Cdd:PRK14098 80 HVKVTALPSSKIQTYFLYNEKYFKRNGLFTDmsLGGDLKGSAEKVIFFNVGVLETLQRLGWKPDIIHCHDWYAGLVPLLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 154 KTRHAHNPFFQRTRSVISIHNAAFQGVFDRQQFWAV--PEIQDYEQRINydyGHINLLKCGVLYADKINAVSPNYASELL 231
Cdd:PRK14098 160 KTVYADHEFFKDIKTVLTIHNVYRQGVLPFKVFQKLlpEEVCSGLHREG---DEVNMLYTGVEHADLLTTTSPRYAEEIA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 232 THLG-AHGMASVFQQRASDLRGILNGCDYQDWDPAFDPLLPATYDADHLAGKHTCKRALQQETGLPVGN-LPIYGMVCRL 309
Cdd:PRK14098 237 GDGEeAFGLDKVLEERKMRLHGILNGIDTRQWNPSTDKLIKKRYSIERLDGKLENKKALLEEVGLPFDEeTPLVGVIINF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 310 TEQKGVHLLIPALDKFLQHQVQVVIVGSGDPSLAAQLQTIAQQHPDRFAFINAYDDRLAHLVEAGADFFLMPSLFEPCGL 389
Cdd:PRK14098 317 DDFQGAELLAESLEKLVELDIQLVICGSGDKEYEKRFQDFAEEHPEQVSVQTEFTDAFFHLAIAGLDMLLMPGKIESCGM 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 390 NQMYSLAYGTLPLVRAVGGLKDTVVDWDADpaRATGFCFNDPTASTLLDAMRRSLLHYLQEpERFARVQQNAMHTRFDWA 469
Cdd:PRK14098 397 LQMFAMSYGTIPVAYAGGGIVETIEEVSED--KGSGFIFHDYTPEALVAKLGEALALYHDE-ERWEELVLEAMERDFSWK 473
|
490
....*....|....*.
gi 752533439 470 DSIPLYEQMYQDALAP 485
Cdd:PRK14098 474 NSAEEYAQLYRELLGP 489
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
8-245 |
1.09e-84 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 260.73 E-value: 1.09e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 8 VLFVASEVEGLVKTGGLADVAKALPQHLAREGHDVRIILPFYQTLK-RRDEARLLASRWLPTPQGRDDISYRIYQLELDG 86
Cdd:pfam08323 1 ILFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGNIPeERNQLEDVIRLSVAAGVPVRPLTVGVARLELDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 87 ICVYLLDCPAYFERPQLYAENNQAYPDNGERFAFLAAAALHACEQLNFAPDIVHCNDWHTGLLPLLLKTRHAHNPfFQRT 166
Cdd:pfam08323 81 VDVYFLDNPDYFDRPGLYGDDGRDYEDNAERFAFFSRAALELAKKLGWIPDIIHCHDWHTALVPAYLKEAYADDP-FKNI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 167 RSVISIHNAAFQGVFDRQQFWA--VPEIQDYEQRINYdYGHINLLKCGVLYADKINAVSPNYASELLTHLGAHGMASVFQ 244
Cdd:pfam08323 160 KTVFTIHNLAYQGRFPADLLDLlgLPPEDFNLDGLEF-YGQINFLKAGIVYADAVTTVSPTYAEEIQTPEFGGGLDGLLR 238
|
.
gi 752533439 245 Q 245
Cdd:pfam08323 239 E 239
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
6-486 |
1.85e-75 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 255.60 E-value: 1.85e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 6 LKVLFVASEVEGLVKTGGLADVAKALPQHLAREGHDVRIILPFYQTLK--RRDEARLLASRWLPTPQGRDdISYRIYQLE 83
Cdd:PLN02939 482 LHIVHIAAEMAPVAKVGGLADVVSGLGKALQKKGHLVEIVLPKYDCMQydQIRNLKVLDVVVESYFDGNL-FKNKIWTGT 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 84 LDGICVYLLDC--PA-YFERPQLYAENnqaypDNGERFAFLAAAALHACEQLNFAPDIVHCNDWHTGLLPLLLKTRHAhN 160
Cdd:PLN02939 561 VEGLPVYFIEPqhPSkFFWRAQYYGEH-----DDFKRFSYFSRAALELLYQSGKKPDIIHCHDWQTAFVAPLYWDLYA-P 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 161 PFFQRTRSVISIHNAAFQGV----------FDRQQFWAVPEIQDYEqrinydYGHINLLKCGVLYADKINAVSPNYASEL 230
Cdd:PLN02939 635 KGFNSARICFTCHNFEYQGTapasdlascgLDVHQLDRPDRMQDNA------HGRINVVKGAIVYSNIVTTVSPTYAQEV 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 231 LTHlGAHGMASVFQQRASDLRGILNGCDYQDWDPAFDPLLPATYDADHLAGKHTCKRALQQETGLPVGNL--PIYGMVCR 308
Cdd:PLN02939 709 RSE-GGRGLQDTLKFHSKKFVGILNGIDTDTWNPSTDRFLKVQYNANDLQGKAANKAALRKQLGLSSADAsqPLVGCITR 787
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 309 LTEQKGVHLLIPALDKFLQHQVQVVIVGSGD-PSLAAQLQTIAQQ--HPDRFAFINAYDDRLAHLVEAGADFFLMPSLFE 385
Cdd:PLN02939 788 LVPQKGVHLIRHAIYKTAELGGQFVLLGSSPvPHIQREFEGIADQfqSNNNIRLILKYDEALSHSIYAASDMFIIPSMFE 867
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 386 PCGLNQMYSLAYGTLPLVRAVGGLKDTVVDWDAD---PARATGFCFNDPTASTLLDAMRRSLLHYLQEPERFARVQQNAM 462
Cdd:PLN02939 868 PCGLTQMIAMRYGSVPIVRKTGGLNDSVFDFDDEtipVELRNGFTFLTPDEQGLNSALERAFNYYKRKPEVWKQLVQKDM 947
|
490 500
....*....|....*....|....
gi 752533439 463 HTRFDWADSIPLYEQMYQDALAPA 486
Cdd:PLN02939 948 NIDFSWDSSASQYEELYQRAVARA 971
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
5-482 |
6.22e-71 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 243.62 E-value: 6.22e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 5 PLKVLFVASEVEGLVKTGGLADVAKALPQHLAREGHDVRIILPFYQTLKRRDEARLLASR---WlptpqGRDDIsyRIYQ 81
Cdd:PLN02316 587 PMHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHNVDIILPKYDCLNLSHVKDLHYQRsysW-----GGTEI--KVWF 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 82 LELDGICVYLLDcP--AYFERPQLYAENNqaypdNGERFAFLAAAALHACEQLNFAPDIVHCNDWHTGLLPLLLKTRHAH 159
Cdd:PLN02316 660 GKVEGLSVYFLE-PqnGMFWAGCVYGCRN-----DGERFGFFCHAALEFLLQSGFHPDIIHCHDWSSAPVAWLFKDHYAH 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 160 NPFfQRTRSVISIHNAAFQgvfdrqqfwavpeiqdyeqrinydyghINLLKCGVLYADKINAVSPNYASELLTHlgahgm 239
Cdd:PLN02316 734 YGL-SKARVVFTIHNLEFG---------------------------ANHIGKAMAYADKATTVSPTYSREVSGN------ 779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 240 aSVFQQRASDLRGILNGCDYQDWDPAFDPLLPATYDADHLA-GKHTCKRALQQETGLPVGNLPIYGMVCRLTEQKGVHLL 318
Cdd:PLN02316 780 -SAIAPHLYKFHGILNGIDPDIWDPYNDNFIPVPYTSENVVeGKRAAKEALQQRLGLKQADLPLVGIITRLTHQKGIHLI 858
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 319 IPALDKFLQHQVQVVIVGSG-DPSLAAQLQTIAQQ----HPDRFAFINAYDDRLAHLVEAGADFFLMPSLFEPCGLNQMY 393
Cdd:PLN02316 859 KHAIWRTLERNGQVVLLGSApDPRIQNDFVNLANQlhssHHDRARLCLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLT 938
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 394 SLAYGTLPLVRAVGGLKDTVVDWDADPARA-------TGFCFNDPTASTLLDAMRRSLLHYLQEPERFARVQQNAMHTRF 466
Cdd:PLN02316 939 AMRYGSIPVVRKTGGLFDTVFDVDHDKERAqaqglepNGFSFDGADAAGVDYALNRAISAWYDGRDWFNSLCKRVMEQDW 1018
|
490
....*....|....*.
gi 752533439 467 DWADSIPLYEQMYQDA 482
Cdd:PLN02316 1019 SWNRPALDYMELYHSA 1034
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
7-480 |
4.78e-24 |
|
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: 103.39 E-value: 4.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 7 KVLFVASEVEGlvKTGGLADVAKALPQHLAREGHDVRIILPFYQTLKRRDEARLLASRWLPTPQGRDDISYRIYQLELDG 86
Cdd:cd03801 1 KILLLSPELPP--PVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 87 ICvylldcpayferpqlyaennqaypdngerfaflaaaalhaceqlnFAPDIVHCNDWHTGLLPLLLKTRHahnpffqRT 166
Cdd:cd03801 79 RL---------------------------------------------RKFDVVHAHGLLAALLAALLALLL-------GA 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 167 RSVISIHNAAF---QGVFDRQQFWavpeIQDYEQRINYdyghinllkcgvlyADKINAVSPNYASELLTHLGAHgmasvf 243
Cdd:cd03801 107 PLVVTLHGAEPgrlLLLLAAERRL----LARAEALLRR--------------ADAVIAVSEALRDELRALGGIP------ 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 244 qqrASDLRGILNGCDYQDWDPAFDPLLPATYDAdhlagkhtckralqqetglpvgnlPIYGMVCRLTEQKGVHLLIPALD 323
Cdd:cd03801 163 ---PEKIVVIPNGVDLERFSPPLRRKLGIPPDR------------------------PVLLFVGRLSPRKGVDLLLEALA 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 324 KFLQH--QVQVVIVGSGDPsLAAQLQTIAQQHPDRFAFINAYDDRLAHLVEAGADFFLMPSLFEPCGLNQMYSLAYGTLP 401
Cdd:cd03801 216 KLLRRgpDVRLVIVGGDGP-LRAELEELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPV 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 402 LVRAVGGLKDTVVDwdadpaRATGFCFNDPTASTLLDAMRRsllhYLQEPERFARVQQNA---MHTRFDWADSIPLYEQM 478
Cdd:cd03801 295 VATDVGGLPEVVED------GEGGLVVPPDDVEALADALLR----LLADPELRARLGRAArerVAERFSWERVAERLLDL 364
|
..
gi 752533439 479 YQ 480
Cdd:cd03801 365 YR 366
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
301-461 |
1.08e-16 |
|
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: 77.31 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 301 PIYGMVCRLTEQKGVHLLIPALDKFL--QHQVQVVIVGSGDpsLAAQLQTIAQQH--PDRFAFI-NAYDDRLAHLVEAgA 375
Cdd:pfam00534 3 KIILFVGRLEPEKGLDLLIKAFALLKekNPNLKLVIAGDGE--EEKRLKKLAEKLglGDNVIFLgFVSDEDLPELLKI-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 376 DFFLMPSLFEPCGLNQMYSLAYGTLPLVRAVGGLKDTVVDWDadparaTGFCFNDPTASTLLDAMRRsllhYLQEPERFA 455
Cdd:pfam00534 80 DVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGE------TGFLVKPNNAEALAEAIDK----LLEDEELRE 149
|
....*.
gi 752533439 456 RVQQNA 461
Cdd:pfam00534 150 RLGENA 155
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
305-417 |
1.40e-13 |
|
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: 70.13 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 305 MVCRLTEQKGVHLLIPALDKFLQHQ--VQVVIVGSGDPSLAAQLQTIAQQHPDRFAFINAYDDR-LAHLVEAGADFFLMP 381
Cdd:cd01635 115 SVGRLVPEKGIDLLLEALALLKARLpdLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDeVLELLLAAADVFVLP 194
|
90 100 110
....*....|....*....|....*....|....*.
gi 752533439 382 SLFEPCGLNQMYSLAYGTLPLVRAVGGLKDTVVDWD 417
Cdd:cd01635 195 SRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGE 230
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
366-484 |
1.72e-12 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 64.24 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 366 RLAHLVEA---GADFFLMPSLFEPCGLNQMYSLAYGTLPLVRAVGGLKDTVVDWDadparaTGFCFNDPTAstllDAMRR 442
Cdd:COG0438 9 GLDLLLEAllaAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGE------TGLLVPPGDP----EALAE 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 752533439 443 SLLHYLQEPERFARVQQNA---MHTRFDWADSIPLYEQMYQDALA 484
Cdd:COG0438 79 AILRLLEDPELRRRLGEAArerAEERFSWEAIAERLLALYEELLA 123
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
288-465 |
4.26e-12 |
|
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: 67.38 E-value: 4.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 288 ALQQETGLPVGNLPIYGMVCRLTEQKGVHLLIPALDKfLQHQVQVVIVGSGDPSLAAQLQTIAQQH--PDRFAFInAYDD 365
Cdd:cd03819 170 AEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAE-LKDEPDFRLLVAGDGPERDEIRRLVERLglRDRVTFT-GFRE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 366 RLAHLVEAgADFFLMPSLFEPCGLNQMYSLAYGTLPLVRAVGGLKDTVVdwdadpARATGFCFNDPTASTLLDAMRRSLL 445
Cdd:cd03819 248 DVPAALAA-SDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVV------HGRTGLLVPPGDAEALADAIRAAKL 320
|
170 180
....*....|....*....|
gi 752533439 446 HylqePERFARVQQNAMHTR 465
Cdd:cd03819 321 L----PEAREKLQAAAALTE 336
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
301-461 |
6.24e-11 |
|
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: 63.85 E-value: 6.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 301 PIYGMVCRLTEQKGVHLLIPALDKFLQHQ-VQVVIVGSGdPSLAAqlqtIAQQHPDrFAFINAYDDR-LAHLVeAGADFF 378
Cdd:cd03814 199 PLLLYVGRLAPEKNLEALLDADLPLAASPpVRLVVVGDG-PARAE----LEARGPD-VIFTGFLTGEeLARAY-ASADVF 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 379 LMPSLFEPCGLNQMYSLAYGtLPLV-RAVGGLKDTVvdwdadPARATGFCFNDPTASTLLDAMRrsllHYLQEPERFARV 457
Cdd:cd03814 272 VFPSRTETFGLVVLEAMASG-LPVVaADAGGPRDIV------RPGGTGALVEPGDAAAFAAALR----ALLEDPELRRRM 340
|
....
gi 752533439 458 QQNA 461
Cdd:cd03814 341 AARA 344
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
301-446 |
4.56e-10 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 57.52 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 301 PIYGMVCRLTE-QKGVHLLIPALDKFLQ--HQVQVVIVGSGDPslaAQLQTIAQQHPDRFAFINAYDDRLAHLveAGADF 377
Cdd:pfam13692 2 PVILFVGRLHPnVKGVDYLLEAVPLLRKrdNDVRLVIVGDGPE---EELEELAAGLEDRVIFTGFVEDLAELL--AAADV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 378 FLMPSLFEPCGLNQMYSLAYGtLPLV-RAVGGLKDTVVDWdadparaTGFCFNDPTASTLLDAMRRsLLH 446
Cdd:pfam13692 77 FVLPSLYEGFGLKLLEAMAAG-LPVVaTDVGGIPELVDGE-------NGLLVPPGDPEALAEAILR-LLE 137
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
7-456 |
6.91e-09 |
|
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: 57.37 E-value: 6.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 7 KVLFVASEVEGlvktGGLADVAKALPQHLAREGHDVRIILpfyqtlkRRDEARLLAsrwlptpQGRDDISYRIYQLELDG 86
Cdd:cd03811 1 KILFVIPSLSG----GGAERVLLNLANALDKRGYDVTLVL-------LRDEGDLDK-------QLNGDVKLIRLLIRVLK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 87 ICVYLLDcPAYFERPQLYAENNqaypdngerfaflaaaalhaceqlnfaPDIVHCNDWHTGLLPLLLKTRhahnpffqRT 166
Cdd:cd03811 63 LIKLGLL-KAILKLKRILKRAK---------------------------PDVVISFLGFATYIVAKLAAA--------RS 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 167 RSVISIHNAAfqgvfdrqqfwavpeiqdyeqrINYDYGHINLLKCGVLY--ADKINAVSPNYASELLTHlgahgmasvFQ 244
Cdd:cd03811 107 KVIAWIHSSL----------------------SKLYYLKKKLLLKLKLYkkADKIVCVSKGIKEDLIRL---------GP 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 245 QRASDLRGILNGcdyQDWDpafdpllpatydadhlagkHTCKRALQQETGLPvGNLPIYGMVCRLTEQKGVHLLIPALDK 324
Cdd:cd03811 156 SPPEKIEVIYNP---IDID-------------------RIRALAKEPILNEP-EDGPVILAVGRLDPQKGHDLLIEAFAK 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 325 FLQH--QVQVVIVGSGDpsLAAQLQTIAQQH--PDRFAFINAYDDRLAHLveAGADFFLMPSLFEPCGLNQMYSLAYGTL 400
Cdd:cd03811 213 LRKKypDVKLVILGDGP--LREELEKLAKELglAERVIFLGFQSNPYPYL--KKADLFVLSSRYEGFPNVLLEAMALGTP 288
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 752533439 401 PLVRAVGGLKDTVVDWDadparaTGFCFNDpTASTLLDAMRRSLLHYLQEPERFAR 456
Cdd:cd03811 289 VVSTDCPGPREILDDGE------NGLLVPD-GDAAALAGILAALLQKKLDAALRER 337
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
308-469 |
2.18e-08 |
|
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: 56.09 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 308 RLTEQKGVHLLIPAL--DKFLQHQVQVVIVGSGDPSLAA----QLQTIAQQH--PDRFAFINAYD-DRLAHLVEAgADFF 378
Cdd:cd03800 228 RLDPRKGIDTLVRAFaqLPELRELANLVLVGGPSDDPLSmdreELAELAEELglIDRVRFPGRVSrDDLPELYRA-ADVF 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 379 LMPSLFEPCGLNQMYSLAYGTLPLVRAVGGLKDTVVDwdadpaRATGFCFN--DPtastllDAMRRSLLHYLQEPERFAR 456
Cdd:cd03800 307 VVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRD------GRTGLLVDphDP------EALAAALRRLLDDPALWQR 374
|
170
....*....|....*.
gi 752533439 457 VQQNAM---HTRFDWA 469
Cdd:cd03800 375 LSRAGLeraRAHYTWE 390
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
301-482 |
2.20e-08 |
|
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: 55.85 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 301 PIYGMVCRLTEQKGVHLLIPA---LDKFLQHqVQVVIVGSGdpslaAQLQTIAQQHP-----DRFAFINA--YDDRLAHL 370
Cdd:cd03798 201 FVILFVGRLIPRKGIDLLLEAfarLAKARPD-VVLLIVGDG-----PLREALRALAEdlglgDRVTFTGRlpHEQVPAYY 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 371 veAGADFFLMPSLFEPCGLNQMYSLAYGTLPLVRAVGGLKDTVVDwdadpaRATGFCFNDPTASTLLDAMRRSLL-HYLQ 449
Cdd:cd03798 275 --RACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGD------PETGLLVPPGDADALAAALRRALAePYLR 346
|
170 180 190
....*....|....*....|....*....|....*
gi 752533439 450 E--PERFARVQqnamhTRFDWADSIPLYEQMYQDA 482
Cdd:cd03798 347 ElgEAARARVA-----ERFSWVKAADRIAAAYRDV 376
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
330-482 |
4.10e-07 |
|
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: 51.97 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 330 VQVVIVGSGDPSLAAQLQTIAQQHPDRFAFINAYDDrLAHLVEAgADFFLMPSLFEPCGLNQMYSLAYGTLPLVRAVGGL 409
Cdd:cd04962 227 AKLLLVGDGPERVPAEELARELGVEDRVLFLGKQDD-VEELLSI-ADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGI 304
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 752533439 410 KDTVVDwdadpaRATGFCFN--DptastlLDAMRRSLLHYLQEPERFARVQQNAMHT---RFDWADSIPLYEQMYQDA 482
Cdd:cd04962 305 PEVVKH------GETGFLSDvgD------VDAMAKSALSILEDDELYNRMGRAARKRaaeRFDPERIVPQYEAYYRRL 370
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
308-464 |
5.41e-07 |
|
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: 51.56 E-value: 5.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 308 RLTEQKGVHLLIPALDKFLQHQVQVVIVGSGDPSLAAQLQTIaqqhpDRFAFINAYD-DRLAHLVEAgADFFLMPSLF-E 385
Cdd:cd03823 199 RLTEEKGIDLLVEAFKRLPREDIELVIAGHGPLSDERQIEGG-----RRIAFLGRVPtDDIKDFYEK-IDVLVVPSIWpE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 386 PCGLNQMYSLAYGTLPLVRAVGGLKDTVVDwdadpaRATGFCFNDPTASTLLDAMRRSLLH--YLQEPERFARVQQNAMH 463
Cdd:cd03823 273 PFGLVVREAIAAGLPVIASDLGGIAELIQP------GVNGLLFAPGDAEDLAAAMRRLLTDpaLLERLRAGAEPPRSTES 346
|
.
gi 752533439 464 T 464
Cdd:cd03823 347 Q 347
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
301-479 |
7.12e-07 |
|
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: 51.13 E-value: 7.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 301 PIYGMVCRLTEQKGVHLLIPALDKFLQH-QVQVVIVGSGDpsLAAQLQTIAQQH--PDRFAFINAYDDRLAHLVEAGADF 377
Cdd:cd03817 202 PILLYVGRLAKEKNIDFLLRAFAELKKEpNIKLVIVGDGP--EREELKELARELglADKVIFTGFVPREELPEYYKAADL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 378 FLMPSLFEPCGLNQMYSLAYGtLPLVrAV--GGLKDTVVDWDadparaTGFCF--NDPTASTLLDAMRrsllhylQEPER 453
Cdd:cd03817 280 FVFASTTETQGLVYLEAMAAG-LPVV-AAkdPAASELVEDGE------NGFLFepNDETLAEKLLHLR-------ENLEL 344
|
170 180
....*....|....*....|....*...
gi 752533439 454 FARVQQNAMHTR--FDWADSIPLYEQMY 479
Cdd:cd03817 345 LRKLSKNAEISAreFAFAKSVEKLYEEV 372
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
133-389 |
9.46e-07 |
|
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: 50.82 E-value: 9.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 133 NFAPDIVHCNDWHTGLLPLLLKTRHAHNPFFQRTRSVISIHNAAFQGVFDRQQ--------FWAVPEIQDYEQRINYDYg 204
Cdd:cd03809 52 EYPELSLGVIKIKLWRELALLRWLQILLPKKDKPDLLHSPHNTAPLLLKGCPQvvtihdliPLRYPEFFPKRFRLYYRL- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 205 hinLLKCGVLYADKINAVSPNYASELLTHLGAhgmasvfqqRASDLRGILNGCDyqdwdPAFDPLLPATYDADhlagkht 284
Cdd:cd03809 131 ---LLPISLRRADAIITVSEATRDDIIKFYGV---------PPEKIVVIPLGVD-----PSFFPPESAAVLIA------- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 285 cKRALQQETGLpvgnlpiygMVCRLTEQKGVHLLIPALDKFLQ--HQVQVVIVGSGDPSLAAQLQTI--AQQHPDRFAFI 360
Cdd:cd03809 187 -KYLLPEPYFL---------YVGTLEPRKNHERLLKAFALLKKqgGDLKLVIVGGKGWEDEELLDLVkkLGLGGRVRFLG 256
|
250 260
....*....|....*....|....*....
gi 752533439 361 NAYDDRLAHLVeAGADFFLMPSLFEPCGL 389
Cdd:cd03809 257 YVSDEDLPALY-RGARAFVFPSLYEGFGL 284
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
313-481 |
8.70e-06 |
|
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: 47.71 E-value: 8.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 313 KGVHLLIPALDKFLQHQ-VQVVIVGSGDPSLA-AQLQTIaqqhpdRFAFINayDDRLAHLVEAGADFFLMPSLFEPCGLN 390
Cdd:cd03825 208 KGFDELIEALKLLATKDdLLLVVFGKNDPQIViLPFDII------SLGYID--DDEQLVDIYSAADLFVHPSLADNLPNT 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 391 QMYSLAYGTLPLVRAVGGLKDTVVDwdadpaRATGFCFNDPTASTLLDAMRRSLLHYlQEPERFARVQQNAMHTRFDWAD 470
Cdd:cd03825 280 LLEAMACGTPVVAFDTGGSPEIVQH------GVTGYLVPPGDVQALAEAIEWLLANP-KERESLGERARALAENHFDQRV 352
|
170
....*....|.
gi 752533439 471 SIPLYEQMYQD 481
Cdd:cd03825 353 QAQRYLELYKD 363
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
301-442 |
1.31e-05 |
|
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: 47.20 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 301 PIYGMVCRLTEQKGVHLLIPALDK-FLQH-QVQVVIVGSGDPSLAAQLQTIAQQHPDRFAFINAYDDrLAHLVEAgADFF 378
Cdd:cd03808 190 VVFLFVARLLKDKGIDELIEAAKIlKKKGpNVRFLLVGDGELENPSEILIEKLGLEGRIEFLGFRSD-VPELLAE-SDVF 267
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 752533439 379 LMPSLFEPCGLNQMYSLAYGTLPLVRAVGGLKDTVVDwdadpaRATGFCFNDPTASTLLDAMRR 442
Cdd:cd03808 268 VLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVID------GVNGFLVPPGDVEALADAIEK 325
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
308-403 |
4.98e-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: 42.36 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 308 RLTEQKGVHLLIPALDKFLQHQ--VQVVIVGSGDPSLAAQLQTIAQQH-PDRFAFINA-YDDRLAHLVeAGADFFLMPSL 383
Cdd:cd03821 212 RIHPKKGLDLLIRAARKLAEQGrdWHLVIAGPDDGAYPAFLQLQSSLGlGDRVTFTGPlYGEAKWALY-ASADLFVLPSY 290
|
90 100
....*....|....*....|
gi 752533439 384 FEPCGLNQMYSLAYGtLPLV 403
Cdd:cd03821 291 SENFGNVVAEALACG-LPVV 309
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
305-385 |
5.85e-03 |
|
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: 38.76 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752533439 305 MVCRLTEQKGVHLLIPALDKFLQHQ--VQVVIVGSGDpsLAAQLQtiaqqhpdrfAFINAYDdrLAHLVE---------- 372
Cdd:cd03820 186 AVGRLTYQKGFDLLIEAWALIAKKHpdWKLRIYGDGP--EREELE----------KLIDKLG--LEDRVKllgptkniae 251
|
90
....*....|....*
gi 752533439 373 --AGADFFLMPSLFE 385
Cdd:cd03820 252 eyANSSIFVLSSRYE 266
|
|
| |
