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Conserved domains on  [gi|14043391|gb|AAH07688|]
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Glycogen synthase 1 (muscle) [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glycogen_syn pfam05693
Glycogen synthase; This family consists of the eukaryotic glycogen synthase proteins GYS1, ...
31-663 0e+00

Glycogen synthase; This family consists of the eukaryotic glycogen synthase proteins GYS1, GYS2 and GYS3. Glycogen synthase (GS) is the enzyme responsible for the synthesis of -1,4-linked glucose chains in glycogen. It is the rate limiting enzyme in the synthesis of the polysaccharide, and its activity is highly regulated through phosphorylation at multiple sites and also by allosteric effectors, mainly glucose 6-phosphate (G6P).


:

Pssm-ID: 399009 [Multi-domain]  Cd Length: 639  Bit Score: 1256.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391    31 EVAWEVANKVGGIYTVLQTKAKVTGDEWGDNYFLVGPYTEQGVRTQVELLEAPTPALKRTLDSMNSKGCKVYFGRWLIEG 110
Cdd:pfam05693   1 EVAWEVANKVGGIYTVLRSKAPVTTEEYGDNYCLIGPYKEHKARTEVEELEPENPALRAAVDSMRSRGCKIHYGRWLIEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391   111 GPLVVLLDVGASAWALERWKGELWDTCNIGVPWYDREANDAVLFGFLTTWFLGEFLAQSEEKPHVVAHFHEWLAGVGLCL 190
Cdd:pfam05693  81 APRVILFDLGSAAWKLNEWKGELWEQCGIGIPHHDIETNDAIILGFLVAWFLGEFREHATSTPAVVAHFHEWQAGVGLPL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391   191 CRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFNVDKEAGERQIYHRYCMERAAAHCAHVFTTVSQITAIEAQHLL 270
Cdd:pfam05693 161 TRKRKLDIATVFTTHATLLGRYLCAGGVDFYNNLDKFDVDAEAGKRQIYHRYCLERAAAHTAHVFTTVSEITALEAEHLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391   271 KRKPDIVTPNGLNVKKFSAMHEFQNLHAQSKARIQEFVRGHFYGHLDFNLDKTLYFFIAGRYEFSNKGADVFLEALARLN 350
Cdd:pfam05693 241 KRKPDVVTPNGLNVKKFSAVHEFQNLHAQNKEKINDFVRGHFYGHLDFDLDKTLYFFIAGRYEFSNKGADMFIESLARLN 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391   351 YLLRVNGSEQTVVAFFIMPARTNNFNVETLKGQAVRKQLWDTANTVKEKFGRKLYESLLVGSLPDMNKMLDKEDFTMMKR 430
Cdd:pfam05693 321 HRLKTTGSKVTVVAFLIMPAKTNSFNVESLKGQAVIKQLRDTVNRVKEKVGKRIFDICLQGHLPEMDELLDSDDLVLLKR 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391   431 AIFATQRQSFPPVCTHNMLDDSSDPILTTIRRIGLFNSSADRVKVIFHPEFLSSTSPLLPVDYEEFVRGCHLGVFPSYYE 510
Cdd:pfam05693 401 CIFALQRQSLPPVVTHNMIDDANDPILNSIRRVGLFNSPSDRVKVVFHPEFLSSTNPLLGLDYEEFVRGCHLGVFPSYYE 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391   511 PWGYTPAECTVMGIPSISTNLSGFGCFMEEHIADPSAYGIYILDRRFRSLDDSCSQLTSFLYSFCQQSRRQRIIQRNRTE 590
Cdd:pfam05693 481 PWGYTPAECTVMGIPSVTTNLSGFGCFMEEHIEDPKDYGIYIVDRRFKSPDDSVQQLTQFMYEFCQQSRRQRIIQRNRTE 560
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14043391   591 RLSDLLDWKYLGRYYMSARHMALSKAFPEHFTYEPNEADAAQGYRYPRPASVPPSP------SLSRHSSPHQSEDEEDP 663
Cdd:pfam05693 561 RLSDLLDWKRLGRYYRKARQLALRRAYPDQFKQEVDEIISDNEFKIPRPASVPPSPkstvsmTPSDAPSLHSSDDEDDE 639
 
Name Accession Description Interval E-value
Glycogen_syn pfam05693
Glycogen synthase; This family consists of the eukaryotic glycogen synthase proteins GYS1, ...
31-663 0e+00

Glycogen synthase; This family consists of the eukaryotic glycogen synthase proteins GYS1, GYS2 and GYS3. Glycogen synthase (GS) is the enzyme responsible for the synthesis of -1,4-linked glucose chains in glycogen. It is the rate limiting enzyme in the synthesis of the polysaccharide, and its activity is highly regulated through phosphorylation at multiple sites and also by allosteric effectors, mainly glucose 6-phosphate (G6P).


Pssm-ID: 399009 [Multi-domain]  Cd Length: 639  Bit Score: 1256.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391    31 EVAWEVANKVGGIYTVLQTKAKVTGDEWGDNYFLVGPYTEQGVRTQVELLEAPTPALKRTLDSMNSKGCKVYFGRWLIEG 110
Cdd:pfam05693   1 EVAWEVANKVGGIYTVLRSKAPVTTEEYGDNYCLIGPYKEHKARTEVEELEPENPALRAAVDSMRSRGCKIHYGRWLIEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391   111 GPLVVLLDVGASAWALERWKGELWDTCNIGVPWYDREANDAVLFGFLTTWFLGEFLAQSEEKPHVVAHFHEWLAGVGLCL 190
Cdd:pfam05693  81 APRVILFDLGSAAWKLNEWKGELWEQCGIGIPHHDIETNDAIILGFLVAWFLGEFREHATSTPAVVAHFHEWQAGVGLPL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391   191 CRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFNVDKEAGERQIYHRYCMERAAAHCAHVFTTVSQITAIEAQHLL 270
Cdd:pfam05693 161 TRKRKLDIATVFTTHATLLGRYLCAGGVDFYNNLDKFDVDAEAGKRQIYHRYCLERAAAHTAHVFTTVSEITALEAEHLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391   271 KRKPDIVTPNGLNVKKFSAMHEFQNLHAQSKARIQEFVRGHFYGHLDFNLDKTLYFFIAGRYEFSNKGADVFLEALARLN 350
Cdd:pfam05693 241 KRKPDVVTPNGLNVKKFSAVHEFQNLHAQNKEKINDFVRGHFYGHLDFDLDKTLYFFIAGRYEFSNKGADMFIESLARLN 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391   351 YLLRVNGSEQTVVAFFIMPARTNNFNVETLKGQAVRKQLWDTANTVKEKFGRKLYESLLVGSLPDMNKMLDKEDFTMMKR 430
Cdd:pfam05693 321 HRLKTTGSKVTVVAFLIMPAKTNSFNVESLKGQAVIKQLRDTVNRVKEKVGKRIFDICLQGHLPEMDELLDSDDLVLLKR 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391   431 AIFATQRQSFPPVCTHNMLDDSSDPILTTIRRIGLFNSSADRVKVIFHPEFLSSTSPLLPVDYEEFVRGCHLGVFPSYYE 510
Cdd:pfam05693 401 CIFALQRQSLPPVVTHNMIDDANDPILNSIRRVGLFNSPSDRVKVVFHPEFLSSTNPLLGLDYEEFVRGCHLGVFPSYYE 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391   511 PWGYTPAECTVMGIPSISTNLSGFGCFMEEHIADPSAYGIYILDRRFRSLDDSCSQLTSFLYSFCQQSRRQRIIQRNRTE 590
Cdd:pfam05693 481 PWGYTPAECTVMGIPSVTTNLSGFGCFMEEHIEDPKDYGIYIVDRRFKSPDDSVQQLTQFMYEFCQQSRRQRIIQRNRTE 560
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14043391   591 RLSDLLDWKYLGRYYMSARHMALSKAFPEHFTYEPNEADAAQGYRYPRPASVPPSP------SLSRHSSPHQSEDEEDP 663
Cdd:pfam05693 561 RLSDLLDWKRLGRYYRKARQLALRRAYPDQFKQEVDEIISDNEFKIPRPASVPPSPkstvsmTPSDAPSLHSSDDEDDE 639
GT3_GSY2-like cd03793
glycogen synthase GSY2 and similar proteins; Glycogen synthase, which is most closely related ...
26-615 0e+00

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: 1237.63  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391  26 NAVLFEVAWEVANKVGGIYTVLQTKAKVTGDEWGDNYFLVGPYTEQGVRTQVELLEAPTPALKRTLDSMNSKGCKVYFGR 105
Cdd:cd03793   1 NRFLFEVAWEVANKVGGIYTVIKSKAPVTVEEYGDNYCLIGPYNEATARTEVEILEPGNRPLRAALQSMRSRGIKVHFGR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391 106 WLIEGGPLVVLLDVGASAWALERWKGELWDTCNIGVPWYDREANDAVLFGFLTTWFLGEFLAQSEEKPHVVAHFHEWLAG 185
Cdd:cd03793  81 WLIEGYPKVILFDIGSAAWKLDEWKGELWELCSIGIPWNDRETNDAIVFGYLVAWFLGEFAAQFDPQPAVVAHFHEWQAG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391 186 VGLCLCRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFNVDKEAGERQIYHRYCMERAAAHCAHVFTTVSQITAIE 265
Cdd:cd03793 161 VGLILCRKRKVDVATIFTTHATLLGRYLCAGSVDFYNNLDSFDVDKEAGKRGIYHRYCIERAAAHCAHVFTTVSEITAYE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391 266 AQHLLKRKPDIVTPNGLNVKKFSAMHEFQNLHAQSKARIQEFVRGHFYGHLDFNLDKTLYFFIAGRYEFSNKGADVFLEA 345
Cdd:cd03793 241 AEHLLKRKPDIVTPNGLNVVKFSAMHEFQNLHAQSKEKINEFVRGHFYGHLDFDLDKTLYFFTAGRYEFSNKGADMFIES 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391 346 LARLNYLLRVNGSEQTVVAFFIMPARTNNFNVETLKGQAVRKQLWDTANTVKEKFGRKLYESLLVGSLPDMNKMLDKEDF 425
Cdd:cd03793 321 LARLNYLLKVNGSETTVVAFIIMPAKTNNFNVESLKGQAVTKQLKDTVNTVKEKIGKRIFESCLKGKLPDPEELLSKEDL 400
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391 426 TMMKRAIFATQRQSFPPVCTHNMLDDSSDPILTTIRRIGLFNSSADRVKVIFHPEFLSSTSPLLPVDYEEFVRGCHLGVF 505
Cdd:cd03793 401 VMLKRRIFALQRQSLPPIVTHNMLDDANDPILNHIRRIQLFNSPEDRVKVIFHPEFLSSTNPLLGLDYEEFVRGCHLGVF 480
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391 506 PSYYEPWGYTPAECTVMGIPSISTNLSGFGCFMEEHIADPSAYGIYILDRRFRSLDDSCSQLTSFLYSFCQQSRRQRIIQ 585
Cdd:cd03793 481 PSYYEPWGYTPAECTVMGIPSITTNLSGFGCFMEEHIEDPKSYGIYIVDRRFKSPDESVQQLTQYMYEFCQQSRRQRIIQ 560
                       570       580       590
                ....*....|....*....|....*....|
gi 14043391 586 RNRTERLSDLLDWKYLGRYYMSARHMALSK 615
Cdd:cd03793 561 RNRTERLSDLLDWRYLGRFYRKARQLALRR 590
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
494-534 2.02e-04

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 41.51  E-value: 2.02e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 14043391 494 EEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSISTNLSGF 534
Cdd:COG0438  15 EALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGL 55
 
Name Accession Description Interval E-value
Glycogen_syn pfam05693
Glycogen synthase; This family consists of the eukaryotic glycogen synthase proteins GYS1, ...
31-663 0e+00

Glycogen synthase; This family consists of the eukaryotic glycogen synthase proteins GYS1, GYS2 and GYS3. Glycogen synthase (GS) is the enzyme responsible for the synthesis of -1,4-linked glucose chains in glycogen. It is the rate limiting enzyme in the synthesis of the polysaccharide, and its activity is highly regulated through phosphorylation at multiple sites and also by allosteric effectors, mainly glucose 6-phosphate (G6P).


Pssm-ID: 399009 [Multi-domain]  Cd Length: 639  Bit Score: 1256.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391    31 EVAWEVANKVGGIYTVLQTKAKVTGDEWGDNYFLVGPYTEQGVRTQVELLEAPTPALKRTLDSMNSKGCKVYFGRWLIEG 110
Cdd:pfam05693   1 EVAWEVANKVGGIYTVLRSKAPVTTEEYGDNYCLIGPYKEHKARTEVEELEPENPALRAAVDSMRSRGCKIHYGRWLIEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391   111 GPLVVLLDVGASAWALERWKGELWDTCNIGVPWYDREANDAVLFGFLTTWFLGEFLAQSEEKPHVVAHFHEWLAGVGLCL 190
Cdd:pfam05693  81 APRVILFDLGSAAWKLNEWKGELWEQCGIGIPHHDIETNDAIILGFLVAWFLGEFREHATSTPAVVAHFHEWQAGVGLPL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391   191 CRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFNVDKEAGERQIYHRYCMERAAAHCAHVFTTVSQITAIEAQHLL 270
Cdd:pfam05693 161 TRKRKLDIATVFTTHATLLGRYLCAGGVDFYNNLDKFDVDAEAGKRQIYHRYCLERAAAHTAHVFTTVSEITALEAEHLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391   271 KRKPDIVTPNGLNVKKFSAMHEFQNLHAQSKARIQEFVRGHFYGHLDFNLDKTLYFFIAGRYEFSNKGADVFLEALARLN 350
Cdd:pfam05693 241 KRKPDVVTPNGLNVKKFSAVHEFQNLHAQNKEKINDFVRGHFYGHLDFDLDKTLYFFIAGRYEFSNKGADMFIESLARLN 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391   351 YLLRVNGSEQTVVAFFIMPARTNNFNVETLKGQAVRKQLWDTANTVKEKFGRKLYESLLVGSLPDMNKMLDKEDFTMMKR 430
Cdd:pfam05693 321 HRLKTTGSKVTVVAFLIMPAKTNSFNVESLKGQAVIKQLRDTVNRVKEKVGKRIFDICLQGHLPEMDELLDSDDLVLLKR 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391   431 AIFATQRQSFPPVCTHNMLDDSSDPILTTIRRIGLFNSSADRVKVIFHPEFLSSTSPLLPVDYEEFVRGCHLGVFPSYYE 510
Cdd:pfam05693 401 CIFALQRQSLPPVVTHNMIDDANDPILNSIRRVGLFNSPSDRVKVVFHPEFLSSTNPLLGLDYEEFVRGCHLGVFPSYYE 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391   511 PWGYTPAECTVMGIPSISTNLSGFGCFMEEHIADPSAYGIYILDRRFRSLDDSCSQLTSFLYSFCQQSRRQRIIQRNRTE 590
Cdd:pfam05693 481 PWGYTPAECTVMGIPSVTTNLSGFGCFMEEHIEDPKDYGIYIVDRRFKSPDDSVQQLTQFMYEFCQQSRRQRIIQRNRTE 560
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14043391   591 RLSDLLDWKYLGRYYMSARHMALSKAFPEHFTYEPNEADAAQGYRYPRPASVPPSP------SLSRHSSPHQSEDEEDP 663
Cdd:pfam05693 561 RLSDLLDWKRLGRYYRKARQLALRRAYPDQFKQEVDEIISDNEFKIPRPASVPPSPkstvsmTPSDAPSLHSSDDEDDE 639
GT3_GSY2-like cd03793
glycogen synthase GSY2 and similar proteins; Glycogen synthase, which is most closely related ...
26-615 0e+00

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: 1237.63  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391  26 NAVLFEVAWEVANKVGGIYTVLQTKAKVTGDEWGDNYFLVGPYTEQGVRTQVELLEAPTPALKRTLDSMNSKGCKVYFGR 105
Cdd:cd03793   1 NRFLFEVAWEVANKVGGIYTVIKSKAPVTVEEYGDNYCLIGPYNEATARTEVEILEPGNRPLRAALQSMRSRGIKVHFGR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391 106 WLIEGGPLVVLLDVGASAWALERWKGELWDTCNIGVPWYDREANDAVLFGFLTTWFLGEFLAQSEEKPHVVAHFHEWLAG 185
Cdd:cd03793  81 WLIEGYPKVILFDIGSAAWKLDEWKGELWELCSIGIPWNDRETNDAIVFGYLVAWFLGEFAAQFDPQPAVVAHFHEWQAG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391 186 VGLCLCRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFNVDKEAGERQIYHRYCMERAAAHCAHVFTTVSQITAIE 265
Cdd:cd03793 161 VGLILCRKRKVDVATIFTTHATLLGRYLCAGSVDFYNNLDSFDVDKEAGKRGIYHRYCIERAAAHCAHVFTTVSEITAYE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391 266 AQHLLKRKPDIVTPNGLNVKKFSAMHEFQNLHAQSKARIQEFVRGHFYGHLDFNLDKTLYFFIAGRYEFSNKGADVFLEA 345
Cdd:cd03793 241 AEHLLKRKPDIVTPNGLNVVKFSAMHEFQNLHAQSKEKINEFVRGHFYGHLDFDLDKTLYFFTAGRYEFSNKGADMFIES 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391 346 LARLNYLLRVNGSEQTVVAFFIMPARTNNFNVETLKGQAVRKQLWDTANTVKEKFGRKLYESLLVGSLPDMNKMLDKEDF 425
Cdd:cd03793 321 LARLNYLLKVNGSETTVVAFIIMPAKTNNFNVESLKGQAVTKQLKDTVNTVKEKIGKRIFESCLKGKLPDPEELLSKEDL 400
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391 426 TMMKRAIFATQRQSFPPVCTHNMLDDSSDPILTTIRRIGLFNSSADRVKVIFHPEFLSSTSPLLPVDYEEFVRGCHLGVF 505
Cdd:cd03793 401 VMLKRRIFALQRQSLPPIVTHNMLDDANDPILNHIRRIQLFNSPEDRVKVIFHPEFLSSTNPLLGLDYEEFVRGCHLGVF 480
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391 506 PSYYEPWGYTPAECTVMGIPSISTNLSGFGCFMEEHIADPSAYGIYILDRRFRSLDDSCSQLTSFLYSFCQQSRRQRIIQ 585
Cdd:cd03793 481 PSYYEPWGYTPAECTVMGIPSITTNLSGFGCFMEEHIEDPKSYGIYIVDRRFKSPDESVQQLTQYMYEFCQQSRRQRIIQ 560
                       570       580       590
                ....*....|....*....|....*....|
gi 14043391 586 RNRTERLSDLLDWKYLGRYYMSARHMALSK 615
Cdd:cd03793 561 RNRTERLSDLLDWRYLGRFYRKARQLALRR 590
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
490-534 2.31e-06

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 49.32  E-value: 2.31e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 14043391 490 PVDYEEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSISTNLSGF 534
Cdd:cd01635 178 DEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGI 222
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
494-534 2.02e-04

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 41.51  E-value: 2.02e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 14043391 494 EEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSISTNLSGF 534
Cdd:COG0438  15 EALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGL 55
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
170-284 2.33e-04

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 42.52  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391   170 EEKPHVVaHFHEWLAGVGLCLCRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFnvdkeagerqiyhrycMERAAA 249
Cdd:pfam13439  69 RERPDVV-HAHSPFPLGLAALAARLRLGIPLVVTYHGLFPDYKRLGARLSPLRRLLRR----------------LERRLL 131
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 14043391   250 HCAHVFTTVSQITAIEAQHLLKRKPDIVT--PNGLNV 284
Cdd:pfam13439 132 RRADRVIAVSEAVADELRRLYGVPPEKIRviPNGVDL 168
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
171-359 3.65e-03

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: 40.21  E-value: 3.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391 171 EKPHVVaHFHEWLAGVgLCLCRARRLPVATIFTTHATLLGRYLcagavdfynnlenfnvDKEAGERQIYHRYcmeRAAAH 250
Cdd:cd03801  81 RKFDVV-HAHGLLAAL-LAALLALLLGAPLVVTLHGAEPGRLL----------------LLLAAERRLLARA---EALLR 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14043391 251 CAHVFTTVSQITA---IEAQHLLKRKPDIVtPNGLNVKKFSAmhefqnlhaqskariqeFVRGHFYGHldfnlDKTLYFF 327
Cdd:cd03801 140 RADAVIAVSEALRdelRALGGIPPEKIVVI-PNGVDLERFSP-----------------PLRRKLGIP-----PDRPVLL 196
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 14043391 328 IAGRyeFSN-KGADVFLEALARL-----NYLLRVNGSE 359
Cdd:cd03801 197 FVGR--LSPrKGVDLLLEALAKLlrrgpDVRLVIVGGD 232
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
492-534 7.54e-03

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 37.49  E-value: 7.54e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 14043391   492 DYEEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSISTNLSGF 534
Cdd:pfam13692  66 DLAELLAAADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGI 108
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
474-534 9.34e-03

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: 39.06  E-value: 9.34e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14043391 474 KVIFHPEflsstspLLPVDYEEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSISTNLSGF 534
Cdd:cd03801 249 RVRFLGF-------VPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGL 302
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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