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Conserved domains on  [gi|491925636|ref|WP_005675600|]
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MULTISPECIES: glycogen/starch synthase [Bacteroides]

Protein Classification

glycosyltransferase family protein( domain architecture ID 56)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
10-545 1.51e-81

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.


The actual alignment was detected with superfamily member cd03793:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 590  Bit Score: 266.16  E-value: 1.51e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636  10 YIFESSWEVCNKVGGIYTVLSTRANTLQEKFRDRIFFIGP---DVWQGKENPLFIESDNLCAAWKkhAFEKDELSVRVGR 86
Cdd:cd03793    3 FLFEVAWEVANKVGGIYTVIKSKAPVTVEEYGDNYCLIGPyneATARTEVEILEPGNRPLRAALQ--SMRSRGIKVHFGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636  87 WNIPGEPIVILVDFQPFFEKKDDIYTDMWNRFQVDSLHAYGDYDEASMFSYAAGKVVESFyRYNLTETDKVVYQAHEWMT 166
Cdd:cd03793   81 WLIEGYPKVILFDIGSAAWKLDEWKGELWELCSIGIPWNDRETNDAIVFGYLVAWFLGEF-AAQFDPQPAVVAHFHEWQA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636 167 GMGALYIQEAVPEIGTIFTTHATSIGRSIAGNNKPLYDYLFAYNGDQMAQELNMQSKHSIEKQTAHYVDCFTTVSQITNN 246
Cdd:cd03793  160 GVGLILCRKRKVDVATIFTTHATLLGRYLCAGSVDFYNNLDSFDVDKEAGKRGIYHRYCIERAAAHCAHVFTTVSEITAY 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636 247 ECKELLDKPADVVLMNGFEddfVPKGSTFTgKRKRARALMLNVANKLL-GTNMG------DDTLIIGTSGRYEFKNKGID 319
Cdd:cd03793  240 EAEHLLKRKPDIVTPNGLN---VVKFSAMH-EFQNLHAQSKEKINEFVrGHFYGhldfdlDKTLYFFTAGRYEFSNKGAD 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636 320 VFLESLNRLN---RDKNLHKNVLAFI---------NVPSWVG--------DPREDLQERLkSKEKFDT--------PLEV 371
Cdd:cd03793  316 MFIESLARLNyllKVNGSETTVVAFIimpaktnnfNVESLKGqavtkqlkDTVNTVKEKI-GKRIFESclkgklpdPEEL 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636 372 ----------------------PFITHWLHNMTHDQVLDMLKYLGMGNRPGDKVKVIFVPCYLDGRDGIMNKEYYDILLG 429
Cdd:cd03793  395 lskedlvmlkrrifalqrqslpPIVTHNMLDDANDPILNHIRRIQLFNSPEDRVKVIFHPEFLSSTNPLLGLDYEEFVRG 474
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636 430 QDLSVYASYYEPWGYTPLESVAFHVPTITTDLAGFGLWVnslknQHGIND----GVEVLHRSDYNYSEVADGIKDTITLF 505
Cdd:cd03793  475 CHLGVFPSYYEPWGYTPAECTVMGIPSITTNLSGFGCFM-----EEHIEDpksyGIYIVDRRFKSPDESVQQLTQYMYEF 549
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|
gi 491925636 506 ADKSEKEIKEIRKRAAEVAEQALWKHFIQYYYEAYDIALC 545
Cdd:cd03793  550 CQQSRRQRIIQRNRTERLSDLLDWRYLGRFYRKARQLALR 589
 
Name Accession Description Interval E-value
GT3_GSY2-like cd03793
glycogen synthase GSY2 and similar proteins; Glycogen synthase, which is most closely related ...
10-545 1.51e-81

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: 266.16  E-value: 1.51e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636  10 YIFESSWEVCNKVGGIYTVLSTRANTLQEKFRDRIFFIGP---DVWQGKENPLFIESDNLCAAWKkhAFEKDELSVRVGR 86
Cdd:cd03793    3 FLFEVAWEVANKVGGIYTVIKSKAPVTVEEYGDNYCLIGPyneATARTEVEILEPGNRPLRAALQ--SMRSRGIKVHFGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636  87 WNIPGEPIVILVDFQPFFEKKDDIYTDMWNRFQVDSLHAYGDYDEASMFSYAAGKVVESFyRYNLTETDKVVYQAHEWMT 166
Cdd:cd03793   81 WLIEGYPKVILFDIGSAAWKLDEWKGELWELCSIGIPWNDRETNDAIVFGYLVAWFLGEF-AAQFDPQPAVVAHFHEWQA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636 167 GMGALYIQEAVPEIGTIFTTHATSIGRSIAGNNKPLYDYLFAYNGDQMAQELNMQSKHSIEKQTAHYVDCFTTVSQITNN 246
Cdd:cd03793  160 GVGLILCRKRKVDVATIFTTHATLLGRYLCAGSVDFYNNLDSFDVDKEAGKRGIYHRYCIERAAAHCAHVFTTVSEITAY 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636 247 ECKELLDKPADVVLMNGFEddfVPKGSTFTgKRKRARALMLNVANKLL-GTNMG------DDTLIIGTSGRYEFKNKGID 319
Cdd:cd03793  240 EAEHLLKRKPDIVTPNGLN---VVKFSAMH-EFQNLHAQSKEKINEFVrGHFYGhldfdlDKTLYFFTAGRYEFSNKGAD 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636 320 VFLESLNRLN---RDKNLHKNVLAFI---------NVPSWVG--------DPREDLQERLkSKEKFDT--------PLEV 371
Cdd:cd03793  316 MFIESLARLNyllKVNGSETTVVAFIimpaktnnfNVESLKGqavtkqlkDTVNTVKEKI-GKRIFESclkgklpdPEEL 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636 372 ----------------------PFITHWLHNMTHDQVLDMLKYLGMGNRPGDKVKVIFVPCYLDGRDGIMNKEYYDILLG 429
Cdd:cd03793  395 lskedlvmlkrrifalqrqslpPIVTHNMLDDANDPILNHIRRIQLFNSPEDRVKVIFHPEFLSSTNPLLGLDYEEFVRG 474
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636 430 QDLSVYASYYEPWGYTPLESVAFHVPTITTDLAGFGLWVnslknQHGIND----GVEVLHRSDYNYSEVADGIKDTITLF 505
Cdd:cd03793  475 CHLGVFPSYYEPWGYTPAECTVMGIPSITTNLSGFGCFM-----EEHIEDpksyGIYIVDRRFKSPDESVQQLTQYMYEF 549
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|
gi 491925636 506 ADKSEKEIKEIRKRAAEVAEQALWKHFIQYYYEAYDIALC 545
Cdd:cd03793  550 CQQSRRQRIIQRNRTERLSDLLDWRYLGRFYRKARQLALR 589
Glycogen_syn pfam05693
Glycogen synthase; This family consists of the eukaryotic glycogen synthase proteins GYS1, ...
13-544 3.94e-75

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: 250.45  E-value: 3.94e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636   13 ESSWEVCNKVGGIYTVLSTRANTLQEKFRDRIFFIGP---DVWQGKENPLFIESDNLCAAWKkhAFEKDELSVRVGRWNI 89
Cdd:pfam05693   1 EVAWEVANKVGGIYTVLRSKAPVTTEEYGDNYCLIGPykeHKARTEVEELEPENPALRAAVD--SMRSRGCKIHYGRWLI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636   90 PGEPIVILVDFQPFFEKKDDIYTDMWNRFQVDSLHAYGDYDEASMFSYAAGKVVESFyRYNLTETDKVVYQAHEWMTGMG 169
Cdd:pfam05693  79 EGAPRVILFDLGSAAWKLNEWKGELWEQCGIGIPHHDIETNDAIILGFLVAWFLGEF-REHATSTPAVVAHFHEWQAGVG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636  170 ALYIQEAVPEIGTIFTTHATSIGRSIAGNNKPLYDYLFAYNGDQMAQELNMQSKHSIEKQTAHYVDCFTTVSQITNNECK 249
Cdd:pfam05693 158 LPLTRKRKLDIATVFTTHATLLGRYLCAGGVDFYNNLDKFDVDAEAGKRQIYHRYCLERAAAHTAHVFTTVSEITALEAE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636  250 ELLDKPADVVLMNGFEddfVPKGST---FTGKRKRARAlmlNVANKLLGTNMG------DDTLIIGTSGRYEFKNKGIDV 320
Cdd:pfam05693 238 HLLKRKPDVVTPNGLN---VKKFSAvheFQNLHAQNKE---KINDFVRGHFYGhldfdlDKTLYFFIAGRYEFSNKGADM 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636  321 FLESLNRLNRDKNLHKN---VLAFI---------NVPSWVG--------DPREDLQERLkSKEKFDTPLE---------- 370
Cdd:pfam05693 312 FIESLARLNHRLKTTGSkvtVVAFLimpaktnsfNVESLKGqavikqlrDTVNRVKEKV-GKRIFDICLQghlpemdell 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636  371 --------------------VPFITHWLHNMTHDQVLDMLKYLGMGNRPGDKVKVIFVPCYLDGRDGIMNKEYYDILLGQ 430
Cdd:pfam05693 391 dsddlvllkrcifalqrqslPPVVTHNMIDDANDPILNSIRRVGLFNSPSDRVKVVFHPEFLSSTNPLLGLDYEEFVRGC 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636  431 DLSVYASYYEPWGYTPLESVAFHVPTITTDLAGFGLWVNSLKNQHGiNDGVEVLHRSDYNYSEVADGIKDTITLFADKSE 510
Cdd:pfam05693 471 HLGVFPSYYEPWGYTPAECTVMGIPSVTTNLSGFGCFMEEHIEDPK-DYGIYIVDRRFKSPDDSVQQLTQFMYEFCQQSR 549
                         570       580       590
                  ....*....|....*....|....*....|....
gi 491925636  511 KEIKEIRKRAAEVAEQALWKHFIQYYYEAYDIAL 544
Cdd:pfam05693 550 RQRIIQRNRTERLSDLLDWKRLGRYYRKARQLAL 583
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
431-544 6.74e-08

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 51.14  E-value: 6.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636 431 DLSVYASYYEPWGYTPLESVAFHVPTITTDLAGFglwvnslknQHGINDGVEVLHRSDYNYSEVADGIkdtITLFADksE 510
Cdd:COG0438   22 DVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGL---------PEVIEDGETGLLVPPGDPEALAEAI---LRLLED--P 87
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 491925636 511 KEIKEIRKRAAEVAEQAL-WKHFIQYYYEAYDIAL 544
Cdd:COG0438   88 ELRRRLGEAARERAEERFsWEAIAERLLALYEELL 122
 
Name Accession Description Interval E-value
GT3_GSY2-like cd03793
glycogen synthase GSY2 and similar proteins; Glycogen synthase, which is most closely related ...
10-545 1.51e-81

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: 266.16  E-value: 1.51e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636  10 YIFESSWEVCNKVGGIYTVLSTRANTLQEKFRDRIFFIGP---DVWQGKENPLFIESDNLCAAWKkhAFEKDELSVRVGR 86
Cdd:cd03793    3 FLFEVAWEVANKVGGIYTVIKSKAPVTVEEYGDNYCLIGPyneATARTEVEILEPGNRPLRAALQ--SMRSRGIKVHFGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636  87 WNIPGEPIVILVDFQPFFEKKDDIYTDMWNRFQVDSLHAYGDYDEASMFSYAAGKVVESFyRYNLTETDKVVYQAHEWMT 166
Cdd:cd03793   81 WLIEGYPKVILFDIGSAAWKLDEWKGELWELCSIGIPWNDRETNDAIVFGYLVAWFLGEF-AAQFDPQPAVVAHFHEWQA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636 167 GMGALYIQEAVPEIGTIFTTHATSIGRSIAGNNKPLYDYLFAYNGDQMAQELNMQSKHSIEKQTAHYVDCFTTVSQITNN 246
Cdd:cd03793  160 GVGLILCRKRKVDVATIFTTHATLLGRYLCAGSVDFYNNLDSFDVDKEAGKRGIYHRYCIERAAAHCAHVFTTVSEITAY 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636 247 ECKELLDKPADVVLMNGFEddfVPKGSTFTgKRKRARALMLNVANKLL-GTNMG------DDTLIIGTSGRYEFKNKGID 319
Cdd:cd03793  240 EAEHLLKRKPDIVTPNGLN---VVKFSAMH-EFQNLHAQSKEKINEFVrGHFYGhldfdlDKTLYFFTAGRYEFSNKGAD 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636 320 VFLESLNRLN---RDKNLHKNVLAFI---------NVPSWVG--------DPREDLQERLkSKEKFDT--------PLEV 371
Cdd:cd03793  316 MFIESLARLNyllKVNGSETTVVAFIimpaktnnfNVESLKGqavtkqlkDTVNTVKEKI-GKRIFESclkgklpdPEEL 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636 372 ----------------------PFITHWLHNMTHDQVLDMLKYLGMGNRPGDKVKVIFVPCYLDGRDGIMNKEYYDILLG 429
Cdd:cd03793  395 lskedlvmlkrrifalqrqslpPIVTHNMLDDANDPILNHIRRIQLFNSPEDRVKVIFHPEFLSSTNPLLGLDYEEFVRG 474
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636 430 QDLSVYASYYEPWGYTPLESVAFHVPTITTDLAGFGLWVnslknQHGIND----GVEVLHRSDYNYSEVADGIKDTITLF 505
Cdd:cd03793  475 CHLGVFPSYYEPWGYTPAECTVMGIPSITTNLSGFGCFM-----EEHIEDpksyGIYIVDRRFKSPDESVQQLTQYMYEF 549
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|
gi 491925636 506 ADKSEKEIKEIRKRAAEVAEQALWKHFIQYYYEAYDIALC 545
Cdd:cd03793  550 CQQSRRQRIIQRNRTERLSDLLDWRYLGRFYRKARQLALR 589
Glycogen_syn pfam05693
Glycogen synthase; This family consists of the eukaryotic glycogen synthase proteins GYS1, ...
13-544 3.94e-75

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: 250.45  E-value: 3.94e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636   13 ESSWEVCNKVGGIYTVLSTRANTLQEKFRDRIFFIGP---DVWQGKENPLFIESDNLCAAWKkhAFEKDELSVRVGRWNI 89
Cdd:pfam05693   1 EVAWEVANKVGGIYTVLRSKAPVTTEEYGDNYCLIGPykeHKARTEVEELEPENPALRAAVD--SMRSRGCKIHYGRWLI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636   90 PGEPIVILVDFQPFFEKKDDIYTDMWNRFQVDSLHAYGDYDEASMFSYAAGKVVESFyRYNLTETDKVVYQAHEWMTGMG 169
Cdd:pfam05693  79 EGAPRVILFDLGSAAWKLNEWKGELWEQCGIGIPHHDIETNDAIILGFLVAWFLGEF-REHATSTPAVVAHFHEWQAGVG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636  170 ALYIQEAVPEIGTIFTTHATSIGRSIAGNNKPLYDYLFAYNGDQMAQELNMQSKHSIEKQTAHYVDCFTTVSQITNNECK 249
Cdd:pfam05693 158 LPLTRKRKLDIATVFTTHATLLGRYLCAGGVDFYNNLDKFDVDAEAGKRQIYHRYCLERAAAHTAHVFTTVSEITALEAE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636  250 ELLDKPADVVLMNGFEddfVPKGST---FTGKRKRARAlmlNVANKLLGTNMG------DDTLIIGTSGRYEFKNKGIDV 320
Cdd:pfam05693 238 HLLKRKPDVVTPNGLN---VKKFSAvheFQNLHAQNKE---KINDFVRGHFYGhldfdlDKTLYFFIAGRYEFSNKGADM 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636  321 FLESLNRLNRDKNLHKN---VLAFI---------NVPSWVG--------DPREDLQERLkSKEKFDTPLE---------- 370
Cdd:pfam05693 312 FIESLARLNHRLKTTGSkvtVVAFLimpaktnsfNVESLKGqavikqlrDTVNRVKEKV-GKRIFDICLQghlpemdell 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636  371 --------------------VPFITHWLHNMTHDQVLDMLKYLGMGNRPGDKVKVIFVPCYLDGRDGIMNKEYYDILLGQ 430
Cdd:pfam05693 391 dsddlvllkrcifalqrqslPPVVTHNMIDDANDPILNSIRRVGLFNSPSDRVKVVFHPEFLSSTNPLLGLDYEEFVRGC 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636  431 DLSVYASYYEPWGYTPLESVAFHVPTITTDLAGFGLWVNSLKNQHGiNDGVEVLHRSDYNYSEVADGIKDTITLFADKSE 510
Cdd:pfam05693 471 HLGVFPSYYEPWGYTPAECTVMGIPSVTTNLSGFGCFMEEHIEDPK-DYGIYIVDRRFKSPDDSVQQLTQFMYEFCQQSR 549
                         570       580       590
                  ....*....|....*....|....*....|....
gi 491925636  511 KEIKEIRKRAAEVAEQALWKHFIQYYYEAYDIAL 544
Cdd:pfam05693 550 RQRIIQRNRTERLSDLLDWKRLGRYYRKARQLAL 583
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
158-540 9.47e-10

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: 60.63  E-value: 9.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636 158 VYQAHEWMTgMGALYIQEAVPEIGTIFTTHATSIGRSiagnnkplydylfayngdqmaQELNMQSKHSIEKQTA--HYVD 235
Cdd:cd03801   85 VVHAHGLLA-ALLAALLALLLGAPLVVTLHGAEPGRL---------------------LLLLAAERRLLARAEAllRRAD 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636 236 CFTTVSQITNNECKELLDKPAD--VVLMNGFEDDFvpkgstFTGKRKRARALmlnvankllgtnmGDDTLIIGTSGRYeF 313
Cdd:cd03801  143 AVIAVSEALRDELRALGGIPPEkiVVIPNGVDLER------FSPPLRRKLGI-------------PPDRPVLLFVGRL-S 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636 314 KNKGIDVFLESLNRLnrdKNLHKNVLAFInvpswVGDPREdLQERLKSKEKfdtplevpfithwlhnmthdqvldmlkyl 393
Cdd:cd03801  203 PRKGVDLLLEALAKL---LRRGPDVRLVI-----VGGDGP-LRAELEELEL----------------------------- 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636 394 gmgnrpGDKVKVIFVPcyldgrdGIMNKEYYDILLGQDLSVYASYYEPWGYTPLESVAFHVPTITTDLAGFGlWVnslkn 473
Cdd:cd03801  245 ------GLGDRVRFLG-------FVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLP-EV----- 305
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491925636 474 qhgINDGVEVLHRSDYNYSEVADGIkdtITLFADKSekEIKEIRKRAAEVAEQAL-WKHFIQYYYEAY 540
Cdd:cd03801  306 ---VEDGEGGLVVPPDDVEALADAL---LRLLADPE--LRARLGRAARERVAERFsWERVAERLLDLY 365
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
431-544 6.74e-08

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 51.14  E-value: 6.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636 431 DLSVYASYYEPWGYTPLESVAFHVPTITTDLAGFglwvnslknQHGINDGVEVLHRSDYNYSEVADGIkdtITLFADksE 510
Cdd:COG0438   22 DVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGL---------PEVIEDGETGLLVPPGDPEALAEAI---LRLLED--P 87
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 491925636 511 KEIKEIRKRAAEVAEQAL-WKHFIQYYYEAYDIAL 544
Cdd:COG0438   88 ELRRRLGEAARERAEERFsWEAIAERLLALYEELL 122
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
301-519 4.42e-06

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: 46.88  E-value: 4.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636  301 DTLIIGTSGRYEfKNKGIDVFLESLNRLnrDKNLHKNVLAFinvpswVGDPREDLQERLKSKEKFdtplevpfithwlhn 380
Cdd:pfam00534   1 KKKIILFVGRLE-PEKGLDLLIKAFALL--KEKNPNLKLVI------AGDGEEEKRLKKLAEKLG--------------- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636  381 mthdqvldmlkylgmgnrPGDKVKVIFvpcyldgrdGIMNKEYYDILLGQDLSVYASYYEPWGYTPLESVAFHVPTITTD 460
Cdd:pfam00534  57 ------------------LGDNVIFLG---------FVSDEDLPELLKIADVFVLPSRYEGFGIVLLEAMACGLPVIASD 109
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 491925636  461 LAGFGlwvnslknqHGINDGVEVLHRSDYNYSEVADGIKDTITLfADKSEKEIKEIRKR 519
Cdd:pfam00534 110 VGGPP---------EVVKDGETGFLVKPNNAEALAEAIDKLLED-EELRERLGENARKR 158
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
304-464 2.02e-04

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 41.73  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636  304 IIGTSGRYEFKNKGIDVFLESLNRL-NRDKNLHknvlaFInvpsWVGD-PREDLQERLKSKEKfdtplEVPFithwlhnm 381
Cdd:pfam13692   3 VILFVGRLHPNVKGVDYLLEAVPLLrKRDNDVR-----LV----IVGDgPEEELEELAAGLED-----RVIF-------- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636  382 tHDQVLDMLKYLGMGnrpgdkvkvifvpcyldgrdgimnkeyydillgqDLSVYASYYEPWGYTPLESVAFHVPTITTDL 461
Cdd:pfam13692  61 -TGFVEDLAELLAAA----------------------------------DVFVLPSLYEGFGLKLLEAMAAGLPVVATDV 105

                  ...
gi 491925636  462 AGF 464
Cdd:pfam13692 106 GGI 108
Glyco_transf_5 pfam08323
Starch synthase catalytic domain;
15-241 3.06e-03

Starch synthase catalytic domain;


Pssm-ID: 400563 [Multi-domain]  Cd Length: 239  Bit Score: 39.62  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636   15 SWEVCN--KVGGIYTVLSTRANTLQEKfrdriffiGPDV-----WQGKENPLFIESDNLCAAWKKHAFEKDELSVRVGRW 87
Cdd:pfam08323   5 ASEVAPfaKTGGLADVVGALPKALAAL--------GHDVrvimpRYGNIPEERNQLEDVIRLSVAAGVPVRPLTVGVARL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636   88 NIPGEPiVILVDFQPFFEKkDDIYTDmwnrfqvdSLHAYGDYDE-ASMFSYAAGKVVEsfyryNLTETDKVVyQAHEWMT 166
Cdd:pfam08323  77 ELDGVD-VYFLDNPDYFDR-PGLYGD--------DGRDYEDNAErFAFFSRAALELAK-----KLGWIPDII-HCHDWHT 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491925636  167 GMGALYIQEAVPE-----IGTIFTTHATSIGRSIAGNNKP---LYDYLFAYNGDQMAQELNMqSKHSIekQTAHYVdcfT 238
Cdd:pfam08323 141 ALVPAYLKEAYADdpfknIKTVFTIHNLAYQGRFPADLLDllgLPPEDFNLDGLEFYGQINF-LKAGI--VYADAV---T 214

                  ...
gi 491925636  239 TVS 241
Cdd:pfam08323 215 TVS 217
 
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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