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Conserved domains on  [gi|1277773221|gb|PIT90149|]
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glycosyl transferase [Candidatus Kuenenbacteria bacterium CG10_big_fil_rev_8_21_14_0_10_36_11]

Protein Classification

GT1_ecORF704_like and LanC_like domain-containing protein( domain architecture ID 10133635)

GT1_ecORF704_like and LanC_like domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
31-404 2.34e-93

mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.


:

Pssm-ID: 340849 [Multi-domain]  Cd Length: 370  Bit Score: 295.83  E-value: 2.34e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221  31 ILYMSSYPPRECGIATYTRDLVKAIDRKfSPYLESKILAMNENGssIYNYCSKVKYQINQTEIEDYINVARKINKDDsIR 110
Cdd:cd03822     2 IAVLGTLPPRKCGIATYTDDLVEGLRKG-GPVVIVVIVSPQDEI--LKDDDFEVPNEIKSWNSNEYFRLLDHLNFKK-PD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 111 LINIQHEFGLFGGEWGDYLLAFLEVVKKPVVVTFHSLI--PNPTPKLKKVIQAIAKRCEKIIVMADMAIEYYECDYGLKK 188
Cdd:cd03822    78 VVHIQHEFGIFGGKYGLYALGLLLHLRIPVITTLHTVLdlSDPGKQALKVLFRIATLSERVVVMAPISRFLLVRIKLIPA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 189 SQLVVIPHGTPVIEPYSSEASKKKLGFEGKMLLSTFGLLNQGKGVEYVIKALPKIIEKHPEVLYLIIGETHPVVRKYEGE 268
Cdd:cd03822   158 VNIEVIPHGVPEVPQDPTTALKRLLLPEGKKVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGELHPSLARYEGE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 269 KYRNKLIKLsqkLNLTNYVKFYNKYLTLEEIINYLKSTDIYLCPPLAVNQITSGTLAYALSAGKAIVSTPFLHAKEVLQQ 348
Cdd:cd03822   238 RYRKAAIEE---LGLQDHVDFHNNFLPEEEVPRYISAADVVVLPYLNTEQSSSGTLSYAIACGKPVISTPLRHAEELLAD 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1277773221 349 GRGEIVGFRDPTGISRVVNALIEKPETRKSMEKQSYLYGQKTSWPIAAIAHLNVFK 404
Cdd:cd03822   315 GRGVLVPFDDPSAIAEAILRLLEDDERRQAIAERAYAYARAMTWESIADRYLRLFN 370
YyaL super family cl27897
Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin ...
607-700 5.41e-07

Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin glycosidase-like domains [General function prediction only];


The actual alignment was detected with superfamily member COG1331:

Pssm-ID: 440942 [Multi-domain]  Cd Length: 672  Bit Score: 52.93  E-value: 5.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 607 ITYDNGRLPEALFLAYEVTKNKLYLKIAKESLDFL-SSLVILNDKLVligqRGWYNHKGK-RAFFDqqplDAASMVQVFL 684
Cdd:COG1331   411 LTSWNGLMIAALAEAGRVLGDPEYLEAAERAADFIlDNLWDPDGRLL----RSYRDGEAGiPGFLE----DYAFLIEALL 482
                          90
                  ....*....|....*.
gi 1277773221 685 RAYQVTDEKKYQHKAL 700
Cdd:COG1331   483 ALYEATGDPRWLERAL 498
LanC_like super family cl04955
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the ...
518-748 4.39e-05

Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the cyclase enzyme of the lanthionine synthetase. Lanthionine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as a precursor peptide and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans), in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. A related domain is also present in LanM and other pro- and eukaryotic proteins with poorly characterized functions.


The actual alignment was detected with superfamily member cd04434:

Pssm-ID: 471159 [Multi-domain]  Cd Length: 351  Bit Score: 46.34  E-value: 4.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 518 ALWAAGFVMNSNLPENIKKTAKFIFDKAIKNIAKLKSP-----RGQAFSLIGLYYYYEAYPNPEIRQKIILLAERLVKFY 592
Cdd:cd04434    57 LLWALLELYEDLGDEKLLDALLDLLDDIALEAKEVWWSgndliLGDAGIILYLLYAAEKTGDEKYKELAAKIGDFLLQAA 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 593 QKEKTKDWCWFEQTITYDN---GRLPEALFLA--YEVTKNKLYLKIAKESLDFLSSLVILNDKLVLIGQ--------RGW 659
Cdd:cd04434   137 EELDNGGNWGLPKGSIYPGfahGTAGIAYALArlYEETGDEDFLDAAKEGAEYLEAIAVGDEDGFLIPLpdekdlfyLGW 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 660 --------------YNHKGKRAFFD-----------QQPLD------------AASMVQVFLRAYQVTDEKKYQHKA--- 699
Cdd:cd04434   217 chgpagtallfyelYKATGDLDLADellegiiktgaPEKLSpgfwnnlclchgTAGVLEHLLYVYRLTGDEREYAKRlad 296
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1277773221 700 -LLAFSWFlgiNSINQPVYDQTTSGCFDGLLPDcvnLNQGAESTISYLLS 748
Cdd:cd04434   297 kLLGRATR---NGEGLRWYQAWTGPGRVDASLG---LMVGAAGIASALLK 340
 
Name Accession Description Interval E-value
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
31-404 2.34e-93

mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.


Pssm-ID: 340849 [Multi-domain]  Cd Length: 370  Bit Score: 295.83  E-value: 2.34e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221  31 ILYMSSYPPRECGIATYTRDLVKAIDRKfSPYLESKILAMNENGssIYNYCSKVKYQINQTEIEDYINVARKINKDDsIR 110
Cdd:cd03822     2 IAVLGTLPPRKCGIATYTDDLVEGLRKG-GPVVIVVIVSPQDEI--LKDDDFEVPNEIKSWNSNEYFRLLDHLNFKK-PD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 111 LINIQHEFGLFGGEWGDYLLAFLEVVKKPVVVTFHSLI--PNPTPKLKKVIQAIAKRCEKIIVMADMAIEYYECDYGLKK 188
Cdd:cd03822    78 VVHIQHEFGIFGGKYGLYALGLLLHLRIPVITTLHTVLdlSDPGKQALKVLFRIATLSERVVVMAPISRFLLVRIKLIPA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 189 SQLVVIPHGTPVIEPYSSEASKKKLGFEGKMLLSTFGLLNQGKGVEYVIKALPKIIEKHPEVLYLIIGETHPVVRKYEGE 268
Cdd:cd03822   158 VNIEVIPHGVPEVPQDPTTALKRLLLPEGKKVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGELHPSLARYEGE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 269 KYRNKLIKLsqkLNLTNYVKFYNKYLTLEEIINYLKSTDIYLCPPLAVNQITSGTLAYALSAGKAIVSTPFLHAKEVLQQ 348
Cdd:cd03822   238 RYRKAAIEE---LGLQDHVDFHNNFLPEEEVPRYISAADVVVLPYLNTEQSSSGTLSYAIACGKPVISTPLRHAEELLAD 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1277773221 349 GRGEIVGFRDPTGISRVVNALIEKPETRKSMEKQSYLYGQKTSWPIAAIAHLNVFK 404
Cdd:cd03822   315 GRGVLVPFDDPSAIAEAILRLLEDDERRQAIAERAYAYARAMTWESIADRYLRLFN 370
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
231-384 3.40e-17

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: 79.24  E-value: 3.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 231 KGVEYVIKALPKIIEKHPEVLYLIIGEthpvvrkyegEKYRNKLIKLSQKLNLTNYVKFYnKYLTLEEIINYLKSTDIYL 310
Cdd:pfam00534  15 KGLDLLIKAFALLKEKNPNLKLVIAGD----------GEEEKRLKKLAEKLGLGDNVIFL-GFVSDEDLPELLKIADVFV 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277773221 311 CP----PLAVnqitsgTLAYALSAGKAIVSTPFLHAKEVLQQG-RGEIVGFRDPTGISRVVNALIEKPETRKSMEKQSY 384
Cdd:pfam00534  84 LPsryeGFGI------VLLEAMACGLPVIASDVGGPPEVVKDGeTGFLVKPNNAEALAEAIDKLLEDEELRERLGENAR 156
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
296-408 1.31e-08

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 53.84  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 296 LEEIIN-YLKSTDIYLCPPLAVNqiTSGTLAYALSAGKAIVSTPFLHAKEVLQQGR-GEIVGFRDPTGISRVVNALIEKP 373
Cdd:COG0438    10 LDLLLEaLLAAADVFVLPSRSEG--FGLVLLEAMAAGLPVIATDVGGLPEVIEDGEtGLLVPPGDPEALAEAILRLLEDP 87
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1277773221 374 ETRKSMEKQSYLYGQKT-SWPIAAIAHLNVFKKIIN 408
Cdd:COG0438    88 ELRRRLGEAARERAEERfSWEAIAERLLALYEELLA 123
YyaL COG1331
Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin ...
607-700 5.41e-07

Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin glycosidase-like domains [General function prediction only];


Pssm-ID: 440942 [Multi-domain]  Cd Length: 672  Bit Score: 52.93  E-value: 5.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 607 ITYDNGRLPEALFLAYEVTKNKLYLKIAKESLDFL-SSLVILNDKLVligqRGWYNHKGK-RAFFDqqplDAASMVQVFL 684
Cdd:COG1331   411 LTSWNGLMIAALAEAGRVLGDPEYLEAAERAADFIlDNLWDPDGRLL----RSYRDGEAGiPGFLE----DYAFLIEALL 482
                          90
                  ....*....|....*.
gi 1277773221 685 RAYQVTDEKKYQHKAL 700
Cdd:COG1331   483 ALYEATGDPRWLERAL 498
LanC_like cd04434
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the ...
518-748 4.39e-05

Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the cyclase enzyme of the lanthionine synthetase. Lanthionine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as a precursor peptide and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans), in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. A related domain is also present in LanM and other pro- and eukaryotic proteins with poorly characterized functions.


Pssm-ID: 271198 [Multi-domain]  Cd Length: 351  Bit Score: 46.34  E-value: 4.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 518 ALWAAGFVMNSNLPENIKKTAKFIFDKAIKNIAKLKSP-----RGQAFSLIGLYYYYEAYPNPEIRQKIILLAERLVKFY 592
Cdd:cd04434    57 LLWALLELYEDLGDEKLLDALLDLLDDIALEAKEVWWSgndliLGDAGIILYLLYAAEKTGDEKYKELAAKIGDFLLQAA 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 593 QKEKTKDWCWFEQTITYDN---GRLPEALFLA--YEVTKNKLYLKIAKESLDFLSSLVILNDKLVLIGQ--------RGW 659
Cdd:cd04434   137 EELDNGGNWGLPKGSIYPGfahGTAGIAYALArlYEETGDEDFLDAAKEGAEYLEAIAVGDEDGFLIPLpdekdlfyLGW 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 660 --------------YNHKGKRAFFD-----------QQPLD------------AASMVQVFLRAYQVTDEKKYQHKA--- 699
Cdd:cd04434   217 chgpagtallfyelYKATGDLDLADellegiiktgaPEKLSpgfwnnlclchgTAGVLEHLLYVYRLTGDEREYAKRlad 296
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1277773221 700 -LLAFSWFlgiNSINQPVYDQTTSGCFDGLLPDcvnLNQGAESTISYLLS 748
Cdd:cd04434   297 kLLGRATR---NGEGLRWYQAWTGPGRVDASLG---LMVGAAGIASALLK 340
LanC_SerThrkinase cd04791
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ...
563-696 2.44e-04

Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of this subgroup lack the zinc binding site and the active site residues, and therefore are most likely inactive. The function of this domain is unknown.


Pssm-ID: 271199 [Multi-domain]  Cd Length: 327  Bit Score: 43.80  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 563 IGLY--YYYEAYPNPEIRQKIILLAERLVKFYQK-EKTKDWCWF-EQTITYDNGRLPEALFL--AYEVTKNKLYLKIAKE 636
Cdd:cd04791    91 IGLAllHLARATGDPEFLERAARIAERLAARLREdDPGVYWNDAgAVRAGLLHGWSGIALFLlrLYEATGDPAYLDLAER 170
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277773221 637 SLDF-LSSLVILNDKLVligqrgWYNHKGKRAFfdqqP-LD--AASMVQVFLRAYQVTDEKKYQ 696
Cdd:cd04791   171 ALRKdLARCVEDDDGAL------LQVDEGNRLL----PyLCsgSAGIGLVLLRYLRHRGDDRYR 224
YihS COG2942
Mannose or cellobiose epimerase, N-acyl-D-glucosamine 2-epimerase family [Carbohydrate ...
557-641 3.32e-03

Mannose or cellobiose epimerase, N-acyl-D-glucosamine 2-epimerase family [Carbohydrate transport and metabolism];


Pssm-ID: 442185  Cd Length: 380  Bit Score: 40.63  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 557 GQAFSLIGLYYYYEAYPNPEIRQKIILLAERLVKF--------YQKEKTKDWCWFEQTITYD-NGRLPEALFLAYEVTKN 627
Cdd:COG2942   110 GHAFALLALAEAYRATGDPEALELAKETFELLERRfwdpehggYAEAFDRDWSPLRPYRGQNaHMHLLEALLALYEATGD 189
                          90
                  ....*....|....
gi 1277773221 628 KLYLKIAKESLDFL 641
Cdd:COG2942   190 ERWLERAEEIADLI 203
 
Name Accession Description Interval E-value
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
31-404 2.34e-93

mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.


Pssm-ID: 340849 [Multi-domain]  Cd Length: 370  Bit Score: 295.83  E-value: 2.34e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221  31 ILYMSSYPPRECGIATYTRDLVKAIDRKfSPYLESKILAMNENGssIYNYCSKVKYQINQTEIEDYINVARKINKDDsIR 110
Cdd:cd03822     2 IAVLGTLPPRKCGIATYTDDLVEGLRKG-GPVVIVVIVSPQDEI--LKDDDFEVPNEIKSWNSNEYFRLLDHLNFKK-PD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 111 LINIQHEFGLFGGEWGDYLLAFLEVVKKPVVVTFHSLI--PNPTPKLKKVIQAIAKRCEKIIVMADMAIEYYECDYGLKK 188
Cdd:cd03822    78 VVHIQHEFGIFGGKYGLYALGLLLHLRIPVITTLHTVLdlSDPGKQALKVLFRIATLSERVVVMAPISRFLLVRIKLIPA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 189 SQLVVIPHGTPVIEPYSSEASKKKLGFEGKMLLSTFGLLNQGKGVEYVIKALPKIIEKHPEVLYLIIGETHPVVRKYEGE 268
Cdd:cd03822   158 VNIEVIPHGVPEVPQDPTTALKRLLLPEGKKVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGELHPSLARYEGE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 269 KYRNKLIKLsqkLNLTNYVKFYNKYLTLEEIINYLKSTDIYLCPPLAVNQITSGTLAYALSAGKAIVSTPFLHAKEVLQQ 348
Cdd:cd03822   238 RYRKAAIEE---LGLQDHVDFHNNFLPEEEVPRYISAADVVVLPYLNTEQSSSGTLSYAIACGKPVISTPLRHAEELLAD 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1277773221 349 GRGEIVGFRDPTGISRVVNALIEKPETRKSMEKQSYLYGQKTSWPIAAIAHLNVFK 404
Cdd:cd03822   315 GRGVLVPFDDPSAIAEAILRLLEDDERRQAIAERAYAYARAMTWESIADRYLRLFN 370
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
32-404 3.26e-33

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: 131.51  E-value: 3.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221  32 LYMSSYPPRECGIATYTRDLVKAIDRK------FSPYLESKILAMNENGSSIYNYCSKVKYQinqteieDYINVARKINK 105
Cdd:cd03801     4 LLSPELPPPVGGAERHVRELARALAARghdvtvLTPADPGEPPEELEDGVIVPLLPSLAALL-------RARRLLRELRP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 106 DDSIRLINIQHEFGLFGGEWGDYLLAFLevvKKPVVVTFHSLIPNPTPKL----KKVIQAIAKRCE---KIIVMADMAIE 178
Cdd:cd03801    77 LLRLRKFDVVHAHGLLAALLAALLALLL---GAPLVVTLHGAEPGRLLLLlaaeRRLLARAEALLRradAVIAVSEALRD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 179 YYECDYGLKKSQLVVIPHGTPvIEPYSSEASKKKLGFEGKMLLSTFGLLNQGKGVEYVIKALPKIIEKHPEVLYLIIGET 258
Cdd:cd03801   154 ELRALGGIPPEKIVVIPNGVD-LERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGD 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 259 HPvvrkyegekYRNKLIKLsqKLNLTNYVKFYNkYLTLEEIINYLKSTDIYLCP------PLAVNQitsgtlayALSAGK 332
Cdd:cd03801   233 GP---------LRAELEEL--ELGLGDRVRFLG-FVPDEELPALYAAADVFVLPsryegfGLVVLE--------AMAAGL 292
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277773221 333 AIVSTPFLHAKEVLQQGR-GEIVGFRDPTGISRVVNALIEKPETRKSMEKQSYLYGQKT-SWPIAAIAHLNVFK 404
Cdd:cd03801   293 PVVATDVGGLPEVVEDGEgGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAERfSWERVAERLLDLYR 366
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
231-384 3.40e-17

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: 79.24  E-value: 3.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 231 KGVEYVIKALPKIIEKHPEVLYLIIGEthpvvrkyegEKYRNKLIKLSQKLNLTNYVKFYnKYLTLEEIINYLKSTDIYL 310
Cdd:pfam00534  15 KGLDLLIKAFALLKEKNPNLKLVIAGD----------GEEEKRLKKLAEKLGLGDNVIFL-GFVSDEDLPELLKIADVFV 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277773221 311 CP----PLAVnqitsgTLAYALSAGKAIVSTPFLHAKEVLQQG-RGEIVGFRDPTGISRVVNALIEKPETRKSMEKQSY 384
Cdd:pfam00534  84 LPsryeGFGI------VLLEAMACGLPVIASDVGGPPEVVKDGeTGFLVKPNNAEALAEAIDKLLEDEELRERLGENAR 156
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
43-381 1.24e-14

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: 75.86  E-value: 1.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221  43 GIATYTRDLVKAIDRKFspyLESKILAMNENGssiyNYCSKVKYQINQTEIEDYINVARKINKDDSIRLIN---IQHEFG 119
Cdd:cd03811    13 GAERVLLNLANALDKRG---YDVTLVLLRDEG----DLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLKrilKRAKPD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 120 LF--GGEWGDYLLAFLEVVKKPVVVTFHSLIPNPTPKLKKVIQAIA--KRCEKIIV----MADMAIEYYecdyGLKKSQL 191
Cdd:cd03811    86 VVisFLGFATYIVAKLAAARSKVIAWIHSSLSKLYYLKKKLLLKLKlyKKADKIVCvskgIKEDLIRLG----PSPPEKI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 192 VVIPHGTPV--IEPySSEASKKKLGFEGKMLLsTFGLLNQGKGVEYVIKALPKIIEKHPEVLYLIIGethpvvrkyEGEK 269
Cdd:cd03811   162 EVIYNPIDIdrIRA-LAKEPILNEPEDGPVIL-AVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILG---------DGPL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 270 yRNKLIKLSQKLNLTNYVKFY----NKYltleeiiNYLKSTDIYLCP------PLavnqitsgTLAYALSAGKAIVSTPF 339
Cdd:cd03811   231 -REELEKLAKELGLAERVIFLgfqsNPY-------PYLKKADLFVLSsryegfPN--------VLLEAMALGTPVVSTDC 294
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1277773221 340 LHAKEVLQQGR-GEIVGFRDPTGISRVVNALIEKPETRKSMEK 381
Cdd:cd03811   295 PGPREILDDGEnGLLVPDGDAAALAGILAALLQKKLDAALRER 337
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
139-385 1.82e-14

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: 75.47  E-value: 1.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 139 PVVVTFHSLIPnPTPKLKKVIQAIAKRCEKIIVMADMAIEYYECDYGLKKSQLVVIPHG--TPVIEPYSSEASKKKLGF- 215
Cdd:cd03819   101 PLVTTVHGSYL-ATYHPKDFALAVRARGDRVIAVSELVRDHLIEALGVDPERIRVIPNGvdTDRFPPEAEAEERAQLGLp 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 216 EGKMLLSTFGLLNQGKGVEYVIKALPKIiEKHPEVLYLIIGETHPvvrkyegekyRNKLIKLSQKLNLTNYVKF--YNky 293
Cdd:cd03819   180 EGKPVVGYVGRLSPEKGWLLLVDAAAEL-KDEPDFRLLVAGDGPE----------RDEIRRLVERLGLRDRVTFtgFR-- 246
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 294 ltlEEIINYLKSTDIYLCPPLavNQITSGTLAYALSAGKAIVSTPFLHAKEVLQQGR-GEIVGFRDPTGISRVVNALIEK 372
Cdd:cd03819   247 ---EDVPAALAASDVVVLPSL--HEEFGRVALEAMACGTPVVATDVGGAREIVVHGRtGLLVPPGDAEALADAIRAAKLL 321
                         250
                  ....*....|...
gi 1277773221 373 PETRKSMEKQSYL 385
Cdd:cd03819   322 PEAREKLQAAAAL 334
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
217-381 1.42e-13

Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.


Pssm-ID: 340829 [Multi-domain]  Cd Length: 350  Bit Score: 72.87  E-value: 1.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 217 GKMLLSTFGLLNQGKGVEYVIKALPKIIEKHPEVLYLIIGethpvvrkyEGEkYRNKLIKLSQKLNLTNYVKFYNkYLTL 296
Cdd:cd03799   173 GKIRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIG---------DGD-LKEQLQQLIQELNIGDCVKLLG-WKPQ 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 297 EEIINYLKSTDIYLCPPLAVNQ----ITSGTLAYALSAGKAIVSTPFLHAKEVLQQG-RGEIVGFRDPTGISRVVNALIE 371
Cdd:cd03799   242 EEIIEILDEADIFIAPSVTAADgdqdGPPNTLKEAMAMGLPVISTEHGGIPELVEDGvSGFLVPERDAEAIAEKLTYLIE 321
                         170
                  ....*....|
gi 1277773221 372 KPETRKSMEK 381
Cdd:cd03799   322 HPAIWPEMGK 331
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
231-371 3.47e-11

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 61.37  E-value: 3.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 231 KGVEYVIKALPKIIEKHPEVLYLIIGEthpvvrkYEGEKYRNKLIKLSQKLNLTNYVkfynkyltlEEIINYLKSTDIYL 310
Cdd:pfam13692  15 KGVDYLLEAVPLLRKRDNDVRLVIVGD-------GPEEELEELAAGLEDRVIFTGFV---------EDLAELLAAADVFV 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277773221 311 CP------PLAVNQitsgtlayALSAGKAIVSTPFLHAKEVLQQGRGEIVGFRDPTGISRVVNALIE 371
Cdd:pfam13692  79 LPslyegfGLKLLE--------AMAAGLPVVATDVGGIPELVDGENGLLVPPGDPEALAEAILRLLE 137
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
36-383 3.52e-11

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: 65.76  E-value: 3.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221  36 SYPPRECGIATYTRDLVKAIDRKfspYLESKILAMNENGSSIYNYCSKVKYQINQTEIEDYINVARKINKDDSIR----- 110
Cdd:cd03817     8 TYLPQVNGVATSVRNLARALEKR---GHEVYVITPSDPGAEDEEEVVRYRSFSIPIRKYHRQHIPFPFKKAVIDRikelg 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 111 --LINIQHEFGLFggewgdylLAFLEVVKK---PVVVTFHSL-------IPNPTPKLKKVIQAIAKR----CEKIIVMAD 174
Cdd:cd03817    85 pdIIHTHTPFSLG--------KLGLRIARKlkiPIVHTYHTMyedylhyIPKGKLLVKAVVRKLVRRfynhTDAVIAPSE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 175 MAIEYYEcDYGLKKsQLVVIPHGTP--VIEPYSSEASKKKLGF--EGKMLLSTfGLLNQGKGVEYVIKALPKIIEKhPEV 250
Cdd:cd03817   157 KIKDTLR-EYGVKG-PIEVIPNGIDldKFEKPLNTEERRKLGLppDEPILLYV-GRLAKEKNIDFLLRAFAELKKE-PNI 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 251 LYLIIGEthpvvrkyeGeKYRNKLIKLSQKLNLTNYVKFYNkYLTLEEIINYLKSTDIYLCPPLAVNQitsgTLAY--AL 328
Cdd:cd03817   233 KLVIVGD---------G-PEREELKELARELGLADKVIFTG-FVPREELPEYYKAADLFVFASTTETQ----GLVYleAM 297
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1277773221 329 SAGKAIVSTPFLHAKEVLQQGRGeivGFRDPTGISRVVNALIEKPETRKSMEKQS 383
Cdd:cd03817   298 AAGLPVVAAKDPAASELVEDGEN---GFLFEPNDETLAEKLLHLRENLELLRKLS 349
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
119-386 2.36e-10

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: 63.00  E-value: 2.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 119 GLFGGewgdylLAFLEVVKKPVVVTFHSL--IPNPTPKLKKVIQAI----AKRCEKIIVMADMAIEYYECDYGLKKSQLV 192
Cdd:cd03808    93 GILGR------LAARLAGVPKVIYTVHGLgfVFTEGKLLRLLYLLLeklaLLFTDKVIFVNEDDRDLAIKKGIIKKKKTV 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 193 VIPH-GTPVIE----PYSSEASKKKLGFEGKMLLStfgllnqgKGVEYVIKALPKIIEKHPEVLYLIIGETHPvvrkyeg 267
Cdd:cd03808   167 LIPGsGVDLDRfqysPESLPSEKVVFLFVARLLKD--------KGIDELIEAAKILKKKGPNVRFLLVGDGEL------- 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 268 ekyRNKLIKLSQKLNLTNYVKFYNKyltLEEIINYLKSTDIYLCP------PLAVNQitsgtlayALSAGKAIVSTPFLH 341
Cdd:cd03808   232 ---ENPSEILIEKLGLEGRIEFLGF---RSDVPELLAESDVFVLPsyreglPRSLLE--------AMAAGRPVITTDVPG 297
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1277773221 342 AKEVLQQGR-GEIVGFRDPTGISRVVNALIEKPETRKSMEKQSYLY 386
Cdd:cd03808   298 CRELVIDGVnGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKR 343
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
123-401 9.27e-10

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: 61.23  E-value: 9.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 123 GEWGDYLLAFLEVVKK---PVVVTFHSLIPNPTPKLKKVIQAIAK-RCEK--------IIVMADMaiEYYECDYGLKKSQ 190
Cdd:cd03821    98 GVWTYTSLAACKLARRrgiPYVVSPHGMLDPWALQQKHWKKRIALhLIERrnlnnaalVHFTSEQ--EADELRRFGLEPP 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 191 LVVIPHG--TPVIEPYSSEASKKKLGFEGKMLLsTFGLLNQGKGVEYVIKALPKIIEKHPEVLYLIIGethpvvrkyEGE 268
Cdd:cd03821   176 IAVIPNGvdIPEFDPGLRDRRKHNGLEDRRIIL-FLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAG---------PDD 245
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 269 KYRNKLIKLSQKLNLTNYVKFYNKyLTLEEIINYLKSTDIYLCP------PLAVnqitsgtlAYALSAGKAIVSTPFLHA 342
Cdd:cd03821   246 GAYPAFLQLQSSLGLGDRVTFTGP-LYGEAKWALYASADLFVLPsysenfGNVV--------AEALACGLPVVITDKCGL 316
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277773221 343 KEVLQQGRGEIVGFRDpTGISRVVNALIEKPETRKSME---KQSYLYGQKTSWPIAAIAHLN 401
Cdd:cd03821   317 SELVEAGCGVVVDPNV-SSLAEALAEALRDPADRKRLGemaRRARQVEENFSWEAVAGQLGE 377
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
36-382 1.31e-09

Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340826 [Multi-domain]  Cd Length: 355  Bit Score: 60.75  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221  36 SYPPRECGIATYTRDLVKAIDRKfspYLESKILAMNENGSSIYN-------YCSKVKYQINQTEIE-DYINVARKINKDD 107
Cdd:cd03795     8 FYYPDIGGIEQVIYDLAEGLKKK---GIEVDVLCFSKEKETPEKeengiriHRVKSFLNVASTPFSpSYIKRFKKLAKEY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 108 SIrlINIQHEFGLfggewGDyLLAFLEVVKKPVVVTFHSLIPNpTPKLKKVIQAIAKR-CEKIIVMADMAIEYYECDYGL 186
Cdd:cd03795    85 DI--IHYHFPNPL-----AD-LLLFFSGAKKPVVVHWHSDIVK-QKKLLKLYKPLMTRfLRRADRIIATSPNYVETSPTL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 187 K--KSQLVVIPHGTPVIEP--YSSEASKKKLGFEGKMLLSTFGLLNQGKGVEYVIKALpKIIEkhpevLYLIIGETHPVV 262
Cdd:cd03795   156 RefKNKVRVIPLGIDKNVYniPRVDFENIKREKKGKKIFLFIGRLVYYKGLDYLIEAA-QYLN-----YPIVIGGEGPLK 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 263 RKYEgekyrnKLIklsqKLNLTNYVKFYnKYLTLEEIINYLKSTDIYLCPPLAVNQITSGTLAYALSAGKAIVST----- 337
Cdd:cd03795   230 PDLE------AQI----ELNLLDNVKFL-GRVDDEEKVIYLHLCDVFVFPSVLRSEAFGIVLLEAMMCGKPVISTnigtg 298
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1277773221 338 -PFLhakeVLQQGRGEIVGFRDPTGISRVVNALIEKPETRKSMEKQ 382
Cdd:cd03795   299 vPYV----NNNGETGLVVPPKDPDALAEAIDKLLSDEELRESYGEN 340
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
43-312 3.58e-09

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: 59.30  E-value: 3.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221  43 GIATYTRDLVKAIDRKFSPYLEskILAmneNGSSIYNYCSKVKYQINQTEIEDYINVARKINKDDSIRLINIQHEFGLFg 122
Cdd:cd03809    15 GIGRYTRELLKALAKNDPDESV--LAV---PPLPGELLRLLREYPELSLGVIKIKLWRELALLRWLQILLPKKDKPDLL- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 123 geWGDYLLAFLEVVKKPVVVTFHSLI----PNPTPK-----LKKVIQAIAKRCEKIIV----MADMAIEYyecdYGLKKS 189
Cdd:cd03809    89 --HSPHNTAPLLLKGCPQVVTIHDLIplryPEFFPKrfrlyYRLLLPISLRRADAIITvseaTRDDIIKF----YGVPPE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 190 QLVVIPHGtpVIEPYSSEASKKKLGFEGKMLLSTFGLLNQ---GKGVEYVIKALPKIIEKHPEVLYLIIGETHPvvrKYE 266
Cdd:cd03809   163 KIVVIPLG--VDPSFFPPESAAVLIAKYLLPEPYFLYVGTlepRKNHERLLKAFALLKKQGGDLKLVIVGGKGW---EDE 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1277773221 267 gekyrnKLIKLSQKLNLTNYVKFYNkYLTLEEIINYLKSTDIYLCP 312
Cdd:cd03809   238 ------ELLDLVKKLGLGGRVRFLG-YVSDEDLPALYRGARAFVFP 276
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
137-379 9.39e-09

Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.


Pssm-ID: 340836 [Multi-domain]  Cd Length: 362  Bit Score: 58.10  E-value: 9.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 137 KKPVVVTFHSLI--PNPTPKLKKVIQAIAKRCEKIIVMADMAIEYYEcDYGLKKSQLVVIPHGtpvIEPYSSEASKKKLG 214
Cdd:cd03807   103 GVKVIWSVRSSNipQRLTRLVRKLCLLLSKFSPATVANSSAVAEFHQ-EQGYAKNKIVVIYNG---IDLFKLSPDDASRA 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 215 F--------EGKMLLSTFGLLNQGKGVEYVIKALPKIIEKHPEVLYLIIGEthpvvrkyeGEKYRNkLIKLSQKLNLTNY 286
Cdd:cd03807   179 RarrrlglaEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGR---------GPERPN-LERLLLELGLEDR 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 287 VKFYNkylTLEEIINYLKSTDIYLCPplAVNQITSGTLAYALSAGKAIVSTPFLHAKEVLQQGRGEIVGFRDPTGISRVV 366
Cdd:cd03807   249 VHLLG---ERSDVPALLPAMDIFVLS--SRTEGFPNALLEAMACGLPVVATDVGGAAELVDDGTGFLVPAGDPQALADAI 323
                         250
                  ....*....|...
gi 1277773221 367 NALIEKPETRKSM 379
Cdd:cd03807   324 RALLEDPEKRARL 336
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
137-406 1.24e-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: 57.77  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 137 KKPVVVTFHS----LIPnPTPKLKKVIQAIAKRCEKII-VMADMAIEYyeCDYGLKKSQLVVIPHG------TPVIEPYS 205
Cdd:cd03798   119 GVPYVVTEHGsdinVFP-PRSLLRKLLRWALRRAARVIaVSKALAEEL--VALGVPRDRVDVIPNGvdparfQPEDRGLG 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 206 SEASKKKLGFEGKmllstfglLNQGKGVEYVIKALPKIIEKHPEVLYLIIGethpvvrkyEGEKyRNKLIKLSQKLNLTN 285
Cdd:cd03798   196 LPLDAFVILFVGR--------LIPRKGIDLLLEAFARLAKARPDVVLLIVG---------DGPL-REALRALAEDLGLGD 257
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 286 YVKFYNkYLTLEEIINYLKSTDIYLCP------PLAVNQitsgtlayALSAGKAIVSTPFLHAKEVLQQGR-GEIVGFRD 358
Cdd:cd03798   258 RVTFTG-RLPHEQVPAYYRACDVFVLPsrhegfGLVLLE--------AMACGLPVVATDVGGIPEVVGDPEtGLLVPPGD 328
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1277773221 359 PTGISRVVNALIEKPETRKSMEKQSYLYGQKTSWPIAAIAHLNVFKKI 406
Cdd:cd03798   329 ADALAAALRRALAEPYLRELGEAARARVAERFSWVKAADRIAAAYRDV 376
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
296-408 1.31e-08

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 53.84  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 296 LEEIIN-YLKSTDIYLCPPLAVNqiTSGTLAYALSAGKAIVSTPFLHAKEVLQQGR-GEIVGFRDPTGISRVVNALIEKP 373
Cdd:COG0438    10 LDLLLEaLLAAADVFVLPSRSEG--FGLVLLEAMAAGLPVIATDVGGLPEVIEDGEtGLLVPPGDPEALAEAILRLLEDP 87
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1277773221 374 ETRKSMEKQSYLYGQKT-SWPIAAIAHLNVFKKIIN 408
Cdd:COG0438    88 ELRRRLGEAARERAEERfSWEAIAERLLALYEELLA 123
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
191-354 1.26e-07

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: 53.18  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 191 LVVIPHGTPVIEPYSSEASKK---KLGFEGKMLLStFGLLNQGKGVEYVIKALPKIIEKHPEVLYLIIGETHPvvrKYEG 267
Cdd:cd01635    81 IVVTVHGPDSLESTRSELLALarlLVSLPLADKVS-VGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGE---REEE 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 268 EKYRNKLIKLSQklnltnyVKFYNKYLTLEEIINYLKSTDIYLCPPLAVNQitSGTLAYALSAGKAIVSTPFLHAKEVLQ 347
Cdd:cd01635   157 EALAAALGLLER-------VVIIGGLVDDEVLELLLAAADVFVLPSRSEGF--GLVLLEAMAAGKPVIATDVGGIPEFVV 227

                  ....*...
gi 1277773221 348 QGR-GEIV 354
Cdd:cd01635   228 DGEnGLLV 235
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
128-384 1.65e-07

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: 54.17  E-value: 1.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 128 YLLAFLEVvKKPVVVTFHS--LIPNPTPKLKKVIQAIAKRCEKIIVMADMAIEYYecdYGLKKSQLVVIPHgtpviePYS 205
Cdd:cd03820   100 TFLALIGL-KSKLIVWEHNnyEAYNKGLRRLLLRRLLYKRADKIVVLTEADKLKK---YKQPNSNVVVIPN------PLS 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 206 SEASKKKLGFEGKMLLSTfGLLNQGKGVEYVIKALPKIIEKHPEVLYLIIGethpvvrkyEGEKyRNKLIKLSQKLNLTN 285
Cdd:cd03820   170 FPSEEPSTNLKSKRILAV-GRLTYQKGFDLLIEAWALIAKKHPDWKLRIYG---------DGPE-REELEKLIDKLGLED 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 286 YVKFYNkylTLEEIINYLKSTDIYLCP------PLavnqitsgTLAYALSAGKAIVSTPFLHA-KEVLQQGR-GEIVGFR 357
Cdd:cd03820   239 RVKLLG---PTKNIAEEYANSSIFVLSsryegfPM--------VLLEAMAYGLPIISFDCPTGpSEIIEDGEnGLLVPNG 307
                         250       260
                  ....*....|....*....|....*..
gi 1277773221 358 DPTGISRVVNALIEKPETRKSMEKQSY 384
Cdd:cd03820   308 DVDALAEALLRLMEDEELRKKMGKNAR 334
YyaL COG1331
Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin ...
607-700 5.41e-07

Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin glycosidase-like domains [General function prediction only];


Pssm-ID: 440942 [Multi-domain]  Cd Length: 672  Bit Score: 52.93  E-value: 5.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 607 ITYDNGRLPEALFLAYEVTKNKLYLKIAKESLDFL-SSLVILNDKLVligqRGWYNHKGK-RAFFDqqplDAASMVQVFL 684
Cdd:COG1331   411 LTSWNGLMIAALAEAGRVLGDPEYLEAAERAADFIlDNLWDPDGRLL----RSYRDGEAGiPGFLE----DYAFLIEALL 482
                          90
                  ....*....|....*.
gi 1277773221 685 RAYQVTDEKKYQHKAL 700
Cdd:COG1331   483 ALYEATGDPRWLERAL 498
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
43-197 1.01e-06

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 49.45  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221  43 GIATYTRDLVKAIDRK------FSPYLESKILAMNENGSSI--YNYCSKVKYQINQTEIEDYINVARKINKDdsirLINI 114
Cdd:pfam13439   2 GVERYVLELARALARRghevtvVTPGGPGPLAEEVVRVVRVprVPLPLPPRLLRSLAFLRRLRRLLRRERPD----VVHA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 115 QHEFGLFGGewgdyLLAFLEVVKKPVVVTFHSLIPNPTPK----------LKKVIQAIAKRCEKIIVMADMAIEYYECDY 184
Cdd:pfam13439  78 HSPFPLGLA-----ALAARLRLGIPLVVTYHGLFPDYKRLgarlsplrrlLRRLERRLLRRADRVIAVSEAVADELRRLY 152
                         170
                  ....*....|...
gi 1277773221 185 GLKKSQLVVIPHG 197
Cdd:pfam13439 153 GVPPEKIRVIPNG 165
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
180-381 2.79e-06

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340841 [Multi-domain]  Cd Length: 474  Bit Score: 50.41  E-value: 2.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 180 YECDYGLKKSQLVVIPHGTPvIEPYS--SEASKKKLGFegkmLLSTFGLLNQGKGVEYVIKALPKIIEKHPEVLYLIIGE 257
Cdd:cd03813   258 RQIRLGADPDKTRVIPNGID-IQRFApaREERPEKEPP----VVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAEGWLIGP 332
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 258 ThpvvrkYEGEKYRNKLIKLSQKLNLTNYVKFynkyLTLEEIINYLKSTDIylcppLAVNQITSG---TLAYALSAGKAI 334
Cdd:cd03813   333 E------DEDPEYAQECKRLVASLGLENKVKF----LGFQNIKEYYPKLGL-----LVLTSISEGqplVILEAMASGVPV 397
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1277773221 335 VSTPFLHAKEVLQQGR------GEIVGFRDPTGISRVVNALIEKPETRKSMEK 381
Cdd:cd03813   398 VATDVGSCRELIYGADdalgqaGLVVPPADPEALAEALIKLLRDPELRQAFGE 450
YyaL COG1331
Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin ...
609-641 4.13e-05

Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin glycosidase-like domains [General function prediction only];


Pssm-ID: 440942 [Multi-domain]  Cd Length: 672  Bit Score: 47.15  E-value: 4.13e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1277773221 609 YDNGRLPEALFLAYEVTKNKLYLKIAKESLDFL 641
Cdd:COG1331   269 YDNALLLRLYAEAYQLTGDPLYRRVAEETLDFL 301
LanC_like cd04434
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the ...
518-748 4.39e-05

Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the cyclase enzyme of the lanthionine synthetase. Lanthionine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as a precursor peptide and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans), in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. A related domain is also present in LanM and other pro- and eukaryotic proteins with poorly characterized functions.


Pssm-ID: 271198 [Multi-domain]  Cd Length: 351  Bit Score: 46.34  E-value: 4.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 518 ALWAAGFVMNSNLPENIKKTAKFIFDKAIKNIAKLKSP-----RGQAFSLIGLYYYYEAYPNPEIRQKIILLAERLVKFY 592
Cdd:cd04434    57 LLWALLELYEDLGDEKLLDALLDLLDDIALEAKEVWWSgndliLGDAGIILYLLYAAEKTGDEKYKELAAKIGDFLLQAA 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 593 QKEKTKDWCWFEQTITYDN---GRLPEALFLA--YEVTKNKLYLKIAKESLDFLSSLVILNDKLVLIGQ--------RGW 659
Cdd:cd04434   137 EELDNGGNWGLPKGSIYPGfahGTAGIAYALArlYEETGDEDFLDAAKEGAEYLEAIAVGDEDGFLIPLpdekdlfyLGW 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 660 --------------YNHKGKRAFFD-----------QQPLD------------AASMVQVFLRAYQVTDEKKYQHKA--- 699
Cdd:cd04434   217 chgpagtallfyelYKATGDLDLADellegiiktgaPEKLSpgfwnnlclchgTAGVLEHLLYVYRLTGDEREYAKRlad 296
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1277773221 700 -LLAFSWFlgiNSINQPVYDQTTSGCFDGLLPDcvnLNQGAESTISYLLS 748
Cdd:cd04434   297 kLLGRATR---NGEGLRWYQAWTGPGRVDASLG---LMVGAAGIASALLK 340
GT28_MurG cd03785
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ...
163-409 6.43e-05

undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic 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: 340818 [Multi-domain]  Cd Length: 350  Bit Score: 45.67  E-value: 6.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 163 AKRCEKIivmadmAIEYYECDYGLKKSQLVVIphGTPVI-EPYSSEASKKKLGF-EGKMLLSTFG------LLNQGkgve 234
Cdd:cd03785   132 SRFADKV------AVSFPETKKYFPAAKVVVT--GNPVReEILNLRKELKRFGLpPDKPTLLVFGgsqgarAINRA---- 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 235 yVIKALPKIIEKHPEVLYliigethpVVRKYEGEKYRNKLIKLSQKLNLTNYVkfynkyltlEEIINYLKSTDIYLCPPL 314
Cdd:cd03785   200 -VPKALPKLLERGIQVIH--------QTGKGDYDEVKKLYEDLGINVKVFPFI---------DDMAAAYAAADLVISRAG 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 315 AvnqitsGTLAYALSAGKAIVSTPFLH---------AKEVLQQGRGEIVGFRDPTG--ISRVVNALIEKPETRKSMEKqs 383
Cdd:cd03785   262 A------STIAELTAAGKPAILIPYPYaaddhqeanARALEKAGAAIVIDQEELTPevLAEAILDLLNDPERLKKMAE-- 333
                         250       260
                  ....*....|....*....|....*.
gi 1277773221 384 ylygqktswPIAAIAHLNVFKKIINL 409
Cdd:cd03785   334 ---------AAKKLAKPDAAERIADL 350
LanM-like cd04792
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; ...
562-644 7.03e-05

Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; LanM-like proteins. LanM is a bifunctional enzyme, involved in the synthesis of class II lantibiotics. It is responsible for both the dehydration and the cyclization of the precursor-peptide during lantibiotic synthesis. The C-terminal domain shows similarity to LanC, the cyclase component of the lan operon, but the N terminus seems to be unrelated to the dehydratase, LanB.


Pssm-ID: 271200 [Multi-domain]  Cd Length: 836  Bit Score: 46.54  E-value: 7.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 562 LIGLYYYYEAYPNPEIRQKIILLAERLVKFYQK-EKTKDWCWFEQT------------ITYdngrlpeALFLAYEVTKNK 628
Cdd:cd04792   598 ILVLLALYERTGDERALELAIACGDHLLKNAVEnDGGARWKTPASSrpltgfahgaagIAW-------ALLRLAAVTGDE 670
                          90
                  ....*....|....*.
gi 1277773221 629 LYLKIAKESLDFLSSL 644
Cdd:cd04792   671 RYLEAAKEALAYERSL 686
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
139-396 9.26e-05

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: 45.31  E-value: 9.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 139 PVVVTFHSL--------IPNPTPKLKKVIQA---IAKRCEKIIVMADMAIEYYECDYGLKKSQLVVIPHGTPV--IEPYS 205
Cdd:cd03800   126 PLVHTFHSLgrvkyrhlGAQDTYHPSLRITAeeqILEAADRVIASTPQEADELISLYGADPSRINVVPPGVDLerFFPVD 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 206 -SEASKKKLGF--EGKMLLStFGLLNQGKGVEYVIKALPKIIEKHPEVLYLIIGEThpvvRKYEGEKYRNKLIKLSQKLN 282
Cdd:cd03800   206 rAEARRARLLLppDKPVVLA-LGRLDPRKGIDTLVRAFAQLPELRELANLVLVGGP----SDDPLSMDREELAELAEELG 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 283 LTNYVKFYnKYLTLEEIINYLKSTDIYLCPPL-------AVNQITSGTlayalsagkAIVSTPFLHAKEVLQQGR-GEIV 354
Cdd:cd03800   281 LIDRVRFP-GRVSRDDLPELYRAADVFVVPSLyepfgltAIEAMACGT---------PVVATAVGGLQDIVRDGRtGLLV 350
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1277773221 355 GFRDPTGISRVVNALIEKPETRKSMEKQSYLYGQKT-SWPIAA 396
Cdd:cd03800   351 DPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHyTWESVA 393
YesR COG4225
Rhamnogalacturonyl hydrolase YesR [Carbohydrate transport and metabolism];
541-695 1.84e-04

Rhamnogalacturonyl hydrolase YesR [Carbohydrate transport and metabolism];


Pssm-ID: 443369  Cd Length: 336  Bit Score: 44.42  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 541 IFDKAIKNIAKLKSPRG------QAFSLIGLYYYYEAYPNPEIRQKIILLAERLVkfyqkEKTKDWCWFEQTItyDNGRL 614
Cdd:COG4225     1 VADSQLKRYWDIDPGKFpkwdytQGVTLYGLLKLAEATGDKKYLDYIKRWFDFFI-----DEGNTYKLPPYNL--DDIAP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 615 PEALFLAYEVTKNKLYLKIAKESLDFlsslvilndklVLIGQR----GWYNHKgkraffDQQP----LDAASMVQVFL-R 685
Cdd:COG4225    74 GLALLELYEQTGDPKYLKAADTLADW-----------QLNTQPrtseGGFWHK------KIYPnqlwLDGLYMAVPFLaQ 136
                         170
                  ....*....|
gi 1277773221 686 AYQVTDEKKY 695
Cdd:COG4225   137 YGKLTGDPKY 146
LanC_SerThrkinase cd04791
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ...
563-696 2.44e-04

Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of this subgroup lack the zinc binding site and the active site residues, and therefore are most likely inactive. The function of this domain is unknown.


Pssm-ID: 271199 [Multi-domain]  Cd Length: 327  Bit Score: 43.80  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 563 IGLY--YYYEAYPNPEIRQKIILLAERLVKFYQK-EKTKDWCWF-EQTITYDNGRLPEALFL--AYEVTKNKLYLKIAKE 636
Cdd:cd04791    91 IGLAllHLARATGDPEFLERAARIAERLAARLREdDPGVYWNDAgAVRAGLLHGWSGIALFLlrLYEATGDPAYLDLAER 170
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277773221 637 SLDF-LSSLVILNDKLVligqrgWYNHKGKRAFfdqqP-LD--AASMVQVFLRAYQVTDEKKYQ 696
Cdd:cd04791   171 ALRKdLARCVEDDDGAL------LQVDEGNRLL----PyLCsgSAGIGLVLLRYLRHRGDDRYR 224
YihS COG2942
Mannose or cellobiose epimerase, N-acyl-D-glucosamine 2-epimerase family [Carbohydrate ...
557-641 3.32e-03

Mannose or cellobiose epimerase, N-acyl-D-glucosamine 2-epimerase family [Carbohydrate transport and metabolism];


Pssm-ID: 442185  Cd Length: 380  Bit Score: 40.63  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 557 GQAFSLIGLYYYYEAYPNPEIRQKIILLAERLVKF--------YQKEKTKDWCWFEQTITYD-NGRLPEALFLAYEVTKN 627
Cdd:COG2942   110 GHAFALLALAEAYRATGDPEALELAKETFELLERRfwdpehggYAEAFDRDWSPLRPYRGQNaHMHLLEALLALYEATGD 189
                          90
                  ....*....|....
gi 1277773221 628 KLYLKIAKESLDFL 641
Cdd:COG2942   190 ERWLERAEEIADLI 203
LcnDR2 COG4403
Lantibiotic modifying enzyme [Defense mechanisms];
557-644 8.97e-03

Lantibiotic modifying enzyme [Defense mechanisms];


Pssm-ID: 443528 [Multi-domain]  Cd Length: 405  Bit Score: 39.34  E-value: 8.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277773221 557 GQAFSLIGLYYYYEAYPNPEIRQKIILLAERLVKFYQKEKTKdWCWfeQTITYDNGRLP----------EALFLAYEVTK 626
Cdd:COG4403   162 GAAGAILALLALYRATGDPAALDLAIRCGDRLLAAAVRDDGG-RAW--PTPEPAGRPLTgfahgaagiaYALLRLAAATG 238
                          90
                  ....*....|....*...
gi 1277773221 627 NKLYLKIAKESLDFLSSL 644
Cdd:COG4403   239 DERYLEAAREALAYERSL 256
 
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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