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Conserved domains on  [gi|14035914|emb|CAC38553|]
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unnamed protein product [Homo sapiens]

Protein Classification

chitobiosyldiphosphodolichol beta-mannosyltransferase( domain architecture ID 10133598)

chitobiosyldiphosphodolichol beta-mannosyltransferase catalyzes the addition of the first of nine mannose moieties to form a dolichol-lipid linked oligosaccharide intermediate required for proper N-linked glycosylation

CAZY:  GT33
EC:  2.4.1.142
Gene Symbol:  ALG1
Gene Ontology:  GO:0004578|GO:0006486|GO:0006488
SCOP:  3001586

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GT33_ALG1-like cd03816
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is ...
1-380 0e+00

chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is most closely related to the GT33 family of glycosyltransferases. The yeast gene ALG1 has been shown to function as a mannosyltransferase that catalyzes the formation of dolichol pyrophosphate (Dol-PP)-GlcNAc2Man from GDP-Man and Dol-PP-Glc-NAc2, and participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. In humans ALG1 has been associated with the congenital disorders of glycosylation (CDG) designated as subtype CDG-Ik.


:

Pssm-ID: 340843 [Multi-domain]  Cd Length: 411  Bit Score: 607.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914   1 MQYHALSLAMHGFSVTLLGFCNSKPHDELLQNNRIQIVGLTELQSLAVGPRVFQYGVKVVLQAMYLLWKLMWREPGAYIF 80
Cdd:cd03816  20 MQYHALSLARHGWRVDLIGYLESPPHDELLSHPNITIHALPPPPTKNKLPFLLFAPLKVLLQALSLLWLLYELRPADYIL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914  81 LQNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPNHPLVLLAKWYEKFFGRLSHLNLCVTNAMREDLA--DN 158
Cdd:cd03816 100 VQNPPSIPTLAIAWLYCRLRRTKLIIDWHNFGYTILALKLGENHPLVRLAKWYEKTFGRMADAHLCVTKAMQRDLQqfEN 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914 159 WHIRAVTVYDKPASFFKETPLDLQHRLFMKLgsmhspfrarsepedpvtersaFTERDAGSGLVTRLRERPALLVSSTSW 238
Cdd:cd03816 180 WNIRATVLYDRPPSHFRPIPLEEKHELFLEL----------------------ALFRELAEGAVSYKEGRPALLVSSTSW 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914 239 TEDEDFSILLAALEKFEQLTLDGH-NLPSLVCVITGKGPLREYYSRLIHQKHFQHIQVCTPWLEAEDYPLLLGSADLGVC 317
Cdd:cd03816 238 TPDEDFSILLDALKAYESSAATEPaLLPSLLCIITGKGPLKEMYLELIKELKLKKVTIRTPWLSAEDYPRLLASADLGVC 317
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14035914 318 LHTSSSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFEDSEELAAQLQMLFSNFP 380
Cdd:cd03816 318 LHTSSSGLDLPMKVVDMFGCGLPVCAMDFKCIGELVKHGVNGLVFGDSEELAEQLIDLLSDFD 380
 
Name Accession Description Interval E-value
GT33_ALG1-like cd03816
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is ...
1-380 0e+00

chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is most closely related to the GT33 family of glycosyltransferases. The yeast gene ALG1 has been shown to function as a mannosyltransferase that catalyzes the formation of dolichol pyrophosphate (Dol-PP)-GlcNAc2Man from GDP-Man and Dol-PP-Glc-NAc2, and participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. In humans ALG1 has been associated with the congenital disorders of glycosylation (CDG) designated as subtype CDG-Ik.


Pssm-ID: 340843 [Multi-domain]  Cd Length: 411  Bit Score: 607.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914   1 MQYHALSLAMHGFSVTLLGFCNSKPHDELLQNNRIQIVGLTELQSLAVGPRVFQYGVKVVLQAMYLLWKLMWREPGAYIF 80
Cdd:cd03816  20 MQYHALSLARHGWRVDLIGYLESPPHDELLSHPNITIHALPPPPTKNKLPFLLFAPLKVLLQALSLLWLLYELRPADYIL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914  81 LQNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPNHPLVLLAKWYEKFFGRLSHLNLCVTNAMREDLA--DN 158
Cdd:cd03816 100 VQNPPSIPTLAIAWLYCRLRRTKLIIDWHNFGYTILALKLGENHPLVRLAKWYEKTFGRMADAHLCVTKAMQRDLQqfEN 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914 159 WHIRAVTVYDKPASFFKETPLDLQHRLFMKLgsmhspfrarsepedpvtersaFTERDAGSGLVTRLRERPALLVSSTSW 238
Cdd:cd03816 180 WNIRATVLYDRPPSHFRPIPLEEKHELFLEL----------------------ALFRELAEGAVSYKEGRPALLVSSTSW 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914 239 TEDEDFSILLAALEKFEQLTLDGH-NLPSLVCVITGKGPLREYYSRLIHQKHFQHIQVCTPWLEAEDYPLLLGSADLGVC 317
Cdd:cd03816 238 TPDEDFSILLDALKAYESSAATEPaLLPSLLCIITGKGPLKEMYLELIKELKLKKVTIRTPWLSAEDYPRLLASADLGVC 317
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14035914 318 LHTSSSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFEDSEELAAQLQMLFSNFP 380
Cdd:cd03816 318 LHTSSSGLDLPMKVVDMFGCGLPVCAMDFKCIGELVKHGVNGLVFGDSEELAEQLIDLLSDFD 380
PLN02275 PLN02275
transferase, transferring glycosyl groups
1-376 1.77e-143

transferase, transferring glycosyl groups


Pssm-ID: 215155 [Multi-domain]  Cd Length: 371  Bit Score: 412.14  E-value: 1.77e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914    1 MQYHALSLAMH-GFSVTLLGFCNSKPHDELLQNNRIQI---VGLTELQSLAVGPRVFQYGVKVVLQAMYLLWKLMWREPG 76
Cdd:PLN02275  21 MQYHALSLARQaSFQVDVVAYGGSEPIPALLNHPSIHIhlmVQPRLLQRLPRVLYALALLLKVAIQFLMLLWFLCVKIPR 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914   77 AYIFL-QNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPNHPLVLLAKWYEKFFGRLSHLNLCVTNAMREDL 155
Cdd:PLN02275 101 PDVFLvQNPPSVPTLAVVKLACWLRRAKFVIDWHNFGYTLLALSLGRSHPLVRLYRWYERHYGKMADGHLCVTKAMQHEL 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914  156 ADNWHIRAVTVYDKPASFFKETPLdlqhrlfmklgsmhspfrarsepedpvtersafterdagsglVTRLRE-RPALLVS 234
Cdd:PLN02275 181 DQNWGIRATVLYDQPPEFFRPASL------------------------------------------EIRLRPnRPALVVS 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914  235 STSWTEDEDFSILLAALEKFEQL---TLDGHN--------LPSLVCVITGKGPLREYYSRLIHQKHFQHIQVCTPWLEAE 303
Cdd:PLN02275 219 STSWTPDEDFGILLEAAVMYDRRvaaRLNESDsasgkqslYPRLLFIITGKGPQKAMYEEKISRLNLRHVAFRTMWLEAE 298
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14035914  304 DYPLLLGSADLGVCLHTSSSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFEDSEELAAQLQMLF 376
Cdd:PLN02275 299 DYPLLLGSADLGVSLHTSSSGLDLPMKVVDMFGCGLPVCAVSYSCIGELVKDGKNGLLFSSSSELADQLLELL 371
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
282-384 8.75e-09

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 53.07  E-value: 8.75e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914 282 SRLIHQKHFQHIqvctpwLEAedyplLLGSADlgVCLHTSSSGlDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLV 361
Cdd:COG0438   2 GRLVPRKGLDLL------LEA-----LLAAAD--VFVLPSRSE-GFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLL 67
                        90       100
                ....*....|....*....|....*
gi 14035914 362 FE--DSEELAAQLQMLFSNfPDLRA 384
Cdd:COG0438  68 VPpgDPEALAEAILRLLED-PELRR 91
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
247-384 1.41e-08

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: 53.43  E-value: 1.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914   247 LLAALEKFEQltldghNLPSLVCVITGKGPLREYYSRLIHQKHFQHIQVCTPWLEAEDYPLLLGSADLGVCLHTSSSgld 326
Cdd:pfam00534  20 LIKAFALLKE------KNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVFVLPSRYEG--- 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914   327 LPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFE--DSEELAAQLQMLFSNfPDLRA 384
Cdd:pfam00534  91 FGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKpnNAEALAEAIDKLLED-EELRE 149
 
Name Accession Description Interval E-value
GT33_ALG1-like cd03816
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is ...
1-380 0e+00

chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is most closely related to the GT33 family of glycosyltransferases. The yeast gene ALG1 has been shown to function as a mannosyltransferase that catalyzes the formation of dolichol pyrophosphate (Dol-PP)-GlcNAc2Man from GDP-Man and Dol-PP-Glc-NAc2, and participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. In humans ALG1 has been associated with the congenital disorders of glycosylation (CDG) designated as subtype CDG-Ik.


Pssm-ID: 340843 [Multi-domain]  Cd Length: 411  Bit Score: 607.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914   1 MQYHALSLAMHGFSVTLLGFCNSKPHDELLQNNRIQIVGLTELQSLAVGPRVFQYGVKVVLQAMYLLWKLMWREPGAYIF 80
Cdd:cd03816  20 MQYHALSLARHGWRVDLIGYLESPPHDELLSHPNITIHALPPPPTKNKLPFLLFAPLKVLLQALSLLWLLYELRPADYIL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914  81 LQNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPNHPLVLLAKWYEKFFGRLSHLNLCVTNAMREDLA--DN 158
Cdd:cd03816 100 VQNPPSIPTLAIAWLYCRLRRTKLIIDWHNFGYTILALKLGENHPLVRLAKWYEKTFGRMADAHLCVTKAMQRDLQqfEN 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914 159 WHIRAVTVYDKPASFFKETPLDLQHRLFMKLgsmhspfrarsepedpvtersaFTERDAGSGLVTRLRERPALLVSSTSW 238
Cdd:cd03816 180 WNIRATVLYDRPPSHFRPIPLEEKHELFLEL----------------------ALFRELAEGAVSYKEGRPALLVSSTSW 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914 239 TEDEDFSILLAALEKFEQLTLDGH-NLPSLVCVITGKGPLREYYSRLIHQKHFQHIQVCTPWLEAEDYPLLLGSADLGVC 317
Cdd:cd03816 238 TPDEDFSILLDALKAYESSAATEPaLLPSLLCIITGKGPLKEMYLELIKELKLKKVTIRTPWLSAEDYPRLLASADLGVC 317
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14035914 318 LHTSSSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFEDSEELAAQLQMLFSNFP 380
Cdd:cd03816 318 LHTSSSGLDLPMKVVDMFGCGLPVCAMDFKCIGELVKHGVNGLVFGDSEELAEQLIDLLSDFD 380
PLN02275 PLN02275
transferase, transferring glycosyl groups
1-376 1.77e-143

transferase, transferring glycosyl groups


Pssm-ID: 215155 [Multi-domain]  Cd Length: 371  Bit Score: 412.14  E-value: 1.77e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914    1 MQYHALSLAMH-GFSVTLLGFCNSKPHDELLQNNRIQI---VGLTELQSLAVGPRVFQYGVKVVLQAMYLLWKLMWREPG 76
Cdd:PLN02275  21 MQYHALSLARQaSFQVDVVAYGGSEPIPALLNHPSIHIhlmVQPRLLQRLPRVLYALALLLKVAIQFLMLLWFLCVKIPR 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914   77 AYIFL-QNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPNHPLVLLAKWYEKFFGRLSHLNLCVTNAMREDL 155
Cdd:PLN02275 101 PDVFLvQNPPSVPTLAVVKLACWLRRAKFVIDWHNFGYTLLALSLGRSHPLVRLYRWYERHYGKMADGHLCVTKAMQHEL 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914  156 ADNWHIRAVTVYDKPASFFKETPLdlqhrlfmklgsmhspfrarsepedpvtersafterdagsglVTRLRE-RPALLVS 234
Cdd:PLN02275 181 DQNWGIRATVLYDQPPEFFRPASL------------------------------------------EIRLRPnRPALVVS 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914  235 STSWTEDEDFSILLAALEKFEQL---TLDGHN--------LPSLVCVITGKGPLREYYSRLIHQKHFQHIQVCTPWLEAE 303
Cdd:PLN02275 219 STSWTPDEDFGILLEAAVMYDRRvaaRLNESDsasgkqslYPRLLFIITGKGPQKAMYEEKISRLNLRHVAFRTMWLEAE 298
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14035914  304 DYPLLLGSADLGVCLHTSSSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFEDSEELAAQLQMLF 376
Cdd:PLN02275 299 DYPLLLGSADLGVSLHTSSSGLDLPMKVVDMFGCGLPVCAVSYSCIGELVKDGKNGLLFSSSSELADQLLELL 371
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
5-384 1.58e-09

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: 59.09  E-value: 1.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914   5 ALSLAMHGFSVTLLGFCNSKPHDELLQNNRIQIvgltelqsLAVGPRVFQYGVKVVLQamylLWKLMWREPGAYIFLQNP 84
Cdd:cd03801  24 ARALAARGHDVTVLTPADPGEPPEELEDGVIVP--------LLPSLAALLRARRLLRE----LRPLLRLRKFDVVHAHGL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914  85 PGLPSIAVCWFvgcLCGSKLVIDWHNYGYSIMGLVHGPNHPLvlLAKWyeKFFGRLSHLNLCVTNAMREDLADNWHI--- 161
Cdd:cd03801  92 LAALLAALLAL---LLGAPLVVTLHGAEPGRLLLLLAAERRL--LARA--EALLRRADAVIAVSEALRDELRALGGIppe 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914 162 RAVTVYdkpasffkeTPLDLQHrlfmklgsmhSPFRARSEPEDPVTERSAFTerdagsglVTRLRERPALLVsstswted 241
Cdd:cd03801 165 KIVVIP---------NGVDLER----------FSPPLRRKLGIPPDRPVLLF--------VGRLSPRKGVDL-------- 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914 242 edfsiLLAALEKFEQLtldghnLPSLVCVITGKGPlrEYYSRLIHQKHFQHIQV-CTPWLEAEDYPLLLGSADLGVCLHT 320
Cdd:cd03801 210 -----LLEALAKLLRR------GPDVRLVIVGGDG--PLRAELEELELGLGDRVrFLGFVPDEELPALYAAADVFVLPSR 276
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14035914 321 SSSgldLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFE--DSEELAAQLQMLFSNfPDLRA 384
Cdd:cd03801 277 YEG---FGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPpdDVEALADALLRLLAD-PELRA 338
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
282-384 8.75e-09

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 53.07  E-value: 8.75e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914 282 SRLIHQKHFQHIqvctpwLEAedyplLLGSADlgVCLHTSSSGlDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLV 361
Cdd:COG0438   2 GRLVPRKGLDLL------LEA-----LLAAAD--VFVLPSRSE-GFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLL 67
                        90       100
                ....*....|....*....|....*
gi 14035914 362 FE--DSEELAAQLQMLFSNfPDLRA 384
Cdd:COG0438  68 VPpgDPEALAEAILRLLED-PELRR 91
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
5-384 1.34e-08

Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.


Pssm-ID: 340825 [Multi-domain]  Cd Length: 391  Bit Score: 56.20  E-value: 1.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914   5 ALSLAMHGFSVTLLGFCNSKPHDELLQNN-------RIQIVGLTELQSLAVGPRVFQYgvkVVLQAMYLLWKLMWREPGA 77
Cdd:cd03794  24 AKELVRRGHEVTVLTPSPNYPLGRIFAGAtetkdgiRVIRVKLGPIKKNGLIRRLLNY---LSFALAALLKLLVREERPD 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914  78 YIFLQNPPGLPSIAVCWFVGcLCGSKLVID----WHNygySIMGLVHGPNHPLVLLAKWYEKFFGRLSHLNLCVTNAMRE 153
Cdd:cd03794 101 VIIAYSPPITLGLAALLLKK-LRGAPFILDvrdlWPE---SLIALGVLKKGSLLKLLKKLERKLYRLADAIIVLSPGLKE 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914 154 dladnwHIRAVTVYDKPASFFKEtpldlqhrlfmklGSMHSPFRarsePEDPVTERSAFTERDagsglvtrlrerPALLV 233
Cdd:cd03794 177 ------YLLRKGVPKEKIIVIPN-------------WADLEEFK----PPPKDELRKKLGLDD------------KFVVV 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914 234 SSTSWTEDEDFSILLAALEKFEQLtldghnlPSLVCVITGKGPLREYYSRLIHQKHfqhIQVCT--PWLEAEDYPLLLGS 311
Cdd:cd03794 222 YAGNIGKAQGLETLLEAAERLKRR-------PDIRFLFVGDGDEKERLKELAKARG---LDNVTflGRVPKEEVPELLSA 291
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14035914 312 ADLG-VCLHTS-SSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFE--DSEELAAQLQMLFSNfPDLRA 384
Cdd:cd03794 292 ADVGlVPLKDNpANRGSSPSKLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEpgDPEALADAILELLDD-PELRR 367
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
247-384 1.41e-08

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: 53.43  E-value: 1.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914   247 LLAALEKFEQltldghNLPSLVCVITGKGPLREYYSRLIHQKHFQHIQVCTPWLEAEDYPLLLGSADLGVCLHTSSSgld 326
Cdd:pfam00534  20 LIKAFALLKE------KNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVFVLPSRYEG--- 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914   327 LPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFE--DSEELAAQLQMLFSNfPDLRA 384
Cdd:pfam00534  91 FGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKpnNAEALAEAIDKLLED-EELRE 149
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
204-362 1.24e-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: 52.02  E-value: 1.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914 204 DPVTERSAFTERDAGSGLVTRLRERPALLVSStsWTEDEDFSILLAALEKFeqltldGHNLPSLVCVITGKGPLREYYSR 283
Cdd:cd01635  87 GPDSLESTRSELLALARLLVSLPLADKVSVGR--LVPEKGIDLLLEALALL------KARLPDLVLVLVGGGGEREEEEA 158
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914 284 LI-HQKHFQHIQVCTPWLEAEDYPLLLGSADLGVCLHTSSSgldLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVF 362
Cdd:cd01635 159 LAaALGLLERVVIIGGLVDDEVLELLLAAADVFVLPSRSEG---FGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
12-383 3.65e-06

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: 48.51  E-value: 3.65e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914  12 GFSVTLLGFCNSKPHDELLqNNRIQIVGLTELQSLAVGPRVFqygvKVVLQAMYLLWKLM------WREPGAYIF-LQNP 84
Cdd:cd03811  29 GYDVTLVLLRDEGDLDKQL-NGDVKLIRLLIRVLKLIKLGLL----KAILKLKRILKRAKpdvvisFLGFATYIVaKLAA 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914  85 PGLPSIAVCwfvgclcgsklvidwHNYgYSImglvhgpNHPLVLLAKWYEKFFGRLSHLnLCVTNAMREDLADNWHI--- 161
Cdd:cd03811 104 ARSKVIAWI---------------HSS-LSK-------LYYLKKKLLLKLKLYKKADKI-VCVSKGIKEDLIRLGPSppe 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914 162 RAVTVYDkpasffketPLDLQHrlfmklgsmhspFRARSEPEDPVTERSAFTerdagsgLVT--RLrerpallvsstswT 239
Cdd:cd03811 160 KIEVIYN---------PIDIDR------------IRALAKEPILNEPEDGPV-------ILAvgRL-------------D 198
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914 240 EDEDFSILLAAlekFEQLTLDGHNLPslvCVITGKGPLREYYSRLIHQkhfqhiqvctpwLEAEDYPLLLG--------- 310
Cdd:cd03811 199 PQKGHDLLIEA---FAKLRKKYPDVK---LVILGDGPLREELEKLAKE------------LGLAERVIFLGfqsnpypyl 260
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14035914 311 -SADLGVclHTSSS-GLdlPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFE--DSEELAAQLQMLFSNFPDLR 383
Cdd:cd03811 261 kKADLFV--LSSRYeGF--PNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPdgDAAALAGILAALLQKKLDAA 333
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
61-385 5.00e-05

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 44.89  E-value: 5.00e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914  61 LQAMYLLWKLMWREPGAYIFLQNP-PG-LPSIAvcwfvGCLCGSKLVIdwhnygYSI--MGLVHGPNHPLVLLAKWYEKF 136
Cdd:cd03808  67 LKALFKLYKLLKKEKPDIVHCHTPkPGiLGRLA-----ARLAGVPKVI------YTVhgLGFVFTEGKLLRLLYLLLEKL 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914 137 FGRLSHLNLCVTNAMREDLADNWHIRAVTVYDKPASffketPLDLQHRlfmklgsmhsPFRARSEPEDPVTersaFterd 216
Cdd:cd03808 136 ALLFTDKVIFVNEDDRDLAIKKGIIKKKKTVLIPGS-----GVDLDRF----------QYSPESLPSEKVV----F---- 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914 217 agsGLVTRLRErpallvsstswteDEDFSILLAALEKFEQltldghNLPSLVCVITGKGPLREYYSRLIHQKHFQHIQVC 296
Cdd:cd03808 193 ---LFVARLLK-------------DKGIDELIEAAKILKK------KGPNVRFLLVGDGELENPSEILIEKLGLEGRIEF 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914 297 TPWLEaeDYPLLLGSADLgVCLHTSSSGLdlPMKVV------------DMFGCClpvcavnfkclhELVKHEENGLVFE- 363
Cdd:cd03808 251 LGFRS--DVPELLAESDV-FVLPSYREGL--PRSLLeamaagrpvittDVPGCR------------ELVIDGVNGFLVPp 313
                       330       340
                ....*....|....*....|...
gi 14035914 364 -DSEELAAQLQMLFSNfPDLRAS 385
Cdd:cd03808 314 gDVEALADAIEKLIED-PELRKE 335
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
244-370 3.20e-04

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: 42.27  E-value: 3.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914 244 FSILLAALEKFeqltldgHNLPSLVCVITGKGPLREYYSRLIHQKHFQHIQVCTPWLEAEDYPLLLGSADLGVclHTSSS 323
Cdd:cd03817 216 IDFLLRAFAEL-------KKEPNIKLVIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFV--FASTT 286
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 14035914 324 GLdLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFEDSEELAA 370
Cdd:cd03817 287 ET-QGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPNDETLA 332
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
271-383 7.47e-04

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: 41.07  E-value: 7.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14035914 271 ITGKGPLREYYSRLIHQKHFQH-IQVCTPWLEAEDYpllLGSADLGVClhtSSS--GLdlPMKVVDMFGCCLPVcaVNFK 347
Cdd:cd03820 217 IYGDGPEREELEKLIDKLGLEDrVKLLGPTKNIAEE---YANSSIFVL---SSRyeGF--PMVLLEAMAYGLPI--ISFD 286
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 14035914 348 CLH---ELVKHEENGLVFE--DSEELAAQLQMLFSNfPDLR 383
Cdd:cd03820 287 CPTgpsEIIEDGENGLLVPngDVDALAEALLRLMED-EELR 326
 
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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