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Conserved domains on  [gi|568913710|ref|XP_006498112|]
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polypeptide N-acetylgalactosaminyltransferase 5 isoform X1 [Mus musculus]

Protein Classification

polypeptide N-acetylgalactosaminyltransferase( domain architecture ID 11551840)

polypeptide N-acetylgalactosaminyltransferase catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor

CAZY:  GT2
EC:  2.4.1.41
Gene Ontology:  GO:0004653|GO:0030246|GO:0046872
SCOP:  3000077|3000678

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
489-790 1.01e-174

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


:

Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 508.28  E-value: 1.01e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710 489 SIIMCFVDEVWSALLRSVHSVLNRSPPHLIKEILLVDDFSTKEYLKADLD-KYMSQFPKVRILRLKERHGLIRARLAGAQ 567
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEeYYKKYLPKVKVLRLKKREGLIRARIAGAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710 568 NATGDVLTFLDSHVECNVGWLEPLLERVYLNRKKVACPVIEVINDKDMSYMTVDNFQRGVFTWPMNFGWKTIPPDVVAKN 647
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEERRRE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710 648 giKETDIIRCPVMAGGLFSIDKSYFYELGTYDPGLDVWGGENMELSFKVWMCGGEIEIIPCSRVGHIFRND-NPYSFPKD 726
Cdd:cd02510  161 --SPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKrKPYTFPGG 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568913710 727 rMKTVERNLVRVAEVWLDDYRELFYGHGDHLidQGLDVGNLTQQRELRKKLKCKSFKWYLDNVF 790
Cdd:cd02510  239 -SGTVLRNYKRVAEVWMDEYKEYFYKARPEL--RNIDYGDLSERKALRERLKCKSFKWYLENVY 299
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
805-925 3.46e-15

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.


:

Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 72.54  E-value: 3.46e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710   805 INMALGKCVSI--ENITVTLEDCDGSSQLQQFNYTWVRLIKH--GEWCVAPIPEKGS-LTLYHCDNRNNRLKWLHKSASA 879
Cdd:smart00458   2 ISGNTGKCLDVngNKNPVGLFDCHGTGGNQLWKLTSDGAIRIkdTDLCLTANGNTGStVTLYSCDGTNDNQYWEVNKDGT 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 568913710   880 FHpelvdhivfeNYQQLLCMEGNFSQK--TLKLAACNPmELQQKWKFE 925
Cdd:smart00458  82 IR----------NPDSGKCLDVKDGNTgtKVILWTCSG-NPNQKWIFE 118
 
Name Accession Description Interval E-value
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
489-790 1.01e-174

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 508.28  E-value: 1.01e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710 489 SIIMCFVDEVWSALLRSVHSVLNRSPPHLIKEILLVDDFSTKEYLKADLD-KYMSQFPKVRILRLKERHGLIRARLAGAQ 567
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEeYYKKYLPKVKVLRLKKREGLIRARIAGAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710 568 NATGDVLTFLDSHVECNVGWLEPLLERVYLNRKKVACPVIEVINDKDMSYMTVDNFQRGVFTWPMNFGWKTIPPDVVAKN 647
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEERRRE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710 648 giKETDIIRCPVMAGGLFSIDKSYFYELGTYDPGLDVWGGENMELSFKVWMCGGEIEIIPCSRVGHIFRND-NPYSFPKD 726
Cdd:cd02510  161 --SPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKrKPYTFPGG 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568913710 727 rMKTVERNLVRVAEVWLDDYRELFYGHGDHLidQGLDVGNLTQQRELRKKLKCKSFKWYLDNVF 790
Cdd:cd02510  239 -SGTVLRNYKRVAEVWMDEYKEYFYKARPEL--RNIDYGDLSERKALRERLKCKSFKWYLENVY 299
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
489-669 5.08e-33

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 125.20  E-value: 5.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710  489 SIIMCFVDEvWSALLRSVHSVLNRspPHLIKEILLVDDFSTkEYLKADLDKYMSQFPKVRILRLKERHGLIRARLAGAQN 568
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQ--TYPNFEIIVVDDGST-DGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710  569 ATGDVLTFLDSHVECNVGWLEPLLERVYLNRKKVACPVIEVINDKDmsymtvdnfqrgVFTWPMNFGWKTIPPDVVAKNG 648
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGET------------GEYRRASRITLSRLPFFLGLRL 144
                         170       180
                  ....*....|....*....|.
gi 568913710  649 IKETDIIRCPVMAGGLFSIDK 669
Cdd:pfam00535 145 LGLNLPFLIGGFALYRREALE 165
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
805-925 3.46e-15

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 72.54  E-value: 3.46e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710   805 INMALGKCVSI--ENITVTLEDCDGSSQLQQFNYTWVRLIKH--GEWCVAPIPEKGS-LTLYHCDNRNNRLKWLHKSASA 879
Cdd:smart00458   2 ISGNTGKCLDVngNKNPVGLFDCHGTGGNQLWKLTSDGAIRIkdTDLCLTANGNTGStVTLYSCDGTNDNQYWEVNKDGT 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 568913710   880 FHpelvdhivfeNYQQLLCMEGNFSQK--TLKLAACNPmELQQKWKFE 925
Cdd:smart00458  82 IR----------NPDSGKCLDVKDGNTgtKVILWTCSG-NPNQKWIFE 118
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
800-922 1.84e-13

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 67.94  E-value: 1.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710  800 ASGVLINMALGKCVSIE-----NITVTLEDCDGSSQLQQFNYTWVRLIKH--GEWC--VAPIPEKGSLTLYHCDNRNNRL 870
Cdd:pfam00652   1 ATGRIRNRASGKCLDVPggssaGGPVGLYPCHGSNGNQLWTLTGDGTIRSvaSDLCldVGSTADGAKVVLWPCHPGNGNQ 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568913710  871 KWLHKSASafhpelvDHIVfeNYQQLLCME---GNFSQKTLKLAACNPMELQQKW 922
Cdd:pfam00652  81 RWRYDEDG-------TQIR--NPQSGKCLDvsgAGTSNGKVILWTCDSGNPNQQW 126
RICIN cd00161
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication. ...
810-924 4.52e-10

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication. The domain is found in a variety of molecules serving diverse functions such as enzymatic activity, inhibitory toxicity and signal transduction. Highly specific ligand binding occurs on exposed surfaces of the compact domain sturcture.


Pssm-ID: 238092 [Multi-domain]  Cd Length: 124  Bit Score: 58.29  E-value: 4.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710 810 GKCVSI----ENITVTLEDCDGSSQLQQFNYTWVRLIKHG--EWC--VAPIPEKGSLTLYHCDNRNNRLKWLHKSASAFH 881
Cdd:cd00161   10 GLCLDVnggsDGGPVQLYPCHGNGNNQKWTLTSDGTIRIKssNLCldVGGDAPGSKVRLYTCSGGSDNQRWTFNKDGTIR 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568913710 882 pelvdhivfeNYQQLLCME---GNFSQKTLKLAACNPmELQQKWKF 924
Cdd:cd00161   90 ----------NLKSGKCLDvkgGNTNGTNLILWTCDG-GPNQKWKF 124
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
484-599 1.09e-09

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


Pssm-ID: 223539 [Multi-domain]  Cd Length: 291  Bit Score: 60.48  E-value: 1.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710 484 DLPTTSIIMCFVDEVwSALLRSVHSVLNRSPPHLikEILLVDDFSTKEYLKAdLDKYMSQFPKVRILRLKERHGLIRARL 563
Cdd:COG0463    1 MMPKVSVVIPTYNEE-EYLPEALESLLNQTYKDF--EIIVVDDGSTDGTTEI-AIEYGAKDVRVIRLINERNGGLGAARN 76
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568913710 564 AGAQNATGDVLTFLDS---HVECNVGWLEPLLERVYLNR 599
Cdd:COG0463   77 AGLEYARGDYIVFLDAddqHPPELIPLVAAGGDGDYIAR 115
PRK10073 PRK10073
putative glycosyl transferase; Provisional
520-578 9.55e-05

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 45.42  E-value: 9.55e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568913710 520 EILLVDDFSTKEYLKAdLDKYMSQFPKVRILRlKERHGLIRARLAGAQNATGDVLTFLD 578
Cdd:PRK10073  37 EIIIVNDGSTDNSVEI-AKHYAENYPHVRLLH-QANAGVSVARNTGLAVATGKYVAFPD 93
 
Name Accession Description Interval E-value
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
489-790 1.01e-174

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 508.28  E-value: 1.01e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710 489 SIIMCFVDEVWSALLRSVHSVLNRSPPHLIKEILLVDDFSTKEYLKADLD-KYMSQFPKVRILRLKERHGLIRARLAGAQ 567
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEeYYKKYLPKVKVLRLKKREGLIRARIAGAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710 568 NATGDVLTFLDSHVECNVGWLEPLLERVYLNRKKVACPVIEVINDKDMSYMTVDNFQRGVFTWPMNFGWKTIPPDVVAKN 647
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEERRRE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710 648 giKETDIIRCPVMAGGLFSIDKSYFYELGTYDPGLDVWGGENMELSFKVWMCGGEIEIIPCSRVGHIFRND-NPYSFPKD 726
Cdd:cd02510  161 --SPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKrKPYTFPGG 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568913710 727 rMKTVERNLVRVAEVWLDDYRELFYGHGDHLidQGLDVGNLTQQRELRKKLKCKSFKWYLDNVF 790
Cdd:cd02510  239 -SGTVLRNYKRVAEVWMDEYKEYFYKARPEL--RNIDYGDLSERKALRERLKCKSFKWYLENVY 299
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
489-669 5.08e-33

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 125.20  E-value: 5.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710  489 SIIMCFVDEvWSALLRSVHSVLNRspPHLIKEILLVDDFSTkEYLKADLDKYMSQFPKVRILRLKERHGLIRARLAGAQN 568
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQ--TYPNFEIIVVDDGST-DGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710  569 ATGDVLTFLDSHVECNVGWLEPLLERVYLNRKKVACPVIEVINDKDmsymtvdnfqrgVFTWPMNFGWKTIPPDVVAKNG 648
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGET------------GEYRRASRITLSRLPFFLGLRL 144
                         170       180
                  ....*....|....*....|.
gi 568913710  649 IKETDIIRCPVMAGGLFSIDK 669
Cdd:pfam00535 145 LGLNLPFLIGGFALYRREALE 165
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
805-925 3.46e-15

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 72.54  E-value: 3.46e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710   805 INMALGKCVSI--ENITVTLEDCDGSSQLQQFNYTWVRLIKH--GEWCVAPIPEKGS-LTLYHCDNRNNRLKWLHKSASA 879
Cdd:smart00458   2 ISGNTGKCLDVngNKNPVGLFDCHGTGGNQLWKLTSDGAIRIkdTDLCLTANGNTGStVTLYSCDGTNDNQYWEVNKDGT 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 568913710   880 FHpelvdhivfeNYQQLLCMEGNFSQK--TLKLAACNPmELQQKWKFE 925
Cdd:smart00458  82 IR----------NPDSGKCLDVKDGNTgtKVILWTCSG-NPNQKWIFE 118
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
502-604 1.20e-13

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 69.46  E-value: 1.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710 502 LLRSVHSVLNRSPPHLikEILLVDDFSTKEYLkADLDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLDSHV 581
Cdd:cd00761   12 LERCLESLLAQTYPNF--EVIVVDDGSTDGTL-EILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEYILFLDADD 88
                         90       100
                 ....*....|....*....|...
gi 568913710 582 ECNVGWLEPLLERVYLNRKKVAC 604
Cdd:cd00761   89 LLLPDWLERLVAELLADPEADAV 111
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
800-922 1.84e-13

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 67.94  E-value: 1.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710  800 ASGVLINMALGKCVSIE-----NITVTLEDCDGSSQLQQFNYTWVRLIKH--GEWC--VAPIPEKGSLTLYHCDNRNNRL 870
Cdd:pfam00652   1 ATGRIRNRASGKCLDVPggssaGGPVGLYPCHGSNGNQLWTLTGDGTIRSvaSDLCldVGSTADGAKVVLWPCHPGNGNQ 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568913710  871 KWLHKSASafhpelvDHIVfeNYQQLLCME---GNFSQKTLKLAACNPMELQQKW 922
Cdd:pfam00652  81 RWRYDEDG-------TQIR--NPQSGKCLDvsgAGTSNGKVILWTCDSGNPNQQW 126
RICIN cd00161
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication. ...
810-924 4.52e-10

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication. The domain is found in a variety of molecules serving diverse functions such as enzymatic activity, inhibitory toxicity and signal transduction. Highly specific ligand binding occurs on exposed surfaces of the compact domain sturcture.


Pssm-ID: 238092 [Multi-domain]  Cd Length: 124  Bit Score: 58.29  E-value: 4.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710 810 GKCVSI----ENITVTLEDCDGSSQLQQFNYTWVRLIKHG--EWC--VAPIPEKGSLTLYHCDNRNNRLKWLHKSASAFH 881
Cdd:cd00161   10 GLCLDVnggsDGGPVQLYPCHGNGNNQKWTLTSDGTIRIKssNLCldVGGDAPGSKVRLYTCSGGSDNQRWTFNKDGTIR 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568913710 882 pelvdhivfeNYQQLLCME---GNFSQKTLKLAACNPmELQQKWKF 924
Cdd:cd00161   90 ----------NLKSGKCLDvkgGNTNGTNLILWTCDG-GPNQKWKF 124
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
484-599 1.09e-09

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


Pssm-ID: 223539 [Multi-domain]  Cd Length: 291  Bit Score: 60.48  E-value: 1.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710 484 DLPTTSIIMCFVDEVwSALLRSVHSVLNRSPPHLikEILLVDDFSTKEYLKAdLDKYMSQFPKVRILRLKERHGLIRARL 563
Cdd:COG0463    1 MMPKVSVVIPTYNEE-EYLPEALESLLNQTYKDF--EIIVVDDGSTDGTTEI-AIEYGAKDVRVIRLINERNGGLGAARN 76
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568913710 564 AGAQNATGDVLTFLDS---HVECNVGWLEPLLERVYLNR 599
Cdd:COG0463   77 AGLEYARGDYIVFLDAddqHPPELIPLVAAGGDGDYIAR 115
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
486-579 1.08e-08

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 56.06  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710 486 PTTSIIM--CFVDEVWsaLLRSVHSVLNRSPPHLikEILLVDDFSTKEYLKADLDKYMSQFPKVRILRLKERHGLIRARL 563
Cdd:cd04184    1 PLISIVMpvYNTPEKY--LREAIESVRAQTYPNW--ELCIADDASTDPEVKRVLKKYAAQDPRIKVVFREENGGISAATN 76
                         90
                 ....*....|....*.
gi 568913710 564 AGAQNATGDVLTFLDS 579
Cdd:cd04184   77 SALELATGEFVALLDH 92
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
484-725 1.95e-07

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 224136 [Multi-domain]  Cd Length: 439  Bit Score: 54.56  E-value: 1.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710 484 DLPTTSIIMCFVDEVWSALLRSVHSVLNRSPPhlIKEILLVDDFSTK---EYLKADLDKYMsqfPKVRILRL-KERHGLI 559
Cdd:COG1215   52 LLPKVSVIIPAYNEEPEVLEETLESLLSQDYP--RYEVIVVDDGSTDetyEILEELGAEYG---PNFRVIYPeKKNGGKA 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710 560 RARLAGAQNATGDVLTFLDSHVECNVGWLEPLLERVYLNRKKVACPVIEVINDKDMSYMTVdNFQRGVFTWPMNFGWKti 639
Cdd:COG1215  127 GALNNGLKRAKGDVVVILDADTVPEPDALRELVSPFEDPPVGAVVGTPRIRNRPDPSNLLG-RIQAIEYLSAFYFRLR-- 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710 640 ppdVVAKNGiketdiiRCPVMAGGLFSIDKSYFYELGTYDPgldVWGGENMELSFKVWMCGGEIEIIPCSrvghIFRNDN 719
Cdd:COG1215  204 ---AASKGG-------LISFLSGSSSAFRRSALEEVGGWLE---DTITEDADLTLRLHLRGYRVVYVPEA----IVWTEA 266

                 ....*.
gi 568913710 720 PYSFPK 725
Cdd:COG1215  267 PETLKE 272
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
501-579 7.09e-07

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 50.26  E-value: 7.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710 501 ALLRSVHSVLNRSPPHlikEILLVDDFSTkeylkaD-----LDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLT 575
Cdd:cd04179   14 ELVERLLAVLEEGYDY---EIIVVDDGST------DgtaeiARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARGDIVV 84

                 ....
gi 568913710 576 FLDS 579
Cdd:cd04179   85 TMDA 88
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
501-579 7.52e-06

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 47.47  E-value: 7.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710 501 ALLRSVHSVLNRSPPHLikEILLVDDFSTkeylkaD-----LDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLT 575
Cdd:cd04187   14 ELYERLKAVLESLGYDY--EIIFVDDGST------DrtleiLRELAARDPRVKVIRLSRNFGQQAALLAGLDHARGDAVI 85

                 ....
gi 568913710 576 FLDS 579
Cdd:cd04187   86 TMDA 89
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
520-580 8.92e-05

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 44.83  E-value: 8.92e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568913710 520 EILLVDDFSTKEYLKAdLDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLD---SH 580
Cdd:cd06442   29 EIIVVDDNSPDGTAEI-VRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAARGDVIVVMDadlSH 91
PRK10073 PRK10073
putative glycosyl transferase; Provisional
520-578 9.55e-05

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 45.42  E-value: 9.55e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568913710 520 EILLVDDFSTKEYLKAdLDKYMSQFPKVRILRlKERHGLIRARLAGAQNATGDVLTFLD 578
Cdd:PRK10073  37 EIIIVNDGSTDNSVEI-AKHYAENYPHVRLLH-QANAGVSVARNTGLAVATGKYVAFPD 93
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
508-593 2.50e-04

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 43.76  E-value: 2.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710 508 SVLNRSPPHLIKEILLVDDFS---TKEYLKadldKYMSQFPKVRILRLKERHgLIRARLAGAQNATGDVLTFLDSHVECN 584
Cdd:cd02525   21 SLLNQSYPKDLIEIIVVDGGStdgTREIVQ----EYAAKDPRIRLIDNPKRI-QSAGLNIGIRNSRGDIIIRVDAHAVYP 95

                 ....*....
gi 568913710 585 VGWLEPLLE 593
Cdd:cd02525   96 KDYILELVE 104
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
490-612 2.98e-04

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 43.43  E-value: 2.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710 490 IIMCFVDEVWSaLLRSVHSVLNRSPPHLIKEILLVDDFS---TKEYLKADLDKymsQFPKVRILRLKERH--GLIRARLA 564
Cdd:cd04192    1 VVIAARNEAEN-LPRLLQSLSALDYPKEKFEVILVDDHStdgTVQILEFAAAK---PNFQLKILNNSRVSisGKKNALTT 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568913710 565 GAQNATGDVLTFLDShvECNV--GWLEPLLERVYLNR-KKVACPVIEVIND 612
Cdd:cd04192   77 AIKAAKGDWIVTTDA--DCVVpsNWLLTFVAFIQKEQiGLVAGPVIYFKGK 125
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
661-716 1.41e-03

N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of galactosyltransferases from a wide range of Metazoa with three related galactosyltransferases activities, all three of which are possessed by one sequence in some cases. EC:2.4.1.90, N-acetyllactosamine synthase; EC:2.4.1.38, Beta-N-acetylglucosaminyl-glycopeptide beta-1,4- galactosyltransferase; and EC:2.4.1.22 Lactose synthase. Note that N-acetyllactosamine synthase is a component of Lactose synthase along with alpha-lactalbumin, in the absence of alpha-lactalbumin EC:2.4.1.90 is the catalyzed reaction.


Pssm-ID: 426936 [Multi-domain]  Cd Length: 77  Bit Score: 38.36  E-value: 1.41e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568913710  661 AGGLFSIDKSYFYELGTYDPGLDVWGGENMELSFKVWMCGGEIEIIPCSR-VGHIFR 716
Cdd:pfam02709  20 FGGVLALSREDFLRINGFSNFFWGWGGEDDDLYARLLLSGLEIERPPKGTgRYHMLK 76
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
502-594 5.54e-03

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 38.69  E-value: 5.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710 502 LLRSVHSVLNRSPPHLikEILLVDDFSTKEylkaDLDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLDSHV 581
Cdd:cd04186   12 LKACLDSLLAQTYPDF--EVIVVDNASTDG----SVELLRELFPEVRLIRNGENLGFGAGNNQGIREAKGDYVLLLNPDT 85
                         90
                 ....*....|...
gi 568913710 582 ECNVGWLEPLLER 594
Cdd:cd04186   86 VVEPGALLELLDA 98
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
504-681 9.14e-03

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 37.98  E-value: 9.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710 504 RSVHSVLNRSPPHLikEILLVDDFSTKEYLKADLDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLDSHVEC 583
Cdd:cd06423   14 RTIESLLALDYPKL--EVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKENGGKAGALNAGLRHAKGDIVVVLDADTIL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913710 584 NVGWLEPLLERVYLNRKKVA-CPVIEVINDKD--------MSYMTVDNFQRGVFTWpmnfgwktippdvvaKNGIketdi 654
Cdd:cd06423   92 EPDALKRLVVPFFADPKVGAvQGRVRVRNGSEnlltrlqaIEYLSIFRLGRRAQSA---------------LGGV----- 151
                        170       180
                 ....*....|....*....|....*..
gi 568913710 655 ircPVMAGGLFSIDKSYFYELGTYDPG 681
Cdd:cd06423  152 ---LVLSGAFGAFRREALREVGGWDED 175
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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