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Conserved domains on  [gi|21358257|ref|NP_648800|]
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polypeptide N-Acetylgalactosaminyltransferase 8 [Drosophila melanogaster]

Protein Classification

polypeptide N-acetylgalactosaminyltransferase( domain architecture ID 11551826)

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 ...
131-430 1.42e-156

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: 450.50  E-value: 1.42e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 131 SVVITYHNEEASVLLRTLSSLRSRTPIQLLREVILVDDGSTQADEKLNDFIKI-KFLNMVQHRRITTQVGLMHARVVGAE 209
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYkKYLPKVKVLRLKKREGLIRARIAGAR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 210 LALADVLVFLDSHVEVTKGWLEPLIAPILEDNRTCTTPIIDTIDFDNFAYRRGK-PSRGFFNWEFNYIQLPLLKEE--AV 286
Cdd:cd02510  81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSgDARGGFDWSLHFKWLPLPEEErrRE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 287 AMPAPHKNPIMNGGLFAIGREWFSELGGYDKGLKIWGAEQFELSLKLWLCGGQILEVPCSRVGHLFRDGnfQIRYTNKDK 366
Cdd:cd02510 161 SPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRK--RKPYTFPGG 238
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21358257 367 NSekkLISRNYRRVAEIWLDEYKDKLFANMPHLTVIPVGNLAEQRDLKNRLHCKPFKWFLDNLA 430
Cdd:cd02510 239 SG---TVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_Pgant8-like cd23461
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
445-573 4.22e-56

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 8 (Pgant8) and similar proteins; This subfamily includes Pgant8 (also called pp-GaNTase 8, protein-UDP acetylgalactosaminyltransferase 8, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8), Pgant10 (also called polypeptide N-acetylgalactosaminyltransferase 10, pp-GaNTase 10, protein-UDP acetylgalactosaminyltransferase 10, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10), Pgant11 (also called polypeptide N-acetylgalactosaminyltransferase 11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11) and Pgant12 (also called polypeptide N-acetylgalactosaminyltransferase 12, pp-GaNTase 12, protein-UDP acetylgalactosaminyltransferase 12, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12). They function as GalNAc transferases (EC 2.4.1.41) that catalyze 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. Pgant8 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers both EA2 and the diglycosylated Muc5AC-3/13 as substrates, albeit at very low levels for Muc5AC-3/13. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


:

Pssm-ID: 467339  Cd Length: 128  Bit Score: 185.30  E-value: 4.22e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 445 YASGVLQSISSPKLCLDRKDPSHGQP-KLAPCSSDHVFPSPEQYWSLTNHRELRSG--FYCLEVRnhGVNVHIYQCHGQS 521
Cdd:cd23461   1 FASGVIQSVAFPNLCLDILGRSHGGPpVLAKCSSNKSMPGTFQNFSLTFHRQIKHGtsDDCLEVR--GNNVRLSRCHYQG 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 21358257 522 GNQFWSFDSKTHQVISGQQQNfrHCLEAQPELNAVTSSVCDPKNHKQQWKFG 573
Cdd:cd23461  79 GNQYWKYDYETHQLINGGQNN--KCLEADVESLKITLSICDSDNVEQKWKWG 128
 
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 ...
131-430 1.42e-156

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: 450.50  E-value: 1.42e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 131 SVVITYHNEEASVLLRTLSSLRSRTPIQLLREVILVDDGSTQADEKLNDFIKI-KFLNMVQHRRITTQVGLMHARVVGAE 209
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYkKYLPKVKVLRLKKREGLIRARIAGAR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 210 LALADVLVFLDSHVEVTKGWLEPLIAPILEDNRTCTTPIIDTIDFDNFAYRRGK-PSRGFFNWEFNYIQLPLLKEE--AV 286
Cdd:cd02510  81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSgDARGGFDWSLHFKWLPLPEEErrRE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 287 AMPAPHKNPIMNGGLFAIGREWFSELGGYDKGLKIWGAEQFELSLKLWLCGGQILEVPCSRVGHLFRDGnfQIRYTNKDK 366
Cdd:cd02510 161 SPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRK--RKPYTFPGG 238
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21358257 367 NSekkLISRNYRRVAEIWLDEYKDKLFANMPHLTVIPVGNLAEQRDLKNRLHCKPFKWFLDNLA 430
Cdd:cd02510 239 SG---TVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_Pgant8-like cd23461
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
445-573 4.22e-56

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 8 (Pgant8) and similar proteins; This subfamily includes Pgant8 (also called pp-GaNTase 8, protein-UDP acetylgalactosaminyltransferase 8, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8), Pgant10 (also called polypeptide N-acetylgalactosaminyltransferase 10, pp-GaNTase 10, protein-UDP acetylgalactosaminyltransferase 10, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10), Pgant11 (also called polypeptide N-acetylgalactosaminyltransferase 11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11) and Pgant12 (also called polypeptide N-acetylgalactosaminyltransferase 12, pp-GaNTase 12, protein-UDP acetylgalactosaminyltransferase 12, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12). They function as GalNAc transferases (EC 2.4.1.41) that catalyze 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. Pgant8 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers both EA2 and the diglycosylated Muc5AC-3/13 as substrates, albeit at very low levels for Muc5AC-3/13. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467339  Cd Length: 128  Bit Score: 185.30  E-value: 4.22e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 445 YASGVLQSISSPKLCLDRKDPSHGQP-KLAPCSSDHVFPSPEQYWSLTNHRELRSG--FYCLEVRnhGVNVHIYQCHGQS 521
Cdd:cd23461   1 FASGVIQSVAFPNLCLDILGRSHGGPpVLAKCSSNKSMPGTFQNFSLTFHRQIKHGtsDDCLEVR--GNNVRLSRCHYQG 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 21358257 522 GNQFWSFDSKTHQVISGQQQNfrHCLEAQPELNAVTSSVCDPKNHKQQWKFG 573
Cdd:cd23461  79 GNQYWKYDYETHQLINGGQNN--KCLEADVESLKITLSICDSDNVEQKWKWG 128
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
131-311 2.13e-23

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: 97.08  E-value: 2.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257   131 SVVITYHNEEAsVLLRTLSSLRSRTPiqLLREVILVDDGSTQADEKLNDFIKIKFLNmVQHRRITTQVGLMHARVVGAEL 210
Cdd:pfam00535   1 SVIIPTYNEEK-YLLETLESLLNQTY--PNFEIIVVDDGSTDGTVEIAEEYAKKDPR-VRVIRLPENRGKAGARNAGLRA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257   211 ALADVLVFLDSHVEVTKGWLEPLIAPILEDNRTCTTPIIDTIDFDNFAYRRGKPSRGFFNWEFNYIQLPllkeeavampa 290
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLL----------- 145
                         170       180
                  ....*....|....*....|.
gi 21358257   291 PHKNPIMNGGLFAIGREWFSE 311
Cdd:pfam00535 146 GLNLPFLIGGFALYRREALEE 166
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
446-570 9.11e-22

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 91.05  E-value: 9.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257   446 ASGVLQSISSpKLCLDR--KDPSHGQPKLAPCSSDhvfpSPEQYWSLTNHRELRSGF--YCLEVRN--HGVNVHIYQCHG 519
Cdd:pfam00652   1 ATGRIRNRAS-GKCLDVpgGSSAGGPVGLYPCHGS----NGNQLWTLTGDGTIRSVAsdLCLDVGStaDGAKVVLWPCHP 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 21358257   520 QSGNQFWSFDSKTHQVISGQQQNfrhCLEAQPELNA---VTSSVCDPKNHKQQW 570
Cdd:pfam00652  76 GNGNQRWRYDEDGTQIRNPQSGK---CLDVSGAGTSngkVILWTCDSGNPNQQW 126
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
128-386 8.39e-18

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 81.96  E-value: 8.39e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 128 PSVSVVITYHNEeASVLLRTLSSLRSRTPIQLlrEVILVDDGSTqaDEKLNDFIKIKFLNmVQHRRITTQVGLMHARVVG 207
Cdd:COG1216   3 PKVSVVIPTYNR-PELLRRCLESLLAQTYPPF--EVIVVDNGST--DGTAELLAALAFPR-VRVIRNPENLGFAAARNLG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 208 AELALADVLVFLDSHVEVTKGWLEPLIApilednrtcttpiidtidFDNFAYRrgkpsrgffnwefnyiqlpllkeeava 287
Cdd:COG1216  77 LRAAGGDYLLFLDDDTVVEPDWLERLLA------------------AACLLIR--------------------------- 111
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 288 mpaphknpimngglfaigREWFSELGGYDKGLKIWGAEqFELSLKLWLCGGQILEVPCSRVGHLFRdgnfqiryTNKDKN 367
Cdd:COG1216 112 ------------------REVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGG--------ASSGPL 164
                       250
                ....*....|....*....
gi 21358257 368 SEKKLISRNYRRVAEIWLD 386
Cdd:COG1216 165 LRAYYLGRNRLLFLRKHGP 183
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
457-572 3.00e-11

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 60.60  E-value: 3.00e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257    457 KLCLDRKDpSHGQPKLAPCSSdhvfPSPEQYWSLTNHRELRSGF--YCLEVRNH-GVNVHIYQCHGQSGNQFWSFDSKT- 532
Cdd:smart00458   7 GKCLDVNG-NKNPVGLFDCHG----TGGNQLWKLTSDGAIRIKDtdLCLTANGNtGSTVTLYSCDGTNDNQYWEVNKDGt 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 21358257    533 -HQVISGQqqnfrhCLEA--QPELNAVTSSVCDPKNHkQQWKF 572
Cdd:smart00458  82 iRNPDSGK------CLDVkdGNTGTKVILWTCSGNPN-QKWIF 117
PRK10073 PRK10073
putative glycosyl transferase; Provisional
124-269 1.31e-03

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 41.18  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257  124 MEKLPSVSVVITYHNEE-------ASVLLRTLSSLrsrtpiqllrEVILVDDGSTqaDEKLNdfIKIKFLNMVQHRRITT 196
Cdd:PRK10073   2 MNSTPKLSIIIPLYNAGkdfrafmESLIAQTWTAL----------EIIIVNDGST--DNSVE--IAKHYAENYPHVRLLH 67
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21358257  197 QV--GLMHARVVGAELALADVLVFLDSHVEVTKGWLEPLIAPILEDN---RTCTTpiidtidfdNFAYRRGKPSRGFF 269
Cdd:PRK10073  68 QAnaGVSVARNTGLAVATGKYVAFPDADDVVYPTMYETLMTMALEDDldvAQCNA---------DWCFRDTGETWQSI 136
 
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 ...
131-430 1.42e-156

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: 450.50  E-value: 1.42e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 131 SVVITYHNEEASVLLRTLSSLRSRTPIQLLREVILVDDGSTQADEKLNDFIKI-KFLNMVQHRRITTQVGLMHARVVGAE 209
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYkKYLPKVKVLRLKKREGLIRARIAGAR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 210 LALADVLVFLDSHVEVTKGWLEPLIAPILEDNRTCTTPIIDTIDFDNFAYRRGK-PSRGFFNWEFNYIQLPLLKEE--AV 286
Cdd:cd02510  81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSgDARGGFDWSLHFKWLPLPEEErrRE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 287 AMPAPHKNPIMNGGLFAIGREWFSELGGYDKGLKIWGAEQFELSLKLWLCGGQILEVPCSRVGHLFRDGnfQIRYTNKDK 366
Cdd:cd02510 161 SPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRK--RKPYTFPGG 238
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21358257 367 NSekkLISRNYRRVAEIWLDEYKDKLFANMPHLTVIPVGNLAEQRDLKNRLHCKPFKWFLDNLA 430
Cdd:cd02510 239 SG---TVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_Pgant8-like cd23461
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
445-573 4.22e-56

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 8 (Pgant8) and similar proteins; This subfamily includes Pgant8 (also called pp-GaNTase 8, protein-UDP acetylgalactosaminyltransferase 8, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8), Pgant10 (also called polypeptide N-acetylgalactosaminyltransferase 10, pp-GaNTase 10, protein-UDP acetylgalactosaminyltransferase 10, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10), Pgant11 (also called polypeptide N-acetylgalactosaminyltransferase 11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11) and Pgant12 (also called polypeptide N-acetylgalactosaminyltransferase 12, pp-GaNTase 12, protein-UDP acetylgalactosaminyltransferase 12, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12). They function as GalNAc transferases (EC 2.4.1.41) that catalyze 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. Pgant8 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers both EA2 and the diglycosylated Muc5AC-3/13 as substrates, albeit at very low levels for Muc5AC-3/13. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467339  Cd Length: 128  Bit Score: 185.30  E-value: 4.22e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 445 YASGVLQSISSPKLCLDRKDPSHGQP-KLAPCSSDHVFPSPEQYWSLTNHRELRSG--FYCLEVRnhGVNVHIYQCHGQS 521
Cdd:cd23461   1 FASGVIQSVAFPNLCLDILGRSHGGPpVLAKCSSNKSMPGTFQNFSLTFHRQIKHGtsDDCLEVR--GNNVRLSRCHYQG 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 21358257 522 GNQFWSFDSKTHQVISGQQQNfrHCLEAQPELNAVTSSVCDPKNHKQQWKFG 573
Cdd:cd23461  79 GNQYWKYDYETHQLINGGQNN--KCLEADVESLKITLSICDSDNVEQKWKWG 128
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
445-573 1.80e-24

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 9 (Pgant9) and similar proteins; The subfamily includes Pgant9 (also called pp-GaNTase 9, protein-UDP acetylgalactosaminyltransferase 9, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9), Pgant4 (also called pp-GaNTase 4, N-acetylgalactosaminyltransferase 4, protein-UDP acetylgalactosaminyltransferase 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4) and Pgant6 (also called pp-GaNTase 6, N-acetylgalactosaminyltransferase 6, protein-UDP acetylgalactosaminyltransferase 6, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6). They function as GalNAc transferases (EC 2.4.1.41) that catalyze 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. Pgant9 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Pgant4 and Pgant6 do not act as a peptide transferase, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. They prefer the diglycosylated Muc5AC-3/13 as a substrate. Pgant6 may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467340 [Multi-domain]  Cd Length: 126  Bit Score: 98.59  E-value: 1.80e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 445 YASGVLQSISsPKLCLD---RKDPSHGQPKLAPCSsdhvFPSPEQYWSLTNHRELRSGFYCLEVRNHGVNVHIYQCHGQS 521
Cdd:cd23462   3 LAYGEIRNLA-GKLCLDapgRKKELNKPVGLYPCH----GQGGNQYWMLTKDGEIRRDDLCLDYAGGSGDVTLYPCHGMK 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 21358257 522 GNQFWSFDSKTHQVISGqqqNFRHCLEAQPELNAVTSSVCDPKNHKQQWKFG 573
Cdd:cd23462  78 GNQFWIYDEETKQIVHG---TSKKCLELSDDSSKLVMEPCNGSSPRQQWEFE 126
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
131-311 2.13e-23

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: 97.08  E-value: 2.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257   131 SVVITYHNEEAsVLLRTLSSLRSRTPiqLLREVILVDDGSTQADEKLNDFIKIKFLNmVQHRRITTQVGLMHARVVGAEL 210
Cdd:pfam00535   1 SVIIPTYNEEK-YLLETLESLLNQTY--PNFEIIVVDDGSTDGTVEIAEEYAKKDPR-VRVIRLPENRGKAGARNAGLRA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257   211 ALADVLVFLDSHVEVTKGWLEPLIAPILEDNRTCTTPIIDTIDFDNFAYRRGKPSRGFFNWEFNYIQLPllkeeavampa 290
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLL----------- 145
                         170       180
                  ....*....|....*....|.
gi 21358257   291 PHKNPIMNGGLFAIGREWFSE 311
Cdd:pfam00535 146 GLNLPFLIGGFALYRREALEE 166
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
458-572 2.26e-22

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 3 (Pgant3) and similar proteins; Pgant3, also called pp-GaNTase 3, protein-UDP acetylgalactosaminyltransferase 3, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, functions as a GalNAc transferase (EC 2.4.1.41) that 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. Pgant3 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers EA2 as a substrate and has weak activity toward Muc5AC-3, -13 and -3/13 substrates. Pgant3 plays a critical role in the regulation of integrin-mediated cell adhesion during wing development by influencing, via glycosylation, the secretion and localization of the integrin ligand Tig to the basal cell layer interface. It may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Together with Pgant35A, Pgant3 regulates integrin levels and activity-dependent integrin signaling at the synapse in neurons and muscles. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467338 [Multi-domain]  Cd Length: 121  Bit Score: 92.51  E-value: 2.26e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 458 LCLDRKDPSHGQ--PKLAPCSSDHvfpsPEQYWSLTNHRELRSGFYCLEVRNhGVNVHIYQCHGQSGNQFWSFDSKTHQV 535
Cdd:cd23460  12 LCLDWAGESNGDktVALKPCHGGG----GNQFWMYTGDGQIRQDHLCLTADE-GNKVTLRECADQLPSQEWSYDEKTGTI 86
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 21358257 536 isgQQQNFRHCLEAQPELNAVTSSVCDPKNHKQQWKF 572
Cdd:cd23460  87 ---RHRSTGLCLTLDANNDVVILKECDSNSLWQKWIF 120
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
446-570 9.11e-22

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 91.05  E-value: 9.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257   446 ASGVLQSISSpKLCLDR--KDPSHGQPKLAPCSSDhvfpSPEQYWSLTNHRELRSGF--YCLEVRN--HGVNVHIYQCHG 519
Cdd:pfam00652   1 ATGRIRNRAS-GKCLDVpgGSSAGGPVGLYPCHGS----NGNQLWTLTGDGTIRSVAsdLCLDVGStaDGAKVVLWPCHP 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 21358257   520 QSGNQFWSFDSKTHQVISGQQQNfrhCLEAQPELNA---VTSSVCDPKNHKQQW 570
Cdd:pfam00652  76 GNGNQRWRYDEDGTQIRNPQSGK---CLDVSGAGTSngkVILWTCDSGNPNQQW 126
beta-trefoil_Ricin_GALNT10-like cd23439
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
446-572 4.82e-19

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 10 (GALNT10)-like subfamily; The GALNT10-like subfamily includes GALNT10 and GALNTL6. They act as GalNAc transferases (EC 2.4.1.41) that catalyze 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. GALNT10 has activity toward Muc5Ac and EA2 peptide substrates. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467317 [Multi-domain]  Cd Length: 126  Bit Score: 83.16  E-value: 4.82e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 446 ASGVLQSISSpKLCLDRKDPSHGQP-KLAPCSSDHvfPSPEQYWSLTNHRELRSGF--YCLEVRNHGVN--VHIYQCHGQ 520
Cdd:cd23439   1 ASGEIRNVGS-GLCIDTKHGGENDEvRLSKCVKDG--GGGEQQFELTWHEDIRPKKrkVCFDVSSHTPGapVILYACHGM 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21358257 521 SGNQFWSFDSKTHQ---VISgqqqnfRHCLEAQPELNAVTSSVCDPKNHKQQWKF 572
Cdd:cd23439  78 KGNQLWKYRPNTKQlyhPVS------GLCLDADPGSGKVFMNHCDESSDTQKWTW 126
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
128-386 8.39e-18

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 81.96  E-value: 8.39e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 128 PSVSVVITYHNEeASVLLRTLSSLRSRTPIQLlrEVILVDDGSTqaDEKLNDFIKIKFLNmVQHRRITTQVGLMHARVVG 207
Cdd:COG1216   3 PKVSVVIPTYNR-PELLRRCLESLLAQTYPPF--EVIVVDNGST--DGTAELLAALAFPR-VRVIRNPENLGFAAARNLG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 208 AELALADVLVFLDSHVEVTKGWLEPLIApilednrtcttpiidtidFDNFAYRrgkpsrgffnwefnyiqlpllkeeava 287
Cdd:COG1216  77 LRAAGGDYLLFLDDDTVVEPDWLERLLA------------------AACLLIR--------------------------- 111
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 288 mpaphknpimngglfaigREWFSELGGYDKGLKIWGAEqFELSLKLWLCGGQILEVPCSRVGHLFRdgnfqiryTNKDKN 367
Cdd:COG1216 112 ------------------REVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGG--------ASSGPL 164
                       250
                ....*....|....*....
gi 21358257 368 SEKKLISRNYRRVAEIWLD 386
Cdd:COG1216 165 LRAYYLGRNRLLFLRKHGP 183
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
128-361 1.37e-16

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 78.59  E-value: 1.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 128 PSVSVVITYHNEEASvLLRTLSSLRSRTPIQLlrEVILVDDGSTQA-DEKLNDFIKIkfLNMVQHRRITTQVGLMHARVV 206
Cdd:COG0463   2 PLVSVVIPTYNEEEY-LEEALESLLAQTYPDF--EIIVVDDGSTDGtAEILRELAAK--DPRIRVIRLERNRGKGAARNA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 207 GAELALADVLVFLDSHVEVTKGWLEPLIAPILEDNrtcttpiIDTIDFDNFAYRRGKPSRGFFNWEFNYIQLPLlkeeav 286
Cdd:COG0463  77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGP-------ADLVYGSRLIREGESDLRRLGSRLFNLVRLLT------ 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21358257 287 ampaphKNPIMNGGLFAIGREWFSELgGYDKGLkiwgAEQFELsLKLWLCGGQILEVPcsrvgHLFRDGNFQIRY 361
Cdd:COG0463 144 ------NLPDSTSGFRLFRREVLEEL-GFDEGF----LEDTEL-LRALRHGFRIAEVP-----VRYRAGESKLNL 201
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
119-355 3.23e-16

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


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 79.79  E-value: 3.23e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 119 KLKYPMEKLPSVSVVITYHNEEAsVLLRTLSSLRSRTPIQLLREVILVDDGSTQA-DEKLNDFIKiKFLNmVQHRRITTQ 197
Cdd:COG1215  20 RRRRAPADLPRVSVIIPAYNEEA-VIEETLRSLLAQDYPKEKLEVIVVDDGSTDEtAEIARELAA-EYPR-VRVIERPEN 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 198 VGLMHARVVGAELALADVLVFLDSHVEVTKGWLEPLIAPilednrtcttpiidtidfdnfayrrgkpsrgffnwefnyiq 277
Cdd:COG1215  97 GGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAA----------------------------------------- 135
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21358257 278 lplLKEEAVAmpaphknpiMNGGLFAIGREWFSELGGYDKGLkiwGAEQFELSLKLWLCGGQILEVPCSRVGHLFRDG 355
Cdd:COG1215 136 ---FADPGVG---------ASGANLAFRREALEEVGGFDEDT---LGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPET 198
beta-trefoil_Ricin_GALNT1-like cd23433
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
457-573 8.58e-15

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 1 (GALNT1)-like subfamily; The GALNT1-like subfamily includes GALNT1 and GALNT13. They catalyze 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. GALNT1 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. GALNT13 has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. It can glycosylate SDC3. It may be responsible for the synthesis of Tn antigen in neuronal cells. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467311 [Multi-domain]  Cd Length: 127  Bit Score: 71.19  E-value: 8.58e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 457 KLCLD---RKdpSHGQPKLAPCssdHVFPSpEQYWSLTNHRELRSGFYCLEVRNHGVNVHIYQCHGQSGNQFWSFDSKTH 533
Cdd:cd23433  15 NLCLDtmgRK--AGEKVGLSSC---HGQGG-NQVFSYTAKGEIRSDDLCLDASRKGGPVKLEKCHGMGGNQEWEYDKETK 88
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 21358257 534 Q---VISGQqqnfrhCLEAQPE--LNAVTSSVCDPKNHkQQWKFG 573
Cdd:cd23433  89 QirhVNSGL------CLTAPNEddPNEPVLRPCDGGPS-QKWELE 126
beta-trefoil_Ricin_GALNTL6 cd23477
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
441-583 1.74e-13

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase-like 6 (GALNTL6) and similar proteins; GALNTL6 (EC 2.4.1.41), also called polypeptide GalNAc transferase 17, GalNAc-T17, pp-GaNTase 17, protein-UDP acetylgalactosaminyltransferase 17, putative polypeptide N-acetylgalactosaminyltransferase 17, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 17, 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. GALNTL6 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467355  Cd Length: 148  Bit Score: 68.04  E-value: 1.74e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 441 DPAEYASGVLQSISSpKLCLDRKDPSHGQP-KLAPC---SSDHVFpSPEQYWSLTNHRELRSG------FYCLEVRNHGV 510
Cdd:cd23477   1 EPPPAAWGEIRNVAA-NLCVDSKHGATGTElRLDICvkdGSERTW-SHEQLFTFGWREDIRPGeplhtrKFCFDAISHNS 78
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21358257 511 NVHIYQCHGQSGNQFWSF-DSKT--HQVISGqqqnfrhCLEAQPELNAVTSSVCDPKNHKQQWKFGYLNSQRLQHF 583
Cdd:cd23477  79 PVTLYDCHGMKGNQLWSYrKDKTlfHPVSNS-------CMDCNPADKKIFMNRCDPLSETQQWIFEHTNMTVLEKF 147
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
132-241 3.31e-12

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: 64.45  E-value: 3.31e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 132 VVITYHNEEaSVLLRTLSSLRSRTPIQLlrEVILVDDGSTQAD-EKLNDFIKIKFLnmVQHRRITTQVGLMHARVVGAEL 210
Cdd:cd00761   1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGSTDGTlEILEEYAKKDPR--VIRVINEENQGLAAARNAGLKA 75
                        90       100       110
                ....*....|....*....|....*....|.
gi 21358257 211 ALADVLVFLDSHVEVTKGWLEPLIAPILEDN 241
Cdd:cd00761  76 ARGEYILFLDADDLLLPDWLERLVAELLADP 106
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
486-573 1.03e-11

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 7 (GALNT7) and similar proteins; GALNT7 (EC 2.4.1.41), also called polypeptide GalNAc transferase 7, GalNAc-T7, pp-GaNTase 7, protein-UDP acetylgalactosaminyltransferase 7, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7, acts as glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Its appropriate peptide substrate remains unidentified. GALNT7 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467315 [Multi-domain]  Cd Length: 124  Bit Score: 62.31  E-value: 1.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 486 QYWSLTNHRELRSGFYCLEVRNHGVNVHIYQCHGqSGNQFWSFDSKTHQvisgqqqnFRH-----CLEAQPELNAVTSSV 560
Cdd:cd23437  40 QLFRLNEAGQLAVGEQCLTASGSGGKVKLRKCNL-GETGKWEYDEATGQ--------IRHkgtgkCLDLNEGTNKLILQP 110
                        90
                ....*....|...
gi 21358257 561 CDPKNHKQQWKFG 573
Cdd:cd23437 111 CDSSSPSQKWEFN 123
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
457-572 3.00e-11

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 60.60  E-value: 3.00e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257    457 KLCLDRKDpSHGQPKLAPCSSdhvfPSPEQYWSLTNHRELRSGF--YCLEVRNH-GVNVHIYQCHGQSGNQFWSFDSKT- 532
Cdd:smart00458   7 GKCLDVNG-NKNPVGLFDCHG----TGGNQLWKLTSDGAIRIKDtdLCLTANGNtGSTVTLYSCDGTNDNQYWEVNKDGt 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 21358257    533 -HQVISGQqqnfrhCLEA--QPELNAVTSSVCDPKNHkQQWKF 572
Cdd:smart00458  82 iRNPDSGK------CLDVkdGNTGTKVILWTCSGNPN-QKWIF 117
beta-trefoil_Ricin_GALNT10 cd23476
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
458-586 3.77e-11

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 10 (GALNT10) and similar proteins; GALNT10 (EC 2.4.1.41), also called polypeptide GalNAc transferase 10, GalNAc-T10, pp-GaNTase 10, protein-UDP acetylgalactosaminyltransferase 10, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10, 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. GALNT10 has activity toward Muc5Ac and EA2 peptide substrates. GALNT10 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467354  Cd Length: 150  Bit Score: 61.52  E-value: 3.77e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 458 LCLDRKDPSHGQP-KLAPC--SSDHVFPSPEQYWSLTNHRELRSG------FYCLEVRNHGVNVHIYQCHGQSGNQFWSF 528
Cdd:cd23476  17 LCADTKHGALGSPlRLEGCvkGRGEAAWNNGQVFTFGWREDIRPGdpqhtkKFCFDAISHNSPVTLYDCHGMKGNQLWRY 96
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 529 --DSKTHQVISGQqqnfrhCLEAQPELNAVTSSVCDPKNHKQQWKFGYLNSQRLQHFWDN 586
Cdd:cd23476  97 rkDKTLYHPVSNS------CMDCSESDHRIFMNTCNPSSPTQQWLFEHTNSTVLEKFNRN 150
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
453-572 1.29e-10

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14)-like subfamily; The GALNT14-like subfamily includes GALNT14 and GALNT16. They act as GalNAc transferases (EC 2.4.1.41) that catalyze 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. GALNT14 displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). It may be involved in O-glycosylation in the kidney. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467319 [Multi-domain]  Cd Length: 122  Bit Score: 58.95  E-value: 1.29e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 453 ISSPKLCLD---RKDPSHGQPKLAPCSSDhvfpSPEQYWSLTNHRELRSGFYCLEVRNHGVN--VHIYQChGQSGNQFWS 527
Cdd:cd23441   8 IKQGNLCLDsdeQLFQGPALLILAPCSNS----SDSQEWSFTKDGQLQTQGLCLTVDSSSKDlpVVLETC-SDDPKQKWT 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 21358257 528 FDSKT--HQViSGQqqnfrhCLEAQPELNAVTsSVCDPKNHKQQWKF 572
Cdd:cd23441  83 RTGRQlvHSE-SGL------CLDSRKKKGLVV-SPCRSGAPSQKWDF 121
beta-trefoil_Ricin_GALNT11 cd23440
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
458-572 1.47e-10

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 11 (GALNT11) and similar proteins; GALNT11 (EC 2.4.1.41), also called polypeptide GalNAc transferase 11, GalNAc-T11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11, 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. It is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes its activation, modulating the balance between motile and immotile (sensory) cilia at the left-right organizer (LRO). GALNT11 displays the same enzyme activity toward MUC1, MUC4, and EA2 as GALNT1. It is not involved in glycosylation of erythropoietin (EPO). GALNT11 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467318 [Multi-domain]  Cd Length: 127  Bit Score: 58.93  E-value: 1.47e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 458 LCLDRKDPSHGQP---KLAPCSSDhvfpSPEQYWSLTNHRELR-SGFYCLEVRNHGVNV-HIYQCHGQSGNQFWSF--DS 530
Cdd:cd23440  15 LCLVAEDEVSQKGsllVLRPCSRN----DKKQLWYYTEDGELRlANLLCLDSSETSSDFpRLMKCHGSGGSQQWRFkkDN 90
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 21358257 531 KTHQVISGQqqnfrhCLEAQPELNAVTSS--VCDpKNHKQQWKF 572
Cdd:cd23440  91 RLYNPASGQ------CLAASKNGTSGYVTmdICS-DSPSQKWVF 127
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
131-351 3.29e-10

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: 59.11  E-value: 3.29e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 131 SVVITYHNEEasVLLRTLSSLRSRTPIQLlrEVILVDDGSTQADEklnDFIKIKFLnmvQHRRITTQ--VGLMHARVVGA 208
Cdd:cd04186   1 IIIVNYNSLE--YLKACLDSLLAQTYPDF--EVIVVDNASTDGSV---ELLRELFP---EVRLIRNGenLGFGAGNNQGI 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 209 ELALADVLVFLDSHVEVTKGWLEPLIAPILEDNRTcttpiidtidfdnfayrrgkpsrgffnwefnyiqlpllkeeAVAM 288
Cdd:cd04186  71 REAKGDYVLLLNPDTVVEPGALLELLDAAEQDPDV-----------------------------------------GIVG 109
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21358257 289 paphknPIMNGGLFAIGREWFSELGGYDKGLKIWGaEQFELSLKLWLCGGQILEVPCSRVGHL 351
Cdd:cd04186 110 ------PKVSGAFLLVRREVFEEVGGFDEDFFLYY-EDVDLCLRARLAGYRVLYVPQAVIYHH 165
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
132-316 1.05e-09

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: 58.01  E-value: 1.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 132 VVITYHNEEAsVLLRTLSSLRSRTpiQLLREVILVDDGSTQAD-EKLNDFIKIKFLNMVQHRRITTQ-------VGLMHA 203
Cdd:cd06423   1 IIVPAYNEEA-VIERTIESLLALD--YPKLEVIVVDDGSTDDTlEILEELAALYIRRVLVVRDKENGgkagalnAGLRHA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 204 RvvgaelalADVLVFLDSHVEVTKGWLEPLIAPILEDNRT---CTTP-IIDTidFDNFAYRrgkpsrgFFNWEFNYIQLp 279
Cdd:cd06423  78 K--------GDIVVVLDADTILEPDALKRLVVPFFADPKVgavQGRVrVRNG--SENLLTR-------LQAIEYLSIFR- 139
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 21358257 280 LLKeeaVAMPAPHKNPIMNGGLFAIGREWFSELGGYD 316
Cdd:cd06423 140 LGR---RAQSALGGVLVLSGAFGAFRREALREVGGWD 173
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
129-378 6.84e-09

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: 56.86  E-value: 6.84e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 129 SVSVVITYHNEEASV--LLRTLssLRSRTPIQLLrEVILVDDGSTQADEKL-----NDFIKIKFLNMVqhRRITTQvglm 201
Cdd:cd02525   1 FVSIIIPVRNEEKYIeeLLESL--LNQSYPKDLI-EIIVVDGGSTDGTREIvqeyaAKDPRIRLIDNP--KRIQSA---- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 202 hARVVGAELALADVLVFLDSHVEVTKGWLEPLIAPILEDNRTCTTPIIDTIDFDNF-----------------AYRRGKP 264
Cdd:cd02525  72 -GLNIGIRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFqkaiavaqssplgsggsAYRGGAV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 265 SRGFfnwefnyiqlpllkeeavAMPAPHknpimngGLFAigREWFSELGGYDKGLKIwgAEQFELSLKLWLCGGQILEVP 344
Cdd:cd02525 151 KIGY------------------VDTVHH-------GAYR--REVFEKVGGFDESLVR--NEDAELNYRLRKAGYKIWLSP 201
                       250       260       270
                ....*....|....*....|....*....|....
gi 21358257 345 CSRVGHLFRDgNFqirytnkdknseKKLISRNYR 378
Cdd:cd02525 202 DIRVYYYPRS-TL------------KKLARQYFR 222
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
501-582 1.44e-08

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 53.30  E-value: 1.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257   501 YCLEVRNH---GVNVHIYQCHGQSGNQFWSFDsKTHQVISGQQQNfrhCLEAQ--PELNAVTSSVCDPKNHKQQWKFGYl 575
Cdd:pfam00652  12 KCLDVPGGssaGGPVGLYPCHGSNGNQLWTLT-GDGTIRSVASDL---CLDVGstADGAKVVLWPCHPGNGNQRWRYDE- 86

                  ....*..
gi 21358257   576 NSQRLQH 582
Cdd:pfam00652  87 DGTQIRN 93
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
495-582 3.49e-08

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 2 (GALNT2) and similar proteins; GALNT2 (EC 2.4.1.41), also called polypeptide GalNAc transferase 2, GalNAc-T2, pp-GaNTase 2, protein-UDP acetylgalactosaminyltransferase 2, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2, 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. GALNT2 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. It is probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region. It is also involved in O-linked glycosylation of APOC-III, ANGPTL3 and PLTP. It participates in the regulation of HDL-C metabolism. GALNT2 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467312 [Multi-domain]  Cd Length: 121  Bit Score: 51.94  E-value: 3.49e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 495 ELRSGFYCLEVRNHGVN--VHIYQCHGQSGNQFWSFdSKTHQVisgqqqnfRH---CLEA--QPELNAVTSSVCDPKNHK 567
Cdd:cd23434   4 SLKQGNLCLDTLGHKAGgtVGLYPCHGTGGNQEWSF-TKDGQI--------KHddlCLTVvdRAPGSLVTLQPCREDDSN 74
                        90
                ....*....|....*
gi 21358257 568 QQWKFGYLNSQrLQH 582
Cdd:cd23434  75 QKWEQIENNSK-LRH 88
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
486-572 3.18e-07

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 2 (GALNT2) and similar proteins; GALNT2 (EC 2.4.1.41), also called polypeptide GalNAc transferase 2, GalNAc-T2, pp-GaNTase 2, protein-UDP acetylgalactosaminyltransferase 2, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2, 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. GALNT2 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. It is probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region. It is also involved in O-linked glycosylation of APOC-III, ANGPTL3 and PLTP. It participates in the regulation of HDL-C metabolism. GALNT2 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467312 [Multi-domain]  Cd Length: 121  Bit Score: 49.24  E-value: 3.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 486 QYWSLTNHRELRSGFYCLEV--RNHGVNVHIYQCHGQSGNQFWSFDSKTHQVISGQQQnfrHCLEAQPE-LNAVTSSVCD 562
Cdd:cd23434  35 QEWSFTKDGQIKHDDLCLTVvdRAPGSLVTLQPCREDDSNQKWEQIENNSKLRHVGSN---LCLDSRNAkSGGLTVETCD 111
                        90
                ....*....|
gi 21358257 563 PKNHKQQWKF 572
Cdd:cd23434 112 PSSGSQQWKF 121
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
131-333 3.93e-07

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 51.89  E-value: 3.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257   131 SVVITYHN-EEASVLLRTLSSLRSRTPIQLlrEVILVDDGSTQ-ADEKLNDFIKIKFLNMVQHRRITTqVGLMHARVVGA 208
Cdd:pfam10111   1 SVVIPVYNgEKTHWIQERILNQTFQYDPEF--ELIIINDGSTDkTLEEVSSIKDHNLQVYYPNAPDTT-YSLAASRNRGT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257   209 ELALADVLVFLDSHVEVTKGWLEPLIAPILEDNrtcTTPIIDTIDFDNFAYRRGKPSRGFFNWEFNYIQLPLLKEEAVAM 288
Cdd:pfam10111  78 SHAIGEYISFIDGDCLWSPDKFEKQLKIATSLA---LQENIQAAVVLPVTDLNDESSNFLRRGGDLTASGDVLRDLLVFY 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 21358257   289 PAPHKNPIMNGGLFAIGREWFSELGGYDKGLKIWGAEQFELSLKL 333
Cdd:pfam10111 155 SPLAIFFAPNSSNALINRQAFIEVGGFDESFRGHGAEDFDIFLRL 199
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
495-582 4.45e-07

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 7 (GALNT7) and similar proteins; GALNT7 (EC 2.4.1.41), also called polypeptide GalNAc transferase 7, GalNAc-T7, pp-GaNTase 7, protein-UDP acetylgalactosaminyltransferase 7, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7, acts as glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Its appropriate peptide substrate remains unidentified. GALNT7 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467315 [Multi-domain]  Cd Length: 124  Bit Score: 48.83  E-value: 4.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 495 ELRSGF--YCLEVRNHGVN--VHIYQCHGQSGNQFWSFDSKtHQVISGQQqnfrhCLEAQPELNAVTSSVCDPKNhKQQW 570
Cdd:cd23437   7 EIRNLGtgLCLDTMGHQNGgpVGLYPCHGMGGNQLFRLNEA-GQLAVGEQ-----CLTASGSGGKVKLRKCNLGE-TGKW 79
                        90
                ....*....|..
gi 21358257 571 KFGyLNSQRLQH 582
Cdd:cd23437  80 EYD-EATGQIRH 90
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
132-322 4.55e-07

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: 51.14  E-value: 4.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 132 VVITYHNEEASvLLRTLSSLRSRT-PIQLLrEVILVDDGSTQADEKLNDFIKIKflNMVQHRRITTQ----VGLMHARVV 206
Cdd:cd04192   1 VVIAARNEAEN-LPRLLQSLSALDyPKEKF-EVILVDDHSTDGTVQILEFAAAK--PNFQLKILNNSrvsiSGKKNALTT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 207 GAELALADVLVFLDSHVEVTKGWLEPLIAPILEDNRTcttpIIdtidfdnFAYRRGKPSRGFFN----WEFNYIQLpllk 282
Cdd:cd04192  77 AIKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIG----LV-------AGPVIYFKGKSLLAkfqrLDWLSLLG---- 141
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 21358257 283 eeAVAMPAPHKNPIM-NGGLFAIGREWFSELGGYDKGLKIW 322
Cdd:cd04192 142 --LIAGSFGLGKPFMcNGANMAYRKEAFFEVGGFEGNDHIA 180
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
127-312 5.24e-07

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. 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 of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 51.04  E-value: 5.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 127 LPSVSVVITYHNEEAsVLLRTLSSLRSRTPIQLLREVILVDDGSTQA-DEKLNDFIK--IKFLNMVQHRrittqvGLMHA 203
Cdd:cd06439  28 LPTVTIIIPAYNEEA-VIEAKLENLLALDYPRDRLEIIVVSDGSTDGtAEIAREYADkgVKLLRFPERR------GKAAA 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 204 RVVGAELALADVLVFLDSHVEVTKGWLEPLIAPiLEDNR----TCTTPIIDTIDFDNF--AYRRgkpsrgFFNWefnyiq 277
Cdd:cd06439 101 LNRALALATGEIVVFTDANALLDPDALRLLVRH-FADPSvgavSGELVIVDGGGSGSGegLYWK------YENW------ 167
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 21358257 278 lplLKE-EAvampAPHKNPIMNGGLFAIGREWFSEL 312
Cdd:cd06439 168 ---LKRaES----RLGSTVGANGAIYAIRRELFRPL 196
beta-trefoil_Ricin_GALNT15 cd23442
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
445-571 1.60e-06

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 15 (GALNT15) and similar proteins; GALNT15 (EC 2.4.1.41), also called polypeptide GalNAc transferase 15, GalNAc-T15, polypeptide GalNAc transferase-like protein 2, GalNAc-T-like protein 2, pp-GaNTase-like protein 2, polypeptide N-acetylgalactosaminyltransferase-like protein 2, protein-UDP acetylgalactosaminyltransferase-like protein 2, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 2, 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. Although it displays a much weaker activity toward all substrates tested compared to GALNT2, GALNT15 can transfer up to seven GalNAc residues to the Muc5AC peptide, suggesting that it can fill vicinal Thr/Ser residues in cooperation with other GALNT proteins. It prefers Muc1a as its substrate. GALNT15 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467320 [Multi-domain]  Cd Length: 124  Bit Score: 47.44  E-value: 1.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 445 YASGVLQSISSPkLCLD---RKDPSHGQPKLAPCSSDHvfpsPEQYWSLTNHRELRSGF--YCLEVRNHgvNVHIYQCHG 519
Cdd:cd23442   3 YFSGQLYNTGTG-YCADyihGWRLAGGPVELSPCSGQN----GNQLFEYTSDKEIRFGSlqLCLDVRQE--QVVLQNCTK 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 21358257 520 QSGNQFWSFDsKTHQVIsgqQQNFRHCLEA-QPELNAVTS-SVCDPKNHkQQWK 571
Cdd:cd23442  76 EKTSQKWDFQ-ETGRIV---HILSGKCIEAvESENSKLLFlSPCNGQRN-QMWK 124
beta-trefoil_Ricin_Pgant1-like cd23459
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
458-572 1.75e-06

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 1 (Pgant1) and similar proteins; Pgant1, also called pp-GaNTase 1, protein-UDP acetylgalactosaminyltransferase 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1, functions as a GalNAc transferase (EC 2.4.1.41) that 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. Pgant1 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers the monoglycosylated Muc5AC-3 as a substrate. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467337 [Multi-domain]  Cd Length: 132  Bit Score: 47.31  E-value: 1.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 458 LCLD--RKDPSHGQP-KLAPCssdHVFPSPEQYWSLTNHRELRSGFYCLEVRNH-GVNVHIYQCHG-QSGNQFWSFDSkt 532
Cdd:cd23459  17 LCLDtlQRDEDKGYNlGLYPC---QGGLSSNQLFSLSKKGELRREESCADVQGTeESKVILITCHGlEKFNQKWKHTK-- 91
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 21358257 533 HQVISGQQQNfrHCLEAQPELN--AVTSSVCDPKNHkQQWKF 572
Cdd:cd23459  92 GGQIVHLASG--KCLDAEGLKSgdDVTLAKCDGSLS-QKWTF 130
beta-trefoil_Ricin_GALNT1 cd23466
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
486-570 1.75e-06

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 1 (GALNT1) and similar proteins; GALNT1 (EC 2.4.1.41), also called polypeptide GalNAc transferase 1, GalNAc-T1, pp-GaNTase 1, protein-UDP acetylgalactosaminyltransferase 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1, 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. It has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. GALNT1 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain is required in the glycopeptide specificity of enzyme activity but not for activity with naked peptide substrates, suggesting that it triggers the catalytic domain to act on GalNAc-glycopeptide substrates.


Pssm-ID: 467344  Cd Length: 127  Bit Score: 47.35  E-value: 1.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 486 QYWSLTNHRELRSGFYCLEVRNHGVNVHIYQCHGQSGNQFWSFDSKThqvISGQQQNFRHCLEAQPELNAVTSSVCD-PK 564
Cdd:cd23466  41 QVFSYTANKEIRTDDLCLDVSKLNGPVMMLKCHHLKGNQLWEYDPVK---LTLLHVNSNQCLDKATEEDSQVPSIRDcNG 117

                ....*.
gi 21358257 565 NHKQQW 570
Cdd:cd23466 118 SRSQQW 123
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
130-333 6.43e-06

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily 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: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 47.57  E-value: 6.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 130 VSVVITYHNEEASvLLRTLSSLRSRTPIQLlrEVILVDDGSTQADEKLndfikikflnmVQ---HRRITTQVG---LMHA 203
Cdd:cd02522   1 LSIIIPTLNEAEN-LPRLLASLRRLNPLPL--EIIVVDGGSTDGTVAI-----------ARsagVVVISSPKGrarQMNA 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 204 rvvGAELALADVLVFLDSHVEVTKGWLEPLIApILEDNRtcttpiidtIDFDNFAYRRGKPSRGFF------NWEFNYIQ 277
Cdd:cd02522  67 ---GAAAARGDWLLFLHADTRLPPDWDAAIIE-TLRADG---------AVAGAFRLRFDDPGPRLRllelgaNLRSRLFG 133
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21358257 278 LPLlkeeavampaphknpimnG--GLFaIGREWFSELGGYDKGLKIwgaEQFELSLKL 333
Cdd:cd02522 134 LPY------------------GdqGLF-IRRELFEELGGFPELPLM---EDVELVRRL 169
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
501-572 9.16e-06

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 3 (GALNT3)-like subfamily; The GALNT3-like subfamily includes GALNT3, GALNT4, GALNT6 and GALNT12. They act as GalNAc transferases (EC 2.4.1.41) that catalyze 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. GALNT3 has activity toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. It probably glycosylates fibronectin in vivo as well as FGF23. It plays a central role in phosphate homeostasis. GALNT4 shows highest activity towards Muc7, EA2 and Muc2, with a lower activity compared to GALNT2. It glycosylates 'Thr-57' of SELPLG. GALNT6 may participate in the synthesis of oncofetal fibronectin. It has activity toward Muc1a, Muc2, EA2 and fibronectin peptides. GALNT12 has activity toward non-glycosylated peptides such as Muc5AC, Muc1a and EA2, and no detectable activity with non-glycosylated Muc2 and Muc7. It displays enzymatic activity toward the Gal-NAc-Muc5AC glycopeptide, but no detectable activity to mono-GalNAc-glycosylated Muc1a, Muc2, Muc7 and EA2. It may play an important role in the initial step of mucin-type oligosaccharide biosynthesis in digestive organs. Members of this family comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which are characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467313 [Multi-domain]  Cd Length: 128  Bit Score: 45.40  E-value: 9.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 501 YCLEVRNH----GVNVHIYQCHGQSGNQFWSFDSKTHqvisgqqqnFRH------CLEAQPELNAVTSSvCDPKNH---- 566
Cdd:cd23435  14 LCLDVNNPngqgGKPVIMYGCHGLGGNQYFEYTSKGE---------IRHnigkelCLHASGSDEVILQH-CTSKGKdvpp 83

                ....*.
gi 21358257 567 KQQWKF 572
Cdd:cd23435  84 EQKWLF 89
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
447-573 2.47e-05

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 3 (GALNT3)-like subfamily; The GALNT3-like subfamily includes GALNT3, GALNT4, GALNT6 and GALNT12. They act as GalNAc transferases (EC 2.4.1.41) that catalyze 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. GALNT3 has activity toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. It probably glycosylates fibronectin in vivo as well as FGF23. It plays a central role in phosphate homeostasis. GALNT4 shows highest activity towards Muc7, EA2 and Muc2, with a lower activity compared to GALNT2. It glycosylates 'Thr-57' of SELPLG. GALNT6 may participate in the synthesis of oncofetal fibronectin. It has activity toward Muc1a, Muc2, EA2 and fibronectin peptides. GALNT12 has activity toward non-glycosylated peptides such as Muc5AC, Muc1a and EA2, and no detectable activity with non-glycosylated Muc2 and Muc7. It displays enzymatic activity toward the Gal-NAc-Muc5AC glycopeptide, but no detectable activity to mono-GalNAc-glycosylated Muc1a, Muc2, Muc7 and EA2. It may play an important role in the initial step of mucin-type oligosaccharide biosynthesis in digestive organs. Members of this family comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which are characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467313 [Multi-domain]  Cd Length: 128  Bit Score: 44.24  E-value: 2.47e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 447 SGVLQSISSpKLCLDRKDP---SHGQPKLAPCssdHVFPSpEQYWSLTNHRELR--SGF-YCLEVRNHGvNVHIYQCHGQ 520
Cdd:cd23435   4 YGALRNKGS-ELCLDVNNPngqGGKPVIMYGC---HGLGG-NQYFEYTSKGEIRhnIGKeLCLHASGSD-EVILQHCTSK 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21358257 521 S----GNQFWSFDskthqvisgQQQNFRH-----CLEAQPELnaVTSSVCDPKNHKQQWKFG 573
Cdd:cd23435  78 GkdvpPEQKWLFT---------QDGTIRNpasglCLHASGYK--VLLRTCNPSDDSQKWTFI 128
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
132-241 2.48e-05

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: 45.26  E-value: 2.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 132 VVITYHNEEASvLLRTLSSLRSRTPIQLLREVILVDDGST-----QADEKLNDFIKIKFLNMVQHRrittqvGLMHARVV 206
Cdd:cd04179   1 VVIPAYNEEEN-IPELVERLLAVLEEGYDYEIIVVDDGSTdgtaeIARELAARVPRVRVIRLSRNF------GKGAAVRA 73
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 21358257 207 GAELALADVLVFLDS----HVEVtkgwLEPLIAPILEDN 241
Cdd:cd04179  74 GFKAARGDIVVTMDAdlqhPPED----IPKLLEKLLEGG 108
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
299-352 2.80e-05

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: 460659 [Multi-domain]  Cd Length: 78  Bit Score: 42.60  E-value: 2.80e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 21358257   299 GGLFAIGREWFSELGGYDKGLKIWGAEQFELSLKLWLCGGQIlEVPCSRVGHLF 352
Cdd:pfam02709  21 GGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEI-ERPPGDIGRYY 73
beta-trefoil_Ricin_GALNT13 cd23467
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
486-570 6.74e-05

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 13 (GALNT13) and similar proteins; GALNT13 (EC 2.4.1.41), also called polypeptide GalNAc transferase 13, GalNAc-T13, pp-GaNTase 13, protein-UDP acetylgalactosaminyltransferase 13, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13, 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. It has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. It can glycosylate SDC3. It may be responsible for the synthesis of Tn antigen in neuronal cells. GALNT13 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). The model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467345  Cd Length: 127  Bit Score: 42.71  E-value: 6.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 486 QYWSLTNHRELRSGFYCLEVRNHGVNVHIYQCHGQSGNQFWSFDSKThqvISGQQQNFRHCLEAQPELNAVTSSVCDPKN 565
Cdd:cd23467  41 QVFSYTADKEIRTDDLCLDVSRLNGPVVMLKCHHMRGNQLWEYDAER---LTLRHVNSNQCLDEPSEEDKMVPTMKDCSG 117

                ....*.
gi 21358257 566 HK-QQW 570
Cdd:cd23467 118 SRsQQW 123
beta-trefoil_Ricin_SCDase cd23456
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ...
458-532 7.20e-05

ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide N-deacylase (SCDase) and similar proteins; SCDase (EC 3.5.1.69) is an enzyme which hydrolyzes the N-acyl linkage between fatty acid and sphingosine in ceramide of various glycosphingolipids and sphingomyelin. Shewanella algae SCDase contains two ricin B-type lectin domains at its C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.


Pssm-ID: 467334 [Multi-domain]  Cd Length: 122  Bit Score: 42.73  E-value: 7.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 458 LCLDRKDP-SHGQP-KLAPCSSDHvfpspEQYWSLTNHRELRS---GFYCLEV---RNHGVNVHIYQCHgQSGNQFWSFD 529
Cdd:cd23456  12 LCLDVSGGaTNGANvVVYDCNNSN-----SQKWYYDATGRLHSkanPGKCLDAggeNSNGANVVLWACN-DSANQRWDFD 85

                ...
gi 21358257 530 SKT 532
Cdd:cd23456  86 GNF 88
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
129-240 7.21e-05

Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 44.55  E-value: 7.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 129 SVSVVITYHNEEASVLLRTLSSLRSRTPIqllrEVILVDDGSTQAD----EKLNDFIKIkFLNMVQH---RRITTqVGLM 201
Cdd:cd06434   1 DVTVIIPVYDEDPDVFRECLRSILRQKPL----EIIVVTDGDDEPYlsilSQTVKYGGI-FVITVPHpgkRRALA-EGIR 74
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 21358257 202 HARVvgaelalaDVLVFLDSHVEVTKGWLEPLIAPiLED 240
Cdd:cd06434  75 HVTT--------DIVVLLDSDTVWPPNALPEMLKP-FED 104
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
453-528 9.05e-05

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 42.11  E-value: 9.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257    453 ISSPKLCLDRKDPSHGQPKLAPCSSDhvfpSPEQYWSLTNHRELRSGF--YCLEVR--NHGVNVHIYQCHGQSgNQFWSF 528
Cdd:smart00458  43 IKDTDLCLTANGNTGSTVTLYSCDGT----NDNQYWEVNKDGTIRNPDsgKCLDVKdgNTGTKVILWTCSGNP-NQKWIF 117
beta-trefoil_Ricin_GALNT5 cd23436
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
486-573 1.64e-04

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 5 (GALNT5) and similar proteins; GALNT5 (EC 2.4.1.41), also called polypeptide GalNAc transferase 5, GalNAc-T5, pp-GaNTase 5, protein-UDP acetylgalactosaminyltransferase 5, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5, 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. GALNT5 has activity toward EA2 peptide substrate but has a weak activity toward Muc2 or Muc1b substrates. GALNT5 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467314  Cd Length: 132  Bit Score: 41.70  E-value: 1.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 486 QYWSLTNHRELRSGFYCLEVRNHGVNVHIYQCHGQSGNQFWSFDSKT-------HQVISGQQQNFrhCLEAQPELNAVTS 558
Cdd:cd23436  37 QHFNYTWLRLIRQGELCLAPVEAEGALTLHPCDNTNNGLRWLHKSLIafpelmdHIMLEHQSQPT--CLEADPSQKILRL 114
                        90
                ....*....|....*
gi 21358257 559 SVCDPKNHKQQWKFG 573
Cdd:cd23436 115 NACDSFKRYQKWRFG 129
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
458-570 3.83e-04

ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a carbohydrate-binding domain formed from presumed gene triplication. It shows a beta-trefoil fold characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain was originally found in Ricin, which is a legume lectin from the seeds of the castor bean plant, Ricinus communis. It is also found in many carbohydrate-recognition proteins like plant and bacterial AB-toxins, glycosidases, or proteases, which serve diverse functions such as inhibitory toxicity, enzymatic activity, and signal transduction. The ricin B-type lectin domain can be present in one or more copies and has been shown in some instances to bind simple sugars, such as galactose or lactose. The most characteristic, though not completely conserved, sequence feature is the presence of a Q-W pattern. Consequently, the ricin B-type lectin domain has also been referred as the (QxW)3 domain and the three homologous regions as the QxW repeats. A disulfide bond is also conserved in some QxW repeats.


Pssm-ID: 467293 [Multi-domain]  Cd Length: 134  Bit Score: 40.82  E-value: 3.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 458 LCLDRKDPSH--GQP-KLAPCSSdhvfpSPEQYWSLTNhreLRSGFY---------CLEVRNH----GVNVHIYQCHGqS 521
Cdd:cd00161  12 KCLDVAGGSTanGAPvQQWTCNG-----GANQQWTLTP---VGDGYYtirnvasgkCLDVAGGstanGANVQQWTCNG-G 82
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21358257 522 GNQFWSFDSK---THQVISgqqQNFRHCLEAQPELNAVTSSV----CDPKNHkQQW 570
Cdd:cd00161  83 DNQQWRLEPVgdgYYRIVN---KHSGKCLDVSGGSTANGANVqqwtCNGGAN-QQW 134
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
502-571 8.10e-04

ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) family; The MRC family includes MRC1-2, receptor-type tyrosine-protein phosphatase beta (PTPRB) isoform e, secretory phospholipase A2 receptor (PLA2R1), and lymphocyte antigen 75 (Ly-75). MRC1 mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains, and acts as a phagocytic receptor for bacteria, fungi, and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC2 may play a role as an endocytotic lectin receptor displaying calcium-dependent lectin activity. It internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. It may be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. It may contribute to cellular uptake, remodeling, and degradation of extracellular collagen matrices. It may play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. It may participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). PTPRB (EC 3.1.3.48), also called protein-tyrosine phosphatase beta, plays an important role in blood vessel remodeling and angiogenesis. It is not necessary for the initial formation of the blood vessels but is essential for their maintenance and remodeling. It is also essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells that requires the presence of plakoglobin. PLA2R1 is a receptor for secretory phospholipase A2 (sPLA2). It acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. It can also bind to snake PA2-like toxins. It may be involved in responses in proinflammatory cytokine productions during endotoxic shock. It also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. Ly-75 acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. It causes reduced proliferation of B-lymphocytes. All family members contain a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. One member of this family, MRC1, is missing the gamma subdomain.


Pssm-ID: 467784 [Multi-domain]  Cd Length: 119  Bit Score: 39.50  E-value: 8.10e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21358257 502 CLEVRNHGVNVHIYQCHGQSGNQFWSFDSkTHQVISgqqQNFRHCLEAQ--PELNAVTSSVCDPKNHKQQWK 571
Cdd:cd23385  13 CLAARSSSSKVSLSTCNPNSPNQQWKWTS-GHRLFN---VGTGKCLGVSssSPSSPLRLFECDSEDELQKWK 80
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
132-221 9.32e-04

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: 40.54  E-value: 9.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 132 VVITYHNEEASV--LLRTLSSLRSRTPIQLlrEVILVDDGST-QADEKLNDFIK----IKFL----NMVQHRRITTqvGL 200
Cdd:cd04187   1 IVVPVYNEEENLpeLYERLKAVLESLGYDY--EIIFVDDGSTdRTLEILRELAArdprVKVIrlsrNFGQQAALLA--GL 76
                        90       100
                ....*....|....*....|.
gi 21358257 201 MHARvvgaelalADVLVFLDS 221
Cdd:cd04187  77 DHAR--------GDAVITMDA 89
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
447-530 1.14e-03

ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1,4-beta-xylanase and similar proteins; The family includes Streptomyces olivaceoviridis endo-1,4-beta-xylanase (XLN, EC 3.2.1.8), Streptomyces avermitilis beta-L-arabinopyranosidase (EC 3.2.1.185), and Streptomyces coelicolor extracellular exo-alpha-L-arabinofuranosidase (ABF, EC 3.2.1.55). XLN, also called xylanase, or 1,4-beta-D-xylan xylanohydrolase, belongs to the glycosyl hydrolase 10 (cellulase F) family. It contributes to hydrolyze hemicellulose, the major component of plant cell walls. XLN contains a (beta/alpha)8-barrel as a catalytic domain, a family 13 carbohydrate binding module (CBM13) as a xylan binding domain (XBD) and a Gly/Pro-rich linker between them. Beta-L-arabinopyranosidase belongs to the glycosyl hydrolase 27 (GH27) family. It has a GH27 catalytic domain, an antiparallel beta-domain containing Greek key motifs, another antiparallel beta-domain forming a jellyroll structure, and a CBM13 module. ScAraf62A, also called ABF, or arabinosidase, or arabinoxylan arabinofuranohydrolase, belongs to the glycosyl hydrolase 62 (GH62) family. It is involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. It acts synergistically with xylanases and binds specifically to xylan. ScAraf62A comprises a CBM13 module at its N-terminus and a catalytic domain at its C-terminus. This model corresponds to the CBM13 module, which is a ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding pocket.


Pssm-ID: 467297 [Multi-domain]  Cd Length: 130  Bit Score: 39.26  E-value: 1.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 447 SGVLQSISSPKlCLD-----RKDPSHGQpkLAPCSSdhvfpSPEQYWSLTNHRELRSGF-YCLEV----RNHGVNVHIYQ 516
Cdd:cd23418   5 GGQIRGYGSGR-CLDvpggsTTNGTRLI--LWDCHG-----GANQQFTFTSAGELRVGGdKCLDAagggTTNGTPVVIWP 76
                        90
                ....*....|....
gi 21358257 517 CHGQSgNQFWSFDS 530
Cdd:cd23418  77 CNGGA-NQKWRFNS 89
PRK10073 PRK10073
putative glycosyl transferase; Provisional
124-269 1.31e-03

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 41.18  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257  124 MEKLPSVSVVITYHNEE-------ASVLLRTLSSLrsrtpiqllrEVILVDDGSTqaDEKLNdfIKIKFLNMVQHRRITT 196
Cdd:PRK10073   2 MNSTPKLSIIIPLYNAGkdfrafmESLIAQTWTAL----------EIIIVNDGST--DNSVE--IAKHYAENYPHVRLLH 67
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21358257  197 QV--GLMHARVVGAELALADVLVFLDSHVEVTKGWLEPLIAPILEDN---RTCTTpiidtidfdNFAYRRGKPSRGFF 269
Cdd:PRK10073  68 QAnaGVSVARNTGLAVATGKYVAFPDADDVVYPTMYETLMTMALEDDldvAQCNA---------DWCFRDTGETWQSI 136
beta-trefoil_Ricin_SCDase_rpt1 cd23499
first ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ...
507-572 2.21e-03

first ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide N-deacylase (SCDase) and similar proteins; SCDase (EC 3.5.1.69) is an enzyme which hydrolyzes the N-acyl linkage between fatty acid and sphingosine in ceramide of various glycosphingolipids and sphingomyelin. Shewanella algae SCDase contains two ricin B-type lectin domains at its C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. The model corresponds to the first lectin domain.


Pssm-ID: 467377 [Multi-domain]  Cd Length: 131  Bit Score: 38.58  E-value: 2.21e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21358257 507 NHGVNVHIYQCHGQSGNQFWSFDSKTHQVISgqQQNFRHCLEAQ-PELN--AVTSSVCDPKNHkQQWKF 572
Cdd:cd23499  24 VNGANVILWDCADKSADQRWIYDAASGMLRN--KANPSYCLDNRgQAYNggEVVLWQCEDSDN-LRWTY 89
beta-trefoil_Ricin_SCDase_rpt1 cd23499
first ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ...
446-528 3.85e-03

first ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide N-deacylase (SCDase) and similar proteins; SCDase (EC 3.5.1.69) is an enzyme which hydrolyzes the N-acyl linkage between fatty acid and sphingosine in ceramide of various glycosphingolipids and sphingomyelin. Shewanella algae SCDase contains two ricin B-type lectin domains at its C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. The model corresponds to the first lectin domain.


Pssm-ID: 467377 [Multi-domain]  Cd Length: 131  Bit Score: 37.81  E-value: 3.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358257 446 ASGVLQSISSPKLCLDRKDPSH--GQPKLAPCSsdhvfPSPEQYWSLTNHReLRSGF---YCLEV--RNHGVNVHIYQCH 518
Cdd:cd23499  48 ASGMLRNKANPSYCLDNRGQAYngGEVVLWQCE-----DSDNLRWTYDNGV-LRSKHnpnIVLDAygRDNNSQVGQWEYH 121
                        90
                ....*....|
gi 21358257 519 GqSGNQFWSF 528
Cdd:cd23499 122 G-GANQQWEL 130
 
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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