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Conserved domains on  [gi|701367534|ref|XP_009986101|]
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PREDICTED: LOW QUALITY PROTEIN: polypeptide N-acetylgalactosaminyltransferase 16 [Tauraco erythrolophus]

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
PubMed:  12634319|12691742|9445404|8844840
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 ...
 73-361 6.52e-172

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: 485.56  E-value: 6.52e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534  73 SLIITFHNEARSTLLRTVKSVLNRTPPSLIQEIILVDDFSSDPEDCQLL-----TKIPKVKCLRNTRREGLIRSRVRGAE 147
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLeeyykKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534 148 VATADILT------*VTGGGLQPMLQRVKEDYTRVVSPIIDVISLDNFAYLAASADLRGGFDWSLHFKWEQIPIEQKmSR 221
Cdd:cd02510   81 AATGDVLVfldshcEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEER-RR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534 222 TDPTQSIRTPVIAGGIFVIDKSWFNHLGKYDTQMDIWGGENFELSFRVWMCGGSLEIVPCSRVGHVFR-KRHPYDFPEGN 300
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701367534 301 AlTYIKNTKRTAEVWMDEYKQYYYEARPSAIGKSFGSVADRVEQRRKLNCKSFQWYLENVY 361
Cdd:cd02510  240 G-TVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT16 cd23479
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 367-495 4.93e-82

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 16 (GALNT16) and similar proteins; GALNT16 (EC 2.4.1.41), also called polypeptide GalNAc transferase 16, GalNAc-T16, polypeptide GalNAc transferase-like protein 1, GalNAc-T-like protein 1, pp-GaNTase-like protein 1, polypeptide N-acetylgalactosaminyltransferase-like protein 1, protein-UDP acetylgalactosaminyltransferase-like protein 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 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. GALNT16 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: 467357  Cd Length: 129  Bit Score: 250.11  E-value: 4.93e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534 367 PEKELIPGIIKQGGNCLESRAQDTTGNTLAGMGICKGTVNNPPVTQEWVFSDPLIRQQDKCLSIASFSTGSQITLEACNQ 446
Cdd:cd23479    1 PEKEAIPGLIRQGGNCLESQGQDTTGDTLLGLGECRGTASNLPASQEWVLSDPLIRQQDKCLAITSFSPGSKVILELCNQ 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 701367534 447 KDGRQKWKMKGSFIQHFVSGLCLENQTGRVVTNPCQADVPGQQWELLQA 495
Cdd:cd23479   81 KDGRQKWKLKGSFIQHQVSGLCLDSQSGRVVINQCQADLASQQWELLQV 129
 
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 ...
 73-361 6.52e-172

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: 485.56  E-value: 6.52e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534  73 SLIITFHNEARSTLLRTVKSVLNRTPPSLIQEIILVDDFSSDPEDCQLL-----TKIPKVKCLRNTRREGLIRSRVRGAE 147
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLeeyykKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534 148 VATADILT------*VTGGGLQPMLQRVKEDYTRVVSPIIDVISLDNFAYLAASADLRGGFDWSLHFKWEQIPIEQKmSR 221
Cdd:cd02510   81 AATGDVLVfldshcEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEER-RR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534 222 TDPTQSIRTPVIAGGIFVIDKSWFNHLGKYDTQMDIWGGENFELSFRVWMCGGSLEIVPCSRVGHVFR-KRHPYDFPEGN 300
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701367534 301 AlTYIKNTKRTAEVWMDEYKQYYYEARPSAIGKSFGSVADRVEQRRKLNCKSFQWYLENVY 361
Cdd:cd02510  240 G-TVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT16 cd23479
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 367-495 4.93e-82

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 16 (GALNT16) and similar proteins; GALNT16 (EC 2.4.1.41), also called polypeptide GalNAc transferase 16, GalNAc-T16, polypeptide GalNAc transferase-like protein 1, GalNAc-T-like protein 1, pp-GaNTase-like protein 1, polypeptide N-acetylgalactosaminyltransferase-like protein 1, protein-UDP acetylgalactosaminyltransferase-like protein 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 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. GALNT16 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: 467357  Cd Length: 129  Bit Score: 250.11  E-value: 4.93e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534 367 PEKELIPGIIKQGGNCLESRAQDTTGNTLAGMGICKGTVNNPPVTQEWVFSDPLIRQQDKCLSIASFSTGSQITLEACNQ 446
Cdd:cd23479    1 PEKEAIPGLIRQGGNCLESQGQDTTGDTLLGLGECRGTASNLPASQEWVLSDPLIRQQDKCLAITSFSPGSKVILELCNQ 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 701367534 447 KDGRQKWKMKGSFIQHFVSGLCLENQTGRVVTNPCQADVPGQQWELLQA 495
Cdd:cd23479   81 KDGRQKWKLKGSFIQHQVSGLCLDSQSGRVVINQCQADLASQQWELLQV 129
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 73-247 6.82e-21

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: 89.38  E-value: 6.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534   73 SLIITFHNEArSTLLRTVKSVLNRTPPSLiqEIILVDDFSSD--PEDCQ-LLTKIPKVKCLRNTRREGLIRSRVRGAEVA 149
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQTYPNF--EIIVVDDGSTDgtVEIAEeYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534  150 TADILT------*VTGGGLQPMLQRVKEDYTRVVSPIIDVISLDNFAYlaasadlrggfdWSLHFKWEQIPIEQKMSRTD 223
Cdd:pfam00535  78 TGDYIAfldaddEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEY------------RRASRITLSRLPFFLGLRLL 145

                         170       180
                  ....*....|....*....|....
gi 701367534  224 PTQsirTPVIAGGIFVIDKSWFNH 247
Cdd:pfam00535 146 GLN---LPFLIGGFALYRREALEE 166
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
377-490 1.85e-20

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 86.82  E-value: 1.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534  377 KQGGNCLESRAQDTTGNTLaGMGICKGTVNNppvtQEWVFS-DPLIRQ--QDKCLSIASFSTGSQITLEACNQKDGRQKW 453
Cdd:pfam00652   8 RASGKCLDVPGGSSAGGPV-GLYPCHGSNGN----QLWTLTgDGTIRSvaSDLCLDVGSTADGAKVVLWPCHPGNGNQRW 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 701367534  454 --KMKGSFIQHFVSGLCLE-----NQTGRVVTNPCQADVPGQQW 490
Cdd:pfam00652  83 ryDEDGTQIRNPQSGKCLDvsgagTSNGKVILWTCDSGNPNQQW 126
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 73-154 1.05e-10

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 61.26  E-value: 1.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534  73 SLIITFHNEARsTLLRTVKSVLNRTPPSLiqEIILVDDFSSD--PEDCQ-LLTKIPKVKCLRNTRREGLIRSRVRGAEVA 149
Cdd:COG0463    5 SVVIPTYNEEE-YLEEALESLLAQTYPDF--EIIVVDDGSTDgtAEILReLAAKDPRIRVIRLERNRGKGAARNAGLAAA 81


                 ....*
gi 701367534 150 TADIL 154
Cdd:COG0463   82 RGDYI 86
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 375-492 3.05e-10

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 57.52  E-value: 3.05e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534   375 IIKQGGNCLesraQDTTGNTLAGMGICKGTVNNppvtQEWVF-SDPLIRQQ--DKCLSiASFSTGSQITLEACNQKDGRQ 451
Cdd:smart00458   2 ISGNTGKCL----DVNGNKNPVGLFDCHGTGGN----QLWKLtSDGAIRIKdtDLCLT-ANGNTGSTVTLYSCDGTNDNQ 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 701367534   452 KWKMKGSF-IQHFVSGLCLE----NQTGRVVTNPCQADvPGQQWEL 492
Cdd:smart00458  73 YWEVNKDGtIRNPDSGKCLDvkdgNTGTKVILWTCSGN-PNQKWIF 117
 
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 ...
 73-361 6.52e-172

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: 485.56  E-value: 6.52e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534  73 SLIITFHNEARSTLLRTVKSVLNRTPPSLIQEIILVDDFSSDPEDCQLL-----TKIPKVKCLRNTRREGLIRSRVRGAE 147
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLeeyykKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534 148 VATADILT------*VTGGGLQPMLQRVKEDYTRVVSPIIDVISLDNFAYLAASADLRGGFDWSLHFKWEQIPIEQKmSR 221
Cdd:cd02510   81 AATGDVLVfldshcEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEER-RR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534 222 TDPTQSIRTPVIAGGIFVIDKSWFNHLGKYDTQMDIWGGENFELSFRVWMCGGSLEIVPCSRVGHVFR-KRHPYDFPEGN 300
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701367534 301 AlTYIKNTKRTAEVWMDEYKQYYYEARPSAIGKSFGSVADRVEQRRKLNCKSFQWYLENVY 361
Cdd:cd02510  240 G-TVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT16 cd23479
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 367-495 4.93e-82

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 16 (GALNT16) and similar proteins; GALNT16 (EC 2.4.1.41), also called polypeptide GalNAc transferase 16, GalNAc-T16, polypeptide GalNAc transferase-like protein 1, GalNAc-T-like protein 1, pp-GaNTase-like protein 1, polypeptide N-acetylgalactosaminyltransferase-like protein 1, protein-UDP acetylgalactosaminyltransferase-like protein 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 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. GALNT16 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: 467357  Cd Length: 129  Bit Score: 250.11  E-value: 4.93e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534 367 PEKELIPGIIKQGGNCLESRAQDTTGNTLAGMGICKGTVNNPPVTQEWVFSDPLIRQQDKCLSIASFSTGSQITLEACNQ 446
Cdd:cd23479    1 PEKEAIPGLIRQGGNCLESQGQDTTGDTLLGLGECRGTASNLPASQEWVLSDPLIRQQDKCLAITSFSPGSKVILELCNQ 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 701367534 447 KDGRQKWKMKGSFIQHFVSGLCLENQTGRVVTNPCQADVPGQQWELLQA 495
Cdd:cd23479   81 KDGRQKWKLKGSFIQHQVSGLCLDSQSGRVVINQCQADLASQQWELLQV 129
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 370-491 6.54e-29

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: 110.57  E-value: 6.54e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534 370 ELIPGIIKQGGNCLESRAQDTTGNTLAGMGICkgtvNNPPVTQEWVFS-DPLIRQQDKCLSIASFSTGSQITLEACNQkD 448
Cdd:cd23441    2 ELAYGQIKQGNLCLDSDEQLFQGPALLILAPC----SNSSDSQEWSFTkDGQLQTQGLCLTVDSSSKDLPVVLETCSD-D 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 701367534 449 GRQKWKMKGSFIQHFVSGLCLENQTG-RVVTNPCQADVPGQQWE 491
Cdd:cd23441   77 PKQKWTRTGRQLVHSESGLCLDSRKKkGLVVSPCRSGAPSQKWD 120
beta-trefoil_Ricin_GALNT14 cd23478
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 366-492 7.29e-25

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14) and similar proteins; GALNT14 (EC 2.4.1.41), also called polypeptide GalNAc transferase 14, GalNAc-T14, pp-GaNTase 14, protein-UDP acetylgalactosaminyltransferase 14, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14, 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. 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. GALNT14 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: 467356  Cd Length: 140  Bit Score: 99.94  E-value: 7.29e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534 366 VPEKELI-PGIIKQGGNCLESRAQDTTGNTLAGMGICKGTVNNPPVTQEWVF-SDPLIRQQDKCLSIASFSTGSQITLEA 443
Cdd:cd23478    1 IPDESDIqSGVIRQRQNCLESRRVEGQELPNLSLSPCIKSKGVPAKSQEWAYtYNQQIRQQQLCLSVHTLFPGSPVVLVP 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 701367534 444 CNQKDGRQKWKMKGSFIQHFVSGLCLENQT--------GRVVTNPCQADVPGQQWEL 492
Cdd:cd23478   81 CKEGDGKQRWTKVGSHIEHMASRFCLDTEMfgdgtessKEIVINPCESSAMSQRWDM 137
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 73-247 6.82e-21

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: 89.38  E-value: 6.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534   73 SLIITFHNEArSTLLRTVKSVLNRTPPSLiqEIILVDDFSSD--PEDCQ-LLTKIPKVKCLRNTRREGLIRSRVRGAEVA 149
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQTYPNF--EIIVVDDGSTDgtVEIAEeYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534  150 TADILT------*VTGGGLQPMLQRVKEDYTRVVSPIIDVISLDNFAYlaasadlrggfdWSLHFKWEQIPIEQKMSRTD 223
Cdd:pfam00535  78 TGDYIAfldaddEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEY------------RRASRITLSRLPFFLGLRLL 145

                         170       180
                  ....*....|....*....|....
gi 701367534  224 PTQsirTPVIAGGIFVIDKSWFNH 247
Cdd:pfam00535 146 GLN---LPFLIGGFALYRREALEE 166
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 374-492 1.08e-20

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: 87.38  E-value: 1.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534 374 GIIKQGGNCLesraqDTTGNTL---AGMGICKGTVNNppvtQEWVFS-DPLIRQQDKCLSIASFSTGSQITLEACNQKDG 449
Cdd:cd23434    3 GSLKQGNLCL-----DTLGHKAggtVGLYPCHGTGGN----QEWSFTkDGQIKHDDLCLTVVDRAPGSLVTLQPCREDDS 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 701367534 450 RQKWKM--KGSFIQHFVSGLCLEN---QTGRVVTNPCQADVPGQQWEL 492
Cdd:cd23434   74 NQKWEQieNNSKLRHVGSNLCLDSrnaKSGGLTVETCDPSSGSQQWKF 121
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
377-490 1.85e-20

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 86.82  E-value: 1.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534  377 KQGGNCLESRAQDTTGNTLaGMGICKGTVNNppvtQEWVFS-DPLIRQ--QDKCLSIASFSTGSQITLEACNQKDGRQKW 453
Cdd:pfam00652   8 RASGKCLDVPGGSSAGGPV-GLYPCHGSNGN----QLWTLTgDGTIRSvaSDLCLDVGSTADGAKVVLWPCHPGNGNQRW 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 701367534  454 --KMKGSFIQHFVSGLCLE-----NQTGRVVTNPCQADVPGQQW 490
Cdd:pfam00652  83 ryDEDGTQIRNPQSGKCLDvsgagTSNGKVILWTCDSGNPNQQW 126
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 374-492 2.77e-12

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: 63.54  E-value: 2.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534 374 GIIK-QGGN-CLESRAQDTTGNTLAGMGICKGTVNNppvtQEWVFS-DPLIRQQDKCLSIASfsTGSQITLEACNQKDGR 450
Cdd:cd23462    6 GEIRnLAGKlCLDAPGRKKELNKPVGLYPCHGQGGN----QYWMLTkDGEIRRDDLCLDYAG--GSGDVTLYPCHGMKGN 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 701367534 451 QKWK--MKGSFIQHFVSGLCLE--NQTGRVVTNPCQADVPGQQWEL 492
Cdd:cd23462   80 QFWIydEETKQIVHGTSKKCLElsDDSSKLVMEPCNGSSPRQQWEF 125
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 73-154 1.05e-10

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 61.26  E-value: 1.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534  73 SLIITFHNEARsTLLRTVKSVLNRTPPSLiqEIILVDDFSSD--PEDCQ-LLTKIPKVKCLRNTRREGLIRSRVRGAEVA 149
Cdd:COG0463    5 SVVIPTYNEEE-YLEEALESLLAQTYPDF--EIIVVDDGSTDgtAEILReLAAKDPRIRVIRLERNRGKGAARNAGLAAA 81


                 ....*
gi 701367534 150 TADIL 154
Cdd:COG0463   82 RGDYI 86
beta-trefoil_Ricin_GALNT1-like cd23433
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 382-492 1.76e-10

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: 58.48  E-value: 1.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534 382 CLesraqDTTG---NTLAGMGICKGTVNNppvtQEWVFSDPL-IRQQDKCLSIASfsTGSQITLEACNQKDGRQKWKM-K 456
Cdd:cd23433   17 CL-----DTMGrkaGEKVGLSSCHGQGGN----QVFSYTAKGeIRSDDLCLDASR--KGGPVKLEKCHGMGGNQEWEYdK 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 701367534 457 GSF-IQHFVSGLCL----ENQTGRVVTNPCQADvPGQQWEL 492
Cdd:cd23433   86 ETKqIRHVNSGLCLtapnEDDPNEPVLRPCDGG-PSQKWEL 125
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 375-492 3.05e-10

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 57.52  E-value: 3.05e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534   375 IIKQGGNCLesraQDTTGNTLAGMGICKGTVNNppvtQEWVF-SDPLIRQQ--DKCLSiASFSTGSQITLEACNQKDGRQ 451
Cdd:smart00458   2 ISGNTGKCL----DVNGNKNPVGLFDCHGTGGN----QLWKLtSDGAIRIKdtDLCLT-ANGNTGSTVTLYSCDGTNDNQ 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 701367534   452 KWKMKGSF-IQHFVSGLCLE----NQTGRVVTNPCQADvPGQQWEL 492
Cdd:smart00458  73 YWEVNKDGtIRNPDSGKCLDvkdgNTGTKVILWTCSGN-PNQKWIF 117
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 64-154 3.07e-09

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: 58.21  E-value: 3.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534  64 RYDTDLPATSLIITFHNEARsTLLRTVKSVLNRTPPSLIQEIILVDDFSSDP--EDC-QLLTKIPKVKCLRNTRREGLIR 140
Cdd:COG1215   23 RAPADLPRVSVIIPAYNEEA-VIEETLRSLLAQDYPKEKLEVIVVDDGSTDEtaEIArELAAEYPRVRVIERPENGGKAA 101

                         90
                 ....*....|....
gi 701367534 141 SRVRGAEVATADIL 154
Cdd:COG1215  102 ALNAGLKAARGDIV 115
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
70-292 3.41e-09

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 56.54  E-value: 3.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534  70 PATSLIITFHNEArSTLLRTVKSVLNRTPPSLiqEIILVDDFSSDPEDCQLLT-KIPKVKCLRNTRREGLIRSRVRGAEV 148
Cdd:COG1216    3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPPF--EVIVVDNGSTDGTAELLAAlAFPRVRVIRNPENLGFAAARNLGLRA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534 149 ATADIlt*vtggglqpmlqrvkedytrvvspiidVISLDNfaylaasaDLRGGFDWslhfkweqipIEQkmsrtdptqsi 228
Cdd:COG1216   80 AGGDY-----------------------------LLFLDD--------DTVVEPDW----------LER----------- 101

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 701367534 229 rtpVIAGGIFVIDKSWFNHLGKYDTQMDIWGGEnFELSFRVWMCGGSLEIVPCSRVGHVFRKRH 292
Cdd:COG1216  102 ---LLAAACLLIRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGASS 161
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 377-491 5.63e-09

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: 54.22  E-value: 5.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534 377 KQGGNCLesraqDTTGNT---LAGMGICKGTVNNppvtQEWVFSDP-LIRQQDKCLSIASfsTGSQITLEACNqKDGRQK 452
Cdd:cd23437   11 LGTGLCL-----DTMGHQnggPVGLYPCHGMGGN----QLFRLNEAgQLAVGEQCLTASG--SGGKVKLRKCN-LGETGK 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 701367534 453 WK--MKGSFIQHFVSGLCLE--NQTGRVVTNPCQADVPGQQWE 491
Cdd:cd23437   79 WEydEATGQIRHKGTGKCLDlnEGTNKLILQPCDSSSPSQKWE 121
beta-trefoil_Ricin_GALNT10-like cd23439
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 374-490 8.09e-09

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: 53.88  E-value: 8.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534 374 GIIKQGGN--CLESraQDTTGNTLAGMGICKGTVNNppVTQEWVFS---DplIRQQDK--CLSIASFSTGSQITLEACNQ 446
Cdd:cd23439    3 GEIRNVGSglCIDT--KHGGENDEVRLSKCVKDGGG--GEQQFELTwheD--IRPKKRkvCFDVSSHTPGAPVILYACHG 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 701367534 447 KDGRQKWKM--KGSFIQHFVSGLCLE--NQTGRVVTNPCQADVPGQQW 490
Cdd:cd23439   77 MKGNQLWKYrpNTKQLYHPVSGLCLDadPGSGKVFMNHCDESSDTQKW 124
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
422-492 1.76e-08

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 52.92  E-value: 1.76e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701367534  422 RQQDKCLSI-ASFSTGSQITLEACNQKDGRQKWKMKGS-FIQHFVSGLCLENQT----GRVVTNPCQADVPGQQWEL 492
Cdd:pfam00652   8 RASGKCLDVpGGSSAGGPVGLYPCHGSNGNQLWTLTGDgTIRSVASDLCLDVGStadgAKVVLWPCHPGNGNQRWRY 84
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 375-493 3.85e-08

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: 51.67  E-value: 3.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534 375 IIKQGGN-CLESRAQDTTGNTLAgMGICKGTVNNppvtQEWVFS-DPLIRQQDKCLSIASfstGSQITLEACNQKDGRQK 452
Cdd:cd23460    5 IKHTESGlCLDWAGESNGDKTVA-LKPCHGGGGN----QFWMYTgDGQIRQDHLCLTADE---GNKVTLRECADQLPSQE 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 701367534 453 W--KMKGSFIQHFVSGLCLE--NQTGRVVTNPCQADVPGQQWELL 493
Cdd:cd23460   77 WsyDEKTGTIRHRSTGLCLTldANNDVVILKECDSNSLWQKWIFQ 121
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 75-155 6.60e-08

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: 52.12  E-value: 6.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534  75 IITFHNEARsTLLRTVKSVLNRTPPSLiqEIILVDDFSSD--PEDCQ-LLTKIPKVKCLRNTRREGLIRSRVRGAEVATA 151
Cdd:cd00761    2 IIPAYNEEP-YLERCLESLLAQTYPNF--EVIVVDDGSTDgtLEILEeYAKKDPRVIRVINEENQGLAAARNAGLKAARG 78


                 ....
gi 701367534 152 DILT 155
Cdd:cd00761   79 EYIL 82
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
 380-490 5.90e-07

ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and similar proteins; Glucan endo-1,3-beta-glucosidase (EC 3.2.1.39), also called (1->3)-beta-glucan endohydrolase, or (1->3)-beta-glucanase, or laminarinase, belongs to the glycosyl hydrolase 64 (GH64) family. It catalyzes hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans. It has been implicated in the defense against fungal pathogens. Glucan endo-1,3-beta-glucosidase contains a C-terminal 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 bears a potential sugar binding site.


Pssm-ID: 467329 [Multi-domain]  Cd Length: 125  Bit Score: 48.48  E-value: 5.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534 380 GNCLESRAQDTTGNTLAGMGICKGTVNnppvtQEWVF-SDPLIRQQDKCLSIASFST--GSQITLEACNQKdGRQKWKMK 456
Cdd:cd23451   11 GKCLDVPGSSTADGNPVQIYTCNGTAA-----QKWTLgTDGTLRVLGKCLDVSGGGTanGTLVQLWDCNGT-GAQKWVPR 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 701367534 457 -GSFIQHFVSGLCLENQTG------RVVTNPCQAdVPGQQW 490
Cdd:cd23451   85 aDGTLYNPQSGKCLDAPGGsttdgtQLQLYTCNG-TAAQQW 124
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
 420-491 8.58e-07

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: 47.98  E-value: 8.58e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 701367534 420 LIR--QQDKCLSIASfsTGSQITLEACNQKDGRQKWK-MKGSFIQHFVSGLCL----ENQTGRVVTNPCQADVPGQQWE 491
Cdd:cd23385    4 LIYneDLGKCLAARS--SSSKVSLSTCNPNSPNQQWKwTSGHRLFNVGTGKCLgvssSSPSSPLRLFECDSEDELQKWK 80
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 233-293 3.23e-06

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: 44.91  E-value: 3.23e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701367534  233 IAGGIFVIDKSWFNHLGKYDTQMDIWGGENFELSFRVWMCGGSLEIVPCsRVGHVFRKRHP 293
Cdd:pfam02709  19 YFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPG-DIGRYYMLYHK 78
beta-trefoil_Ricin_SCDase_rpt2 cd23500
second ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ...
 426-491 3.39e-06

second 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 second lectin domain.


Pssm-ID: 467378 [Multi-domain]  Cd Length: 128  Bit Score: 46.30  E-value: 3.39e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 701367534 426 KCLSIA--SFSTGSQITLEACNQKDGrQKWK---MKGSFIQHFVSGLCLE-------NQTgRVVTNPCQADVPGQQWE 491
Cdd:cd23500   12 KCLSAAngSQLNGSLVQLDACHASAG-QLWYfdpKKGTIRSALDGNKCLAipggntgNHT-QLQLADCDASNPAQQFN 87
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 377-490 4.54e-06

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: 46.19  E-value: 4.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534 377 KQGGNCLESRAQDTTGNTLAGMGICKGTVNnppvtQEWVFSD--PLIRQQDKCLSIA--SFSTGSQITLEACNQkDGRQK 452
Cdd:cd23418   11 YGSGRCLDVPGGSTTNGTRLILWDCHGGAN-----QQFTFTSagELRVGGDKCLDAAggGTTNGTPVVIWPCNG-GANQK 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 701367534 453 WK--MKGSFIQHfVSGLCL-----ENQTG-RVVTNPCQADvPGQQW 490
Cdd:cd23418   85 WRfnSDGTIRNV-NSGLCLdvaggGTANGtRLILWSCNGG-SNQRW 128
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 75-286 1.61e-05

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: 45.24  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534  75 IITFHNEARsTLLRTVKSVLNRTPPSLiqEIILVDDFSSDPEDCQLLTKIPKVKCLRNTRREGLIRSRVRGAEVATADIL 154
Cdd:cd04186    2 IIVNYNSLE-YLKACLDSLLAQTYPDF--EVIVVDNASTDGSVELLRELFPEVRLIRNGENLGFGAGNNQGIREAKGDYV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534 155 ------T*VTGGGLQPMLQRVkedytrvvspiidvisldnfaylaasadlrggfdwslhfkweqipieqkmsRTDPTQSI 228
Cdd:cd04186   79 lllnpdTVVEPGALLELLDAA---------------------------------------------------EQDPDVGI 107

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 701367534 229 RTPVIAGGIFVIDKSWFNHLGKYDTQMDIWgGENFELSFRVWMCGGSLEIVPCSRVGH 286
Cdd:cd04186  108 VGPKVSGAFLLVRREVFEEVGGFDEDFFLY-YEDVDLCLRARLAGYRVLYVPQAVIYH 164
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 74-154 2.39e-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: 44.87  E-value: 2.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534  74 LIITFHNEARsTLLRTVKSVLNRTPPSLIQEIILVDDFSSD--PEDCQLLTKI-PKVKCLRNTRREGLIRSRVRGAEVAT 150
Cdd:cd04179    1 VVIPAYNEEE-NIPELVERLLAVLEEGYDYEIIVVDDGSTDgtAEIARELAARvPRVRVIRLSRNFGKGAAVRAGFKAAR 79


                 ....
gi 701367534 151 ADIL 154
Cdd:cd04179   80 GDIV 83
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 74-134 3.24e-05

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: 44.39  E-value: 3.24e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701367534  74 LIITFHNEARS--TLLRTVKSVLNRTPPSLiqEIILVDDFSSDPED---CQLLTKIPKVKCLRNTR 134
Cdd:cd04187    1 IVVPVYNEEENlpELYERLKAVLESLGYDY--EIIFVDDGSTDRTLeilRELAARDPRVKVIRLSR 64
beta-trefoil_Ricin_hemolysin cd23423
ricin B-type lectin domain, beta-trefoil fold, found in bacterial hemolysin and similar ...
 420-491 1.04e-04

ricin B-type lectin domain, beta-trefoil fold, found in bacterial hemolysin and similar proteins; Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cytolysis by forming heptameric pores in target host membranes. After binding to target membranes, the protein assembles into a heptameric pre-pore complex. Proteolytic cleavage triggers a conformation change that is required for membrane insertion and pore formation. Hemolysin may be called "cytolysin" or "cytolytic toxin", according to a specific action for certain cells. For example, this subfamily includes Vibrio vulnificus cytolysin that attack blood cell membranes and cause cell rupture, thereby liberating hemoglobins. Members of this subfamily contain a 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. Each subdomain may harbor a putative sugar-binding pocket.


Pssm-ID: 467301 [Multi-domain]  Cd Length: 119  Bit Score: 41.98  E-value: 1.04e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701367534 420 LIRQQDKCLSIASFStgsQITLEACNQKDGRQKWKMKGsfIQHFVS----GLCLE-NQTGRVVTNPCQADVpGQQWE 491
Cdd:cd23423    9 SLSFNNRCLTVDNNG---RVTLESCDSGDRNQSWILDS--EGRYRSrvapDLCLDaDDDGLLTLEQCSLSL-TQKWE 79
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 382-454 1.56e-04

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: 41.55  E-value: 1.56e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701367534 382 CLEsraqdTTGNTLAGMGICKGTVNNPPVTQEWVFS-DPLIRQ--QDKCLSiasfSTGSQITLEACNQKDGRQKWK 454
Cdd:cd23435   60 CLH-----ASGSDEVILQHCTSKGKDVPPEQKWLFTqDGTIRNpaSGLCLH----ASGYKVLLRTCNPSDDSQKWT 126
beta-trefoil_Ricin_SCDase_rpt2 cd23500
second ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ...
 377-458 1.83e-04

second 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 second lectin domain.


Pssm-ID: 467378 [Multi-domain]  Cd Length: 128  Bit Score: 41.30  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534 377 KQGGNCLESRAQDTTGNTLAGMGICKGTVNnppvtQEWVFsDP---LIRQQ---DKCLSIASFSTG--SQITLEACNQKD 448
Cdd:cd23500    8 KRSGKCLSAANGSQLNGSLVQLDACHASAG-----QLWYF-DPkkgTIRSAldgNKCLAIPGGNTGnhTQLQLADCDASN 81

                         90
                 ....*....|
gi 701367534 449 GRQKWKMKGS 458
Cdd:cd23500   82 PAQQFNYDGG 91
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 70-290 2.43e-04

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


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 42.74  E-value: 2.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534   70 PATSLIITFHNEArSTLLRTVKSVLNRTPPSLiqEIILVDDFSSD--PEDCQLLTKIP---KVKCLRNTRREGL---IRS 141
Cdd:pfam13641   2 PDVSVVVPAFNED-SVLGRVLEAILAQPYPPV--EVVVVVNPSDAetLDVAEEIAARFpdvRLRVIRNARLLGPtgkSRG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534  142 RVRGAEVATADILT*VTG------GGLQPMLQRVKedyTRVVSPIIDVISLDNFAYLAASADlrggfdwSLHFKWEQIPI 215
Cdd:pfam13641  79 LNHGFRAVKSDLVVLHDDdsvlhpGTLKKYVQYFD---SPKVGAVGTPVFSLNRSTMLSALG-------ALEFALRHLRM 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701367534  216 EQKmsrtdpTQSIRTPVIAGGIFVIDKSWFNHLGKYDTQMDIWggENFELSFRVWMCGGSLEIVPCSRVGHVFRK 290
Cdd:pfam13641 149 MSL------RLALGVLPLSGAGSAIRREVLKELGLFDPFFLLG--DDKSLGRRLRRHGWRVAYAPDAAVRTVFPT 215
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 74-136 3.21e-04

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


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 42.28  E-value: 3.21e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 701367534  74 LIITFHNEARsTLLRTVKSVLNRTPPSLIQEIILVDDFSSDpEDCQLLT-----KIPKVKCLRNTRRE 136
Cdd:cd04192    1 VVIAARNEAE-NLPRLLQSLSALDYPKEKFEVILVDDHSTD-GTVQILEfaaakPNFQLKILNNSRVS 66
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 73-289 4.12e-04

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


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 42.22  E-value: 4.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534  73 SLIITFHNEARsTLLRTVKSVLNRTPPSLIQEIILVDDFSSD--PEDCQLLT-KIPKVKCLRNTRReglIRS--RVRGAE 147
Cdd:cd02525    3 SIIIPVRNEEK-YIEELLESLLNQSYPKDLIEIIVVDGGSTDgtREIVQEYAaKDPRIRLIDNPKR---IQSagLNIGIR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534 148 VATADILT*VTGGGLQPmlqrvkEDYtrvVSPIIDVIsldnfayLAASADLRGGFDWSLHFKWEQIPIEQKMS------- 220
Cdd:cd02525   79 NSRGDIIIRVDAHAVYP------KDY---ILELVEAL-------KRTGADNVGGPMETIGESKFQKAIAVAQSsplgsgg 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701367534 221 ---RTDPTQSIRTPVIAGGIFviDKSWFNHLGKYDTQMDIwgGENFELSFRVWMCGGSLEIVPCSRVGHVFR 289
Cdd:cd02525  143 sayRGGAVKIGYVDTVHHGAY--RREVFEKVGGFDESLVR--NEDAELNYRLRKAGYKIWLSPDIRVYYYPR 210
beta-trefoil_Ricin_GALNT10 cd23476
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 418-490 5.85e-04

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: 40.33  E-value: 5.85e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701367534 418 DPlirQQDKCLSIASFSTGSQITLEACNQKDGRQKWKM-KGSFIQHFVSGLCLENQTG--RVVTNPCQADVPGQQW 490
Cdd:cd23476   62 DP---QHTKKFCFDAISHNSPVTLYDCHGMKGNQLWRYrKDKTLYHPVSNSCMDCSESdhRIFMNTCNPSSPTQQW 134
beta-trefoil_Ricin_RIPs_II_rpt2 cd23444
second ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating ...
 375-492 8.26e-04

second ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating proteins (RIPs); Type II ribosome-inactivating proteins (RIPs) inhibit translation in eukaryotes by irreversibly inactivating the 28S rRNA and preventing the binding of elongation factor II to the ribosome. They consist of a catalytic A-chain which has rRNA N-glycosidase activity and a lectin B-chain containing two ricin B-type lectin domains 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 lectin chain facilitates the internalization of the catalytic chain on binding to the cell surface. The two chains are connected by a disulfide bridge. This model corresponds to the second ricin B-type lectin domain. Members of this family includes Ricinus communis ricin, bitter gourd (Momordica charantia) seed lectin (BGSL), snake gourd (Trichosanthes anguina) seed lectin (SGSL), Sambucus ebulus ebulin I, Sambucus nigra nigrin b (also known as agglutinin V or SNAV), SNAI (also known as agglutinin I), SNAI' and SNAIf, Abrus precatorius abrin (ABR) and agglutinin-I (AAG), and Viscum album beta-galactoside-specific lectins 1-4 (also known as mistletoe lectins or MLs).


Pssm-ID: 467322 [Multi-domain]  Cd Length: 122  Bit Score: 39.18  E-value: 8.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534 375 IIKQGGNCLESraqdtTGNTLAGMGICKGTVNNppvtQEW-VFSDPLIRQ---QDKCLSIASFSTGSQITLEACNQKDGr 450
Cdd:cd23444    6 IVGLNDLCLQA-----NGGNNVWLEECVSNKKE----QKWaLYPDGTIRPnqnRNLCLTSSSDVQGSIIVVLSCSGSSG- 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 701367534 451 QKWKMK--GSfIQHFVSGLCLE-----NQTGRVVTNPcQADVPGQQWEL 492
Cdd:cd23444   76 QRWVFRndGT-ILNLYTGLVMDvkesdPSLKQIILWP-ATGGPNQQWTL 122
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 66-154 1.65e-03

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: 40.26  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534  66 DTDLPATSLIITFHNEARsTLLRTVKSVLNRTPPSLIQEIILVDDFSSDPEDcQLLTKIPK--VKCLRNTRREGLIRSRV 143
Cdd:cd06439   25 PAYLPTVTIIIPAYNEEA-VIEAKLENLLALDYPRDRLEIIVVSDGSTDGTA-EIAREYADkgVKLLRFPERRGKAAALN 102

                         90
                 ....*....|.
gi 701367534 144 RGAEVATADIL 154
Cdd:cd06439  103 RALALATGEIV 113
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
 426-477 2.73e-03

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: 37.96  E-value: 2.73e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 701367534 426 KCLSIASFSTGSQITLEACNQKDGRQKWKMKGSFIQHFV---SGLCLENQTGRVV 477
Cdd:cd23385   52 KCLGVSSSSPSSPLRLFECDSEDELQKWKCSKDGLLLLKglgLLLLYDKSGKNVV 106
beta-trefoil_Ricin_RPI cd23452
ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine ...
 374-454 2.83e-03

ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine protease I (RPI) and similar proteins; RPI, also called serine protease 1, is a major serine protease exhibiting lytic activity toward living yeast cells. It has a lectin-like affinity for mannose. Mannoproteins may be the native substrate for RPI. RPI contains a C-terminal 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. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467330 [Multi-domain]  Cd Length: 125  Bit Score: 37.88  E-value: 2.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534 374 GIIKQGGNCLESRAQDTTGNTLAGMGICKGTVNnppvtQEWVFS---DPLIRQQDKCLSIASFST--GSQITLEACNQKD 448
Cdd:cd23452   46 GTLRALGKCLDVAWGGTDNGTAVQLWTCSGNPA-----QQFVLSgagDLVNPQANKCVDVSGGNSgnGTRLQLWECSGNA 120


                 ....*.
gi 701367534 449 GrQKWK 454
Cdd:cd23452  121 N-QKWR 125
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 74-114 3.74e-03

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 38.81  E-value: 3.74e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 701367534  74 LIITFhNEARsTLLRTVKSVLNrtppsLIQEIILVDDFSSD 114
Cdd:cd02511    5 VIITK-NEER-NIERCLESVKW-----AVDEIIVVDSGSTD 38
beta-trefoil_Ricin_Pgant1-like cd23459
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 421-491 4.82e-03

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: 37.30  E-value: 4.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701367534 421 IRQQDKCLSiASFSTGSQITLEACNQKDGR-QKWKM-KGSFIQHFVSGLCLE---NQTGRVVT-NPCQADvPGQQWE 491
Cdd:cd23459   55 LRREESCAD-VQGTEESKVILITCHGLEKFnQKWKHtKGGQIVHLASGKCLDaegLKSGDDVTlAKCDGS-LSQKWT 129
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 73-351 7.39e-03

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: 38.41  E-value: 7.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534   73 SLIITFHN-EARSTLLRTVKSVLNRTPPSLiqEIILVDDFSSDPedcqLLTKIPKVKCLR--------NTRREGLIRSRV 143
Cdd:pfam10111   1 SVVIPVYNgEKTHWIQERILNQTFQYDPEF--ELIIINDGSTDK----TLEEVSSIKDHNlqvyypnaPDTTYSLAASRN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534  144 RGAEVATADILT*VTG---GGLQPMLQRVKEDYTRVVSPIIDVISLDNFAYL--AASADLRGGFDWSlhfkWEQIPIEQK 218
Cdd:pfam10111  75 RGTSHAIGEYISFIDGdclWSPDKFEKQLKIATSLALQENIQAAVVLPVTDLndESSNFLRRGGDLT----ASGDVLRDL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367534  219 MSRTDPTQSIRTPviAGGIFVIDKSWFNHLGKYDTQMDIWGGENFELSFRVWMCGGSLEIVPcsrVGHVFRKRHPYDFPE 298
Cdd:pfam10111 151 LVFYSPLAIFFAP--NSSNALINRQAFIEVGGFDESFRGHGAEDFDIFLRLAARYPFVAVMP---PQLLYRLSAKSMSPY 225

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 701367534  299 GNALTYIKNTKRTAEVWMDEYKQYYYEARPSaigKSFGSVADRVEQRRKLNCK 351
Cdd:pfam10111 226 SGFRRFLGDLARQAAACGKVLKHAYHDAPPS---LQYLKKYDWANLYRYLSFK 275
 
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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