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Conserved domains on  [gi|1488543073|gb|AYH26526|]
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exotoxin [Pectobacterium parmentieri]

Protein Classification

Glyco_hydro_1 and RICIN domain-containing protein( domain architecture ID 11042861)

Glyco_hydro_1 and RICIN domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GanB COG3867
Arabinogalactan endo-1,4-beta-galactosidase [Carbohydrate transport and metabolism];
1-362 2.08e-153

Arabinogalactan endo-1,4-beta-galactosidase [Carbohydrate transport and metabolism];


:

Pssm-ID: 443076  Cd Length: 382  Bit Score: 442.47  E-value: 2.08e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073   1 MKKNNYSGMISVLLMLFIGFMATNLAKAAPPFAYGADIGWVKQLEDRGVTWRDDAGTQRDVLQILRDHGINAVRLRIFVN 80
Cdd:COG3867     1 MKKLTIARILLLLGLLLLACASNPAAKEAADFIKGADLSYLNEMEDCGGKFYDEDGVPKDPLQILKDHGVNLVRLRLWVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073  81 PDpsalwhkdNTTWTMLGYTDKTRVVDAAQRAKAMGMRVMVDFHYSDVFADPGHQIKPAAWKNYNLSQLTTAVYNHTHEV 160
Cdd:COG3867    81 PY--------WAAPYGGGYNDLADVLAMAKRAKAAGMKVLLDFHYSDFWADPGKQNKPKAWANLSFDQLKDAVYDYTYDV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 161 MTALLSAGVTPEWVQVGNEMNPGILLPEGSTS----RFANLTQLLNAGYDAVKAV--SPSSKVISHLAHGNNNSNARWFF 234
Cdd:COG3867   153 LTALKAAGLLPDMVQVGNEINNGMLWPDGKTEqgpgNWDRLAALLNAGIRAVRDVaaSPDIKVMLHLAQGGNNGLFRWWF 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 235 DNfLTTHGGKTDVIGFSFYPYWEGKNywelTGSLASNLNDMASRYGKEVMVVEVGGLETN-------------------- 294
Cdd:COG3867   233 DN-LTKRGVDFDVIGLSYYPYWHTGS----LDDLGANLNDLASRYGKDVMVVETAYPWTLengdgapnifgtddpyaggy 307

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1488543073 295 ---PTDSYWTIKDTINLVKAVPGNKGIGVFYWEPAGNaSVLPDGYAlGTTTRVSNNVL-----QFTRALDAFAESQ 362
Cdd:COG3867   308 patPQGQADFLRDLIQAVKAVPNGGGLGVFYWEPAWI-PVPGTGWA-GEGSSWENQALfdfdgKALPALDAFKAPA 381
beta-trefoil_Ricin_1,3Gal43A cd23446
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and ...
 369-505 3.84e-67

ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and similar proteins; 1,3Gal43A is an exo-beta-1,3-galactanase that specifically hydrolyses beta-1,3 glycosidic bonds in galactose-based oligosaccharides or polysaccharides, and shows maximum activity towards beta-1,3-galactotetraose. 1,3Gal43A consists of a glycoside hydrolase family 43 (GH43) catalytic domain, a CBM13 carbohydrate binding domain, and a type I dockerin domain. The CBM13 domain is also known as 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. Each subdomain bears a potential sugar binding site.


:

Pssm-ID: 467324 [Multi-domain]  Cd Length: 137  Bit Score: 212.24  E-value: 3.84e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 369 ARYKIANRHSGKSLNVVGGSHEDSALLEQYSDGNWDSQRFYFNAMGNGYFNLVNVNSGKYIDVNFSANEDGAQILQMYNT 448
Cdd:cd23446     1 TYYKLVNRNSGKALDVLSGSTTDGAQIEQWTDNGGTSQQWYFTDVGGGYYKIVNRNSGKALDVNGASTADGAAIIQWTSN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1488543073 449 GHFSQQWLILDAGDGYYKIMNRNSGKLLDVSSRSTENGASGIQWHDNGGLNQLWKIT 505
Cdd:cd23446    81 GGDNQQWQIVDTGDGYYKIVNRNSGKLLDVNGWSTADGADIIQWSDNGGTNQQWQLV 137
 
Name Accession Description Interval E-value
GanB COG3867
Arabinogalactan endo-1,4-beta-galactosidase [Carbohydrate transport and metabolism];
1-362 2.08e-153

Arabinogalactan endo-1,4-beta-galactosidase [Carbohydrate transport and metabolism];


Pssm-ID: 443076  Cd Length: 382  Bit Score: 442.47  E-value: 2.08e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073   1 MKKNNYSGMISVLLMLFIGFMATNLAKAAPPFAYGADIGWVKQLEDRGVTWRDDAGTQRDVLQILRDHGINAVRLRIFVN 80
Cdd:COG3867     1 MKKLTIARILLLLGLLLLACASNPAAKEAADFIKGADLSYLNEMEDCGGKFYDEDGVPKDPLQILKDHGVNLVRLRLWVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073  81 PDpsalwhkdNTTWTMLGYTDKTRVVDAAQRAKAMGMRVMVDFHYSDVFADPGHQIKPAAWKNYNLSQLTTAVYNHTHEV 160
Cdd:COG3867    81 PY--------WAAPYGGGYNDLADVLAMAKRAKAAGMKVLLDFHYSDFWADPGKQNKPKAWANLSFDQLKDAVYDYTYDV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 161 MTALLSAGVTPEWVQVGNEMNPGILLPEGSTS----RFANLTQLLNAGYDAVKAV--SPSSKVISHLAHGNNNSNARWFF 234
Cdd:COG3867   153 LTALKAAGLLPDMVQVGNEINNGMLWPDGKTEqgpgNWDRLAALLNAGIRAVRDVaaSPDIKVMLHLAQGGNNGLFRWWF 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 235 DNfLTTHGGKTDVIGFSFYPYWEGKNywelTGSLASNLNDMASRYGKEVMVVEVGGLETN-------------------- 294
Cdd:COG3867   233 DN-LTKRGVDFDVIGLSYYPYWHTGS----LDDLGANLNDLASRYGKDVMVVETAYPWTLengdgapnifgtddpyaggy 307

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1488543073 295 ---PTDSYWTIKDTINLVKAVPGNKGIGVFYWEPAGNaSVLPDGYAlGTTTRVSNNVL-----QFTRALDAFAESQ 362
Cdd:COG3867   308 patPQGQADFLRDLIQAVKAVPNGGGLGVFYWEPAWI-PVPGTGWA-GEGSSWENQALfdfdgKALPALDAFKAPA 381
Glyco_hydro_53 pfam07745
Glycosyl hydrolase family 53; This domain belongs to family 53 of the glycosyl hydrolase ...
 35-358 5.12e-114

Glycosyl hydrolase family 53; This domain belongs to family 53 of the glycosyl hydrolase classification. These enzymes are enzymes are endo-1,4- beta-galactanases (EC:3.2.1.89). The structure of this domain is known and has a TIM barrel fold.


Pssm-ID: 311610  Cd Length: 333  Bit Score: 340.15  E-value: 5.12e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073  35 GADIGWVKQLEDRGVTWRDDAGTQRDVLQILRDHGINAVRLRIFVNPdpsalwhkdntTWTmlGYTDKTRVVDAAQRAKA 114
Cdd:pfam07745   3 GADISSLNELENAGVTFYNTNGKTQDLFQILKDHGVNSVRLRVWNDP-----------YDG--GNNDLDDVLKIAKRAKA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 115 MGMRVMVDFHYSDVFADPGHQIKPAAWKNYNLSQLTTAVYNHTHEVMTALLSAGVTPEWVQVGNEMNPGILLPEGSTSRF 194
Cdd:pfam07745  70 AGMKVLLDFHYSDTWADPGKQTKPKAWASLDTDQLKKALYNYTYDVLNALKEAGIDPDMVQVGNEINSGFLWPDGKTPNW 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 195 ANLTQLLNAGYDAVKAVSPSSKVISHLAHGNNNSNARWFFDNfLTTHGGKTDVIGFSFYPYWEGKNYweltgSLASNLND 274
Cdd:pfam07745 150 DNMAKLLNSGIKAVREVSPNIKVAIHLANGENNGLYRWWFDN-LTKAGVDFDVIGVSYYPFWSGTLE-----NLTTNLKD 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 275 MASRYGKEVMVVEVG-----------------------GLETNPTDSYWTIKDTINLVKAVPGNKGIGVFYWEPA----G 327
Cdd:pfam07745 224 MASRYGKDVMVVETAypwtlddgdghgnldpetssltsGYPATPQGQATMLRDVIELVNAVPGSRGLGVFYWEPAwipvG 303

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1488543073 328 NASVLPDGYALGTTTrVSNNVLQFTRALDAF 358
Cdd:pfam07745 304 DAGLWGGGSSWDNQA-LFDFNGRALPSLNVF 333
beta-trefoil_Ricin_1,3Gal43A cd23446
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and ...
 369-505 3.84e-67

ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and similar proteins; 1,3Gal43A is an exo-beta-1,3-galactanase that specifically hydrolyses beta-1,3 glycosidic bonds in galactose-based oligosaccharides or polysaccharides, and shows maximum activity towards beta-1,3-galactotetraose. 1,3Gal43A consists of a glycoside hydrolase family 43 (GH43) catalytic domain, a CBM13 carbohydrate binding domain, and a type I dockerin domain. The CBM13 domain is also known as 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. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467324 [Multi-domain]  Cd Length: 137  Bit Score: 212.24  E-value: 3.84e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 369 ARYKIANRHSGKSLNVVGGSHEDSALLEQYSDGNWDSQRFYFNAMGNGYFNLVNVNSGKYIDVNFSANEDGAQILQMYNT 448
Cdd:cd23446     1 TYYKLVNRNSGKALDVLSGSTTDGAQIEQWTDNGGTSQQWYFTDVGGGYYKIVNRNSGKALDVNGASTADGAAIIQWTSN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1488543073 449 GHFSQQWLILDAGDGYYKIMNRNSGKLLDVSSRSTENGASGIQWHDNGGLNQLWKIT 505
Cdd:cd23446    81 GGDNQQWQIVDTGDGYYKIVNRNSGKLLDVNGWSTADGADIIQWSDNGGTNQQWQLV 137
RicinB_lectin_2 pfam14200
Ricin-type beta-trefoil lectin domain-like;
404-492 5.53e-23

Ricin-type beta-trefoil lectin domain-like;


Pssm-ID: 464102 [Multi-domain]  Cd Length: 89  Bit Score: 92.83  E-value: 5.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 404 DSQRFYF-NAMGNGYFNLVNVNSGKYIDVNFSANEDGAQILQMYNTGHFSQQWLILDAGDGYYKIMNRNSGKLLDVSSrS 482
Cdd:pfam14200   1 ANQQWRFgGTVGDGYYTIVNVASGKYLDVAGGSTANGANVQQWTDNGNDNQQWRIVDAGDGYYRIVNKASGKVLDVAG-S 79

                          90
                  ....*....|
gi 1488543073 483 TENGASGIQW 492
Cdd:pfam14200  80 TANGTNVQQW 89
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 400-505 1.50e-06

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 47.12  E-value: 1.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073  400 DGNWDSQRFYFNAMGNgyfnLVNVNSGKYIDVNFSANedgaQILQMY--NTGHFSQQWLIldagDGYYKIMNRNSGKLLD 477
Cdd:smart00458  25 HGTGGNQLWKLTSDGA----IRIKDTDLCLTANGNTG----STVTLYscDGTNDNQYWEV----NKDGTIRNPDSGKCLD 92

                           90       100
                   ....*....|....*....|....*...
gi 1488543073  478 VSSRSTenGASGIQWHDNGGLNQLWKIT 505
Cdd:smart00458  93 VKDGNT--GTKVILWTCSGNPNQKWIFE 118
lectin_2 NF035930
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
 382-502 2.45e-03

lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor.


Pssm-ID: 468267 [Multi-domain]  Cd Length: 238  Bit Score: 39.77  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 382 LNVVGGSHEDSALLEQYSDGNwDSQRFYFNAMGNgyfnlVNVnSGKYIDVNFSANEDGAQILQMYNTGHFSQQWlilDAG 461
Cdd:NF035930  130 LDVSGGLRPGNGLIVYNCNGG-ENQRFTWGRGGE-----LRV-GDLCLDVADGNTRDGARVIAWSCSGGPNQRW---RWR 199

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1488543073 462 DGyyKIMNRNSGKLLDVSSRSTENGASGIQWHDNGGLNQLW 502
Cdd:NF035930  200 GG--QIRSRLSGKCLDIEGGRARPGQPVIVWSCNGGPNQRW 238
 
Name Accession Description Interval E-value
GanB COG3867
Arabinogalactan endo-1,4-beta-galactosidase [Carbohydrate transport and metabolism];
1-362 2.08e-153

Arabinogalactan endo-1,4-beta-galactosidase [Carbohydrate transport and metabolism];


Pssm-ID: 443076  Cd Length: 382  Bit Score: 442.47  E-value: 2.08e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073   1 MKKNNYSGMISVLLMLFIGFMATNLAKAAPPFAYGADIGWVKQLEDRGVTWRDDAGTQRDVLQILRDHGINAVRLRIFVN 80
Cdd:COG3867     1 MKKLTIARILLLLGLLLLACASNPAAKEAADFIKGADLSYLNEMEDCGGKFYDEDGVPKDPLQILKDHGVNLVRLRLWVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073  81 PDpsalwhkdNTTWTMLGYTDKTRVVDAAQRAKAMGMRVMVDFHYSDVFADPGHQIKPAAWKNYNLSQLTTAVYNHTHEV 160
Cdd:COG3867    81 PY--------WAAPYGGGYNDLADVLAMAKRAKAAGMKVLLDFHYSDFWADPGKQNKPKAWANLSFDQLKDAVYDYTYDV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 161 MTALLSAGVTPEWVQVGNEMNPGILLPEGSTS----RFANLTQLLNAGYDAVKAV--SPSSKVISHLAHGNNNSNARWFF 234
Cdd:COG3867   153 LTALKAAGLLPDMVQVGNEINNGMLWPDGKTEqgpgNWDRLAALLNAGIRAVRDVaaSPDIKVMLHLAQGGNNGLFRWWF 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 235 DNfLTTHGGKTDVIGFSFYPYWEGKNywelTGSLASNLNDMASRYGKEVMVVEVGGLETN-------------------- 294
Cdd:COG3867   233 DN-LTKRGVDFDVIGLSYYPYWHTGS----LDDLGANLNDLASRYGKDVMVVETAYPWTLengdgapnifgtddpyaggy 307

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1488543073 295 ---PTDSYWTIKDTINLVKAVPGNKGIGVFYWEPAGNaSVLPDGYAlGTTTRVSNNVL-----QFTRALDAFAESQ 362
Cdd:COG3867   308 patPQGQADFLRDLIQAVKAVPNGGGLGVFYWEPAWI-PVPGTGWA-GEGSSWENQALfdfdgKALPALDAFKAPA 381
Glyco_hydro_53 pfam07745
Glycosyl hydrolase family 53; This domain belongs to family 53 of the glycosyl hydrolase ...
 35-358 5.12e-114

Glycosyl hydrolase family 53; This domain belongs to family 53 of the glycosyl hydrolase classification. These enzymes are enzymes are endo-1,4- beta-galactanases (EC:3.2.1.89). The structure of this domain is known and has a TIM barrel fold.


Pssm-ID: 311610  Cd Length: 333  Bit Score: 340.15  E-value: 5.12e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073  35 GADIGWVKQLEDRGVTWRDDAGTQRDVLQILRDHGINAVRLRIFVNPdpsalwhkdntTWTmlGYTDKTRVVDAAQRAKA 114
Cdd:pfam07745   3 GADISSLNELENAGVTFYNTNGKTQDLFQILKDHGVNSVRLRVWNDP-----------YDG--GNNDLDDVLKIAKRAKA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 115 MGMRVMVDFHYSDVFADPGHQIKPAAWKNYNLSQLTTAVYNHTHEVMTALLSAGVTPEWVQVGNEMNPGILLPEGSTSRF 194
Cdd:pfam07745  70 AGMKVLLDFHYSDTWADPGKQTKPKAWASLDTDQLKKALYNYTYDVLNALKEAGIDPDMVQVGNEINSGFLWPDGKTPNW 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 195 ANLTQLLNAGYDAVKAVSPSSKVISHLAHGNNNSNARWFFDNfLTTHGGKTDVIGFSFYPYWEGKNYweltgSLASNLND 274
Cdd:pfam07745 150 DNMAKLLNSGIKAVREVSPNIKVAIHLANGENNGLYRWWFDN-LTKAGVDFDVIGVSYYPFWSGTLE-----NLTTNLKD 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 275 MASRYGKEVMVVEVG-----------------------GLETNPTDSYWTIKDTINLVKAVPGNKGIGVFYWEPA----G 327
Cdd:pfam07745 224 MASRYGKDVMVVETAypwtlddgdghgnldpetssltsGYPATPQGQATMLRDVIELVNAVPGSRGLGVFYWEPAwipvG 303

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1488543073 328 NASVLPDGYALGTTTrVSNNVLQFTRALDAF 358
Cdd:pfam07745 304 DAGLWGGGSSWDNQA-LFDFNGRALPSLNVF 333
beta-trefoil_Ricin_1,3Gal43A cd23446
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and ...
 369-505 3.84e-67

ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and similar proteins; 1,3Gal43A is an exo-beta-1,3-galactanase that specifically hydrolyses beta-1,3 glycosidic bonds in galactose-based oligosaccharides or polysaccharides, and shows maximum activity towards beta-1,3-galactotetraose. 1,3Gal43A consists of a glycoside hydrolase family 43 (GH43) catalytic domain, a CBM13 carbohydrate binding domain, and a type I dockerin domain. The CBM13 domain is also known as 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. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467324 [Multi-domain]  Cd Length: 137  Bit Score: 212.24  E-value: 3.84e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 369 ARYKIANRHSGKSLNVVGGSHEDSALLEQYSDGNWDSQRFYFNAMGNGYFNLVNVNSGKYIDVNFSANEDGAQILQMYNT 448
Cdd:cd23446     1 TYYKLVNRNSGKALDVLSGSTTDGAQIEQWTDNGGTSQQWYFTDVGGGYYKIVNRNSGKALDVNGASTADGAAIIQWTSN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1488543073 449 GHFSQQWLILDAGDGYYKIMNRNSGKLLDVSSRSTENGASGIQWHDNGGLNQLWKIT 505
Cdd:cd23446    81 GGDNQQWQIVDTGDGYYKIVNRNSGKLLDVNGWSTADGADIIQWSDNGGTNQQWQLV 137
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 369-502 6.00e-40

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: 140.97  E-value: 6.00e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 369 ARYKIANRHSGKSLNVVGGSHEDSALLEQYSDGNWDSQRFYFNAMGNGYFNLVNVNSGKYIDVNFSANEDGAQILQMYNT 448
Cdd:cd00161     1 GTYRIVNAASGKCLDVAGGSTANGAPVQQWTCNGGANQQWTLTPVGDGYYTIRNVASGKCLDVAGGSTANGANVQQWTCN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1488543073 449 GHFSQQWLILDAGDGYYKIMNRNSGKLLDVSSRSTENGASGIQWHDNGGLNQLW 502
Cdd:cd00161    81 GGDNQQWRLEPVGDGYYRIVNKHSGKCLDVSGGSTANGANVQQWTCNGGANQQW 134
beta-trefoil_Ricin_AgaB34-like cd23458
ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 ...
 371-503 1.10e-32

ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 and similar proteins; Beta-agarase (EC 3.2.1.81), also called endo-beta-agarase, is a glycosyl hydrolase family 16 (GH16) member that catalyzes the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea (marine red algae), giving the tetramer as the predominant product. Beta-agarase contains a ricin B-type lectin domain that adopts 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: 467336 [Multi-domain]  Cd Length: 135  Bit Score: 121.28  E-value: 1.10e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 371 YKIANRHSGKSLNVVGGSHEDSALLEQYSDGNWDSQRFYFNAMGNGYFNLVNVNSGKYIDVNFSANEDGAQILQMYNTGH 450
Cdd:cd23458     3 YRIRNRNSGKCIDVAGGSTANGANIQQWDCGSGSNQQWTLVEIDNGYYRIKASHSGKCLDVAGGSTANGANIQQWDCVGG 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1488543073 451 FSQQWLILDAGDGYYKIMNRNSGKLLDVSSRSTENGASGIQWHDNGGLNQLWK 503
Cdd:cd23458    83 ANQQWKLQDLGNGYFELKARHSGKCLDVAGGSTANGASIQQWTCNGNDNQRFK 135
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 416-507 6.81e-25

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: 99.75  E-value: 6.81e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 416 GYFNLVNVNSGKYIDVNFSANEDGAQILQMYNTGHFSQQWLILDAGDGYYKIMNRNSGKLLDVSSRSTENGASGIQWHDN 495
Cdd:cd00161     1 GTYRIVNAASGKCLDVAGGSTANGAPVQQWTCNGGANQQWTLTPVGDGYYTIRNVASGKCLDVAGGSTANGANVQQWTCN 80

                          90
                  ....*....|..
gi 1488543073 496 GGLNQLWKITAN 507
Cdd:cd00161    81 GGDNQQWRLEPV 92
RicinB_lectin_2 pfam14200
Ricin-type beta-trefoil lectin domain-like;
404-492 5.53e-23

Ricin-type beta-trefoil lectin domain-like;


Pssm-ID: 464102 [Multi-domain]  Cd Length: 89  Bit Score: 92.83  E-value: 5.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 404 DSQRFYF-NAMGNGYFNLVNVNSGKYIDVNFSANEDGAQILQMYNTGHFSQQWLILDAGDGYYKIMNRNSGKLLDVSSrS 482
Cdd:pfam14200   1 ANQQWRFgGTVGDGYYTIVNVASGKYLDVAGGSTANGANVQQWTDNGNDNQQWRIVDAGDGYYRIVNKASGKVLDVAG-S 79

                          90
                  ....*....|
gi 1488543073 483 TENGASGIQW 492
Cdd:pfam14200  80 TANGTNVQQW 89
beta-trefoil_Ricin_AgaB34-like cd23458
ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 ...
 416-504 3.53e-20

ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 and similar proteins; Beta-agarase (EC 3.2.1.81), also called endo-beta-agarase, is a glycosyl hydrolase family 16 (GH16) member that catalyzes the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea (marine red algae), giving the tetramer as the predominant product. Beta-agarase contains a ricin B-type lectin domain that adopts 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: 467336 [Multi-domain]  Cd Length: 135  Bit Score: 86.61  E-value: 3.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 416 GYFNLVNVNSGKYIDVNFSANEDGAQILQMY-NTGHfSQQWLILDAGDGYYKIMNRNSGKLLDVSSRSTENGASGIQWHD 494
Cdd:cd23458     1 GTYRIRNRNSGKCIDVAGGSTANGANIQQWDcGSGS-NQQWTLVEIDNGYYRIKASHSGKCLDVAGGSTANGANIQQWDC 79

                          90
                  ....*....|
gi 1488543073 495 NGGLNQLWKI 504
Cdd:cd23458    80 VGGANQQWKL 89
RicinB_lectin_2 pfam14200
Ricin-type beta-trefoil lectin domain-like;
371-444 2.30e-17

Ricin-type beta-trefoil lectin domain-like;


Pssm-ID: 464102 [Multi-domain]  Cd Length: 89  Bit Score: 77.03  E-value: 2.30e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1488543073 371 YKIANRHSGKSLNVVGGSHEDSALLEQYSDGNWDSQRFYFNAMGNGYFNLVNVNSGKYIDVNFSaNEDGAQILQ 444
Cdd:pfam14200  16 YTIVNVASGKYLDVAGGSTANGANVQQWTDNGNDNQQWRIVDAGDGYYRIVNKASGKVLDVAGS-TANGTNVQQ 88
beta-trefoil_Ricin_SaAF-like cd23457
ricin B-type lectin domain, beta-trefoil fold, found in Stigmatella aurantiaca ...
 373-495 1.11e-16

ricin B-type lectin domain, beta-trefoil fold, found in Stigmatella aurantiaca alpha-L-arabinofuranosidase (SaAF) and similar proteins; Alpha-L-arabinofuranosidase (EC 3.2.1.55), also called non-reducing end alpha-L-arabinofuranosidase, or arabinosidase, catalyzes the hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides. It acts on alpha-L-arabinofuranosides, alpha-L-arabinans containing (1,3)- and/or (1,5)-linkages, arabinoxylans and arabinogalactans. Members of this subfamily contain a ricin B-type lectin domain that adopts 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: 467335 [Multi-domain]  Cd Length: 139  Bit Score: 76.69  E-value: 1.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 373 IANRHSGKSLNVVGGSHEDSALLEQYSDGNWDSQRFYFNAMGNGYFNLVNV-NSGKYIDVNFSANEDGAQILQMYNTGHF 451
Cdd:cd23457     7 IVSAQSGKVLSAEGCSTATGTNVEQQSWTGSACQKWQFTPTDNGFYQLRPAsNASLCLAVEGGSLAAGANLVLGACSADS 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1488543073 452 SqQWLILDAGDGYYKIMNRNSGKLLDVSSRSTENGASGIQ--WHDN 495
Cdd:cd23457    87 S-QWRLEPLADGALRLVSRHSGLVLDLDNCSLADGANLQQypWLDN 131
beta-trefoil_Ricin_MOA-like cd23416
ricin B-type lectin domain, beta-trefoil fold, found in Marasmius oreades agglutinin (MOA) and ...
 371-504 5.50e-13

ricin B-type lectin domain, beta-trefoil fold, found in Marasmius oreades agglutinin (MOA) and similar proteins; The family includes Marasmius oreades agglutinin (MOA) and Polyporus squamosus Ricin B-related lectin (PSL). MOA is a lectin isolated from fruiting bodies of the mushroom M. oreades. It specifically binds non-reducing terminal Galalpha(1,3)Gal carbohydrates, such as that which occurs in the xenotransplantation epitope Galalpha(1,3)Galbeta(1,4)GlcNAc and the branched blood group B determinant Galalpha(1,3)[Fucalpha(1,2)]Gal. Polyporus squamosus Ricin B-related lectin (PSL) is a lectin specific for glycans terminating with the sequence Neu5Acalpha2-6Galbeta. Like MOA, PSL is a calcium-dependent cysteine protease. Both MOA and PSL contain an N-terminal ricin B-type lectin domain and a C-terminal agglutinin domain. The ricin B-type lectin domain is a beta-trefoil domain, 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: 467295 [Multi-domain]  Cd Length: 145  Bit Score: 66.22  E-value: 5.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 371 YKIANRHSGKSLNVVGGSHEDSALL----EQYSDGNWDSQ-RFYFNAMGNGYFNLVNVNSGKYIDVNFSANEDGAQILQM 445
Cdd:cd23416     3 YHIRNAGTGTVLDLSGGSSANGTPIqgwqKTGDTGSFNQLwLLEPVPNGSDTYTIQNVRSGTYLDLAGGSSANGTAIVGW 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1488543073 446 YNTGHFSQQWLILDAGDG-YYKIMNRNSGKLLDVSSRSTENG--ASGIQWHDNGGlNQLWKI 504
Cdd:cd23416    83 QSTNNPNQQWVIKPANGGtYYKIQNKGTGTFLDLYGGDSANGtkIVGWTGHWGNP-NQLWLF 143
RicinB_lectin_2 pfam14200
Ricin-type beta-trefoil lectin domain-like;
452-507 8.72e-13

Ricin-type beta-trefoil lectin domain-like;


Pssm-ID: 464102 [Multi-domain]  Cd Length: 89  Bit Score: 63.94  E-value: 8.72e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1488543073 452 SQQW-LILDAGDGYYKIMNRNSGKLLDVSSRSTENGASGIQWHDNGGLNQLWKITAN 507
Cdd:pfam14200   2 NQQWrFGGTVGDGYYTIVNVASGKYLDVAGGSTANGANVQQWTDNGNDNQQWRIVDA 58
beta-trefoil_Ricin_1,3Gal43A cd23446
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and ...
 463-506 1.82e-12

ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and similar proteins; 1,3Gal43A is an exo-beta-1,3-galactanase that specifically hydrolyses beta-1,3 glycosidic bonds in galactose-based oligosaccharides or polysaccharides, and shows maximum activity towards beta-1,3-galactotetraose. 1,3Gal43A consists of a glycoside hydrolase family 43 (GH43) catalytic domain, a CBM13 carbohydrate binding domain, and a type I dockerin domain. The CBM13 domain is also known as 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. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467324 [Multi-domain]  Cd Length: 137  Bit Score: 64.71  E-value: 1.82e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1488543073 463 GYYKIMNRNSGKLLDVSSRSTENGASGIQWHDNGGLNQLWKITA 506
Cdd:cd23446     1 TYYKLVNRNSGKALDVLSGSTTDGAQIEQWTDNGGTSQQWYFTD 44
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
369-502 1.49e-11

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 61.78  E-value: 1.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 369 ARYKIANRHSGKSLNVvGGSHEDSALLEQYS-DGNWDSQRFYFNAMGNgyfnLVNVNSGKYIDVNFSAneDGAQIlQMY- 446
Cdd:pfam00652   1 ATGRIRNRASGKCLDV-PGGSSAGGPVGLYPcHGSNGNQLWTLTGDGT----IRSVASDLCLDVGSTA--DGAKV-VLWp 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1488543073 447 -NTGHFSQQWLILDAGDGyykIMNRNSGKLLDVSSRSTENGASGIQWHDNGGLNQLW 502
Cdd:pfam00652  73 cHPGNGNQRWRYDEDGTQ---IRNPQSGKCLDVSGAGTSNGKVILWTCDSGNPNQQW 126
beta-trefoil_Ricin_HA17-like cd23445
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium botulinum hemagglutinating ...
 371-504 1.16e-09

ricin B-type lectin domain, beta-trefoil fold, found in Clostridium botulinum hemagglutinating proteins, HA17 and HA33, and similar proteins; The subfamily includes Clostridium botulinum hemagglutinating proteins HA17 and HA33, Lysinibacillus sphaericus mosquitocidal toxin (MTX) and Pieris brassicae pierisin. The hemagglutinin (HA) component of the progenitor toxin protects the structural integrity of the neurotoxin. It may increase internalization of the neurotoxin into the bloodstream of the host. The hemagglutinin complex, composed of HA-70 (also known as HA3), HA-33 (also known as HA1) and HA-17 (also known as HA2), agglutinates erythrocytes, whereas the individual components do not. HA-33 is involved in recognition of cell-surface carbohydrates. HA-17 and HA-70 are involved in paracellular barrier disruption by E-cadherin binding. MTX acts as an ADP-ribosyl transferase. Pierisin, also called NAD--DNA ADP-ribosyltransferase, pierisin-2, or pierisin-B, catalyzes the ADP ribosylation of double-stranded DNA by targeting the N2 amino group of dG residues. It induces apoptosis in a range of human cell lines. Members of this subfamily contain at least one 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.


Pssm-ID: 467323 [Multi-domain]  Cd Length: 133  Bit Score: 56.56  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 371 YKIANRHSG-KSLNVVGGSHedSALLEQYSDGN---WdsqRFYFNAMGNGYFNLVNVNSGKYIDVNfsaNEDGAQILQMY 446
Cdd:cd23445     3 YKIVTALNSnKVLDMNSNSN--NVVLWDNNGGNnqkW---RFEYDSGKNAYQIKNLDNTNLVLAWN---SSSSNNVFAST 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1488543073 447 NTGHFSQQWLILDAGDGYYKIMN-RNSGKLLDVSSRSTENGASGIQWHDNGGLNQLWKI 504
Cdd:cd23445    75 NTSKDEQYWKLEEAGDGYYIIKNyADPNLVLDVEGSNTANGTNIIVYPRNGSNNQKFKL 133
beta-trefoil_Ricin_MOA-like cd23416
ricin B-type lectin domain, beta-trefoil fold, found in Marasmius oreades agglutinin (MOA) and ...
 420-505 4.48e-09

ricin B-type lectin domain, beta-trefoil fold, found in Marasmius oreades agglutinin (MOA) and similar proteins; The family includes Marasmius oreades agglutinin (MOA) and Polyporus squamosus Ricin B-related lectin (PSL). MOA is a lectin isolated from fruiting bodies of the mushroom M. oreades. It specifically binds non-reducing terminal Galalpha(1,3)Gal carbohydrates, such as that which occurs in the xenotransplantation epitope Galalpha(1,3)Galbeta(1,4)GlcNAc and the branched blood group B determinant Galalpha(1,3)[Fucalpha(1,2)]Gal. Polyporus squamosus Ricin B-related lectin (PSL) is a lectin specific for glycans terminating with the sequence Neu5Acalpha2-6Galbeta. Like MOA, PSL is a calcium-dependent cysteine protease. Both MOA and PSL contain an N-terminal ricin B-type lectin domain and a C-terminal agglutinin domain. The ricin B-type lectin domain is a beta-trefoil domain, 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: 467295 [Multi-domain]  Cd Length: 145  Bit Score: 55.04  E-value: 4.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 420 LVNVNSGKYIDVNFSANEDGAQIL---QMYNTGHFSQQWLIL--DAGDGYYKIMNRNSGKLLDVSSRSTENGASGIQWHD 494
Cdd:cd23416     5 IRNAGTGTVLDLSGGSSANGTPIQgwqKTGDTGSFNQLWLLEpvPNGSDTYTIQNVRSGTYLDLAGGSSANGTAIVGWQS 84

                          90
                  ....*....|.
gi 1488543073 495 NGGLNQLWKIT 505
Cdd:cd23416    85 TNNPNQQWVIK 95
COG3934 COG3934
Endo-1,4-beta-mannosidase [Carbohydrate transport and metabolism];
51-323 6.44e-09

Endo-1,4-beta-mannosidase [Carbohydrate transport and metabolism];


Pssm-ID: 443135 [Multi-domain]  Cd Length: 331  Bit Score: 57.67  E-value: 6.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073  51 WRD-DAGTQRDVLQILRDHGINAVRlrIFV-------NP---DPSALWHKDnttwtmlgytdktRVVDAAQRAkamGMRV 119
Cdd:COG3934    23 WRDwDPDRVRRELDDLAALGLDVVR--VFLlwedfqpNPgliNEEALERLD-------------YFLDAAAER---GLKV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 120 MVDF----------------------HYSDVFADPghQIKpAAWKNYnLSQLTTAVYNHThevmtALLSagvtpeWvQVG 177
Cdd:COG3934    85 VLTLfnnwwsghmsgynwlpswvggwHRRNFYTDP--EAV-EAQKAY-VRTLANRYKDDP-----AILG------W-ELG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 178 NEMNPGillpeGSTSRFANLTQLLNAGYDAVKAVSPSskvisHL-AHGNNNSNARWFFDNFLTTHGGK-TDVIGFSFYPY 255
Cdd:COG3934   149 NEPRNF-----GDPASPEAALAWLREMAAAIKSLDPN-----HLvSSGDEGDYWEVDDHPFVPAHAAPlIDYLTVHLYPF 218

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1488543073 256 WEGKNYWELTGSLASNLNDMASRYGKEVMVVEVG----GLETNPTDSYWTIKDTINLVKAVPGNkgIGVFYW 323
Cdd:COG3934   219 NWGWVDRPRSTDKAAYLIELARALGKPVVLEEFGaprdSPQASEEDRAEFYRTVLEAALTLAGA--AGANWW 288
beta-trefoil_Ricin_EW29-like cd23449
ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa ...
 373-505 8.81e-09

ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa galactose-binding lectin (EW29) and similar proteins; EW29 is a galactose-binding lectin from the earthworm Lumbricus terrestris. It contains 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 second ricin B-type lectin domain may harbor two sugar-binding pockets in subdomains alpha and gamma. EW29 uses these two sugar-binding sites for its function as a single domain-type hemagglutinin.


Pssm-ID: 467327 [Multi-domain]  Cd Length: 128  Bit Score: 53.83  E-value: 8.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 373 IANRHSGKSLNVVGGSHEDSAL--LEQYSDGNWDSQRFYFNAmGNGYF-----NLVnvnsgkyidvnFSANEDGAQILQM 445
Cdd:cd23449     5 IKSKLNGKVLDVEGANAKPGAKviMWEKKGGAEDNQLWYEDE-VTGTIrsklnDFC-----------LDASGDKGLILNP 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1488543073 446 YNTGHFSQQWLIldAGDgyyKIMNR-NSGKLLDVSSRSTENGASGIQWHDNGGLNQLWKIT 505
Cdd:cd23449    73 YDPSNPKQQWKI--SGN---KIQNRsNPDNVLDIKGGSKDDGARLCAWEYNGGPNQLWDFE 128
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 371-502 9.10e-09

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: 53.89  E-value: 9.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 371 YKIANRHSGKSLNVVGGSHEDSALLEQYSDGNWDSQRFYFNAMGngyfnLVNVNSGKYIDVNFSANEDGAQiLQMYN-TG 449
Cdd:cd23418     6 GQIRGYGSGRCLDVPGGSTTNGTRLILWDCHGGANQQFTFTSAG-----ELRVGGDKCLDAAGGGTTNGTP-VVIWPcNG 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1488543073 450 HFSQQWLILDAGdgyyKIMNRNSGKLLDVSSRSTENGASGIQWHDNGGLNQLW 502
Cdd:cd23418    80 GANQKWRFNSDG----TIRNVNSGLCLDVAGGGTANGTRLILWSCNGGSNQRW 128
beta-trefoil_Ricin_EndoBetaGal-like cd23432
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium perfringens GlcNac-alpha-1, ...
 371-491 1.18e-08

ricin B-type lectin domain, beta-trefoil fold, found in Clostridium perfringens GlcNac-alpha-1,4-Gal-releasing endo-beta-galactosidase (Endo-beta-Gal(GnGa)) and similar proteins; Endo-beta-Gal(GnGa) can release disaccharide GlcNAc-alpha-1,4Gal from O-glycans expressed in the gastric gland mucous cell-type mucin. It 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 may harbor a sugar-binding pocket.


Pssm-ID: 467310  Cd Length: 127  Bit Score: 53.50  E-value: 1.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 371 YKIANRHSGKSLNVVGGshedsALLEQYSDGNWDSQRFYFNAMGNGYFNLVNVNSGKYIDVNfsANEDGAQILQMYNTGH 450
Cdd:cd23432     3 VRIKNRWTGQYLYEENG-----KVKYGTPPEDDTSAQWIIEDVGDGYVRIKNRATGHYLHIE--NNTGYLESGPIPPGWW 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1488543073 451 fSQQWLILDAGDGYYKIMNR-NSGKLLdvssrSTENGASGIQ 491
Cdd:cd23432    76 -SAQWTLEPVGTGYVRIRNRwKPNQYL-----HIENQTGYAQ 111
beta-trefoil_Ricin_SSA cd23426
ricin B-type lectin domain, beta-trefoil fold, found in Sclerotinia sclerotiorum agglutinin ...
 371-503 5.44e-08

ricin B-type lectin domain, beta-trefoil fold, found in Sclerotinia sclerotiorum agglutinin (SSA) and similar proteins; SSA acts as a lectin that primarily recognizes glycans with a non-reducing terminal N-acetylgalactosamine (GalNAc), with a preference for the alpha-over the beta-anomer. It can also bind non-reducing terminal galactose (Gal) residues but with a lower affinity. SSA strongly interacts with glycolipid type glycans with terminal non-reducing Gal or GalNAc but fails to bind sialylated or fucosylated forms of the same glycans. It also strongly interacts with galactosylated N-glycans, displaying highest affinity for alpha-1-3 branched mono-antennary N-glycans but also binding to multi-antennary glycans. SSA is a homodimeric protein. The monomer contains a ricin B-type lectin domain with 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: 467304 [Multi-domain]  Cd Length: 147  Bit Score: 51.97  E-value: 5.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 371 YKIANRH-SGKSLNVVGGSHEDSALLEQYSDG-NWDSQRFYFNAMGNGY-----FNLVNVNSGKYIdvnfSANEDGAQIL 443
Cdd:cd23426     5 YEIVPYHaPNKNLNLWGGSKEDGTKVRLYSRGtASKNAHWQIVYAGGGGsgkdeYHIINVNSGLYL----TATDKGNGKV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1488543073 444 QMYNTG--HFSQQWLILDAGD--GYYKIMNRNSGKL-LDVSSRSTENGASGIQW-HDNGGLNQLWK 503
Cdd:cd23426    81 TTNTTSprNPRARWNIVPARNgtGTYWINSVANKKLqLNVAGYGTADGTPVIIWaGADGAENQQFY 146
beta-trefoil_Ricin_RPI cd23452
ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine ...
 377-503 2.32e-07

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: 49.82  E-value: 2.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 377 HSGKSLNVVGGSHEDSALLEQYSDGNWDSQRFYFNAMGNGYFNlvnvnsGKYIDVNFSANEDGAQILQMYNTGHFSQQWL 456
Cdd:cd23452     9 LANKCIDVPNSSTTDGAPLQLWDCNGTNAQKWTFASDGTLRAL------GKCLDVAWGGTDNGTAVQLWTCSGNPAQQFV 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1488543073 457 ILDAGDgyykIMNRNSGKLLDVSSRSTENGASGIQWHDNGGLNQLWK 503
Cdd:cd23452    83 LSGAGD----LVNPQANKCVDVSGGNSGNGTRLQLWECSGNANQKWR 125
beta-trefoil_Ricin_MPL_CNL cd23422
ricin B-type lectin domain, beta-trefoil fold, found in Macrolepiota procera ricin B-like ...
 367-505 3.90e-07

ricin B-type lectin domain, beta-trefoil fold, found in Macrolepiota procera ricin B-like lectin (MPL), Clitocybe nebularis lectin (CNL), and similar proteins; MPL and CNL are a homodimeric ricin B-like lectins with a beta-trefoil fold that 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. Their alpha subunit may harbor a sugar-binding pocket. MPL has the highest specificity for terminal N-acetyllactosamine and other beta-galactosides. CNL induces maturation and activation of dendritic cells via the toll-like receptor 4 pathway. It is specific for terminal, non-reducing N-acetylgalactosamine (Gal-NAc)-containing carbohydrates including N,N'-diacetyllactosediamine/LDN (GalNAcbeta1-4GlcNAc, LacdiNAc). It is also specific for carbohydrates containing N-acetylglucosamine (-GlcNAc) or N-acetyllactosamine (-Galbeta1-4GlcNAc) at the reducing end.


Pssm-ID: 467300 [Multi-domain]  Cd Length: 135  Bit Score: 49.24  E-value: 3.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 367 NGARYKIANRHSGKSLNVVGGSHEdSALLEQYSDGNWdsQRFYFNAMGNGYFNLVNVNSGKYIDVNFSAnEDGAQILqmy 446
Cdd:cd23422     1 SGGTYKIVNVKSGTVLDLSGDDNT-SVVGWPFHGGEN--QQWTLEPTPGGGYTIQSVSTGKYLGIEGGP-RDGTRLV--- 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1488543073 447 nTGHFSQQWLILDAG--DGYYKIMNRNSGKLLDVSSRSTENGaSGIQ-WHDNGGLNQLWKIT 505
Cdd:cd23422    74 -GSDQPFVWDIEPDEgdSGAFRIFVPGTNLVLDLDDGGSAPG-TPVQlWERSEGPNQLWRFE 133
beta-trefoil_Ricin_MTX-like_rpt1-3 cd23497
first, second and third ricin B-type lectin domains, beta-trefoil fold, found in ...
 434-505 6.65e-07

first, second and third ricin B-type lectin domains, beta-trefoil fold, found in Lysinibacillus sphaericus mosquitocidal toxin (MTX) and similar proteins; This subfamily includes Lysinibacillus sphaericus MTX and Pieris brassicae pierisin. MTX acts as an ADP-ribosyl transferase. Pierisin, also called NAD--DNA ADP-ribosyltransferase, pierisin-2, or pierisin-B, catalyzes the ADP ribosylation of double-stranded DNA by targeting the N2 amino group of dG residues. It induces apoptosis in a range of human cell lines. Members of this family contain four 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 model corresponds to the first, second and third ricin B-type lectin domains. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467375 [Multi-domain]  Cd Length: 139  Bit Score: 48.51  E-value: 6.65e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1488543073 434 SANEDGAQILQMYNTGHFSQQ-WLILDAGDGYYKIMN-RNSGKLLDVSSRSTENGASGIQWHDNGGLNQLWKIT 505
Cdd:cd23497    66 SNASSKEMVIRGYTGSGSDNQyWRIERTEDGYYKLRNlADLKKVLDLANGNTNNGTRIQVYDNNGTSAQKWIIK 139
beta-trefoil_Ricin_AgaB34-like cd23458
ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 ...
 463-507 7.41e-07

ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 and similar proteins; Beta-agarase (EC 3.2.1.81), also called endo-beta-agarase, is a glycosyl hydrolase family 16 (GH16) member that catalyzes the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea (marine red algae), giving the tetramer as the predominant product. Beta-agarase contains a ricin B-type lectin domain that adopts 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: 467336 [Multi-domain]  Cd Length: 135  Bit Score: 48.47  E-value: 7.41e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1488543073 463 GYYKIMNRNSGKLLDVSSRSTENGASGIQWHDNGGLNQLWKITAN 507
Cdd:cd23458     1 GTYRIRNRNSGKCIDVAGGSTANGANIQQWDCGSGSNQQWTLVEI 45
beta-trefoil_Ricin_RSA cd23455
ricin B-type lectin domain, beta-trefoil fold, found in Rhizoctonia solani agglutinin (RSA) ...
 371-504 1.08e-06

ricin B-type lectin domain, beta-trefoil fold, found in Rhizoctonia solani agglutinin (RSA) and similar proteins; RSA is a 15.5-kDa lectin accumulated in the mycelium and sclerotia of the soil born plant pathogenic fungus R. solani. It may act as a storage protein implicated in fungal insecticidal activity. It displays high selectivity towards terminal non-reducing N-acetylgalactosamine residues. RSA reveals a domain-swapping dimeric assembly. Each monomer contains a ricin B-type lectin domain that adopts 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: 467333 [Multi-domain]  Cd Length: 131  Bit Score: 47.70  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 371 YKIANRHSGKSLNVVGGSHEDSALLEQYSDGNWDSQRFYFNAMGNG-YFNLVNVNSGKYidVNFSANEDGAQILqmynTG 449
Cdd:cd23455     3 YRIKNVATGTVLDLYLGSSAEGTPVQGYQPNGGDNQKWQLEWVGSGnGVTLRNVASGTY--AGFPAHADGGQVV----GS 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1488543073 450 HFSQQWLILDAGDGYYKIMNRNSGKLLDVSSRSTENGASGIQWHDNGGLNQLWKI 504
Cdd:cd23455    77 NNPVLFTIVAADGGYQIQPVDDPDLVLDLAGSNDEDGTPVILYNNDGGDNQKWYF 131
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 400-505 1.50e-06

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 47.12  E-value: 1.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073  400 DGNWDSQRFYFNAMGNgyfnLVNVNSGKYIDVNFSANedgaQILQMY--NTGHFSQQWLIldagDGYYKIMNRNSGKLLD 477
Cdd:smart00458  25 HGTGGNQLWKLTSDGA----IRIKDTDLCLTANGNTG----STVTLYscDGTNDNQYWEV----NKDGTIRNPDSGKCLD 92

                           90       100
                   ....*....|....*....|....*...
gi 1488543073  478 VSSRSTenGASGIQWHDNGGLNQLWKIT 505
Cdd:smart00458  93 VKDGNT--GTKVILWTCSGNPNQKWIFE 118
beta-trefoil_Ricin_SCDase_rpt2 cd23500
second ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ...
 378-503 4.87e-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: 45.92  E-value: 4.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 378 SGKSLNVVGGSHEDSALLEQYSDGNWDSQRFYFN-AMGngyfNLVN-VNSGKYIDVNFSANEDGAQI-LQMYNTGHFSQQ 454
Cdd:cd23500    10 SGKCLSAANGSQLNGSLVQLDACHASAGQLWYFDpKKG----TIRSaLDGNKCLAIPGGNTGNHTQLqLADCDASNPAQQ 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1488543073 455 WlilDAGDGYYKiMNRNSGKLLDVSSRSteNGASGIQWHDNGGLNQLWK 503
Cdd:cd23500    86 F---NYDGGVFR-SRLNSNQVIDASGGS--DGSELILYDYHGGSNQRWR 128
beta-trefoil_Ricin_AgaB34-like cd23458
ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 ...
 362-408 5.03e-06

ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 and similar proteins; Beta-agarase (EC 3.2.1.81), also called endo-beta-agarase, is a glycosyl hydrolase family 16 (GH16) member that catalyzes the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea (marine red algae), giving the tetramer as the predominant product. Beta-agarase contains a ricin B-type lectin domain that adopts 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: 467336 [Multi-domain]  Cd Length: 135  Bit Score: 46.16  E-value: 5.03e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1488543073 362 QINFINGARYKIANRHSGKSLNVVGGSHEDSALLEQYSDGNWDSQRF 408
Cdd:cd23458    88 KLQDLGNGYFELKARHSGKCLDVAGGSTANGASIQQWTCNGNDNQRF 134
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 362-408 6.73e-05

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: 42.74  E-value: 6.73e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1488543073 362 QINFINGARYKIANRHSGKSLNVVGGSHEDSALLEQYSDGNWDSQRF 408
Cdd:cd00161    88 RLEPVGDGYYRIVNKHSGKCLDVSGGSTANGANVQQWTCNGGANQQW 134
beta-trefoil_Ricin_SaAF-like cd23457
ricin B-type lectin domain, beta-trefoil fold, found in Stigmatella aurantiaca ...
 416-491 9.86e-05

ricin B-type lectin domain, beta-trefoil fold, found in Stigmatella aurantiaca alpha-L-arabinofuranosidase (SaAF) and similar proteins; Alpha-L-arabinofuranosidase (EC 3.2.1.55), also called non-reducing end alpha-L-arabinofuranosidase, or arabinosidase, catalyzes the hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides. It acts on alpha-L-arabinofuranosides, alpha-L-arabinans containing (1,3)- and/or (1,5)-linkages, arabinoxylans and arabinogalactans. Members of this subfamily contain a ricin B-type lectin domain that adopts 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: 467335 [Multi-domain]  Cd Length: 139  Bit Score: 42.40  E-value: 9.86e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1488543073 416 GYFNLVNVNSGKYIDVNFSANEDGAQILQMYNTGHFSQQWLILDAGDGYYKIMNRNSGKL-LDVSSRSTENGASGIQ 491
Cdd:cd23457     3 GSVAIVSAQSGKVLSAEGCSTATGTNVEQQSWTGSACQKWQFTPTDNGFYQLRPASNASLcLAVEGGSLAAGANLVL 79
beta-trefoil_Ricin_AH cd23415
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ...
 416-505 1.66e-04

ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar proteins; Actinohivin is an actinomycete lectin with a potent specific anti-human immunodeficiency virus (anti-HIV) activity. It inhibits viral entry to cells by binding the high-mannose type sugar chains of gp120. Actinohivin contains 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 contains a sugar-binding pocket.


Pssm-ID: 467294 [Multi-domain]  Cd Length: 120  Bit Score: 41.26  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 416 GYFNLVNVNSGKYIDVNFSANedgaqilqMYnTGHFS----QQWLILDAGDGYYKIMNRNSGKLLDVssrsteNGASGIQ 491
Cdd:cd23415     1 GTVRLRNVATGRCLDSNAGGN--------VY-TGPCNggpyQRWTWSGVGDGTVTLRNAATGRCLDS------NGNGGVY 65

                          90
                  ....*....|....*
gi 1488543073 492 WHD-NGGLNQLWKIT 505
Cdd:cd23415    66 TLPcNGGSYQRWRVT 80
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
 420-507 2.81e-04

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: 40.78  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 420 LVNVNSGKYIDVNFSANEDGaQILQMYN-TGHFSQQWLIldAGDGYYkimnRNSGKLLDVSSRSTENGaSGIQWHD-NGG 497
Cdd:cd23451     5 VRLANAGKCLDVPGSSTADG-NPVQIYTcNGTAAQKWTL--GTDGTL----RVLGKCLDVSGGGTANG-TLVQLWDcNGT 76

                          90
                  ....*....|
gi 1488543073 498 LNQLWKITAN 507
Cdd:cd23451    77 GAQKWVPRAD 86
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
 378-503 3.09e-04

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: 40.78  E-value: 3.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 378 SGKSLNVVGGSHEDSALLEQYSDGNWDSQRFYFNAMGNgyfnlvNVNSGKYIDVNFSANEDGAQIlQMYN-TGHFSQQWL 456
Cdd:cd23451    10 AGKCLDVPGSSTADGNPVQIYTCNGTAAQKWTLGTDGT------LRVLGKCLDVSGGGTANGTLV-QLWDcNGTGAQKWV 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1488543073 457 ILDAGdgyyKIMNRNSGKLLDVSSRSTENGASgIQWHD-NGGLNQLWK 503
Cdd:cd23451    83 PRADG----TLYNPQSGKCLDAPGGSTTDGTQ-LQLYTcNGTAAQQWT 125
beta-trefoil_Ricin_GllA-1 cd23454
GllA-1 domain, beta-trefoil fold, found in Mucor circinelloides Gellins and similar proteins; ...
 416-507 4.84e-04

GllA-1 domain, beta-trefoil fold, found in Mucor circinelloides Gellins and similar proteins; Gellin proteins act as central effectors of wound-induced protoplasmic gelation. They possess ten related N-terminal beta-trefoil domains (Gll-1 to Gll-10) that contribute to distinct gelation-related activities. The beta-trefoil domains show low sequence similarity to members of the functionally diverse ricin B lectin domain family. They 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. Each subdomain bears a potential sugar binding site. Gellin from M. circinelloides has been called GellinA (also known as GllA). The model corresponds to GllA-1 domain, which is a remote family member of the ricin B-type lectin domain.


Pssm-ID: 467332 [Multi-domain]  Cd Length: 136  Bit Score: 40.38  E-value: 4.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 416 GYFNLVNVNSGKYIDVNFSANEDGAQIL--QMYNTGHFSQQWLildAGDGYykIMNRNSGKLLDVSSRSTENGASGIQWH 493
Cdd:cd23454     1 GWFFIKSSSNGLVLDVEHGSLKSGAKVVlaPLKTKDYESQLWR---YDDGY--LVNKASGLVLDIQGGVVKSGTRLVQSP 75

                          90
                  ....*....|....*..
gi 1488543073 494 ---DNGGLNQLWKITAN 507
Cdd:cd23454    76 kkpSKDANNQRWGLTAD 92
beta-trefoil_Ricin_SCDase cd23456
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ...
 371-502 6.40e-04

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: 39.65  E-value: 6.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 371 YKIANRHSGKSLNVVGGShEDSALLEQYSDGNWDSQRFYFNAmgNGYFNLvNVNSGKYIDVNfSANEDGAQIlQMYN-TG 449
Cdd:cd23456     3 FQLKSQASGLCLDVSGGA-TNGANVVVYDCNNSNSQKWYYDA--TGRLHS-KANPGKCLDAG-GENSNGANV-VLWAcND 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1488543073 450 HFSQQWlilDAGDGYykIMNR-NSGKLLDVSsrsTENGASGIQWHDNGGLNQLW 502
Cdd:cd23456    77 SANQRW---DFDGNF--IRSRnNTNLALDAY---GSQGSNVGLWQFHGGANQQW 122
beta-trefoil_Ricin_GllA-1 cd23454
GllA-1 domain, beta-trefoil fold, found in Mucor circinelloides Gellins and similar proteins; ...
 373-504 7.16e-04

GllA-1 domain, beta-trefoil fold, found in Mucor circinelloides Gellins and similar proteins; Gellin proteins act as central effectors of wound-induced protoplasmic gelation. They possess ten related N-terminal beta-trefoil domains (Gll-1 to Gll-10) that contribute to distinct gelation-related activities. The beta-trefoil domains show low sequence similarity to members of the functionally diverse ricin B lectin domain family. They 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. Each subdomain bears a potential sugar binding site. Gellin from M. circinelloides has been called GellinA (also known as GllA). The model corresponds to GllA-1 domain, which is a remote family member of the ricin B-type lectin domain.


Pssm-ID: 467332 [Multi-domain]  Cd Length: 136  Bit Score: 39.99  E-value: 7.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 373 IANRHSGKSLNVVGGSHEDSA--LLEQYSDGNWDSQRFYFNamgNGYfnLVNVNSGKYIDVNFSANEDGAQILQMYNTGH 450
Cdd:cd23454     5 IKSSSNGLVLDVEHGSLKSGAkvVLAPLKTKDYESQLWRYD---DGY--LVNKASGLVLDIQGGVVKSGTRLVQSPKKPS 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1488543073 451 ---FSQQWlILDAgDGYykIMNRNSGKL-LDVSSRSTENGAS-GIQWHDNG--GLNQLWKI 504
Cdd:cd23454    80 kdaNNQRW-GLTA-DGY--IYLLSNPSLvLGIKGNETREGARvILQERKLQkdALNQRWTF 136
beta-trefoil_Ricin_RPI cd23452
ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine ...
 425-506 1.06e-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: 39.04  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 425 SGKYIDVNFSANEDGAQiLQMYN-TGHFSQQWLIldAGDGYYkimnRNSGKLLDVSSRSTENGASGIQWHDNGGLNQLWK 503
Cdd:cd23452    10 ANKCIDVPNSSTTDGAP-LQLWDcNGTNAQKWTF--ASDGTL----RALGKCLDVAWGGTDNGTAVQLWTCSGNPAQQFV 82


                  ...
gi 1488543073 504 ITA 506
Cdd:cd23452    83 LSG 85
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 420-507 1.06e-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: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 420 LVNVNSGKYIDVNFSANEDGAQiLQMYN-TGHFSQQWLILDAGDgyykiMNRNSGKLLDVSSRSTENGASGIQWHDNGGL 498
Cdd:cd23418     8 IRGYGSGRCLDVPGGSTTNGTR-LILWDcHGGANQQFTFTSAGE-----LRVGGDKCLDAAGGGTTNGTPVVIWPCNGGA 81


                  ....*....
gi 1488543073 499 NQLWKITAN 507
Cdd:cd23418    82 NQKWRFNSD 90
beta-trefoil_Ricin_EndoBetaGal-like cd23432
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium perfringens GlcNac-alpha-1, ...
 416-504 1.64e-03

ricin B-type lectin domain, beta-trefoil fold, found in Clostridium perfringens GlcNac-alpha-1,4-Gal-releasing endo-beta-galactosidase (Endo-beta-Gal(GnGa)) and similar proteins; Endo-beta-Gal(GnGa) can release disaccharide GlcNAc-alpha-1,4Gal from O-glycans expressed in the gastric gland mucous cell-type mucin. It 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 may harbor a sugar-binding pocket.


Pssm-ID: 467310  Cd Length: 127  Bit Score: 38.48  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 416 GYFNLVNVNSGKYIdvnfsaNEDGAQILqmYNT---GHFSQQWLILDAGDGYYKIMNRNSGKLLdvssrSTENGASGIQW 492
Cdd:cd23432     1 GYVRIKNRWTGQYL------YEENGKVK--YGTppeDDTSAQWIIEDVGDGYVRIKNRATGHYL-----HIENNTGYLES 67

                          90
                  ....*....|....
gi 1488543073 493 --HDNGGLNQLWKI 504
Cdd:cd23432    68 gpIPPGWWSAQWTL 81
BglC COG2730
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];
55-324 1.83e-03

Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];


Pssm-ID: 442036 [Multi-domain]  Cd Length: 295  Bit Score: 40.41  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073  55 AGTQRDVLQILRDHGINAVRL----RIFVNPDPSALWHKDNttwtmLGYTDktRVVDAAQRAkamGMRVMVDFHysdvfA 130
Cdd:COG2730    25 GNITEEDIDAIADWGFNTVRLpvswERLQDPDNPYTLDEAY-----LERVD--EVVDWAKAR---GLYVILDLH-----H 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 131 DPGHQIkpaaWKNynlsqlttavyNHTHEVMTALlsagvtpeWVQVGNEM--NPGILL------PEGSTSrfANLTQLLN 202
Cdd:COG2730    90 APGYQG----WYD-----------AATQERFIAF--------WRQLAERYkdYPNVLGfellnePHGATW--ADWNALAQ 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 203 AGYDAVKAVSPSSKVIshLAHGNNNSNARWFFDNFLTTHGgktdvIGFS--FYPYWE--GKNYWELTGSLASNLNDM--- 275
Cdd:COG2730   145 RAIDAIRATNPDRLII--VEGNNWGGAHNLRALDPLDDDN-----LVYSvhFYGPFVftHQGAWFAGPTYPANLEARldn 217

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1488543073 276 ----ASRYGKEVMVVEVGGLETNPTDSYWT-IKDTINLVKAvpgnKGIGVFYWE 324
Cdd:COG2730   218 wgdwAADNGVPVFVGEFGAYNDDPDASRLAwLRDLLDYLEE----NGIGWTYWS 267
beta-trefoil_Ricin_AH cd23415
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ...
 404-503 1.93e-03

ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar proteins; Actinohivin is an actinomycete lectin with a potent specific anti-human immunodeficiency virus (anti-HIV) activity. It inhibits viral entry to cells by binding the high-mannose type sugar chains of gp120. Actinohivin contains 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 contains a sugar-binding pocket.


Pssm-ID: 467294 [Multi-domain]  Cd Length: 120  Bit Score: 38.18  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 404 DSQRFYFNAMGNGYFNLVNVNSGKYIDVNfsanedGAQILQMYN-TGHFSQQWLILDAGDGYYKIMNRNSGKLLDvssrS 482
Cdd:cd23415    31 PYQRWTWSGVGDGTVTLRNAATGRCLDSN------GNGGVYTLPcNGGSYQRWRVTSTSGGGVTLRNVATGRCLD----S 100

                          90       100
                  ....*....|....*....|.
gi 1488543073 483 TENGASGIQwHDNGGLNQLWK 503
Cdd:cd23415   101 NGSGGVYTR-PCNGGSYQRWR 120
lectin_2 NF035930
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
 382-502 2.45e-03

lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor.


Pssm-ID: 468267 [Multi-domain]  Cd Length: 238  Bit Score: 39.77  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 382 LNVVGGSHEDSALLEQYSDGNwDSQRFYFNAMGNgyfnlVNVnSGKYIDVNFSANEDGAQILQMYNTGHFSQQWlilDAG 461
Cdd:NF035930  130 LDVSGGLRPGNGLIVYNCNGG-ENQRFTWGRGGE-----LRV-GDLCLDVADGNTRDGARVIAWSCSGGPNQRW---RWR 199

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1488543073 462 DGyyKIMNRNSGKLLDVSSRSTENGASGIQWHDNGGLNQLW 502
Cdd:NF035930  200 GG--QIRSRLSGKCLDIEGGRARPGQPVIVWSCNGGPNQRW 238
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
 376-455 3.67e-03

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: 37.70  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 376 RHSGKSLNVVGGSHEDSALLEQYSDGNWDSQRFYFNAMGNgyfnLVNVNSGKYIDVNFSANEDGAQiLQMYN-TGHFSQQ 454
Cdd:cd23451    49 RVLGKCLDVSGGGTANGTLVQLWDCNGTGAQKWVPRADGT----LYNPQSGKCLDAPGGSTTDGTQ-LQLYTcNGTAAQQ 123


                  .
gi 1488543073 455 W 455
Cdd:cd23451   124 W 124
beta-trefoil_Ricin_Cry35Ab1 cd23448
ricin B-type lectin domain, beta-trefoil fold, found in Bacillus thuringiensis Cry35Ab1 and ...
 415-507 4.74e-03

ricin B-type lectin domain, beta-trefoil fold, found in Bacillus thuringiensis Cry35Ab1 and similar proteins; Cry35Ab1 is an insecticidal protein belonging to the toxin_10 family (Pfam05431) that includes other insecticidal proteins such as the binary toxin BinA/BinB. It acts together with Cry34Ab1 to control corn rootworms. Cry35Ab1 contains 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 bears a potential sugar binding site.


Pssm-ID: 467326  Cd Length: 133  Bit Score: 37.32  E-value: 4.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 415 NGYFNLVNVNSGKYIDVNFSANeDGAQILQMYNTGHFSQQWLILDAGDGYYKIMNRNSGKLLDVSSRSTENgASGIQWHD 494
Cdd:cd23448     1 NKVYNIQNVSSGLYAYSSGSLD-SGGNITQSALEQTGNCRWKFVLLDDGQYKIVSAASNMCLAAASSGEGQ-QNVTTASD 78

                          90
                  ....*....|...
gi 1488543073 495 NGGLNQLWKITAN 507
Cdd:cd23448    79 SDAANQKWNIIKQ 91
beta-trefoil_Ricin_Cry35Ab1 cd23448
ricin B-type lectin domain, beta-trefoil fold, found in Bacillus thuringiensis Cry35Ab1 and ...
 371-502 5.02e-03

ricin B-type lectin domain, beta-trefoil fold, found in Bacillus thuringiensis Cry35Ab1 and similar proteins; Cry35Ab1 is an insecticidal protein belonging to the toxin_10 family (Pfam05431) that includes other insecticidal proteins such as the binary toxin BinA/BinB. It acts together with Cry34Ab1 to control corn rootworms. Cry35Ab1 contains 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 bears a potential sugar binding site.


Pssm-ID: 467326  Cd Length: 133  Bit Score: 37.32  E-value: 5.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488543073 371 YKIANrHSGKSLNVVGGSHEDSALLEQYSDGNWDSQRFYFNAMGNGYFNLVNVNSGKYIDVNfSANEDGAQILQMYNTGH 450
Cdd:cd23448     4 YNIQN-VSSGLYAYSSGSLDSGGNITQSALEQTGNCRWKFVLLDDGQYKIVSAASNMCLAAA-SSGEGQQNVTTASDSDA 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1488543073 451 FSQQWLILDAGDgYYKIMNRNSGKLLDVSSRSTeNGASGIQWHDNGGLNQLW 502
Cdd:cd23448    82 ANQKWNIIKQGS-YYVFRSDSSGRVLTAASGNS-SGSVLIQQANSSGNNQYW 131
 
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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