NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1830131197|ref|WP_168022250|]
View 

RICIN domain-containing protein, partial [Nonomuraea composti]

Protein Classification

RICIN domain-containing protein( domain architecture ID 10069754)

RICIN domain-containing protein may have carbohydrate-binding function

CATH:  2.80.10.50
Gene Ontology:  GO:0030246
PubMed:  8844840|35536958
SCOP:  3000678

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
beta-trefoil_Ricin-like super family cl49609
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
6-80 1.18e-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.


The actual alignment was detected with superfamily member cd23418:

Pssm-ID: 483949 [Multi-domain]  Cd Length: 130  Bit Score: 91.64  E-value: 1.18e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1830131197   6 SQVQIWDCNGQANQQWASTSAGELKTSDGRCLDVNAAGTADGTAVITWTCNGQNNQKWRLNSDGSITAVGANKCL 80
Cdd:cd23418    28 TRLILWDCHGGANQQFTFTSAGELRVGGDKCLDAAGGGTTNGTPVVIWPCNGGANQKWRFNSDGTIRNVNSGLCL 102
 
Name Accession Description Interval E-value
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
6-80 1.18e-25

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: 91.64  E-value: 1.18e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1830131197   6 SQVQIWDCNGQANQQWASTSAGELKTSDGRCLDVNAAGTADGTAVITWTCNGQNNQKWRLNSDGSITAVGANKCL 80
Cdd:cd23418    28 TRLILWDCHGGANQQFTFTSAGELRVGGDKCLDAAGGGTTNGTPVVIWPCNGGANQKWRFNSDGTIRNVNSGLCL 102
lectin_2 NF035930
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
9-80 2.32e-13

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: 62.11  E-value: 2.32e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1830131197   9 QIWDCNGQANQQWASTSAGELKTSDgRCLDVNAAGTADGTAVITWTCNGQNNQKWRlNSDGSITAVGANKCL 80
Cdd:NF035930  143 IVYNCNGGENQRFTWGRGGELRVGD-LCLDVADGNTRDGARVIAWSCSGGPNQRWR-WRGGQIRSRLSGKCL 212
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
6-80 2.66e-13

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 59.85  E-value: 2.66e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1830131197   6 SQVQIWDCNGQAN-QQWASTSAGELKT-SDGRCLDVnaAGTADGTAVITWTCN-GQNNQKWRLNSDGS-ITAVGANKCL 80
Cdd:pfam00652  24 GPVGLYPCHGSNGnQLWTLTGDGTIRSvASDLCLDV--GSTADGAKVVLWPCHpGNGNQRWRYDEDGTqIRNPQSGKCL 100
lectin_1 NF035929
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
8-65 2.39e-11

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: 468266 [Multi-domain]  Cd Length: 837  Bit Score: 57.29  E-value: 2.39e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1830131197   8 VQIWDCNGQANQQWASTSAGEL-KTSDGRCLDVNAAGTADGTAVITWTCNGQNNQKWRL 65
Cdd:NF035929  778 VQLWTCNGTGAQQWKPGAAGSLvNPESGLCLDDPNSSTTEGTQLQIYTCNGTAAQNWTL 836
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
6-80 4.41e-11

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 54.05  E-value: 4.41e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1830131197    6 SQVQIWDCNGQA-NQQWASTSAGELKT-SDGRCLDVNAAGTadgTAVITWTCNGQN-NQKWRLNSDGSITAVGANKCL 80
Cdd:smart00458  17 NPVGLFDCHGTGgNQLWKLTSDGAIRIkDTDLCLTANGNTG---STVTLYSCDGTNdNQYWEVNKDGTIRNPDSGKCL 91
lectin_2 NF035930
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
6-63 8.13e-11

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: 55.18  E-value: 8.13e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1830131197   6 SQVQIWDCNGQANQQWaSTSAGELKTSD-GRCLDVNAAGTADGTAVITWTCNGQNNQKW 63
Cdd:NF035930  181 ARVIAWSCSGGPNQRW-RWRGGQIRSRLsGKCLDIEGGRARPGQPVIVWSCNGGPNQRW 238
 
Name Accession Description Interval E-value
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
6-80 1.18e-25

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: 91.64  E-value: 1.18e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1830131197   6 SQVQIWDCNGQANQQWASTSAGELKTSDGRCLDVNAAGTADGTAVITWTCNGQNNQKWRLNSDGSITAVGANKCL 80
Cdd:cd23418    28 TRLILWDCHGGANQQFTFTSAGELRVGGDKCLDAAGGGTTNGTPVVIWPCNGGANQKWRFNSDGTIRNVNSGLCL 102
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
6-80 1.20e-18

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: 73.52  E-value: 1.20e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1830131197   6 SQVQIWDCNGQANQQWASTSAGELKTSdGRCLDVNAAGTADGTAVITWTCNGQNNQKWRLNSDGSITAVGANKCL 80
Cdd:cd23451    25 NPVQIYTCNGTAAQKWTLGTDGTLRVL-GKCLDVSGGGTANGTLVQLWDCNGTGAQKWVPRADGTLYNPQSGKCL 98
beta-trefoil_Ricin_RPI cd23452
ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine ...
6-80 1.86e-17

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: 70.62  E-value: 1.86e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1830131197   6 SQVQIWDCNGQANQQWASTSAGELKtSDGRCLDVNAAGTADGTAVITWTCNGQNNQKWRLNSDGSITAVGANKCL 80
Cdd:cd23452    25 APLQLWDCNGTNAQKWTFASDGTLR-ALGKCLDVAWGGTDNGTAVQLWTCSGNPAQQFVLSGAGDLVNPQANKCV 98
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
6-80 1.27e-16

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: 68.55  E-value: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830131197   6 SQVQIWDCNGQANQQW----ASTSAGELK-TSDGRCLDVNAAGTADGTAVITWTCNGQNNQKWRL----NSDGSITAVGA 76
Cdd:cd00161    25 APVQQWTCNGGANQQWtltpVGDGYYTIRnVASGKCLDVAGGSTANGANVQQWTCNGGDNQQWRLepvgDGYYRIVNKHS 104

                  ....
gi 1830131197  77 NKCL 80
Cdd:cd00161   105 GKCL 108
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
8-64 1.97e-16

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: 68.15  E-value: 1.97e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1830131197   8 VQIWDCNGQANQQWASTSAGELKTS-DGRCLDVNAAGTADGTAVITWTCNGQNNQKWR 64
Cdd:cd23418    72 VVIWPCNGGANQKWRFNSDGTIRNVnSGLCLDVAGGGTANGTRLILWSCNGGSNQRWR 129
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
6-64 3.29e-14

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: 62.35  E-value: 3.29e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830131197   6 SQVQIWDCNGQANQQWASTSAGELK-TSDGRCLDVNAAGTADGTAVITWTCNGQNNQKWR 64
Cdd:cd23451    66 TLVQLWDCNGTGAQKWVPRADGTLYnPQSGKCLDAPGGSTTDGTQLQLYTCNGTAAQQWT 125
lectin_2 NF035930
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
9-80 2.32e-13

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: 62.11  E-value: 2.32e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1830131197   9 QIWDCNGQANQQWASTSAGELKTSDgRCLDVNAAGTADGTAVITWTCNGQNNQKWRlNSDGSITAVGANKCL 80
Cdd:NF035930  143 IVYNCNGGENQRFTWGRGGELRVGD-LCLDVADGNTRDGARVIAWSCSGGPNQRWR-WRGGQIRSRLSGKCL 212
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
6-80 2.66e-13

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 59.85  E-value: 2.66e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1830131197   6 SQVQIWDCNGQAN-QQWASTSAGELKT-SDGRCLDVnaAGTADGTAVITWTCN-GQNNQKWRLNSDGS-ITAVGANKCL 80
Cdd:pfam00652  24 GPVGLYPCHGSNGnQLWTLTGDGTIRSvASDLCLDV--GSTADGAKVVLWPCHpGNGNQRWRYDEDGTqIRNPQSGKCL 100
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
6-63 6.10e-13

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: 59.31  E-value: 6.10e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1830131197   6 SQVQIWDCNGQANQQW----ASTSAGELKT-SDGRCLDVNAAGTADGTAVITWTCNGQNNQKW 63
Cdd:cd00161    72 ANVQQWTCNGGDNQQWrlepVGDGYYRIVNkHSGKCLDVSGGSTANGANVQQWTCNGGANQQW 134
beta-trefoil_Ricin_AgaB34-like cd23458
ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 ...
6-80 9.06e-12

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: 56.18  E-value: 9.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830131197   6 SQVQIWDCNGQANQQWASTSAG----ELKTS-DGRCLDVNAAGTADGTAVITWTCNGQNNQKWRLNSDG----SITAVGA 76
Cdd:cd23458    25 ANIQQWDCGSGSNQQWTLVEIDngyyRIKAShSGKCLDVAGGSTANGANIQQWDCVGGANQQWKLQDLGngyfELKARHS 104

                  ....
gi 1830131197  77 NKCL 80
Cdd:cd23458   105 GKCL 108
lectin_1 NF035929
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
8-65 2.39e-11

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: 468266 [Multi-domain]  Cd Length: 837  Bit Score: 57.29  E-value: 2.39e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1830131197   8 VQIWDCNGQANQQWASTSAGEL-KTSDGRCLDVNAAGTADGTAVITWTCNGQNNQKWRL 65
Cdd:NF035929  778 VQLWTCNGTGAQQWKPGAAGSLvNPESGLCLDDPNSSTTEGTQLQIYTCNGTAAQNWTL 836
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
27-80 2.43e-11

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: 55.03  E-value: 2.43e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1830131197  27 GELKTSD-GRCLDVNAAGTADGTAVITWTCNGQNNQKWRLNSDGSITAVGanKCL 80
Cdd:cd23451     3 GPVRLANaGKCLDVPGSSTADGNPVQIYTCNGTAAQKWTLGTDGTLRVLG--KCL 55
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
6-80 4.41e-11

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 54.05  E-value: 4.41e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1830131197    6 SQVQIWDCNGQA-NQQWASTSAGELKT-SDGRCLDVNAAGTadgTAVITWTCNGQN-NQKWRLNSDGSITAVGANKCL 80
Cdd:smart00458  17 NPVGLFDCHGTGgNQLWKLTSDGAIRIkDTDLCLTANGNTG---STVTLYSCDGTNdNQYWEVNKDGTIRNPDSGKCL 91
lectin_2 NF035930
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
6-63 8.13e-11

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: 55.18  E-value: 8.13e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1830131197   6 SQVQIWDCNGQANQQWaSTSAGELKTSD-GRCLDVNAAGTADGTAVITWTCNGQNNQKW 63
Cdd:NF035930  181 ARVIAWSCSGGPNQRW-RWRGGQIRSRLsGKCLDIEGGRARPGQPVIVWSCNGGPNQRW 238
beta-trefoil_Ricin_1,3Gal43A cd23446
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and ...
7-70 8.41e-11

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: 53.93  E-value: 8.41e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1830131197   7 QVQIWDCNGQANQQWASTSAGE-----LKTSDGRCLDVNAAGTADGTAVITWTCNGQNNQKWRLNSDGS 70
Cdd:cd23446    26 QIEQWTDNGGTSQQWYFTDVGGgyykiVNRNSGKALDVNGASTADGAAIIQWTSNGGDNQQWQIVDTGD 94
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
33-80 1.34e-10

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: 53.12  E-value: 1.34e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1830131197  33 DGRCLDVNAAGTADGTAVITWTCNGQNNQKWRLNSDGSITaVGANKCL 80
Cdd:cd23418    13 SGRCLDVPGGSTTNGTRLILWDCHGGANQQFTFTSAGELR-VGGDKCL 59
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
34-80 1.72e-10

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: 52.76  E-value: 1.72e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1830131197  34 GRCLDVNAAGTADGTAVITWTCNGQNNQKWRL----NSDGSITAVGANKCL 80
Cdd:cd00161    11 GKCLDVAGGSTANGAPVQQWTCNGGANQQWTLtpvgDGYYTIRNVASGKCL 61
beta-trefoil_Ricin_AgaB34-like cd23458
ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 ...
8-64 1.75e-10

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: 52.71  E-value: 1.75e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1830131197   8 VQIWDCNGQANQQWASTSAG----ELKTS-DGRCLDVNAAGTADGTAVITWTCNGQNNQKWR 64
Cdd:cd23458    74 IQQWDCVGGANQQWKLQDLGngyfELKARhSGKCLDVAGGSTANGASIQQWTCNGNDNQRFK 135
beta-trefoil_Ricin_RPI cd23452
ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine ...
6-64 3.96e-09

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: 49.05  E-value: 3.96e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830131197   6 SQVQIWDCNGQANQQWASTSAGEL-KTSDGRCLDVNAAGTADGTAVITWTCNGQNNQKWR 64
Cdd:cd23452    66 TAVQLWTCSGNPAQQFVLSGAGDLvNPQANKCVDVSGGNSGNGTRLQLWECSGNANQKWR 125
RicinB_lectin_2 pfam14200
Ricin-type beta-trefoil lectin domain-like;
17-80 7.43e-09

Ricin-type beta-trefoil lectin domain-like;


Pssm-ID: 464102 [Multi-domain]  Cd Length: 89  Bit Score: 47.76  E-value: 7.43e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1830131197 17 ANQQW---ASTSAGELK---TSDGRCLDVNAAGTADGTAVITWTCNGQNNQKWRLNSDGS----ITAVGANKCL 80
Cdd:pfam14200  1 ANQQWrfgGTVGDGYYTivnVASGKYLDVAGGSTANGANVQQWTDNGNDNQQWRIVDAGDgyyrIVNKASGKVL 74
beta-trefoil_Ricin_1,3Gal43A cd23446
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and ...
11-65 2.66e-08

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: 47.38  E-value: 2.66e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830131197  11 WDCNGQANQQWASTSAGE-----LKTSDGRCLDVNAAGTADGTAVITWTCNGQNNQKWRL 65
Cdd:cd23446    77 WTSNGGDNQQWQIVDTGDgyykiVNRNSGKLLDVNGWSTADGADIIQWSDNGGTNQQWQL 136
beta-trefoil_Ricin_AgaB34-like cd23458
ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 ...
34-80 3.22e-08

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: 46.93  E-value: 3.22e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1830131197  34 GRCLDVNAAGTADGTAVITWTCNGQNNQKWRLNSDG----SITAVGANKCL 80
Cdd:cd23458    11 GKCIDVAGGSTANGANIQQWDCGSGSNQQWTLVEIDngyyRIKASHSGKCL 61
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
33-80 6.53e-08

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 45.99  E-value: 6.53e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1830131197  33 DGRCLDVNAaGTADGTAVITWTCNG-QNNQKWRLNSDGSITAVGANKCL 80
Cdd:pfam00652  10 SGKCLDVPG-GSSAGGPVGLYPCHGsNGNQLWTLTGDGTIRSVASDLCL 57
beta-trefoil_Ricin_vlAKAP cd23463
ricin B-type lectin domain, beta-trefoil fold, found in very large A-kinase anchor protein ...
3-72 8.10e-08

ricin B-type lectin domain, beta-trefoil fold, found in very large A-kinase anchor protein (vlAKAP) and similar proteins; vlAKAP, also called beta/gamma crystallin domain-containing protein 3 (CRYBG3), is an anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA). It binds to the dimeric RII-alpha regulatory subunit of PKA (PRKAR2A/PRKAR2B). vlAKAP belongs to the beta/gamma-crystallin family. It contains 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 may harbor a sugar-binding pocket.


Pssm-ID: 467341  Cd Length: 136  Bit Score: 45.89  E-value: 8.10e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1830131197   3 PSTSQVQIWDCNGQANQQWASTSaGELKTSDGR-CLDVNAAGTADGTAVITWTCNGQNNQKWRLNSDGSIT 72
Cdd:cd23463    26 PRATSVCVSQYNGKDTQIWYYCR-GLLKSKANDaCLDVIGGKDNPGSKVALWTEHGKTHQKWRINEDGTIS 95
beta-trefoil_Ricin_RIPs_II_rpt1 cd23443
first ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating ...
33-80 2.04e-07

first 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 first ricin B-type lectin domain. Members of this subfamily 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: 467321 [Multi-domain]  Cd Length: 123  Bit Score: 44.59  E-value: 2.04e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1830131197  33 DGRCLDVNAAGTADGTAVITWTC-NGQNNQKWRLNSDGSITAVGanKCL 80
Cdd:cd23443     9 DGLCVDVKDGYYSDGNPVILWPCkSQDANQLWTFKRDGTIRSNG--KCL 55
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
6-63 5.25e-07

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 43.67  E-value: 5.25e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1830131197   6 SQVQIWDCN-GQANQQWASTSAGE--LKTSDGRCLDVNAAGTADGtAVITWTC-NGQNNQKW 63
Cdd:pfam00652  66 AKVVLWPCHpGNGNQRWRYDEDGTqiRNPQSGKCLDVSGAGTSNG-KVILWTCdSGNPNQQW 126
beta-trefoil_Ricin_BGSL_rpt1 cd23481
first ricin B-type lectin domain, beta-trefoil fold, found in bitter gourd (Momordica ...
33-80 6.83e-07

first ricin B-type lectin domain, beta-trefoil fold, found in bitter gourd (Momordica charantia) seed lectin (BGSL) and similar proteins; 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. BGSL is a non-toxic four-chain type II RIP resulting from covalent association through a disulfide bridge between two identical copies of a two-chain unit. The two-chain unit consists of a catalytic A-chain and a lectin B-chain. The catalytic A-chain cannot firmly bind adenine due to the substitution of an aromatic residue involved in ensuring the proper orientation of the base in toxic RIPs, by a glycyl residue. BGSL is a galactose-specific lectin containing two ricin B-type lectin domains in its B-chain. 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. This model corresponds to the first ricin B-type lectin domain. In BGSL, sugar does not bind at the 2gamma site. Its 1alpha site binds sugar, which is similar to that in snake gourd (Trichosanthes anguina) seed lectin (SGSL).


Pssm-ID: 467359  Cd Length: 132  Bit Score: 43.61  E-value: 6.83e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1830131197  33 DGRCLDVNAAGTADGTAVITWTCNGQNNQKWRLNSDGSITAVGanKCL 80
Cdd:cd23481    16 DGLCVDVYGALTADGSRVILYPCGQQQNQQWTFYPDNTIRSLG--KCL 61
beta-trefoil_Ricin_SCDase cd23456
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ...
6-68 2.05e-06

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: 41.96  E-value: 2.05e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1830131197   6 SQVQIWDCNGQANQQWASTSAGELKTS--DGRCLDVNAaGTADGTAVITWTCNGQNNQKWRLNSD 68
Cdd:cd23456    24 ANVVVYDCNNSNSQKWYYDATGRLHSKanPGKCLDAGG-ENSNGANVVLWACNDSANQRWDFDGN 87
beta-trefoil_Ricin_SGSL_rpt1 cd23482
first ricin B-type lectin domain, beta-trefoil fold, found in snake gourd (Trichosanthes ...
18-80 2.22e-06

first ricin B-type lectin domain, beta-trefoil fold, found in snake gourd (Trichosanthes anguina) seed lectin (SGSL) and similar proteins; 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. SGSL is a non-toxic three-chain type II RIP consisting of Aalpha, Abeta and B chains with Abeta and B being disulfide-linked. The Aalpha and Abeta chains constitute the rRNA glycosidase domain and the B chain contains two ricin B-type carbohydrate-binding lectin domains. SGSL may have no glycosidase activity due to small changes in both the nucleotide binding and carbohydrate binding capabilities. It binds galactose and derivatives with a preference for the beta-anomeric forms. It also binds prophyrins. SGSL has hemagglutinating activity towards rabbit and human erythrocytes. 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. This model corresponds to the first ricin B-type lectin domain.


Pssm-ID: 467360  Cd Length: 135  Bit Score: 42.43  E-value: 2.22e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1830131197  18 NQQWASTSAGELKTSDGRCLDVNAAGTADGTAVITWTCNGQNNQKWRLNSDGSITAVGanKCL 80
Cdd:cd23482     1 NECLVETRTTRISGRDALCVDVAGALTSDGSRLILYPCGQQVNQKWTFHSDGTVRSLG--KCL 61
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
3-65 3.01e-06

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 41.73  E-value: 3.01e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1830131197    3 PSTSQVQIWDCNGQA-NQQWASTSAGELKTSD-GRCLDVNAAGTadGTAVITWTCNGQNNQKWRL 65
Cdd:smart00458  55 NTGSTVTLYSCDGTNdNQYWEVNKDGTIRNPDsGKCLDVKDGNT--GTKVILWTCSGNPNQKWIF 117
beta-trefoil_Ricin_HA17-like cd23445
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium botulinum hemagglutinating ...
33-65 3.98e-06

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: 41.54  E-value: 3.98e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1830131197  33 DGRCLDVNAAGTADGTAVITWTCNGQNNQKWRL 65
Cdd:cd23445   101 PNLVLDVEGSNTANGTNIIVYPRNGSNNQKFKL 133
beta-trefoil_Ricin_GALNT1-like cd23433
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
13-80 6.18e-06

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: 40.76  E-value: 6.18e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1830131197  13 CNGQ-ANQQWASTSAGELKtSDGRCLDVnaagTADGTAVITWTCNGQN-NQKWRLNSD-GSITAVGANKCL 80
Cdd:cd23433    34 CHGQgGNQVFSYTAKGEIR-SDDLCLDA----SRKGGPVKLEKCHGMGgNQEWEYDKEtKQIRHVNSGLCL 99
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
6-80 8.14e-06

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: 40.38  E-value: 8.14e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1830131197   6 SQVQIWDCNGQ-ANQQWASTSAGELKTSDgRCLDVnaAGTADGTAVITWTCNGQN-NQKWRLNSDGS-ITAVGANKCL 80
Cdd:cd23434    21 GTVGLYPCHGTgGNQEWSFTKDGQIKHDD-LCLTV--VDRAPGSLVTLQPCREDDsNQKWEQIENNSkLRHVGSNLCL 95
beta-trefoil_Ricin_ebulin-like_rpt1 cd23483
first ricin B-type lectin domain, beta-trefoil fold, found in Sambucus ebulus ebulin I and ...
33-80 8.84e-06

first ricin B-type lectin domain, beta-trefoil fold, found in Sambucus ebulus ebulin I and similar proteins; The family includes Sambucus ebulus ebulin I and Sambucus nigra nigrin b (also known as agglutinin V or SNAV), SNAI (also known as agglutinin I), SNAI' and SNAIf. Ebulin l is a type II ribosome-inactivating protein (RIP) isolated from the leaves of Sambucus ebulus. It is a disulfide-linked heterodimer composed of a toxic A chain and a galactoside-specific lectin B chain. It is considered a nontoxic type II RIP due to a reduced cytotoxicity on whole cells and animals as compared with other toxic type II RIP like ricins. Ebulin l binds an A-chain substrate analogue, pteroic acid. It binds bind galactose and lactose in subdomain 1alpha in a similar manner to that of ricin. In contrast, it binds only the monosaccharide galactose, and not the disaccharide lactose in subdomain 2gamma. SNAV is a non-toxic GalNAc-specific type II RIP which strongly inhibits mammalian protein synthesis but does not affect plant nor bacterial protein synthesis. SNAI is a Neu5Ac(alpha2-6)Gal/GalNAc-specific agglutinin. It also acts as a type II RIP that strongly inhibits mammalian but not plant ribosomes. SNAI' is another NeuAc(alpha2,6)Gal/GalNAc binding type II RIP from elderberry (Sambucus nigra) bark. It is a minor bark protein which closely resembles the major Neu5Ac(alpha2,6)Gal/GalNAc binding type II RIP, SNAI, with respect to its carbohydrate-binding specificity and ribosome-inactivating activity but has a different molecular structure due to a single cysteine residue present in the B chain of SNAI but absent from SNAI'. SNAIf is a fruit-specific SNAI. It functions as a fetuin-binding fruit lectin. Like Ebulin l, SNAV, SNAI, SNAI' and SNAIf consist of a sugar-binding B chain linked via a disulfide bond to the catalytically active A chain. The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain. It may also be responsible for cell agglutination (lectin activity). The B chain 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. This model corresponds to the first ricin B-type lectin domain.


Pssm-ID: 467361 [Multi-domain]  Cd Length: 127  Bit Score: 40.57  E-value: 8.84e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1830131197  33 DGRCLDVNAAGTADGTAVITWTCNGQNNQKWRLNSDGSITAVGanKCL 80
Cdd:cd23483    10 DGLCVDVRNGYDTDGTPVQLWPCGTQRNQQWTFDTDGTIRSMG--KCM 55
beta-trefoil_Ricin_1,3Gal43A cd23446
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and ...
34-69 1.76e-05

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: 39.67  E-value: 1.76e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1830131197  34 GRCLDVNAAGTADGTAVITWTCNGQNNQKWRLNSDG 69
Cdd:cd23446    11 GKALDVLSGSTTDGAQIEQWTDNGGTSQQWYFTDVG 46
beta-trefoil_Ricin_SCDase_rpt2 cd23500
second ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ...
6-64 2.19e-05

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: 39.37  E-value: 2.19e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1830131197   6 SQVQIWDCNGQA-NQQWasTSAGEL---KTSDGRCLDVNaaGTADGTAVITWTCNGQNNQKWR 64
Cdd:cd23500    70 TQLQLADCDASNpAQQF--NYDGGVfrsRLNSNQVIDAS--GGSDGSELILYDYHGGSNQRWR 128
beta-trefoil_Ricin_AH cd23415
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ...
7-64 2.61e-05

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: 39.34  E-value: 2.61e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1830131197   7 QVQIWDCNGQANQQW----ASTSAGELK-TSDGRCLDVNAAGtadgtAVITWTCNGQNNQKWR 64
Cdd:cd23415    63 GVYTLPCNGGSYQRWrvtsTSGGGVTLRnVATGRCLDSNGSG-----GVYTRPCNGGSYQRWR 120
beta-trefoil_Ricin_abrin-like_rpt1 cd23484
first ricin B-type lectin domain, beta-trefoil fold, found in Abrus precatorius abrin, ...
33-80 2.72e-05

first ricin B-type lectin domain, beta-trefoil fold, found in Abrus precatorius abrin, agglutinin-I and similar proteins; This subfamily includes Abrus precatorius abrin (ABR) and agglutinin-I (AAG), which share a high degree of sequence similarity and belong to the type II ribosome-inactivating protein (RIP) family. Type II RIPs inhibit protein synthesis in eukaryotic cells and can also induce apoptosis. They are two-polypeptide proteins with a toxic A chain and a lectin-like B chain linked by a disulfide bond. The A chain of abrin and agglutinin-I is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. Agglutinin-I is less toxic than abrin. The B chain is a galactose-specific lectin that facilitates the binding to the cell membrane that precedes endocytosis. The B-chain 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. This model corresponds to the first ricin B-type lectin domain.


Pssm-ID: 467362  Cd Length: 137  Bit Score: 39.23  E-value: 2.72e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1830131197  33 DGRCLDVNAAGTADGTAVITWTCNGQ--NNQKWRLNSDGSITAVGanKCL 80
Cdd:cd23484    18 DGMCVDVYDNGYHNGNRIIMWKCKDRleENQLWTLKSDKTIRSNG--KCL 65
beta-trefoil_Ricin_ebulin-like_rpt1 cd23483
first ricin B-type lectin domain, beta-trefoil fold, found in Sambucus ebulus ebulin I and ...
8-72 2.73e-05

first ricin B-type lectin domain, beta-trefoil fold, found in Sambucus ebulus ebulin I and similar proteins; The family includes Sambucus ebulus ebulin I and Sambucus nigra nigrin b (also known as agglutinin V or SNAV), SNAI (also known as agglutinin I), SNAI' and SNAIf. Ebulin l is a type II ribosome-inactivating protein (RIP) isolated from the leaves of Sambucus ebulus. It is a disulfide-linked heterodimer composed of a toxic A chain and a galactoside-specific lectin B chain. It is considered a nontoxic type II RIP due to a reduced cytotoxicity on whole cells and animals as compared with other toxic type II RIP like ricins. Ebulin l binds an A-chain substrate analogue, pteroic acid. It binds bind galactose and lactose in subdomain 1alpha in a similar manner to that of ricin. In contrast, it binds only the monosaccharide galactose, and not the disaccharide lactose in subdomain 2gamma. SNAV is a non-toxic GalNAc-specific type II RIP which strongly inhibits mammalian protein synthesis but does not affect plant nor bacterial protein synthesis. SNAI is a Neu5Ac(alpha2-6)Gal/GalNAc-specific agglutinin. It also acts as a type II RIP that strongly inhibits mammalian but not plant ribosomes. SNAI' is another NeuAc(alpha2,6)Gal/GalNAc binding type II RIP from elderberry (Sambucus nigra) bark. It is a minor bark protein which closely resembles the major Neu5Ac(alpha2,6)Gal/GalNAc binding type II RIP, SNAI, with respect to its carbohydrate-binding specificity and ribosome-inactivating activity but has a different molecular structure due to a single cysteine residue present in the B chain of SNAI but absent from SNAI'. SNAIf is a fruit-specific SNAI. It functions as a fetuin-binding fruit lectin. Like Ebulin l, SNAV, SNAI, SNAI' and SNAIf consist of a sugar-binding B chain linked via a disulfide bond to the catalytically active A chain. The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain. It may also be responsible for cell agglutination (lectin activity). The B chain 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. This model corresponds to the first ricin B-type lectin domain.


Pssm-ID: 467361 [Multi-domain]  Cd Length: 127  Bit Score: 39.42  E-value: 2.73e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1830131197   8 VQIWDCNGQANQQWASTSAGELKtSDGRCLdvNAAGTADGTAVITWTCN--GQNNQKWRLNSDGSIT 72
Cdd:cd23483    27 VQLWPCGTQRNQQWTFDTDGTIR-SMGKCM--TANGLNSGSYVMIYNCStaAPEATKWVVSIDGTIT 90
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
7-80 2.78e-05

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


Pssm-ID: 467313 [Multi-domain]  Cd Length: 128  Bit Score: 39.24  E-value: 2.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830131197   7 QVQIWDCNGQ-ANQQWASTSAGELKTSDGR--CLDVNaagtaDGTAVITWTCNGQN-----NQKWRLNSDGSITAVGANK 78
Cdd:cd23435    28 PVIMYGCHGLgGNQYFEYTSKGEIRHNIGKelCLHAS-----GSDEVILQHCTSKGkdvppEQKWLFTQDGTIRNPASGL 102

                  ..
gi 1830131197  79 CL 80
Cdd:cd23435   103 CL 104
beta-trefoil_Ricin_AH cd23415
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ...
12-80 3.00e-05

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: 38.95  E-value: 3.00e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1830131197  12 DCNGQANQQWASTSAGELKTS-----DGRCLDVNAAGtadgtAVITWTCNGQNNQKWRLNSDGS----ITAVGANKCL 80
Cdd:cd23415    26 PCNGGPYQRWTWSGVGDGTVTlrnaaTGRCLDSNGNG-----GVYTLPCNGGSYQRWRVTSTSGggvtLRNVATGRCL 98
beta-trefoil_Ricin_SCDase_rpt2 cd23500
second ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ...
32-80 3.55e-05

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: 38.98  E-value: 3.55e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1830131197  32 SDGRCLDVNAAGTADGTAVITWTCNGQNNQKWRLN-SDGSI-TAVGANKCL 80
Cdd:cd23500     9 RSGKCLSAANGSQLNGSLVQLDACHASAGQLWYFDpKKGTIrSALDGNKCL 59
beta-trefoil_Ricin_ebulin-like_rpt2 cd23490
second ricin B-type lectin domain, beta-trefoil fold, found in Sambucus ebulus ebulin I and ...
19-77 4.66e-05

second ricin B-type lectin domain, beta-trefoil fold, found in Sambucus ebulus ebulin I and similar proteins; This subfamily includes Sambucus ebulus ebulin I and Sambucus nigra nigrin b (also known as agglutinin V or SNAV), SNAI (also known as agglutinin I), SNAI' and SNAIf. Ebulin l is a type II ribosome-inactivating protein (RIP) isolated from the leaves of Sambucus ebulus. It is a disulfide-linked heterodimer composed of a toxic A chain and a galactoside-specific lectin B chain. It is considered a nontoxic type II RIP due to a reduced cytotoxicity on whole cells and animals as compared with other toxic type II RIP like ricin. Ebulin l binds an A-chain substrate analogue, pteroic acid. It binds bind galactose and lactose in subdomain 1alpha in a similar manner to that of ricin. In contrast, it binds only the monosaccharide galactose, and not the disaccharide lactose in subdomain 2gamma. SNAV is a non-toxic GalNAc-specific type II RIP which strongly inhibits mammalian protein synthesis but does not affect plant nor bacterial protein synthesis. SNAI is Neu5Ac(alpha2-6)Gal/GalNAc specific agglutinin. It also acts as a type II RIP that strongly inhibits mammalian but not plant ribosomes. SNAI' is another NeuAc(alpha2,6)Gal/GalNAc binding type II RIP from elderberry (Sambucus nigra) bark. It is a minor bark protein which closely resembles the major Neu5Ac(alpha2,6)Gal/GalNAc binding type II RIP, SNAI, with respect to its carbohydrate-binding specificity and ribosome-inactivating activity but has a different molecular structure due to a single cysteine residue present in the B chain of SNAI but absent from SNAI'. SNAIf is fruit specific SNAI. It functions as fetuin-binding fruit lectin. Like Ebulin l, SNAV, SNAI, SNAI' and SNAIf consist of a sugar-binding B chain linked via a disulfide bond to the catalytically active A chain. The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain. It may also be responsible for cell agglutination (lectin activity). The B chain 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 model corresponds to the second ricin B-type lectin domain.


Pssm-ID: 467368 [Multi-domain]  Cd Length: 125  Bit Score: 38.59  E-value: 4.66e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1830131197  19 QQWASTSAGELKTSDGRCLDVNAAGTADGTAVITWTCNGQNNQKWRLNSDGSITAVGAN 77
Cdd:cd23490    35 QQWALYGDGTIRVNSDRSLCVTSNGYNSKDLIIILKCQGLPNQRWVFNTDGTIVNPNSK 93
beta-trefoil_Ricin_SGSL_rpt2 cd23489
second ricin B-type lectin domain, beta-trefoil fold, found in snake gourd (Trichosanthes ...
19-78 4.73e-05

second ricin B-type lectin domain, beta-trefoil fold, found in snake gourd (Trichosanthes anguina) seed lectin (SGSL) and similar proteins; 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. SGSL is a non-toxic three-chain type II RIPs consisting of Aalpha, Abeta and B chains with Abeta and B being disulfide-linked. The Aalpha and Abeta chains constitute the rRNA glycosidase domain and the B chain contains two ricin B-type carbohydrate-binding lectin domains. SGSL may have no glycosidase activity due to small changes in both the nucleotide binding and carbohydrate binding capabilities. It binds galactose and derivatives with a preference for the beta-anomeric forms. It also binds prophyrins. SGSL has hemagglutinating activity towards rabbit and human erythrocytes. The ricin B-type lectin domain shows 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 second ricin B-type lectin domain.


Pssm-ID: 467367  Cd Length: 128  Bit Score: 38.53  E-value: 4.73e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1830131197  19 QQWASTSAGELKTSDGRCLDVNAAG-TADGTAVIT-WTCNGQNNQKWRLNSDGSITAVGANK 78
Cdd:cd23489    35 QSWALYSDGTIRVDDNRELCVTASSsTYDNWKVITiLNCDGSNNQRWVFLADGSISTPGNQR 96
beta-trefoil_Ricin_RPI cd23452
ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine ...
34-80 4.82e-05

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: 38.65  E-value: 4.82e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1830131197  34 GRCLDVNAAGTADGTAVITWTCNGQNNQKWRLNSDGSITAVGanKCL 80
Cdd:cd23452    11 NKCIDVPNSSTTDGAPLQLWDCNGTNAQKWTFASDGTLRALG--KCL 55
beta-trefoil_Ricin_SCDase_rpt2 cd23500
second ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ...
4-77 5.64e-05

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: 38.21  E-value: 5.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830131197   4 STSQVQIWDCNGQANQQWA-STSAGELKTS--DGRCLDVNAAGTADGTAVITWTCNGQN-NQKW---------RLNSDGS 70
Cdd:cd23500    23 NGSLVQLDACHASAGQLWYfDPKKGTIRSAldGNKCLAIPGGNTGNHTQLQLADCDASNpAQQFnydggvfrsRLNSNQV 102

                  ....*..
gi 1830131197  71 ITAVGAN 77
Cdd:cd23500   103 IDASGGS 109
RicinB_lectin_2 pfam14200
Ricin-type beta-trefoil lectin domain-like;
7-53 7.84e-05

Ricin-type beta-trefoil lectin domain-like;


Pssm-ID: 464102 [Multi-domain]  Cd Length: 89  Bit Score: 37.36  E-value: 7.84e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 1830131197  7 QVQIWDCNGQANQQWASTSAGELK-----TSDGRCLDVnAAGTADGTAVITW 53
Cdd:pfam14200 39 NVQQWTDNGNDNQQWRIVDAGDGYyrivnKASGKVLDV-AGSTANGTNVQQW 89
beta-trefoil_Ricin_RSA cd23455
ricin B-type lectin domain, beta-trefoil fold, found in Rhizoctonia solani agglutinin (RSA) ...
36-65 1.05e-04

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: 37.69  E-value: 1.05e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1830131197  36 CLDVNAAGTADGTAVITWTCNGQNNQKWRL 65
Cdd:cd23455   102 VLDLAGSNDEDGTPVILYNNDGGDNQKWYF 131
beta-trefoil_Ricin_hemolysin cd23423
ricin B-type lectin domain, beta-trefoil fold, found in bacterial hemolysin and similar ...
1-68 1.14e-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: 37.36  E-value: 1.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1830131197   1 DVPSTSQVQIWDCN-GQANQQWASTSAGELK--TSDGRCLDVNAAGTadgtaVITWTCNGQNNQKWRLNSD 68
Cdd:cd23423    18 TVDNNGRVTLESCDsGDRNQSWILDSEGRYRsrVAPDLCLDADDDGL-----LTLEQCSLSLTQKWEWEGD 83
beta-trefoil_Ricin_RIPs_II_rpt2 cd23444
second ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating ...
6-71 1.17e-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: 37.25  E-value: 1.17e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1830131197   6 SQVQIWDC-NGQANQQWASTSAGELKTSDGRCLDVNAAGTADGTAVITWTCNGQNNQKWRLNSDGSI 71
Cdd:cd23444    20 NNVWLEECvSNKKEQKWALYPDGTIRPNQNRNLCLTSSSDVQGSIIVVLSCSGSSGQRWVFRNDGTI 86
beta-trefoil_Ricin_SCDase cd23456
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ...
34-80 1.24e-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: 37.34  E-value: 1.24e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1830131197  34 GRCLDVNAaGTADGTAVITWTCNGQNNQKWRLNSDGSI-TAVGANKCL 80
Cdd:cd23456    11 GLCLDVSG-GATNGANVVVYDCNNSNSQKWYYDATGRLhSKANPGKCL 57
beta-trefoil_Ricin_GALNT11 cd23440
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
12-80 2.08e-04

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


Pssm-ID: 467318 [Multi-domain]  Cd Length: 127  Bit Score: 36.97  E-value: 2.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1830131197  12 DCNGQ-ANQQWASTSAGELKTSDGRCLDVNaagtADGTAVITWT-CNGQ-NNQKWRLNSDGSITAVGANKCL 80
Cdd:cd23440    34 PCSRNdKKQLWYYTEDGELRLANLLCLDSS----ETSSDFPRLMkCHGSgGSQQWRFKKDNRLYNPASGQCL 101
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
3-67 4.56e-04

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: 35.73  E-value: 4.56e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1830131197   3 PSTSQVQIWDCNGQANQQWASTSAGEL--KTSDGRCLDVNaagtADGTAVITWTCNGQN-NQKWRLNS 67
Cdd:cd23437    61 GSGGKVKLRKCNLGETGKWEYDEATGQirHKGTGKCLDLN----EGTNKLILQPCDSSSpSQKWEFNE 124
beta-trefoil_Ricin_AglA cd23425
ricin B-type lectin domain, beta-trefoil fold, found in alpha-galactosidase A (AglA) and ...
13-80 5.04e-04

ricin B-type lectin domain, beta-trefoil fold, found in alpha-galactosidase A (AglA) and similar proteins; AglA (EC 3.2.1.22), also called melibiase A, hydrolyzes a variety of simple alpha-D-galactosides as well as more complex molecules such as oligosaccharides and polysaccharides. It belongs to the glycosyl hydrolase 27 (GH27) family. AglA contains an N-terminal GH27 catalytic domain, an alpha galactosidase C-terminal beta sandwich domain in the middle region, and a carbohydrate-binding domain at the C-terminus. The carbohydrate-binding domain is also known as 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 contain a potential sugar-binding pocket.


Pssm-ID: 467303 [Multi-domain]  Cd Length: 116  Bit Score: 35.88  E-value: 5.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830131197  13 CNGQANQQWASTSAGELKTSD--GRCLdvnaagTADGTAVITWTCNGQNNQKWRLNSDGSITAVGANKCL 80
Cdd:cd23425    28 CDGSDSQIWQVRKSGILRNLSntGQCL------TADGANVSLSPCDTSTSQNWSYEISGNLVNKKTGLCL 91
beta-trefoil_Ricin_CRYBG cd23430
ricin B-type lectin domain, beta-trefoil fold, found in the beta/gamma crystallin ...
9-71 5.37e-04

ricin B-type lectin domain, beta-trefoil fold, found in the beta/gamma crystallin domain-containing protein (CRYBG) family; The CRYBG family includes three members: CRYBG1, CRYBG2, and CRYBG3/vlAKAP. CRYBG1, also called absent in melanoma 1 protein (AIM1), may function as a suppressor of malignant melanoma. It may exert its effects through interactions with the cytoskeleton. CRYBG2 is also called absent in melanoma 1-like protein (AIM1L). CRYBG3/vlAKAP, also called very large A-kinase anchor protein, is an anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA). It binds to the dimeric RII-alpha regulatory subunit of PKA (PRKAR2A/PRKAR2B). CRYBG proteins belong to the beta/gamma-crystallin family. They all contain a ricin B-type lectin domain with a beta-trefoil fold at the C-terminus. The beta-trefoil fold 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: 467308 [Multi-domain]  Cd Length: 133  Bit Score: 36.03  E-value: 5.37e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1830131197   9 QIWD-CNGQANQQWASTSagelktsdgrCLDVNAAGTADGTAVITWTCNGQNNQKWRLNSDGSI 71
Cdd:cd23430    39 QIWYyQEGLIKCRIAEDC----------CLTVIGSLVTPGSKVGLWLEQNADRQFWSLKSDGRI 92
beta-trefoil_Ricin_MytiLec-like cd23417
ricin B-type lectin domain, beta-trefoil fold, found in Mytilus galloprovincialis lectin ...
32-80 7.80e-04

ricin B-type lectin domain, beta-trefoil fold, found in Mytilus galloprovincialis lectin (MytiLec) and similar proteins; MytiLec is a D-galactose-binding lectin from the mussel Mytilus galloprovincialis with cytotoxicity against certain cancer cell types. It has hemagglutinating activity towards rabbit erythrocytes. It induces glycan-mediated cytotoxicity of human globotriaosylceramide-expressing lymphoma cells. The family also includes lectin from the mussel Mytilus californianus (MCL) and lectin from the sea mussel Crenomytilus grayanus (CGL). MCL is specific for binding D-galactose and N-Acetyl-d-galactosamine that contained carbohydrate moieties that were also inhibited by melibiose and raffinose. It can agglutinate all types of human erythrocytes, as well as rabbit red blood cells. CGL is specific for binding GalNAc/Gal-containing carbohydrate moieties. It displays antibacterial, antifungal, and antiviral activities. It also possesses anti-cancer activity through recognizing globotriose Gb3. Members of this family 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 sugar-binding pocket.


Pssm-ID: 467296  Cd Length: 132  Bit Score: 35.39  E-value: 7.80e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1830131197  32 SDGRCLDVNAAGT--ADGTAVITWTCNGQNNQKWRLNSDGSITAVGANKCL 80
Cdd:cd23417     9 ASGKCIHPKGGSCnpPDGTKLVLYSDCSEDRMEFQLDSDGYLKHVCSGKCV 59
beta-trefoil_Ricin_MytiLec-like cd23417
ricin B-type lectin domain, beta-trefoil fold, found in Mytilus galloprovincialis lectin ...
10-80 8.21e-04

ricin B-type lectin domain, beta-trefoil fold, found in Mytilus galloprovincialis lectin (MytiLec) and similar proteins; MytiLec is a D-galactose-binding lectin from the mussel Mytilus galloprovincialis with cytotoxicity against certain cancer cell types. It has hemagglutinating activity towards rabbit erythrocytes. It induces glycan-mediated cytotoxicity of human globotriaosylceramide-expressing lymphoma cells. The family also includes lectin from the mussel Mytilus californianus (MCL) and lectin from the sea mussel Crenomytilus grayanus (CGL). MCL is specific for binding D-galactose and N-Acetyl-d-galactosamine that contained carbohydrate moieties that were also inhibited by melibiose and raffinose. It can agglutinate all types of human erythrocytes, as well as rabbit red blood cells. CGL is specific for binding GalNAc/Gal-containing carbohydrate moieties. It displays antibacterial, antifungal, and antiviral activities. It also possesses anti-cancer activity through recognizing globotriose Gb3. Members of this family 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 sugar-binding pocket.


Pssm-ID: 467296  Cd Length: 132  Bit Score: 35.39  E-value: 8.21e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1830131197  10 IWDCNGQANQQWASTSAGELK-TSDGRCLDVNAAGTADGTAVITWTCNGQNNQKWRLNSDGSITAVGANKCL 80
Cdd:cd23417    31 LYSDCSEDRMEFQLDSDGYLKhVCSGKCVCPKGGSADNGTKLVLHSNCGDDRAKFRRTSKGSLQHKSSGKCV 102
beta-trefoil_Ricin_hemolysin cd23423
ricin B-type lectin domain, beta-trefoil fold, found in bacterial hemolysin and similar ...
33-80 8.59e-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: 35.05  E-value: 8.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1830131197  33 DGRCLDVNAAGTadgtaVITWTCN-GQNNQKWRLNSDGS-ITAVGANKCL 80
Cdd:cd23423    13 NNRCLTVDNNGR-----VTLESCDsGDRNQSWILDSEGRyRSRVAPDLCL 57
beta-trefoil_Ricin_AH cd23415
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ...
32-80 1.49e-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: 34.33  E-value: 1.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1830131197  32 SDGRCLDVNAAGTadgtaVITWTCNGQNNQKWRLNSDGSITA----VGANKCL 80
Cdd:cd23415     9 ATGRCLDSNAGGN-----VYTGPCNGGPYQRWTWSGVGDGTVtlrnAATGRCL 56
beta-trefoil_Ricin_Pgant1-like cd23459
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
4-63 2.07e-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: 34.22  E-value: 2.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1830131197   4 STSQVQIWDC--NGQANQQWASTSAGELKTSD-GRCLDvnAAGTADGTAVITWTCNGQNNQKW 63
Cdd:cd23459    68 EESKVILITChgLEKFNQKWKHTKGGQIVHLAsGKCLD--AEGLKSGDDVTLAKCDGSLSQKW 128
beta-trefoil_Ricin_HA33_rpt2 cd23496
second ricin B-type lectin domain, beta-trefoil fold, found in Clostridium botulinum ...
34-66 2.63e-03

second ricin B-type lectin domain, beta-trefoil fold, found in Clostridium botulinum hemagglutinating protein HA33 and similar proteins; HA33, also called HA1, is a hemagglutinin (HA) 33 kDa subcomponent, which is associated with the large botulinum neurotoxin secreted complexes and plays a critical role in toxin protection, internalization, and possibly activation. HA33 is involved with internalization of the toxin into the bloodstream by binding to oligosaccharides lining the intestine. HA33 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. Each subdomain may harbor a potential sugar binding site. The model corresponds to the second ricin B-type lectin domain.


Pssm-ID: 467374 [Multi-domain]  Cd Length: 136  Bit Score: 34.04  E-value: 2.63e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1830131197  34 GRCLDVNAAGTADGTAVITWTCNGQNNQKWRLN 66
Cdd:cd23496   104 NKVLDVYNSQTANGTHVQVFSYHGNTNQKWIIN 136
beta-trefoil_Ricin_SCDase cd23456
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ...
6-63 3.97e-03

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: 33.48  E-value: 3.97e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1830131197   6 SQVQIWDCNGQANQQWASTSAGELKTSD-GRCLDVNAAGtadGTAVITWTCNGQNNQKW 63
Cdd:cd23456    67 ANVVLWACNDSANQRWDFDGNFIRSRNNtNLALDAYGSQ---GSNVGLWQFHGGANQQW 122
beta-trefoil_Ricin_CELIII-like_rpt2 cd23420
second ricin B-type lectin domain, beta-trefoil fold, found in Cucumaria echinata Ca2 ...
5-64 5.37e-03

second ricin B-type lectin domain, beta-trefoil fold, found in Cucumaria echinata Ca2+-dependent hemolytic lectin CEL-III and similar proteins; CEL-III is a Ca2+-dependent and galactose-specific lectin that exhibits hemolytic and hemagglutinating activities. It functions as an oligomer that forms an ion-permeable pore in the cell membrane. CEL-III consists of three domains: two N-terminal ricin B-type lectin domains, and a C-terminal pore-forming domain. The ricin B-type lectin domains show a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (called alpha, beta, and gamma, respectively) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding site. The model corresponds to the second ricin B-type lectin domain.


Pssm-ID: 467299 [Multi-domain]  Cd Length: 133  Bit Score: 33.29  E-value: 5.37e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1830131197   5 TSQVQIWDCNGQANQQWASTSA---GE----LKTSDGRCLDVnaAGTADGTAVITWTCNGQNNQKWR 64
Cdd:cd23420    66 SGNVGIYRCEDLRDQMWSRPNQycnGDycsfLNKESNKCLDV--SGDQGTGDVGTYQCDGLPDQRFK 130
beta-trefoil_Ricin_RSA cd23455
ricin B-type lectin domain, beta-trefoil fold, found in Rhizoctonia solani agglutinin (RSA) ...
37-70 5.56e-03

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: 33.07  E-value: 5.56e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1830131197  37 LDVNAAGTADGTAVITWTCNGQNNQKWRLNSDGS 70
Cdd:cd23455    14 LDLYLGSSAEGTPVQGYQPNGGDNQKWQLEWVGS 47
beta-trefoil_Ricin_SCDase_rpt1 cd23499
first ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ...
1-63 5.77e-03

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


Pssm-ID: 467377 [Multi-domain]  Cd Length: 131  Bit Score: 33.19  E-value: 5.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1830131197   1 DVPSTSQVQIWDCNGQ-ANQQWASTSA-GELKTSDGR--CLDvNAAGTADGTAVITWTCNGQNNQKW 63
Cdd:cd23499    22 DVVNGANVILWDCADKsADQRWIYDAAsGMLRNKANPsyCLD-NRGQAYNGGEVVLWQCEDSDNLRW 87
beta-trefoil_Ricin_AtEULS3-like cd23431
ricin B-type lectin domain, beta-trefoil fold, found in Arabidopsis thaliana Ricin B-like ...
38-65 6.26e-03

ricin B-type lectin domain, beta-trefoil fold, found in Arabidopsis thaliana Ricin B-like lectin EULS3 (AtEULS3) and similar proteins; AtEULS3, also called euonymus lectin S3, is a Ricin B-like lectin that binds carbohydrates in vitro. It interacts through its lectin domain with glycan structures containing one or more Lewis X, Lewis Y or lactosamine motifs. It has been implicated in abiotic stress responses, abscisic acid-induced stomatal closure, as well as disease resistance against Pseudomonas syringae through its involvement in stomatal movement. All subfamily members 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 may harbor a sugar-binding pocket.


Pssm-ID: 467309  Cd Length: 152  Bit Score: 33.10  E-value: 6.26e-03
                          10        20
                  ....*....|....*....|....*...
gi 1830131197  38 DVNAAGTADGTAVITWTCNGQNNQKWRL 65
Cdd:cd23431   123 DKKHGGVKDGTPVVLFKWHEGDNQLWKL 150
beta-trefoil_Ricin_MOA-like cd23416
ricin B-type lectin domain, beta-trefoil fold, found in Marasmius oreades agglutinin (MOA) and ...
6-65 6.96e-03

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: 33.09  E-value: 6.96e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830131197   6 SQVQIWDCNGQ---ANQQW---ASTSAGELKT----SDGRCLDVNAAGTADGTAVITWTCNGQNNQKWRL 65
Cdd:cd23416    25 TPIQGWQKTGDtgsFNQLWllePVPNGSDTYTiqnvRSGTYLDLAGGSSANGTAIVGWQSTNNPNQQWVI 94
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH