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Conserved domains on  [gi|1699430374|gb|QDI72814|]
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hydrolase [Streptomyces calvus]

Protein Classification

RICIN domain-containing protein( domain architecture ID 12006040)

RICIN domain-containing protein may have carbohydrate-binding function; similar to Mycobacterium tuberculosis protein Rv1419

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
390-513 9.93e-19

Ricin-type beta-trefoil lectin domain;


:

Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 82.19  E-value: 9.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699430374 390 TRLRNAASGLCLDTRGEPRDGSGTRLAECSSAWT-QQWTYEDDGLLRSVADpGLCLDSHKDA--GVVVLGTCadagDPRS 466
Cdd:pfam00652   3 GRIRNRASGKCLDVPGGSSAGGPVGLYPCHGSNGnQLWTLTGDGTIRSVAS-DLCLDVGSTAdgAKVVLWPC----HPGN 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1699430374 467 GDVRYDLTAPGELLTRWDGQLAL--APATPDANADIVVKVRDRTVDQRW 513
Cdd:pfam00652  78 GNQRWRYDEDGTQIRNPQSGKCLdvSGAGTSNGKVILWTCDSGNPNQQW 126
 
Name Accession Description Interval E-value
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
390-513 9.93e-19

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 82.19  E-value: 9.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699430374 390 TRLRNAASGLCLDTRGEPRDGSGTRLAECSSAWT-QQWTYEDDGLLRSVADpGLCLDSHKDA--GVVVLGTCadagDPRS 466
Cdd:pfam00652   3 GRIRNRASGKCLDVPGGSSAGGPVGLYPCHGSNGnQLWTLTGDGTIRSVAS-DLCLDVGSTAdgAKVVLWPC----HPGN 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1699430374 467 GDVRYDLTAPGELLTRWDGQLAL--APATPDANADIVVKVRDRTVDQRW 513
Cdd:pfam00652  78 GNQRWRYDEDGTQIRNPQSGKCLdvSGAGTSNGKVILWTCDSGNPNQQW 126
beta-trefoil_Ricin_SCDase cd23456
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ...
 392-460 2.07e-13

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: 67.00  E-value: 2.07e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1699430374 392 LRNAASGLCLDTRGEPRDGSGTRLAECSSAWTQQWTYEDDGLLRSVADPGLCLD---SHKDAGVVVLGTCAD 460
Cdd:cd23456     5 LKSQASGLCLDVSGGATNGANVVVYDCNNSNSQKWYYDATGRLHSKANPGKCLDaggENSNGANVVLWACND 76
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 391-458 2.01e-06

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 46.74  E-value: 2.01e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1699430374  391 RLRNAASGLCLDTRGeprDGSGT-RLAECSSAW-TQQWTYEDDGLLRSVaDPGLCLDSHKD--AGVVVLGTC 458
Cdd:smart00458  40 AIRIKDTDLCLTANG---NTGSTvTLYSCDGTNdNQYWEVNKDGTIRNP-DSGKCLDVKDGntGTKVILWTC 107
 
Name Accession Description Interval E-value
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
390-513 9.93e-19

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 82.19  E-value: 9.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699430374 390 TRLRNAASGLCLDTRGEPRDGSGTRLAECSSAWT-QQWTYEDDGLLRSVADpGLCLDSHKDA--GVVVLGTCadagDPRS 466
Cdd:pfam00652   3 GRIRNRASGKCLDVPGGSSAGGPVGLYPCHGSNGnQLWTLTGDGTIRSVAS-DLCLDVGSTAdgAKVVLWPC----HPGN 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1699430374 467 GDVRYDLTAPGELLTRWDGQLAL--APATPDANADIVVKVRDRTVDQRW 513
Cdd:pfam00652  78 GNQRWRYDEDGTQIRNPQSGKCLdvSGAGTSNGKVILWTCDSGNPNQQW 126
beta-trefoil_Ricin_SCDase cd23456
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ...
 392-460 2.07e-13

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: 67.00  E-value: 2.07e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1699430374 392 LRNAASGLCLDTRGEPRDGSGTRLAECSSAWTQQWTYEDDGLLRSVADPGLCLD---SHKDAGVVVLGTCAD 460
Cdd:cd23456     5 LKSQASGLCLDVSGGATNGANVVVYDCNNSNSQKWYYDATGRLHSKANPGKCLDaggENSNGANVVLWACND 76
beta-trefoil_Ricin_SCDase_rpt1 cd23499
first ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ...
 391-465 2.39e-12

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: 64.01  E-value: 2.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699430374 391 RLRNAASGLCLDTRG---EPRDGSGTRLAECSS-AWTQQWTYE-DDGLLRSVADPGLCLDS---HKDAGVVVLGTCADAG 462
Cdd:cd23499     4 RIVNRASGKCLDIPGndnDVVNGANVILWDCADkSADQRWIYDaASGMLRNKANPSYCLDNrgqAYNGGEVVLWQCEDSD 83


                  ...
gi 1699430374 463 DPR 465
Cdd:cd23499    84 NLR 86
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 388-513 2.96e-11

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: 61.23  E-value: 2.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699430374 388 GRTRLRNAASGLCLDTRG-EPRDGSGTRLAECSSAWTQQWTYEDDG----LLRSVAdPGLCLD----SHKDAGVVVLGTC 458
Cdd:cd00161     1 GTYRIVNAASGKCLDVAGgSTANGAPVQQWTCNGGANQQWTLTPVGdgyyTIRNVA-SGKCLDvaggSTANGANVQQWTC 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1699430374 459 ADAGD-----PRSGDVRYdltapgELLTRWDGQ-LALAPATPDANADIVVKVRDRTVDQRW 513
Cdd:cd00161    80 NGGDNqqwrlEPVGDGYY------RIVNKHSGKcLDVSGGSTANGANVQQWTCNGGANQQW 134
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 358-461 4.27e-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: 57.76  E-value: 4.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699430374 358 DPTGSTGAAGGRASVpsAAPTGAAA-----VPSAPGRTRLRNAASGLCLDTRG-EPRDGSGTRLAECSSAWTQQWTYEDD 431
Cdd:cd00161    15 DVAGGSTANGAPVQQ--WTCNGGANqqwtlTPVGDGYYTIRNVASGKCLDVAGgSTANGANVQQWTCNGGDNQQWRLEPV 92

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1699430374 432 G----LLRSVAdPGLCLD----SHKDAGVVVLGTCADA 461
Cdd:cd00161    93 GdgyyRIVNKH-SGKCLDvsggSTANGANVQQWTCNGG 129
beta-trefoil_Ricin_SCDase_rpt1 cd23499
first ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ...
 392-445 1.15e-09

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: 56.69  E-value: 1.15e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1699430374 392 LRNAAS-GLCLDTRGEPRDGSGTRLAECSSAWTQQWTYeDDGLLRSVADPGLCLD 445
Cdd:cd23499    52 LRNKANpSYCLDNRGQAYNGGEVVLWQCEDSDNLRWTY-DNGVLRSKHNPNIVLD 105
beta-trefoil_Ricin_AH cd23415
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ...
 388-514 2.85e-09

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: 55.13  E-value: 2.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699430374 388 GRTRLRNAASGLCLDTrgepRDGSGTRLAECSSAWTQQWTYEDDG----LLRSVAdPGLCLDShKDAGVVVLGTCaDAGD 463
Cdd:cd23415     1 GTVRLRNVATGRCLDS----NAGGNVYTGPCNGGPYQRWTWSGVGdgtvTLRNAA-TGRCLDS-NGNGGVYTLPC-NGGS 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1699430374 464 PRSGDVRYDLTAPGELLTRWDGqLALapatpDANADIVVKVR--DRTVDQRWS 514
Cdd:cd23415    74 YQRWRVTSTSGGGVTLRNVATG-RCL-----DSNGSGGVYTRpcNGGSYQRWR 120
beta-trefoil_Ricin_SCDase cd23456
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ...
 391-451 9.32e-09

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: 53.51  E-value: 9.32e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1699430374 391 RLRNAA-SGLCLDTRGEPRDGSGTRLAECSSAWTQQWTYeDDGLLRSVADPGLCLDSHKDAG 451
Cdd:cd23456    46 RLHSKAnPGKCLDAGGENSNGANVVLWACNDSANQRWDF-DGNFIRSRNNTNLALDAYGSQG 106
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
 392-484 1.05e-08

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: 53.49  E-value: 1.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699430374 392 LRNAASGLCLDTRG-EPRDGSGTRLAECSSAWTQQWTYEDDGLLRSvadPGLCLD----SHKDAGVVVLGTCADAG---- 462
Cdd:cd23451     5 VRLANAGKCLDVPGsSTADGNPVQIYTCNGTAAQKWTLGTDGTLRV---LGKCLDvsggGTANGTLVQLWDCNGTGaqkw 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1699430374 463 ---------DPRSG---DVRYDLTAPGELLTRWD 484
Cdd:cd23451    82 vpradgtlyNPQSGkclDAPGGSTTDGTQLQLYT 115
beta-trefoil_Ricin_AH cd23415
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ...
 384-456 6.04e-08

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: 51.28  E-value: 6.04e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1699430374 384 PSAPGRTRLRNAASGLCLDTRGEPrdgsGTRLAECSSA----WTQQWTYEDDGLLRSVAdPGLCLDSHKDAGVVVLG 456
Cdd:cd23415    39 GVGDGTVTLRNAATGRCLDSNGNG----GVYTLPCNGGsyqrWRVTSTSGGGVTLRNVA-TGRCLDSNGSGGVYTRP 110
beta-trefoil_Ricin_GALNT11 cd23440
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 389-462 6.28e-08

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: 51.22  E-value: 6.28e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1699430374 389 RTRLRNAASGLCLDTRGEPRD-GSGTRLAECSSAW-TQQWTYEDDGLLRsvadPG--LCLDSHKD-AGVVVLGTCADAG 462
Cdd:cd23440     5 KGQLKHAGSGLCLVAEDEVSQkGSLLVLRPCSRNDkKQLWYYTEDGELR----LAnlLCLDSSETsSDFPRLMKCHGSG 79
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 391-458 2.01e-06

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 46.74  E-value: 2.01e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1699430374  391 RLRNAASGLCLDTRGeprDGSGT-RLAECSSAW-TQQWTYEDDGLLRSVaDPGLCLDSHKD--AGVVVLGTC 458
Cdd:smart00458  40 AIRIKDTDLCLTANG---NTGSTvTLYSCDGTNdNQYWEVNKDGTIRNP-DSGKCLDVKDGntGTKVILWTC 107
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 394-516 3.08e-06

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 46.35  E-value: 3.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699430374  394 NAASGLCLDTRGEprdGSGTRLAEC-SSAWTQQWTYEDDGLLRSVaDPGLCLDSHKDAGVVV-LGTCADAGDPRSGDVRY 471
Cdd:smart00458   3 SGNTGKCLDVNGN---KNPVGLFDChGTGGNQLWKLTSDGAIRIK-DTDLCLTANGNTGSTVtLYSCDGTNDNQYWEVNK 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1699430374  472 DLTapgelLTRWDGQLALAPATPDANADIVVKVRDRTVDQRWSAE 516
Cdd:smart00458  79 DGT-----IRNPDSGKCLDVKDGNTGTKVILWTCSGNPNQKWIFE 118
beta-trefoil_Ricin_hemolysin cd23423
ricin B-type lectin domain, beta-trefoil fold, found in bacterial hemolysin and similar ...
 398-461 3.38e-06

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: 46.22  E-value: 3.38e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1699430374 398 GLCLDtrgepRDGSGT-RLAECSSAWT-QQWTYEDDGLLRSVADPGLCLDShKDAGVVVLGTCADA 461
Cdd:cd23423    14 NRCLT-----VDNNGRvTLESCDSGDRnQSWILDSEGRYRSRVAPDLCLDA-DDDGLLTLEQCSLS 73
beta-trefoil_Ricin_SGSL_rpt1 cd23482
first ricin B-type lectin domain, beta-trefoil fold, found in snake gourd (Trichosanthes ...
 389-513 5.46e-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: 46.28  E-value: 5.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699430374 389 RTRLRNAASGLCLDTRGE-PRDGSGTRLAECSSAWTQQWTYEDDGLLRSVadpGLCL--DSHKDAGVVVLGTCADAGdpr 465
Cdd:cd23482     8 RTTRISGRDALCVDVAGAlTSDGSRLILYPCGQQVNQKWTFHSDGTVRSL---GKCLatNNSKFGNLVVIYDCSKLA--- 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1699430374 466 SGDVRYDLTAPGELLTRWDGQLALAPATPDANADIVVKVRDRTVDQRW 513
Cdd:cd23482    82 AEDISWDVSVGGTIMNPNYEDLALTSNKATRSTNLTMEVNTYSASQGW 129
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 385-513 8.12e-06

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


Pssm-ID: 467297 [Multi-domain]  Cd Length: 130  Bit Score: 45.42  E-value: 8.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699430374 385 SAPGRTRLRNAASGLCLDTRG-EPRDGSGTRLAECSSAWTQQWTYEDDGLLRSVADpgLCLDSHKDAGV----VVLGTCa 459
Cdd:cd23418     1 PGAGGGQIRGYGSGRCLDVPGgSTTNGTRLILWDCHGGANQQFTFTSAGELRVGGD--KCLDAAGGGTTngtpVVIWPC- 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1699430374 460 dAGDPrsgDVRYDLTAPGELLTRWDGQ-LALAPATPDANADIVVKVRDRTVDQRW 513
Cdd:cd23418    78 -NGGA---NQKWRFNSDGTIRNVNSGLcLDVAGGGTANGTRLILWSCNGGSNQRW 128
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
 388-454 1.12e-05

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


Pssm-ID: 467784 [Multi-domain]  Cd Length: 119  Bit Score: 44.90  E-value: 1.12e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1699430374 388 GRTRLRNAASGLCLDTRGePRDGSGTRLAEC-SSAWTQQWTYEDDGLLRSVADPGLCLDSHKDAGVVV 454
Cdd:cd23385    41 SGHRLFNVGTGKCLGVSS-SSPSSPLRLFECdSEDELQKWKCSKDGLLLLKGLGLLLLYDKSGKNVVV 107
beta-trefoil_Ricin_RIPs_II_rpt2 cd23444
second ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating ...
 397-460 2.77e-05

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: 43.80  E-value: 2.77e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1699430374 397 SGLCLDTRGeprdGSGTRLAECSSAWT-QQWTYEDDGLLRSVADPGLCL--DSHKDAGVVVLGTCAD 460
Cdd:cd23444    10 NDLCLQANG----GNNVWLEECVSNKKeQKWALYPDGTIRPNQNRNLCLtsSSDVQGSIIVVLSCSG 72
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
 392-465 2.77e-05

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


Pssm-ID: 467784 [Multi-domain]  Cd Length: 119  Bit Score: 43.74  E-value: 2.77e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1699430374 392 LRNAASGLCLDTRGeprDGSGTRLAECS-SAWTQQWTYEDDGLLRSVADpGLCL--DSHKDAGVVVLGTCaDAGDPR 465
Cdd:cd23385     5 IYNEDLGKCLAARS---SSSKVSLSTCNpNSPNQQWKWTSGHRLFNVGT-GKCLgvSSSSPSSPLRLFEC-DSEDEL 76
beta-trefoil_Ricin_RPI cd23452
ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine ...
 395-480 2.95e-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: 43.66  E-value: 2.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699430374 395 AASGLCLDTRG-EPRDGSGTRLAECSSAWTQQWTYEDDGLLRSVadpGLCLD----SHKDAGVVVLGTCadAGDPRSgdv 469
Cdd:cd23452     8 GLANKCIDVPNsSTTDGAPLQLWDCNGTNAQKWTFASDGTLRAL---GKCLDvawgGTDNGTAVQLWTC--SGNPAQ--- 79

                          90
                  ....*....|.
gi 1699430374 470 RYDLTAPGELL 480
Cdd:cd23452    80 QFVLSGAGDLV 90
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 392-458 3.09e-05

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: 43.44  E-value: 3.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699430374 392 LRNAASGLCLDTRGE-----------------------------------PRDGSGTR--LAECSSAWTQQWTY-EDDGL 433
Cdd:cd23437     8 IRNLGTGLCLDTMGHqnggpvglypchgmggnqlfrlneagqlavgeqclTASGSGGKvkLRKCNLGETGKWEYdEATGQ 87

                          90       100
                  ....*....|....*....|....*
gi 1699430374 434 LRsVADPGLCLDSHKDAGVVVLGTC 458
Cdd:cd23437    88 IR-HKGTGKCLDLNEGTNKLILQPC 111
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
 358-427 3.13e-05

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: 43.47  E-value: 3.13e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1699430374 358 DPTGSTGAAGGRASVPSAAPTGAAA-VPSAPGRtrLRNAASGLCLD-TRGEPRDGSGTRLAECSSAWTQQWT 427
Cdd:cd23451    56 DVSGGGTANGTLVQLWDCNGTGAQKwVPRADGT--LYNPQSGKCLDaPGGSTTDGTQLQLYTCNGTAAQQWT 125
beta-trefoil_Ricin_SCDase_rpt2 cd23500
second ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ...
 390-445 3.30e-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: 43.61  E-value: 3.30e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1699430374 390 TRLRNAASGLCLD-TRGEPRDGSGTRLAECSSAWTQQWTYE-DDGLLRSVADPGLCLD 445
Cdd:cd23500     3 TTYRSKRSGKCLSaANGSQLNGSLVQLDACHASAGQLWYFDpKKGTIRSALDGNKCLA 60
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 358-426 5.23e-05

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


Pssm-ID: 467293 [Multi-domain]  Cd Length: 134  Bit Score: 43.13  E-value: 5.23e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1699430374 358 DPTGSTGAAGGRASVpsAAPTGAAA-----VPSAPGRTRLRNAASGLCLDTRG-EPRDGSGTRLAECSSAWTQQW 426
Cdd:cd00161    62 DVAGGSTANGANVQQ--WTCNGGDNqqwrlEPVGDGYYRIVNKHSGKCLDVSGgSTANGANVQQWTCNGGANQQW 134
RicinB_lectin_2 pfam14200
Ricin-type beta-trefoil lectin domain-like;
391-445 9.22e-05

Ricin-type beta-trefoil lectin domain-like;


Pssm-ID: 464102 [Multi-domain]  Cd Length: 89  Bit Score: 41.21  E-value: 9.22e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699430374 391 RLRNAASGLCLD-TRGEPRDGSGTRLAECSSAWTQQWTYEDDG----LLRSVADpGLCLD 445
Cdd:pfam14200  17 TIVNVASGKYLDvAGGSTANGANVQQWTDNGNDNQQWRIVDAGdgyyRIVNKAS-GKVLD 75
beta-trefoil_Ricin_AgaB34-like cd23458
ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 ...
 388-465 1.48e-04

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: 41.93  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699430374 388 GRTRLRNAASGLCLD-TRGEPRDGSGTRLAECSSAWTQQWTYE--DDGLLRSVA-DPGLCLD----SHKDAGVVVLGTCA 459
Cdd:cd23458     1 GTYRIRNRNSGKCIDvAGGSTANGANIQQWDCGSGSNQQWTLVeiDNGYYRIKAsHSGKCLDvaggSTANGANIQQWDCV 80


                  ....*.
gi 1699430374 460 DAGDPR 465
Cdd:cd23458    81 GGANQQ 86
beta-trefoil_Ricin-like_rpt1 cd23480
first ricin B-type lectin domain, beta-trefoil fold, found in Ricinus communis ricin, ...
 397-513 1.76e-04

first ricin B-type lectin domain, beta-trefoil fold, found in Ricinus communis ricin, agglutinin and similar proteins; This subfamily includes ricin and agglutinin (RCA), which are toxic lectins from Ricinus communis. Ricin is highly toxic to animal cells, and to a lesser extent to plant cells. As a prototype AB toxin, ricin is composed of two polypeptide chains (A- and B-chain) linked by a disulfide bond. Ricin A chain acts as an RNA N-glycosidase that removes a specific adenine residue from an exposed loop of the 28S rRNA (A4324 in mammals), leading to rRNA breakage. Ricin B functions as a lectin that mediates cell binding via different oligosaccharide residues on the cell surface, including N-acetylglucosamine and galactose residues found in glycolipids and glycoproteins. It is also responsible for cell agglutination. Agglutinin shows high sequence similarity with ricin. It is only a weak toxin but a strong hemagglutinin. By contrast, ricin is a potent toxin but a weak hemagglutinin. Like ricin, agglutinin consists of a sugar-binding B chain linked via a disulfide bond to the catalytically active A chain. The B chain of ricin and agglutinin 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: 467358 [Multi-domain]  Cd Length: 137  Bit Score: 41.59  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699430374 397 SGLCLDTRGEP-RDGSGTRLAECSSA--WTQQWTYEDDGLLRSvadPGLCLDSHKDA-GV-VVLGTCADAGdprSGDVRY 471
Cdd:cd23480    17 NGLCVDVRDEEfFDGNAIQLWPCKSNtdANQLWTLKKDNTIRS---NGKCLTISGSSpGQqVMIYDCNTAA---TDATRW 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1699430374 472 DLTAPGELLTRWDGqLALAPATPDANADIVVKVRDRTVDQRW 513
Cdd:cd23480    91 QIWDNGTIINPRSG-LVLAATSGNSGTKLTVQTNIYAVSQGW 131
beta-trefoil_Ricin_Pgant1-like cd23459
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 392-430 2.43e-04

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: 41.15  E-value: 2.43e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1699430374 392 LRNAASGLCLDTRGEpRDGSGTRLAECSSAWTQQWTYED 430
Cdd:cd23459    95 IVHLASGKCLDAEGL-KSGDDVTLAKCDGSLSQKWTFEH 132
beta-trefoil_Ricin_CRYBG cd23430
ricin B-type lectin domain, beta-trefoil fold, found in the beta/gamma crystallin ...
 391-445 2.60e-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: 41.04  E-value: 2.60e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1699430374 391 RLRNAASGLCLDTRGEPRDGSGTRL--AECSSAWTQQWTYEdDGLLRSVADPGLCLD 445
Cdd:cd23430     4 RLRNKATGLFLSVNGNLEDLKLLRVqvMPDVGADDQIWYYQ-EGLIKCRIAEDCCLT 59
beta-trefoil_Ricin_GllA-1 cd23454
GllA-1 domain, beta-trefoil fold, found in Mucor circinelloides Gellins and similar proteins; ...
 391-449 2.66e-04

GllA-1 domain, beta-trefoil fold, found in Mucor circinelloides Gellins and similar proteins; Gellin proteins act as central effectors of wound-induced protoplasmic gelation. They possess ten related N-terminal beta-trefoil domains (Gll-1 to Gll-10) that contribute to distinct gelation-related activities. The beta-trefoil domains show low sequence similarity to members of the functionally diverse ricin B lectin domain family. They are characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site. Gellin from M. circinelloides has been called GellinA (also known as GllA). The model corresponds to GllA-1 domain, which is a remote family member of the ricin B-type lectin domain.


Pssm-ID: 467332 [Multi-domain]  Cd Length: 136  Bit Score: 41.15  E-value: 2.66e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1699430374 391 RLRNAASGLCLDTRGEpRDGSGTRLAEC-----SSAWTQQWTYEDDGLLRSVADPGLCLDSHKD 449
Cdd:cd23454    48 YLVNKASGLVLDIQGG-VVKSGTRLVQSpkkpsKDANNQRWGLTADGYIYLLSNPSLVLGIKGN 110
beta-trefoil_Ricin_ebulin-like_rpt1 cd23483
first ricin B-type lectin domain, beta-trefoil fold, found in Sambucus ebulus ebulin I and ...
 389-476 3.92e-04

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: 3.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699430374 389 RTRLRNAASGLCLDTR-GEPRDGSGTRLAECSSAWTQQWTYEDDGLLRSVadpGLCL--DSHKDAGVVVLGTCADAG--- 462
Cdd:cd23483     2 FTRRISGRDGLCVDVRnGYDTDGTPVQLWPCGTQRNQQWTFDTDGTIRSM---GKCMtaNGLNSGSYVMIYNCSTAApea 78

                          90       100
                  ....*....|....*....|....*.
gi 1699430374 463 ------------DPRSGDVrydLTAP 476
Cdd:cd23483    79 tkwvvsidgtitNPSSGLV---LTAP 101
beta-trefoil_Ricin_hemolysin cd23423
ricin B-type lectin domain, beta-trefoil fold, found in bacterial hemolysin and similar ...
 391-454 7.82e-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: 39.29  E-value: 7.82e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1699430374 391 RLRNA-ASGLCLDTRgeprDGSGTRLAECSSAWTQQWTYEDDGLLRSVADPGLCLDSHKDAGVVV 454
Cdd:cd23423    46 RYRSRvAPDLCLDAD----DDGLLTLEQCSLSLTQKWEWEGDRLKNRYLDTGWVLTHDAQGGLKL 106
beta-trefoil_Ricin_RIPs_II_rpt1 cd23443
first ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating ...
 398-477 1.15e-03

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: 39.20  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699430374 398 GLCLDTR-GEPRDGSGTRLAECSSAW-TQQWTYEDDGLLRSVadpGLCLDSHKDAGV--VVLGTC--ADAGD-------- 463
Cdd:cd23443    10 GLCVDVKdGYYSDGNPVILWPCKSQDaNQLWTFKRDGTIRSN---GKCLTTNGYSPGsyVVIYDCstAVAEAtkwevsdd 86

                          90
                  ....*....|....*....
gi 1699430374 464 -----PRSGDVrydLTAPG 477
Cdd:cd23443    87 gtiinPASGLV---LTADS 102
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 390-429 1.59e-03

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


Pssm-ID: 467319 [Multi-domain]  Cd Length: 122  Bit Score: 38.54  E-value: 1.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1699430374 390 TRLRNAASGLCLDTRGEPrdgsGTRLAEC-SSAWTQQWTYE 429
Cdd:cd23441    86 RQLVHSESGLCLDSRKKK----GLVVSPCrSGAPSQKWDFT 122
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 399-467 2.02e-03

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: 38.46  E-value: 2.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1699430374 399 LCLDTRGEPRdGSGTRLAECS-SAWTQQWTY-EDDGLLRSVaDPGLCLDS-HKDAGVVVLGTCadagDPRSG 467
Cdd:cd23434    50 LCLTVVDRAP-GSLVTLQPCReDDSNQKWEQiENNSKLRHV-GSNLCLDSrNAKSGGLTVETC----DPSSG 115
beta-trefoil_Ricin_abrin-like_rpt2 cd23491
second ricin B-type lectin domain, beta-trefoil fold, found in Abrus precatorius abrin, ...
 397-461 2.04e-03

second 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 composed of 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. The model corresponds to the second ricin B-type lectin domain.


Pssm-ID: 467369  Cd Length: 124  Bit Score: 38.48  E-value: 2.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1699430374 397 SGLCLDTRGeprdgSGTRLAEC-SSAWTQQWTYEDDGLLRSVADPGLCLDS--HKDAGVVVLGTCADA 461
Cdd:cd23491    10 SDLCMQAQG-----SNVWLAVCdINKKEQQWALYTDGSIRSVQNTNNCLTSkdHKQGSTIVLMGCSNG 72
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 397-454 5.04e-03

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


Pssm-ID: 467319 [Multi-domain]  Cd Length: 122  Bit Score: 37.38  E-value: 5.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1699430374 397 SGLCLdTRGEPRDGSGTRLAECSSAWTQQWTYEDDGLLRSVAdpGLCLDSHKDAGVVV 454
Cdd:cd23441    53 QGLCL-TVDSSSKDLPVVLETCSDDPKQKWTRTGRQLVHSES--GLCLDSRKKKGLVV 107
beta-trefoil_Ricin_GALNT10-like cd23439
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 391-458 5.85e-03

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


Pssm-ID: 467317 [Multi-domain]  Cd Length: 126  Bit Score: 36.94  E-value: 5.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1699430374 391 RLRNAASGLCLDTRGEpRDGSGTRLAECSSAW---TQQW--TYEDDglLRsvadPG---LCLD--SHKDAGVVVLGTC 458
Cdd:cd23439     4 EIRNVGSGLCIDTKHG-GENDEVRLSKCVKDGgggEQQFelTWHED--IR----PKkrkVCFDvsSHTPGAPVILYAC 74
beta-trefoil_Ricin_GALNT1-like cd23433
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 392-462 6.32e-03

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: 36.91  E-value: 6.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1699430374 392 LRNAASGLCLDTRGePRDGSGTRLAEC-SSAWTQQWTYEDDGLLRSvaDpGLCLDSHKDAGVVVLGTCADAG 462
Cdd:cd23433     9 IRNVETNLCLDTMG-RKAGEKVGLSSChGQGGNQVFSYTAKGEIRS--D-DLCLDASRKGGPVKLEKCHGMG 76
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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