NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15608557|ref|NP_215935|]
View 

hypothetical protein Rv1419 [Mycobacterium tuberculosis H37Rv]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
36-153 1.72e-17

Ricin-type beta-trefoil lectin domain;


:

Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 73.72  E-value: 1.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608557    36 PVQLKSRLGDVCLDAPSGSWF-SPLVINPCNGTDF-QRWNLTDDRQVESVAfPGECVNIGNAL---WARLQPCVNWIS-Q 109
Cdd:pfam00652   2 TGRIRNRASGKCLDVPGGSSAgGPVGLYPCHGSNGnQLWTLTGDGTIRSVA-SDLCLDVGSTAdgaKVVLWPCHPGNGnQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 15608557   110 HWTVQPDG--LVKSDLDACLTVLGGPDPGTWVSTRWCDPNAPDQQW 153
Cdd:pfam00652  81 RWRYDEDGtqIRNPQSGKCLDVSGAGTSNGKVILWTCDSGNPNQQW 126
 
Name Accession Description Interval E-value
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
36-153 1.72e-17

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 73.72  E-value: 1.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608557    36 PVQLKSRLGDVCLDAPSGSWF-SPLVINPCNGTDF-QRWNLTDDRQVESVAfPGECVNIGNAL---WARLQPCVNWIS-Q 109
Cdd:pfam00652   2 TGRIRNRASGKCLDVPGGSSAgGPVGLYPCHGSNGnQLWTLTGDGTIRSVA-SDLCLDVGSTAdgaKVVLWPCHPGNGnQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 15608557   110 HWTVQPDG--LVKSDLDACLTVLGGPDPGTWVSTRWCDPNAPDQQW 153
Cdd:pfam00652  81 RWRYDEDGtqIRNPQSGKCLDVSGAGTSNGKVILWTCDSGNPNQQW 126
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 41-156 1.88e-15

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 67.92  E-value: 1.88e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608557     41 SRLGDVCLDAPSGSwfSPLVINPCNGT-DFQRWNLTDDRQVESVAfPGEC--VNIGNALWARLQPCVN-WISQHWTVQPD 116
Cdd:smart00458   3 SGNTGKCLDVNGNK--NPVGLFDCHGTgGNQLWKLTSDGAIRIKD-TDLCltANGNTGSTVTLYSCDGtNDNQYWEVNKD 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 15608557    117 GLVKS-DLDACLTVLGGpDPGTWVSTRWCDPNaPDQQWDSV 156
Cdd:smart00458  80 GTIRNpDSGKCLDVKDG-NTGTKVILWTCSGN-PNQKWIFE 118
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 35-153 8.76e-12

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: 58.92  E-value: 8.76e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608557  35 GPVQLKSRLGDVCLDAPSGSWF--SPLVINPCNGTDFQRWNLTDDR----QVESVAfPGECVNIGNALWA-----RLQPC 103
Cdd:cd00161   1 GTYRIVNAASGKCLDVAGGSTAngAPVQQWTCNGGANQQWTLTPVGdgyyTIRNVA-SGKCLDVAGGSTAnganvQQWTC 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15608557 104 VNWISQHWTVQPDGL-------VKSDLdaCLTVLGG-PDPGTWVSTRWCDpNAPDQQW 153
Cdd:cd00161  80 NGGDNQQWRLEPVGDgyyrivnKHSGK--CLDVSGGsTANGANVQQWTCN-GGANQQW 134
 
Name Accession Description Interval E-value
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
36-153 1.72e-17

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 73.72  E-value: 1.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608557    36 PVQLKSRLGDVCLDAPSGSWF-SPLVINPCNGTDF-QRWNLTDDRQVESVAfPGECVNIGNAL---WARLQPCVNWIS-Q 109
Cdd:pfam00652   2 TGRIRNRASGKCLDVPGGSSAgGPVGLYPCHGSNGnQLWTLTGDGTIRSVA-SDLCLDVGSTAdgaKVVLWPCHPGNGnQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 15608557   110 HWTVQPDG--LVKSDLDACLTVLGGPDPGTWVSTRWCDPNAPDQQW 153
Cdd:pfam00652  81 RWRYDEDGtqIRNPQSGKCLDVSGAGTSNGKVILWTCDSGNPNQQW 126
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 41-156 1.88e-15

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 67.92  E-value: 1.88e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608557     41 SRLGDVCLDAPSGSwfSPLVINPCNGT-DFQRWNLTDDRQVESVAfPGEC--VNIGNALWARLQPCVN-WISQHWTVQPD 116
Cdd:smart00458   3 SGNTGKCLDVNGNK--NPVGLFDCHGTgGNQLWKLTSDGAIRIKD-TDLCltANGNTGSTVTLYSCDGtNDNQYWEVNKD 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 15608557    117 GLVKS-DLDACLTVLGGpDPGTWVSTRWCDPNaPDQQWDSV 156
Cdd:smart00458  80 GTIRNpDSGKCLDVKDG-NTGTKVILWTCSGN-PNQKWIFE 118
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 35-153 8.76e-12

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: 58.92  E-value: 8.76e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608557  35 GPVQLKSRLGDVCLDAPSGSWF--SPLVINPCNGTDFQRWNLTDDR----QVESVAfPGECVNIGNALWA-----RLQPC 103
Cdd:cd00161   1 GTYRIVNAASGKCLDVAGGSTAngAPVQQWTCNGGANQQWTLTPVGdgyyTIRNVA-SGKCLDVAGGSTAnganvQQWTC 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15608557 104 VNWISQHWTVQPDGL-------VKSDLdaCLTVLGG-PDPGTWVSTRWCDpNAPDQQW 153
Cdd:cd00161  80 NGGDNQQWRLEPVGDgyyrivnKHSGK--CLDVSGGsTANGANVQQWTCN-GGANQQW 134
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 38-153 5.93e-07

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: 45.80  E-value: 5.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608557  38 QLKSRLGDVCLDAPSGSW--FSPLVINPCNGTDFQRWNLTDDRQVesVAFPGECVNIGNALWAR-----LQPCVNWISQH 110
Cdd:cd23418   7 QIRGYGSGRCLDVPGGSTtnGTRLILWDCHGGANQQFTFTSAGEL--RVGGDKCLDAAGGGTTNgtpvvIWPCNGGANQK 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15608557 111 WTVQPDG-LVKSDLDACLTVLGG-PDPGTWVSTRWCDpNAPDQQW 153
Cdd:cd23418  85 WRFNSDGtIRNVNSGLCLDVAGGgTANGTRLILWSCN-GGSNQRW 128
beta-trefoil_Ricin_SCDase cd23456
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ...
 37-112 3.85e-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: 43.50  E-value: 3.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608557  37 VQLKSRLGDVCLDAPSG-SWFSPLVINPCNGTDFQRWNLTDDRQVESVAFPGECVNIGNALWAR----LQPCVNWISQHW 111
Cdd:cd23456   3 FQLKSQASGLCLDVSGGaTNGANVVVYDCNNSNSQKWYYDATGRLHSKANPGKCLDAGGENSNGanvvLWACNDSANQRW 82


                .
gi 15608557 112 T 112
Cdd:cd23456  83 D 83
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 38-154 4.63e-06

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: 43.54  E-value: 4.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608557  38 QLKSrlGDVCLDAP----SGSWfsPLVINPCNGTDF-QRWNLTDDRQVESVAFpgeCVNI---GNALWARLQPCVNWISQ 109
Cdd:cd23441   7 QIKQ--GNLCLDSDeqlfQGPA--LLILAPCSNSSDsQEWSFTKDGQLQTQGL---CLTVdssSKDLPVVLETCSDDPKQ 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15608557 110 HWTVQPDGLV--KSDLdaCLTVLGGPDPGtwVSTrwCDPNAPDQQWD 154
Cdd:cd23441  80 KWTRTGRQLVhsESGL--CLDSRKKKGLV--VSP--CRSGAPSQKWD 120
beta-trefoil_Ricin_AglA cd23425
ricin B-type lectin domain, beta-trefoil fold, found in alpha-galactosidase A (AglA) and ...
 63-153 5.35e-06

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: 43.20  E-value: 5.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608557  63 PCNGTDFQRWNLTDDRQVESVAFPGEC-VNIGNALwaRLQPCVNWISQHWTVQPDG-LVKSDLDACLTVlggpDPGTWVS 140
Cdd:cd23425  27 TCDGSDSQIWQVRKSGILRNLSNTGQClTADGANV--SLSPCDTSTSQNWSYEISGnLVNKKTGLCLTE----GNDAQVT 100

                        90
                ....*....|...
gi 15608557 141 TRWCDPNAPDQQW 153
Cdd:cd23425 101 VTDCGNELDSQVF 113
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
 47-153 1.26e-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: 42.32  E-value: 1.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608557  47 CLDAPSGSWF--SPLVINPCNGTDFQRWNLTDDrqvESVAFPGECVNIGNALWAR-----LQPCVNWISQHWTVQPDGLV 119
Cdd:cd23451  13 CLDVPGSSTAdgNPVQIYTCNGTAAQKWTLGTD---GTLRVLGKCLDVSGGGTANgtlvqLWDCNGTGAQKWVPRADGTL 89

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15608557 120 KSDLDA-CLTVLGG-PDPGTWVSTRWCDpNAPDQQW 153
Cdd:cd23451  90 YNPQSGkCLDAPGGsTTDGTQLQLYTCN-GTAAQQW 124
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 44-154 5.41e-05

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: 5.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608557  44 GDVCLDAPSGSWFSPLVINPCNGTD-FQRWNLTDDRQVESVAFpgeCVNIGNALW---ARLQPCVNWIS-QHWTVQPDG- 117
Cdd:cd23434   8 GNLCLDTLGHKAGGTVGLYPCHGTGgNQEWSFTKDGQIKHDDL---CLTVVDRAPgslVTLQPCREDDSnQKWEQIENNs 84

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15608557 118 -LVKSDLDACLTVLGGPDPGTWVSTrwCDPNAPDQQWD 154
Cdd:cd23434  85 kLRHVGSNLCLDSRNAKSGGLTVET--CDPSSGSQQWK 120
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 44-113 7.73e-05

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: 40.03  E-value: 7.73e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15608557  44 GDVCLDAPSGSWF--SPLVINPCNGTDFQRWNLTDDRQVESVAfPGECVNI---GNALWARLQ--PCVNWISQHWTV 113
Cdd:cd23418  55 GDKCLDAAGGGTTngTPVVIWPCNGGANQKWRFNSDGTIRNVN-SGLCLDVaggGTANGTRLIlwSCNGGSNQRWRR 130
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 33-111 2.12e-04

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


Pssm-ID: 467293 [Multi-domain]  Cd Length: 134  Bit Score: 38.89  E-value: 2.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608557  33 ADGPVQLKSRLGDVCLDAPSGSWF--SPLVINPCNGTDFQRWNLTDDR----QVESVAfPGECVNIGNALWA-----RLQ 101
Cdd:cd00161  46 GDGYYTIRNVASGKCLDVAGGSTAngANVQQWTCNGGDNQQWRLEPVGdgyyRIVNKH-SGKCLDVSGGSTAnganvQQW 124

                        90
                ....*....|
gi 15608557 102 PCVNWISQHW 111
Cdd:cd00161 125 TCNGGANQQW 134
beta-trefoil_Ricin_AH cd23415
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ...
 35-153 1.31e-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: 36.64  E-value: 1.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608557  35 GPVQLKSRLGDVCLDA-PSGSwfspLVINPCNGTDFQRWNLT----DDRQVESVAfPGEC--VNIGNALWARlqPCVNWI 107
Cdd:cd23415   1 GTVRLRNVATGRCLDSnAGGN----VYTGPCNGGPYQRWTWSgvgdGTVTLRNAA-TGRCldSNGNGGVYTL--PCNGGS 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15608557 108 SQHWTVQPDGLVKSDL-----DACLTVlggpDPGTWVSTRWCDPNaPDQQW 153
Cdd:cd23415  74 YQRWRVTSTSGGGVTLrnvatGRCLDS----NGSGGVYTRPCNGG-SYQRW 119
beta-trefoil_Ricin_CRYBG cd23430
ricin B-type lectin domain, beta-trefoil fold, found in the beta/gamma crystallin ...
 108-153 1.53e-03

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: 36.80  E-value: 1.53e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 15608557 108 SQHWTVQpDGLVKSDL--DACLTVLGGPD-PGTWVSTrWCDPNAPDQQW 153
Cdd:cd23430  38 DQIWYYQ-EGLIKCRIaeDCCLTVIGSLVtPGSKVGL-WLEQNADRQFW 84
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 31-72 1.92e-03

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: 36.58  E-value: 1.92e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 15608557  31 ASADGPVQLKSRLGDVCLDAPSGSWFS--PLVINPCNGTDFQRW 72
Cdd:cd00161  91 PVGDGYYRIVNKHSGKCLDVSGGSTANgaNVQQWTCNGGANQQW 134
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 37-153 6.90e-03

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


Pssm-ID: 467338 [Multi-domain]  Cd Length: 121  Bit Score: 34.73  E-value: 6.90e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608557  37 VQLKSRLGDVCLDAPSGSWFSPLV-INPCNGTDF-QRWNLTDDRQVESVAFpgeCVNIGNALWARLQPC-VNWISQHWTV 113
Cdd:cd23460   3 GQIKHTESGLCLDWAGESNGDKTVaLKPCHGGGGnQFWMYTGDGQIRQDHL---CLTADEGNKVTLRECaDQLPSQEWSY 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15608557 114 QPDG--LVKSDLDACLTVLGGPDPGTWVStrwCDPNAPDQQW 153
Cdd:cd23460  80 DEKTgtIRHRSTGLCLTLDANNDVVILKE---CDSNSLWQKW 118
 
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