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Conserved domains on  [gi|18404934|ref|NP_565899|]
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hydroxyproline-rich glycoprotein family protein [Arabidopsis thaliana]

Protein Classification

RICIN domain-containing protein( domain architecture ID 10624646)

RICIN domain-containing protein may have carbohydrate-binding function; similar to Sclerotinia sclerotiorum agglutinin, a lectin that primarily recognizes glycans with a non-reducing terminal N-acetylgalactosamine (GalNAc), with a preference for the alpha- over the beta-anomer

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
beta-trefoil_Ricin_AtEULS3-like cd23431
ricin B-type lectin domain, beta-trefoil fold, found in Arabidopsis thaliana Ricin B-like ...
 165-316 2.25e-84

ricin B-type lectin domain, beta-trefoil fold, found in Arabidopsis thaliana Ricin B-like lectin EULS3 (AtEULS3) and similar proteins; AtEULS3, also called euonymus lectin S3, is a Ricin B-like lectin that binds carbohydrates in vitro. It interacts through its lectin domain with glycan structures containing one or more Lewis X, Lewis Y or lactosamine motifs. It has been implicated in abiotic stress responses, abscisic acid-induced stomatal closure, as well as disease resistance against Pseudomonas syringae through its involvement in stomatal movement. All subfamily members contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.


:

Pssm-ID: 467309  Cd Length: 152  Bit Score: 250.74  E-value: 2.25e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404934 165 GRATVKVYSKAEPNYNLTIRDGKVILAPADPSDEAQHWYKDEKYSTKVKDADGHPCFALVNKATGEAMKHSVGATHPVHL 244
Cdd:cd23431   1 GARTVRIYCKANPGYNLTVRGGGVVLAPADPSDPYQLWFKDESWSTSVTDAEGLPAFALVNKATGQALRHGPGENEQVTL 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18404934 245 IRYVPDKLDESVLWTESKDFGDGYRTIRMVNNTRLNVDAYHGDSKSGGVRDGTTIVLWDWNKGDNQLWKIFP 316
Cdd:cd23431  81 APYNPDKLDNSLLWTESADVGDGYHTIRPVDNTSLNLDALHGDKKHGGVKDGTPVVLFKWHEGDNQLWKLVP 152
dnaA super family cl42516
chromosomal replication initiator protein DnaA;
14-113 4.02e-04

chromosomal replication initiator protein DnaA;


The actual alignment was detected with superfamily member PRK14086:

Pssm-ID: 455861 [Multi-domain]  Cd Length: 617  Bit Score: 42.12  E-value: 4.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404934   14 DDGEDDRQSFGVPPPHVDAPPQPHGLYQSQPHFDPYAPTPQAPAPYRSETQFEPHAPPPYRSEPyfETPAPPPSFGHVSH 93
Cdd:PRK14086 163 DDYGWQQQRLGFPPRAPYASPASYAPEQERDREPYDAGRPEYDQRRRDYDHPRPDWDRPRRDRT--DRPEPPPGAGHVHR 240

                         90       100
                 ....*....|....*....|...
gi 18404934   94 ---VGHQSPNESYPPEHHRYGGY 113
Cdd:PRK14086 241 ggpGPPERDDAPVVPIRPSAPGP 263
 
Name Accession Description Interval E-value
beta-trefoil_Ricin_AtEULS3-like cd23431
ricin B-type lectin domain, beta-trefoil fold, found in Arabidopsis thaliana Ricin B-like ...
 165-316 2.25e-84

ricin B-type lectin domain, beta-trefoil fold, found in Arabidopsis thaliana Ricin B-like lectin EULS3 (AtEULS3) and similar proteins; AtEULS3, also called euonymus lectin S3, is a Ricin B-like lectin that binds carbohydrates in vitro. It interacts through its lectin domain with glycan structures containing one or more Lewis X, Lewis Y or lactosamine motifs. It has been implicated in abiotic stress responses, abscisic acid-induced stomatal closure, as well as disease resistance against Pseudomonas syringae through its involvement in stomatal movement. All subfamily members contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.


Pssm-ID: 467309  Cd Length: 152  Bit Score: 250.74  E-value: 2.25e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404934 165 GRATVKVYSKAEPNYNLTIRDGKVILAPADPSDEAQHWYKDEKYSTKVKDADGHPCFALVNKATGEAMKHSVGATHPVHL 244
Cdd:cd23431   1 GARTVRIYCKANPGYNLTVRGGGVVLAPADPSDPYQLWFKDESWSTSVTDAEGLPAFALVNKATGQALRHGPGENEQVTL 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18404934 245 IRYVPDKLDESVLWTESKDFGDGYRTIRMVNNTRLNVDAYHGDSKSGGVRDGTTIVLWDWNKGDNQLWKIFP 316
Cdd:cd23431  81 APYNPDKLDNSLLWTESADVGDGYHTIRPVDNTSLNLDALHGDKKHGGVKDGTPVVLFKWHEGDNQLWKLVP 152
RicinB_lectin_2 pfam14200
Ricin-type beta-trefoil lectin domain-like;
199-302 3.05e-05

Ricin-type beta-trefoil lectin domain-like;


Pssm-ID: 464102 [Multi-domain]  Cd Length: 89  Bit Score: 41.98  E-value: 3.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404934   199 AQHWYkdekystkVKDADGHPCFALVNKATGEAMKHSVGATHPVHLIRYVPDKLDESVLWTeSKDFGDGYRTIRMVNNTr 278
Cdd:pfam14200   2 NQQWR--------FGGTVGDGYYTIVNVASGKYLDVAGGSTANGANVQQWTDNGNDNQQWR-IVDAGDGYYRIVNKASG- 71

                          90       100
                  ....*....|....*....|....
gi 18404934   279 LNVDAYHGDSksggvrDGTTIVLW 302
Cdd:pfam14200  72 KVLDVAGSTA------NGTNVQQW 89
dnaA PRK14086
chromosomal replication initiator protein DnaA;
14-113 4.02e-04

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 42.12  E-value: 4.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404934   14 DDGEDDRQSFGVPPPHVDAPPQPHGLYQSQPHFDPYAPTPQAPAPYRSETQFEPHAPPPYRSEPyfETPAPPPSFGHVSH 93
Cdd:PRK14086 163 DDYGWQQQRLGFPPRAPYASPASYAPEQERDREPYDAGRPEYDQRRRDYDHPRPDWDRPRRDRT--DRPEPPPGAGHVHR 240

                         90       100
                 ....*....|....*....|...
gi 18404934   94 ---VGHQSPNESYPPEHHRYGGY 113
Cdd:PRK14086 241 ggpGPPERDDAPVVPIRPSAPGP 263
 
Name Accession Description Interval E-value
beta-trefoil_Ricin_AtEULS3-like cd23431
ricin B-type lectin domain, beta-trefoil fold, found in Arabidopsis thaliana Ricin B-like ...
 165-316 2.25e-84

ricin B-type lectin domain, beta-trefoil fold, found in Arabidopsis thaliana Ricin B-like lectin EULS3 (AtEULS3) and similar proteins; AtEULS3, also called euonymus lectin S3, is a Ricin B-like lectin that binds carbohydrates in vitro. It interacts through its lectin domain with glycan structures containing one or more Lewis X, Lewis Y or lactosamine motifs. It has been implicated in abiotic stress responses, abscisic acid-induced stomatal closure, as well as disease resistance against Pseudomonas syringae through its involvement in stomatal movement. All subfamily members contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.


Pssm-ID: 467309  Cd Length: 152  Bit Score: 250.74  E-value: 2.25e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404934 165 GRATVKVYSKAEPNYNLTIRDGKVILAPADPSDEAQHWYKDEKYSTKVKDADGHPCFALVNKATGEAMKHSVGATHPVHL 244
Cdd:cd23431   1 GARTVRIYCKANPGYNLTVRGGGVVLAPADPSDPYQLWFKDESWSTSVTDAEGLPAFALVNKATGQALRHGPGENEQVTL 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18404934 245 IRYVPDKLDESVLWTESKDFGDGYRTIRMVNNTRLNVDAYHGDSKSGGVRDGTTIVLWDWNKGDNQLWKIFP 316
Cdd:cd23431  81 APYNPDKLDNSLLWTESADVGDGYHTIRPVDNTSLNLDALHGDKKHGGVKDGTPVVLFKWHEGDNQLWKLVP 152
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 167-312 7.67e-06

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: 44.67  E-value: 7.67e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404934 167 ATVKVYSKAePNYNLTIRDG------KVILAPADPSDeAQHWYKDekystkvkdADGHPCFALVNKATGEAM---KHSVG 237
Cdd:cd00161   1 GTYRIVNAA-SGKCLDVAGGstangaPVQQWTCNGGA-NQQWTLT---------PVGDGYYTIRNVASGKCLdvaGGSTA 69

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18404934 238 ATHPVHLiryVPDKLDESVLWTESkDFGDGYRTIRMVNNTR-LNVDayhgdskSGGVRDGTTIVLWDWNKGDNQLW 312
Cdd:cd00161  70 NGANVQQ---WTCNGGDNQQWRLE-PVGDGYYRIVNKHSGKcLDVS-------GGSTANGANVQQWTCNGGANQQW 134
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 265-316 1.18e-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: 44.28  E-value: 1.18e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 18404934 265 GDGYRTIRMVNNTR-LNVDayhgdskSGGVRDGTTIVLWDWNKGDNQLWKIFP 316
Cdd:cd00161  46 GDGYYTIRNVASGKcLDVA-------GGSTANGANVQQWTCNGGDNQQWRLEP 91
beta-trefoil_Ricin_EW29-like cd23449
ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa ...
 187-314 1.50e-05

ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa galactose-binding lectin (EW29) and similar proteins; EW29 is a galactose-binding lectin from the earthworm Lumbricus terrestris. It contains two ricin B-type lectin domains with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The second ricin B-type lectin domain may harbor two sugar-binding pockets in subdomains alpha and gamma. EW29 uses these two sugar-binding sites for its function as a single domain-type hemagglutinin.


Pssm-ID: 467327 [Multi-domain]  Cd Length: 128  Bit Score: 43.82  E-value: 1.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404934 187 KVILAPADPSDEA-QHWYKDEKYST---KVKDadghpcFALVnkatgeamkhsvgATHPVHLI--RYVPDKldESVLWTE 260
Cdd:cd23449  26 KVIMWEKKGGAEDnQLWYEDEVTGTirsKLND------FCLD-------------ASGDKGLIlnPYDPSN--PKQQWKI 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 18404934 261 SKDfgdgyrTIRMVNNTRLNVDAYHGDSKsggvrDGTTIVLWDWNKGDNQLWKI 314
Cdd:cd23449  85 SGN------KIQNRSNPDNVLDIKGGSKD-----DGARLCAWEYNGGPNQLWDF 127
beta-trefoil_Ricin_1,3Gal43A cd23446
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and ...
 263-314 2.49e-05

ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and similar proteins; 1,3Gal43A is an exo-beta-1,3-galactanase that specifically hydrolyses beta-1,3 glycosidic bonds in galactose-based oligosaccharides or polysaccharides, and shows maximum activity towards beta-1,3-galactotetraose. 1,3Gal43A consists of a glycoside hydrolase family 43 (GH43) catalytic domain, a CBM13 carbohydrate binding domain, and a type I dockerin domain. The CBM13 domain is also known as the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467324 [Multi-domain]  Cd Length: 137  Bit Score: 43.52  E-value: 2.49e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 18404934 263 DFGDGYRTIRMVNNTR-LNVDayhGDSKSggvrDGTTIVLWDWNKGDNQLWKI 314
Cdd:cd23446  44 DVGGGYYKIVNRNSGKaLDVN---GASTA----DGAAIIQWTSNGGDNQQWQI 89
RicinB_lectin_2 pfam14200
Ricin-type beta-trefoil lectin domain-like;
199-302 3.05e-05

Ricin-type beta-trefoil lectin domain-like;


Pssm-ID: 464102 [Multi-domain]  Cd Length: 89  Bit Score: 41.98  E-value: 3.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404934   199 AQHWYkdekystkVKDADGHPCFALVNKATGEAMKHSVGATHPVHLIRYVPDKLDESVLWTeSKDFGDGYRTIRMVNNTr 278
Cdd:pfam14200   2 NQQWR--------FGGTVGDGYYTIVNVASGKYLDVAGGSTANGANVQQWTDNGNDNQQWR-IVDAGDGYYRIVNKASG- 71

                          90       100
                  ....*....|....*....|....
gi 18404934   279 LNVDAYHGDSksggvrDGTTIVLW 302
Cdd:pfam14200  72 KVLDVAGSTA------NGTNVQQW 89
beta-trefoil_Ricin_HA17-like cd23445
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium botulinum hemagglutinating ...
 262-314 4.91e-05

ricin B-type lectin domain, beta-trefoil fold, found in Clostridium botulinum hemagglutinating proteins, HA17 and HA33, and similar proteins; The subfamily includes Clostridium botulinum hemagglutinating proteins HA17 and HA33, Lysinibacillus sphaericus mosquitocidal toxin (MTX) and Pieris brassicae pierisin. The hemagglutinin (HA) component of the progenitor toxin protects the structural integrity of the neurotoxin. It may increase internalization of the neurotoxin into the bloodstream of the host. The hemagglutinin complex, composed of HA-70 (also known as HA3), HA-33 (also known as HA1) and HA-17 (also known as HA2), agglutinates erythrocytes, whereas the individual components do not. HA-33 is involved in recognition of cell-surface carbohydrates. HA-17 and HA-70 are involved in paracellular barrier disruption by E-cadherin binding. MTX acts as an ADP-ribosyl transferase. Pierisin, also called NAD--DNA ADP-ribosyltransferase, pierisin-2, or pierisin-B, catalyzes the ADP ribosylation of double-stranded DNA by targeting the N2 amino group of dG residues. It induces apoptosis in a range of human cell lines. Members of this subfamily contain at least one ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467323 [Multi-domain]  Cd Length: 133  Bit Score: 42.31  E-value: 4.91e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 18404934 262 KDFGDGYRTIRMVNNTRLNVDAYhgdskSGGVRDGTTIVLWDWNKGDNQLWKI 314
Cdd:cd23445  86 EEAGDGYYIIKNYADPNLVLDVE-----GSNTANGTNIIVYPRNGSNNQKFKL 133
RicinB_lectin_2 pfam14200
Ricin-type beta-trefoil lectin domain-like;
257-316 1.84e-04

Ricin-type beta-trefoil lectin domain-like;


Pssm-ID: 464102 [Multi-domain]  Cd Length: 89  Bit Score: 39.67  E-value: 1.84e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18404934   257 LWTESKDFGDGYRTIRMVN-NTRLNVDAyhgdsksGGVRDGTTIVLWDWNKGDNQLWKIFP 316
Cdd:pfam14200   4 QWRFGGTVGDGYYTIVNVAsGKYLDVAG-------GSTANGANVQQWTDNGNDNQQWRIVD 57
dnaA PRK14086
chromosomal replication initiator protein DnaA;
14-113 4.02e-04

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 42.12  E-value: 4.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404934   14 DDGEDDRQSFGVPPPHVDAPPQPHGLYQSQPHFDPYAPTPQAPAPYRSETQFEPHAPPPYRSEPyfETPAPPPSFGHVSH 93
Cdd:PRK14086 163 DDYGWQQQRLGFPPRAPYASPASYAPEQERDREPYDAGRPEYDQRRRDYDHPRPDWDRPRRDRT--DRPEPPPGAGHVHR 240

                         90       100
                 ....*....|....*....|...
gi 18404934   94 ---VGHQSPNESYPPEHHRYGGY 113
Cdd:PRK14086 241 ggpGPPERDDAPVVPIRPSAPGP 263
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 287-316 5.27e-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: 39.28  E-value: 5.27e-04
                        10        20        30
                ....*....|....*....|....*....|
gi 18404934 287 DSKSGGVRDGTTIVLWDWNKGDNQLWKIFP 316
Cdd:cd00161  15 DVAGGSTANGAPVQQWTCNGGANQQWTLTP 44
PHA03247 PHA03247
large tegument protein UL36; Provisional
 21-105 5.32e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 5.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404934    21 QSFGVPPPHVDAPPQPHGLYQSQPHFDPYA---PTPQAPAPYRSETQFEPHAPPPYRSEPyfETPAPPPSFGHVSHVGHQ 97
Cdd:PHA03247 2896 ESFALPPDQPERPPQPQAPPPPQPQPQPPPppqPQPPPPPPPRPQPPLAPTTDPAGAGEP--SGAVPQPWLGALVPGRVA 2973


                  ....*...
gi 18404934    98 SPNESYPP 105
Cdd:PHA03247 2974 VPRFRVPQ 2981
beta-trefoil_Ricin_1,3Gal43A cd23446
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and ...
 221-314 5.48e-04

ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and similar proteins; 1,3Gal43A is an exo-beta-1,3-galactanase that specifically hydrolyses beta-1,3 glycosidic bonds in galactose-based oligosaccharides or polysaccharides, and shows maximum activity towards beta-1,3-galactotetraose. 1,3Gal43A consists of a glycoside hydrolase family 43 (GH43) catalytic domain, a CBM13 carbohydrate binding domain, and a type I dockerin domain. The CBM13 domain is also known as the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467324 [Multi-domain]  Cd Length: 137  Bit Score: 39.29  E-value: 5.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404934 221 FALVNKATGEAMKHSVGATHP-VHLIRYvPDKLDESVLWtESKDFGDGYRTIRMVNNTRLNvdayhgDSKSGGVRDGTTI 299
Cdd:cd23446  50 YKIVNRNSGKALDVNGASTADgAAIIQW-TSNGGDNQQW-QIVDTGDGYYKIVNRNSGKLL------DVNGWSTADGADI 121

                        90
                ....*....|....*
gi 18404934 300 VLWDWNKGDNQLWKI 314
Cdd:cd23446 122 IQWSDNGGTNQQWQL 136
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 287-312 1.06e-03

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


Pssm-ID: 467297 [Multi-domain]  Cd Length: 130  Bit Score: 38.48  E-value: 1.06e-03
                        10        20
                ....*....|....*....|....*.
gi 18404934 287 DSKSGGVRDGTTIVLWDWNKGDNQLW 312
Cdd:cd23418 103 DVAGGGTANGTRLILWSCNGGSNQRW 128
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 33-138 3.10e-03

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 39.29  E-value: 3.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404934    33 PPQPHGLYQSQPHFD-PYAPTPQAPAPYRSEtqfePHAPPPYRSEPYFETPAPPPSFGHVShvghQSPNESYPPEHH--- 108
Cdd:PTZ00395  417 PGNSNPGYNNAPNSNtPYNNPPNSNTPYSNP----PNSNPPYSNLPYSNTPYSNAPLSNAP----PSSAKDHHSAYHaay 488

                          90       100       110
                  ....*....|....*....|....*....|
gi 18404934   109 RYGGYQQPSNSLLESHGDHSGVTHVAHHSS 138
Cdd:PTZ00395  489 QHRAANQPAANLPTANQPAANNFHGAAGNS 518
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 266-316 5.42e-03

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


Pssm-ID: 467297 [Multi-domain]  Cd Length: 130  Bit Score: 36.56  E-value: 5.42e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 18404934 266 DGYRTIRMvnNTRLNVDAyhgdsKSGGVRDGTTIVLWDWNKGDNQLWKIFP 316
Cdd:cd23418  46 TSAGELRV--GGDKCLDA-----AGGGTTNGTPVVIWPCNGGANQKWRFNS 89
beta-trefoil_Ricin_SCDase cd23456
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ...
 197-312 6.36e-03

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


Pssm-ID: 467334 [Multi-domain]  Cd Length: 122  Bit Score: 36.18  E-value: 6.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404934 197 DEAQHWYKDEKYSTKVKdADGHPCFAlvnkATGEAMKHSvgathpvhliryvpdKLdesVLWTESK------DFGDGYrt 270
Cdd:cd23456  34 SNSQKWYYDATGRLHSK-ANPGKCLD----AGGENSNGA---------------NV---VLWACNDsanqrwDFDGNF-- 88

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 18404934 271 IRMVNNTRLNVDAYhgdsksggVRDGTTIVLWDWNKGDNQLW 312
Cdd:cd23456  89 IRSRNNTNLALDAY--------GSQGSNVGLWQFHGGANQQW 122
 
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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