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Conserved domains on  [gi|1577429051|ref|NP_777273|]
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beta/gamma crystallin domain-containing protein 3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_Ricin_vlAKAP cd23463
ricin B-type lectin domain, beta-trefoil fold, found in very large A-kinase anchor protein ...
 2817-2952 2.11e-81

ricin B-type lectin domain, beta-trefoil fold, found in very large A-kinase anchor protein (vlAKAP) and similar proteins; vlAKAP, also called beta/gamma crystallin domain-containing protein 3 (CRYBG3), is an anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA). It binds to the dimeric RII-alpha regulatory subunit of PKA (PRKAR2A/PRKAR2B). vlAKAP belongs to the beta/gamma-crystallin family. It contains a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.


:

Pssm-ID: 467341  Cd Length: 136  Bit Score: 264.30  E-value: 2.11e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2817 QPAVYIRIRNRAQDEYLTVTGNPADARTMSVCISPYSGKDTQIWHYCRGLFKSKASHTCLDVIGGRDTPGAKVALWTEHG 2896
Cdd:cd23463      1 QPRVYLRIKNRAQGLYLTTEGNLADPRATSVCVSQYNGKDTQIWYYCRGLLKSKANDACLDVIGGKDNPGSKVALWTEHG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1577429051 2897 QLRQKWRMSRNGTISSYLSDELVLDVKGGNYYDKTHVIVNQPLEGEETQKWDIEIL 2952
Cdd:cd23463     81 KTHQKWRINEDGTISSHLSDDLVLDLKGGNYYDKDHLIVNNPEEDQQTQKWDIELL 136
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2460-2543 9.46e-27

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


:

Pssm-ID: 459639  Cd Length: 82  Bit Score: 105.65  E-value: 9.46e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2460 KVILYEKPHFLGHTKEFSEHIDSVPTFLKSDKdfhgIGSIRVIGGVWVAYEKEHFKGQQFLLEEGDFEDSSACGALSGPI 2539
Cdd:pfam00030    1 KIVLYEKENFQGRSIELTDDCPSLQERGFNSR----VNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDRI 76


                   ....
gi 1577429051 2540 MSFR 2543
Cdd:pfam00030   77 GSLR 80
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2553-2636 6.48e-26

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


:

Pssm-ID: 459639  Cd Length: 82  Bit Score: 103.34  E-value: 6.48e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2553 SITLFESSHLEsGKFIDITnQEISDLEEIGFGSETRSIHVKSGVWVAYHQKFFCGDQYILEKGKYKCFFDWGGSSNTILS 2632
Cdd:pfam00030    1 KIVLYEKENFQ-GRSIELT-DDCPSLQERGFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDRIGS 78


                   ....
gi 1577429051 2633 IRPI 2636
Cdd:pfam00030   79 LRPI 82
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2653-2727 5.50e-22

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


:

Pssm-ID: 459639  Cd Length: 82  Bit Score: 92.17  E-value: 5.50e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1577429051 2653 FSKAGFQGECIDFVKECADLTS--FTP--ASFKVLRGCWLLlYYQEDGFYHQCVLEEGLYVDLTSCGCPSARIRALQPI 2727
Cdd:pfam00030    5 YEKENFQGRSIELTDDCPSLQErgFNSrvNSIRVLSGAWVL-YEHPNFRGRQYVLEPGEYPDWSDWGAPNDRIGSLRPI 82
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2735-2815 4.26e-20

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


:

Pssm-ID: 459639  Cd Length: 82  Bit Score: 86.78  E-value: 4.26e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2735 SISLFALEHCEGRELHLEDAVNSVLNKDLHFYTQSVWIKSGLWIAYEGSNFLGRQILLTPKEIPNWTAFSG-WKTIGSVR 2813
Cdd:pfam00030    1 KIVLYEKENFQGRSIELTDDCPSLQERGFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGApNDRIGSLR 80


                   ..
gi 1577429051 2814 PM 2815
Cdd:pfam00030   81 PI 82
Crystall super family cl02528
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2276-2362 1.03e-10

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


The actual alignment was detected with superfamily member pfam00030:

Pssm-ID: 470604  Cd Length: 82  Bit Score: 60.20  E-value: 1.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2276 KMIIY---DLHGSKYkqEVYCNIPDATTWSFPNGAL-IKVVRGCWILYEKPHFQGQKCVLEEGERVLDRDWLLQNRKhpe 2351
Cdd:pfam00030    1 KIVLYekeNFQGRSI--ELTDDCPSLQERGFNSRVNsIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDR--- 75

                           90
                   ....*....|.
gi 1577429051 2352 rnfvLGSIKRV 2362
Cdd:pfam00030   76 ----IGSLRPI 82
 
Name Accession Description Interval E-value
beta-trefoil_Ricin_vlAKAP cd23463
ricin B-type lectin domain, beta-trefoil fold, found in very large A-kinase anchor protein ...
 2817-2952 2.11e-81

ricin B-type lectin domain, beta-trefoil fold, found in very large A-kinase anchor protein (vlAKAP) and similar proteins; vlAKAP, also called beta/gamma crystallin domain-containing protein 3 (CRYBG3), is an anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA). It binds to the dimeric RII-alpha regulatory subunit of PKA (PRKAR2A/PRKAR2B). vlAKAP belongs to the beta/gamma-crystallin family. It contains a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.


Pssm-ID: 467341  Cd Length: 136  Bit Score: 264.30  E-value: 2.11e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2817 QPAVYIRIRNRAQDEYLTVTGNPADARTMSVCISPYSGKDTQIWHYCRGLFKSKASHTCLDVIGGRDTPGAKVALWTEHG 2896
Cdd:cd23463      1 QPRVYLRIKNRAQGLYLTTEGNLADPRATSVCVSQYNGKDTQIWYYCRGLLKSKANDACLDVIGGKDNPGSKVALWTEHG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1577429051 2897 QLRQKWRMSRNGTISSYLSDELVLDVKGGNYYDKTHVIVNQPLEGEETQKWDIEIL 2952
Cdd:cd23463     81 KTHQKWRINEDGTISSHLSDDLVLDLKGGNYYDKDHLIVNNPEEDQQTQKWDIELL 136
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2460-2543 9.46e-27

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


Pssm-ID: 459639  Cd Length: 82  Bit Score: 105.65  E-value: 9.46e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2460 KVILYEKPHFLGHTKEFSEHIDSVPTFLKSDKdfhgIGSIRVIGGVWVAYEKEHFKGQQFLLEEGDFEDSSACGALSGPI 2539
Cdd:pfam00030    1 KIVLYEKENFQGRSIELTDDCPSLQERGFNSR----VNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDRI 76


                   ....
gi 1577429051 2540 MSFR 2543
Cdd:pfam00030   77 GSLR 80
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2553-2636 6.48e-26

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


Pssm-ID: 459639  Cd Length: 82  Bit Score: 103.34  E-value: 6.48e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2553 SITLFESSHLEsGKFIDITnQEISDLEEIGFGSETRSIHVKSGVWVAYHQKFFCGDQYILEKGKYKCFFDWGGSSNTILS 2632
Cdd:pfam00030    1 KIVLYEKENFQ-GRSIELT-DDCPSLQERGFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDRIGS 78


                   ....
gi 1577429051 2633 IRPI 2636
Cdd:pfam00030   79 LRPI 82
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2653-2727 5.50e-22

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


Pssm-ID: 459639  Cd Length: 82  Bit Score: 92.17  E-value: 5.50e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1577429051 2653 FSKAGFQGECIDFVKECADLTS--FTP--ASFKVLRGCWLLlYYQEDGFYHQCVLEEGLYVDLTSCGCPSARIRALQPI 2727
Cdd:pfam00030    5 YEKENFQGRSIELTDDCPSLQErgFNSrvNSIRVLSGAWVL-YEHPNFRGRQYVLEPGEYPDWSDWGAPNDRIGSLRPI 82
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2735-2815 4.26e-20

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


Pssm-ID: 459639  Cd Length: 82  Bit Score: 86.78  E-value: 4.26e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2735 SISLFALEHCEGRELHLEDAVNSVLNKDLHFYTQSVWIKSGLWIAYEGSNFLGRQILLTPKEIPNWTAFSG-WKTIGSVR 2813
Cdd:pfam00030    1 KIVLYEKENFQGRSIELTDDCPSLQERGFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGApNDRIGSLR 80


                   ..
gi 1577429051 2814 PM 2815
Cdd:pfam00030   81 PI 82
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
2821-2947 1.24e-18

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 84.12  E-value: 1.24e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2821 YIRIRNRAQDEYLTVTGNPADARTmsVCISPYSGKDT-QIW-HYCRGLFKSKASHTCLDVigGRDTPGAKVALWTEH-GQ 2897
Cdd:pfam00652    2 TGRIRNRASGKCLDVPGGSSAGGP--VGLYPCHGSNGnQLWtLTGDGTIRSVASDLCLDV--GSTADGAKVVLWPCHpGN 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1577429051 2898 LRQKWRMSRNGT-ISSYLSDeLVLDVKGGNyYDKTHVIVNQPLEGEETQKW 2947
Cdd:pfam00652   78 GNQRWRYDEDGTqIRNPQSG-KCLDVSGAG-TSNGKVILWTCDSGNPNQQW 126
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 2460-2543 2.47e-18

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 81.79  E-value: 2.47e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051  2460 KVILYEKPHFLGHTKEFSEHIDSVPTFLKSDKdfhgIGSIRVIGGVWVAYEKEHFKGQQFLLEEGDFEDSSACGALSGPI 2539
Cdd:smart00247    1 KITLYEDENFQGRSYELSDDCPSLQDYGSRDN----VSSVRVESGCWVLYEQPNYRGRQYVLEPGEYPDYQEWGGFNDQI 76


                    ....
gi 1577429051  2540 MSFR 2543
Cdd:smart00247   77 SSIR 80
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 2554-2636 2.59e-18

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 81.79  E-value: 2.59e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051  2554 ITLFESSHLeSGKFIDITNqEISDLEEIGFGSETRSIHVKSGVWVAYHQKFFCGDQYILEKGKYKCFFDWGGSSNTILSI 2633
Cdd:smart00247    2 ITLYEDENF-QGRSYELSD-DCPSLQDYGSRDNVSSVRVESGCWVLYEQPNYRGRQYVLEPGEYPDYQEWGGFNDQISSI 79


                    ...
gi 1577429051  2634 RPI 2636
Cdd:smart00247   80 RRI 82
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2276-2362 1.03e-10

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


Pssm-ID: 459639  Cd Length: 82  Bit Score: 60.20  E-value: 1.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2276 KMIIY---DLHGSKYkqEVYCNIPDATTWSFPNGAL-IKVVRGCWILYEKPHFQGQKCVLEEGERVLDRDWLLQNRKhpe 2351
Cdd:pfam00030    1 KIVLYekeNFQGRSI--ELTDDCPSLQERGFNSRVNsIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDR--- 75

                           90
                   ....*....|.
gi 1577429051 2352 rnfvLGSIKRV 2362
Cdd:pfam00030   76 ----IGSLRPI 82
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 2824-2950 3.30e-10

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 59.83  E-value: 3.30e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051  2824 IRNRAQDEYLTVTGNPADARTMSvCISPysgKDTQIWHY-CRGLFKSKASHTCLDVIGGRDTPgakVALWTEHGQ-LRQK 2901
Cdd:smart00458    1 IISGNTGKCLDVNGNKNPVGLFD-CHGT---GGNQLWKLtSDGAIRIKDTDLCLTANGNTGST---VTLYSCDGTnDNQY 73

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 1577429051  2902 WRMSRNGTISSYLSDeLVLDVKGGNyyDKTHVIVNQPlEGEETQKWDIE 2950
Cdd:smart00458   74 WEVNKDGTIRNPDSG-KCLDVKDGN--TGTKVILWTC-SGNPNQKWIFE 118
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 2653-2727 8.17e-10

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 57.52  E-value: 8.17e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051  2653 FSKAGFQGECIDFVKECADLTSF----TPASFKVLRGCWLLlyYQEDGFY-HQCVLEEGLYVDLTSCGCPSARIRALQPI 2727
Cdd:smart00247    5 YEDENFQGRSYELSDDCPSLQDYgsrdNVSSVRVESGCWVL--YEQPNYRgRQYVLEPGEYPDYQEWGGFNDQISSIRRI 82
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 2276-2362 6.17e-09

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 55.21  E-value: 6.17e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051  2276 KMIIYDLHGSKYKQ----EVYCNIPDatTWSFPNGALIKVVRGCWILYEKPHFQGQKCVLEEGERVLDRDWLLQNRKhpe 2351
Cdd:smart00247    1 KITLYEDENFQGRSyelsDDCPSLQD--YGSRDNVSSVRVESGCWVLYEQPNYRGRQYVLEPGEYPDYQEWGGFNDQ--- 75

                            90
                    ....*....|.
gi 1577429051  2352 rnfvLGSIKRV 2362
Cdd:smart00247   76 ----ISSIRRI 82
lectin_2 NF035930
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
 2875-2947 1.31e-08

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


Pssm-ID: 468267 [Multi-domain]  Cd Length: 238  Bit Score: 58.26  E-value: 1.31e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1577429051 2875 CLDVIGGRDTPGAKVALWTEHGQLRQKWRmSRNGTISSYLSDElVLDVKGGNYYDKTHVIVnQPLEGEETQKW 2947
Cdd:NF035930   169 CLDVADGNTRDGARVIAWSCSGGPNQRWR-WRGGQIRSRLSGK-CLDIEGGRARPGQPVIV-WSCNGGPNQRW 238
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 2767-2815 1.82e-06

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 47.89  E-value: 1.82e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1577429051  2767 TQSVWIKSGLWIAYEGSNFLGRQILLTPKEIPNWTAFSGWK-TIGSVRPM 2815
Cdd:smart00247   33 VSSVRVESGCWVLYEQPNYRGRQYVLEPGEYPDYQEWGGFNdQISSIRRI 82
lectin_2 NF035930
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
 2837-2902 1.49e-04

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


Pssm-ID: 468267 [Multi-domain]  Cd Length: 238  Bit Score: 45.93  E-value: 1.49e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1577429051 2837 GNPAD-ARTMSVcisPYSGKDTQIWHYCRGLFKSKASHTCLDVIGGRDTPGAKVALWTEHGQLRQKW 2902
Cdd:NF035930   175 GNTRDgARVIAW---SCSGGPNQRWRWRGGQIRSRLSGKCLDIEGGRARPGQPVIVWSCNGGPNQRW 238
 
Name Accession Description Interval E-value
beta-trefoil_Ricin_vlAKAP cd23463
ricin B-type lectin domain, beta-trefoil fold, found in very large A-kinase anchor protein ...
 2817-2952 2.11e-81

ricin B-type lectin domain, beta-trefoil fold, found in very large A-kinase anchor protein (vlAKAP) and similar proteins; vlAKAP, also called beta/gamma crystallin domain-containing protein 3 (CRYBG3), is an anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA). It binds to the dimeric RII-alpha regulatory subunit of PKA (PRKAR2A/PRKAR2B). vlAKAP belongs to the beta/gamma-crystallin family. It contains a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.


Pssm-ID: 467341  Cd Length: 136  Bit Score: 264.30  E-value: 2.11e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2817 QPAVYIRIRNRAQDEYLTVTGNPADARTMSVCISPYSGKDTQIWHYCRGLFKSKASHTCLDVIGGRDTPGAKVALWTEHG 2896
Cdd:cd23463      1 QPRVYLRIKNRAQGLYLTTEGNLADPRATSVCVSQYNGKDTQIWYYCRGLLKSKANDACLDVIGGKDNPGSKVALWTEHG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1577429051 2897 QLRQKWRMSRNGTISSYLSDELVLDVKGGNYYDKTHVIVNQPLEGEETQKWDIEIL 2952
Cdd:cd23463     81 KTHQKWRINEDGTISSHLSDDLVLDLKGGNYYDKDHLIVNNPEEDQQTQKWDIELL 136
beta-trefoil_Ricin_CRYBG cd23430
ricin B-type lectin domain, beta-trefoil fold, found in the beta/gamma crystallin ...
 2820-2951 3.77e-69

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: 229.01  E-value: 3.77e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2820 VYIRIRNRAQDEYLTVTGNPADARTMSVCISPYSGKDTQIWHYCRGLFKSK-ASHTCLDVIGGRDTPGAKVALWTEHGQL 2898
Cdd:cd23430      1 VYFRLRNKATGLFLSVNGNLEDLKLLRVQVMPDVGADDQIWYYQEGLIKCRiAEDCCLTVIGSLVTPGSKVGLWLEQNAD 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1577429051 2899 RQKWRMSRNGTISSYLSDELVLDVKGGNYYDKTHVIVNQPLEGEETQKWDIEI 2951
Cdd:cd23430     81 RQFWSLKSDGRIYSKLKPNLVLDVKGGTQYDQNHVILNTPSEEKFTQVWEIMV 133
beta-trefoil_Ricin_CRYBG1 cd23464
ricin B-type lectin domain, beta-trefoil fold, found in beta/gamma crystallin ...
 2817-2952 1.07e-28

ricin B-type lectin domain, beta-trefoil fold, found in beta/gamma crystallin domain-containing protein 1 (CRYBG1) and similar proteins; 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. CRYBG1 belongs to the beta/gamma-crystallin family. It contains a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.


Pssm-ID: 467342  Cd Length: 137  Bit Score: 113.36  E-value: 1.07e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2817 QPAVYIRIRNRAQDEYLTVTGNPADARTMSVCISPYSGKDTQIWHYCRGLFKSK-ASHTCLDVIGGRDTPGAKVALWTEH 2895
Cdd:cd23464      1 QKRVYFRLRNKETGCFMSTNGNLDDLKLLRIQVLEDTGSDDQIWVYQDGLIRCRmAEDCCLETVGNLVTAGSKLGLSLEQ 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1577429051 2896 GQLRQKWRMSRNGTISSYLSDELVLDVKGGNYYDKTHVIVNQPLEGEETQKWDIEIL 2952
Cdd:cd23464     81 GKDNQFWSITSDGRIYSKLKPDLVLDIKGGQQYDQNHVILNTFDEEKLTQRWEVEIL 137
beta-trefoil_Ricin_CRYBG2 cd23465
ricin B-type lectin domain, beta-trefoil fold, found in beta/gamma crystallin ...
 2817-2952 2.13e-28

ricin B-type lectin domain, beta-trefoil fold, found in beta/gamma crystallin domain-containing protein 2 (CRYBG2) and similar proteins; CRYBG2, also called absent in melanoma 1-like protein (AIM1L), is a beta/gamma-crystallin family protein with 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: 467343  Cd Length: 136  Bit Score: 112.65  E-value: 2.13e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2817 QPAVYIRIRNRAQDEYLTVTGNPADARTMSVCISPYSGKDTQIWHYCRGLFKSK-ASHTCLDVIGGRDtPGAKVALWTEH 2895
Cdd:cd23465      1 QRRVYFRLRNRELGLYLAVPDGVEDMKAGRVVVTEQQEGMSHVWFYEDGLLKNQmAPTMSLQVIGPPD-NGAKVVLWSET 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1577429051 2896 GQLRQKWRMSRNGTISSYLSDELVLDVKGGNYYDKTHVIVNQPLEGEETQKWDIEIL 2952
Cdd:cd23465     80 RQPRQTWSIQPSGHILSQMFEGMILDVKGGRTYDRDHVVLWEVSEERPSQIWDMEVL 136
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2460-2543 9.46e-27

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


Pssm-ID: 459639  Cd Length: 82  Bit Score: 105.65  E-value: 9.46e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2460 KVILYEKPHFLGHTKEFSEHIDSVPTFLKSDKdfhgIGSIRVIGGVWVAYEKEHFKGQQFLLEEGDFEDSSACGALSGPI 2539
Cdd:pfam00030    1 KIVLYEKENFQGRSIELTDDCPSLQERGFNSR----VNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDRI 76


                   ....
gi 1577429051 2540 MSFR 2543
Cdd:pfam00030   77 GSLR 80
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2553-2636 6.48e-26

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


Pssm-ID: 459639  Cd Length: 82  Bit Score: 103.34  E-value: 6.48e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2553 SITLFESSHLEsGKFIDITnQEISDLEEIGFGSETRSIHVKSGVWVAYHQKFFCGDQYILEKGKYKCFFDWGGSSNTILS 2632
Cdd:pfam00030    1 KIVLYEKENFQ-GRSIELT-DDCPSLQERGFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDRIGS 78


                   ....
gi 1577429051 2633 IRPI 2636
Cdd:pfam00030   79 LRPI 82
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2653-2727 5.50e-22

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


Pssm-ID: 459639  Cd Length: 82  Bit Score: 92.17  E-value: 5.50e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1577429051 2653 FSKAGFQGECIDFVKECADLTS--FTP--ASFKVLRGCWLLlYYQEDGFYHQCVLEEGLYVDLTSCGCPSARIRALQPI 2727
Cdd:pfam00030    5 YEKENFQGRSIELTDDCPSLQErgFNSrvNSIRVLSGAWVL-YEHPNFRGRQYVLEPGEYPDWSDWGAPNDRIGSLRPI 82
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2735-2815 4.26e-20

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


Pssm-ID: 459639  Cd Length: 82  Bit Score: 86.78  E-value: 4.26e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2735 SISLFALEHCEGRELHLEDAVNSVLNKDLHFYTQSVWIKSGLWIAYEGSNFLGRQILLTPKEIPNWTAFSG-WKTIGSVR 2813
Cdd:pfam00030    1 KIVLYEKENFQGRSIELTDDCPSLQERGFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGApNDRIGSLR 80


                   ..
gi 1577429051 2814 PM 2815
Cdd:pfam00030   81 PI 82
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 2821-2947 1.22e-18

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: 84.34  E-value: 1.22e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2821 YIRIRNRAQDEYLTVTGNPADARTmSVCISPYSGKDTQIWHY-----CRGLFKSKASHTCLDVIGGRDTPGAKVALWTEH 2895
Cdd:cd00161      2 TYRIVNAASGKCLDVAGGSTANGA-PVQQWTCNGGANQQWTLtpvgdGYYTIRNVASGKCLDVAGGSTANGANVQQWTCN 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1577429051 2896 GQLRQKWRMSRNG----TISSYLSDeLVLDVKGGNYYDKTHVIVnQPLEGEETQKW 2947
Cdd:cd00161     81 GGDNQQWRLEPVGdgyyRIVNKHSG-KCLDVSGGSTANGANVQQ-WTCNGGANQQW 134
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
2821-2947 1.24e-18

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 84.12  E-value: 1.24e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2821 YIRIRNRAQDEYLTVTGNPADARTmsVCISPYSGKDT-QIW-HYCRGLFKSKASHTCLDVigGRDTPGAKVALWTEH-GQ 2897
Cdd:pfam00652    2 TGRIRNRASGKCLDVPGGSSAGGP--VGLYPCHGSNGnQLWtLTGDGTIRSVASDLCLDV--GSTADGAKVVLWPCHpGN 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1577429051 2898 LRQKWRMSRNGT-ISSYLSDeLVLDVKGGNyYDKTHVIVNQPLEGEETQKW 2947
Cdd:pfam00652   78 GNQRWRYDEDGTqIRNPQSG-KCLDVSGAG-TSNGKVILWTCDSGNPNQQW 126
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 2460-2543 2.47e-18

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 81.79  E-value: 2.47e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051  2460 KVILYEKPHFLGHTKEFSEHIDSVPTFLKSDKdfhgIGSIRVIGGVWVAYEKEHFKGQQFLLEEGDFEDSSACGALSGPI 2539
Cdd:smart00247    1 KITLYEDENFQGRSYELSDDCPSLQDYGSRDN----VSSVRVESGCWVLYEQPNYRGRQYVLEPGEYPDYQEWGGFNDQI 76


                    ....
gi 1577429051  2540 MSFR 2543
Cdd:smart00247   77 SSIR 80
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 2554-2636 2.59e-18

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 81.79  E-value: 2.59e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051  2554 ITLFESSHLeSGKFIDITNqEISDLEEIGFGSETRSIHVKSGVWVAYHQKFFCGDQYILEKGKYKCFFDWGGSSNTILSI 2633
Cdd:smart00247    2 ITLYEDENF-QGRSYELSD-DCPSLQDYGSRDNVSSVRVESGCWVLYEQPNYRGRQYVLEPGEYPDYQEWGGFNDQISSI 79


                    ...
gi 1577429051  2634 RPI 2636
Cdd:smart00247   80 RRI 82
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 2867-2950 1.73e-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: 67.01  E-value: 1.73e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2867 FKSKASHTCLDVIGGRDTPGAKVALWTEHGQLRQKWRMSRNG----TISSYLSDeLVLDVKGGNYYDKTHVIVnQPLEGE 2942
Cdd:cd00161      5 IVNAASGKCLDVAGGSTANGAPVQQWTCNGGANQQWTLTPVGdgyyTIRNVASG-KCLDVAGGSTANGANVQQ-WTCNGG 82


                   ....*...
gi 1577429051 2943 ETQKWDIE 2950
Cdd:cd00161     83 DNQQWRLE 90
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 2818-2947 3.03e-11

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: 63.14  E-value: 3.03e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2818 PAVYIRIRNRAQDEYLTVTGNpADARTMSVCISPYSGKDTQIWHYC-RGLFKSKASHtCLDVIGGRDTPGAKVALWTEHG 2896
Cdd:cd23418      2 GAGGGQIRGYGSGRCLDVPGG-STTNGTRLILWDCHGGANQQFTFTsAGELRVGGDK-CLDAAGGGTTNGTPVVIWPCNG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1577429051 2897 QLRQKWRMSRNGTISSYLSDeLVLDVKGGNYYDKTHVIVnQPLEGEETQKW 2947
Cdd:cd23418     80 GANQKWRFNSDGTIRNVNSG-LCLDVAGGGTANGTRLIL-WSCNGGSNQRW 128
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2276-2362 1.03e-10

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


Pssm-ID: 459639  Cd Length: 82  Bit Score: 60.20  E-value: 1.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2276 KMIIY---DLHGSKYkqEVYCNIPDATTWSFPNGAL-IKVVRGCWILYEKPHFQGQKCVLEEGERVLDRDWLLQNRKhpe 2351
Cdd:pfam00030    1 KIVLYekeNFQGRSI--ELTDDCPSLQERGFNSRVNsIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDR--- 75

                           90
                   ....*....|.
gi 1577429051 2352 rnfvLGSIKRV 2362
Cdd:pfam00030   76 ----IGSLRPI 82
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 2824-2950 3.30e-10

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 59.83  E-value: 3.30e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051  2824 IRNRAQDEYLTVTGNPADARTMSvCISPysgKDTQIWHY-CRGLFKSKASHTCLDVIGGRDTPgakVALWTEHGQ-LRQK 2901
Cdd:smart00458    1 IISGNTGKCLDVNGNKNPVGLFD-CHGT---GGNQLWKLtSDGAIRIKDTDLCLTANGNTGST---VTLYSCDGTnDNQY 73

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 1577429051  2902 WRMSRNGTISSYLSDeLVLDVKGGNyyDKTHVIVNQPlEGEETQKWDIE 2950
Cdd:smart00458   74 WEVNKDGTIRNPDSG-KCLDVKDGN--TGTKVILWTC-SGNPNQKWIFE 118
beta-trefoil_Ricin_GllA-1 cd23454
GllA-1 domain, beta-trefoil fold, found in Mucor circinelloides Gellins and similar proteins; ...
 2824-2949 6.43e-10

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: 59.64  E-value: 6.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2824 IRNRAQDEYLTV-TGNPADARTMSVCISPYSGKDTQIWHYCRGLFKSKASHTCLDVIGGRDTPGAKVALW---TEHGQLR 2899
Cdd:cd23454      5 IKSSSNGLVLDVeHGSLKSGAKVVLAPLKTKDYESQLWRYDDGYLVNKASGLVLDIQGGVVKSGTRLVQSpkkPSKDANN 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1577429051 2900 QKWRMSRNGTISSYLSDELVLDVKGGNYYDKTHVIVNQ--PLEGEETQKWDI 2949
Cdd:cd23454     85 QRWGLTADGYIYLLSNPSLVLGIKGNETREGARVILQErkLQKDALNQRWTF 136
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 2653-2727 8.17e-10

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 57.52  E-value: 8.17e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051  2653 FSKAGFQGECIDFVKECADLTSF----TPASFKVLRGCWLLlyYQEDGFY-HQCVLEEGLYVDLTSCGCPSARIRALQPI 2727
Cdd:smart00247    5 YEDENFQGRSYELSDDCPSLQDYgsrdNVSSVRVESGCWVL--YEQPNYRgRQYVLEPGEYPDYQEWGGFNDQISSIRRI 82
beta-trefoil_Ricin_EW29-like cd23449
ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa ...
 2824-2950 3.68e-09

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


Pssm-ID: 467327 [Multi-domain]  Cd Length: 128  Bit Score: 57.30  E-value: 3.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2824 IRNRAQDEYLTVTGNPADARTMsVCISPYSGKDT--QIWH--YCRGLFKSKASHTCLDVIGGRDTPGAKvalwTEHGQLR 2899
Cdd:cd23449      5 IKSKLNGKVLDVEGANAKPGAK-VIMWEKKGGAEdnQLWYedEVTGTIRSKLNDFCLDASGDKGLILNP----YDPSNPK 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1577429051 2900 QKWRMsRNGTISSYLSDELVLDVKGGNYYDKTHVIVnQPLEGEETQKWDIE 2950
Cdd:cd23449     80 QQWKI-SGNKIQNRSNPDNVLDIKGGSKDDGARLCA-WEYNGGPNQLWDFE 128
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 2276-2362 6.17e-09

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 55.21  E-value: 6.17e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051  2276 KMIIYDLHGSKYKQ----EVYCNIPDatTWSFPNGALIKVVRGCWILYEKPHFQGQKCVLEEGERVLDRDWLLQNRKhpe 2351
Cdd:smart00247    1 KITLYEDENFQGRSyelsDDCPSLQD--YGSRDNVSSVRVESGCWVLYEQPNYRGRQYVLEPGEYPDYQEWGGFNDQ--- 75

                            90
                    ....*....|.
gi 1577429051  2352 rnfvLGSIKRV 2362
Cdd:smart00247   76 ----ISSIRRI 82
lectin_2 NF035930
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
 2875-2947 1.31e-08

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


Pssm-ID: 468267 [Multi-domain]  Cd Length: 238  Bit Score: 58.26  E-value: 1.31e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1577429051 2875 CLDVIGGRDTPGAKVALWTEHGQLRQKWRmSRNGTISSYLSDElVLDVKGGNYYDKTHVIVnQPLEGEETQKW 2947
Cdd:NF035930   169 CLDVADGNTRDGARVIAWSCSGGPNQRWR-WRGGQIRSRLSGK-CLDIEGGRARPGQPVIV-WSCNGGPNQRW 238
RicinB_lectin_2 pfam14200
Ricin-type beta-trefoil lectin domain-like;
2867-2926 7.60e-08

Ricin-type beta-trefoil lectin domain-like;


Pssm-ID: 464102 [Multi-domain]  Cd Length: 89  Bit Score: 52.38  E-value: 7.60e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1577429051 2867 FKSKASHTCLDVIGGRDTPGAKVALWTEHGQLRQKWRMSRNG----TISSYLSDeLVLDVKGGN 2926
Cdd:pfam14200   18 IVNVASGKYLDVAGGSTANGANVQQWTDNGNDNQQWRIVDAGdgyyRIVNKASG-KVLDVAGST 80
beta-trefoil_Ricin_SCDase_rpt2 cd23500
second ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ...
 2867-2948 1.39e-07

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: 52.85  E-value: 1.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2867 FKSKASHTCLDVIGGRDTPGAKVALWTEHGQLRQKWRMS-RNGTISSYLSDELVLDVKGGNYYDKTHVIVNQPLEGEETQ 2945
Cdd:cd23500      5 YRSKRSGKCLSAANGSQLNGSLVQLDACHASAGQLWYFDpKKGTIRSALDGNKCLAIPGGNTGNHTQLQLADCDASNPAQ 84


                   ...
gi 1577429051 2946 KWD 2948
Cdd:cd23500     85 QFN 87
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 2823-2902 6.89e-07

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 50.59  E-value: 6.89e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051  2823 RIRNRAQDEYLTVTGNPADARTMSVCispYSGKDTQIWHYCR-GLFKSKASHTCLDVIGGrdTPGAKVALWTEHGQLRQK 2901
Cdd:smart00458   40 AIRIKDTDLCLTANGNTGSTVTLYSC---DGTNDNQYWEVNKdGTIRNPDSGKCLDVKDG--NTGTKVILWTCSGNPNQK 114


                    .
gi 1577429051  2902 W 2902
Cdd:smart00458  115 W 115
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 2767-2815 1.82e-06

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 47.89  E-value: 1.82e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1577429051  2767 TQSVWIKSGLWIAYEGSNFLGRQILLTPKEIPNWTAFSGWK-TIGSVRPM 2815
Cdd:smart00247   33 VSSVRVESGCWVLYEQPNYRGRQYVLEPGEYPDYQEWGGFNdQISSIRRI 82
beta-trefoil_Ricin_SCDase cd23456
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ...
 2868-2950 1.17e-05

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: 46.97  E-value: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2868 KSKASHTCLDVIGGrDTPGAKVALWTEHGQLRQKWRMSRNGTISSYLSDELVLDVKGGNYYDKThvIVNQPLEGEETQKW 2947
Cdd:cd23456      6 KSQASGLCLDVSGG-ATNGANVVVYDCNNSNSQKWYYDATGRLHSKANPGKCLDAGGENSNGAN--VVLWACNDSANQRW 82


                   ...
gi 1577429051 2948 DIE 2950
Cdd:cd23456     83 DFD 85
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 2833-2903 1.23e-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: 46.96  E-value: 1.23e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1577429051 2833 LTVTGNPADARTmSVCISPYSGKDTQIWH-YCRGLFKSKASHTCLDVIGGRDTPGAKVALWTEHGQLRQKWR 2903
Cdd:cd23418     59 LDAAGGGTTNGT-PVVIWPCNGGANQKWRfNSDGTIRNVNSGLCLDVAGGGTANGTRLILWSCNGGSNQRWR 129
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
 2875-2947 1.38e-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: 46.94  E-value: 1.38e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1577429051 2875 CLDVIGGRDTPGAKVALWTEHGQLRQKWRMSRNGTISSYLSDeLVLDVKGGNYYDKTHVIVnQPLEGEETQKW 2947
Cdd:cd23451     54 CLDVSGGGTANGTLVQLWDCNGTGAQKWVPRADGTLYNPQSG-KCLDAPGGSTTDGTQLQL-YTCNGTAAQQW 124
beta-trefoil_Ricin_MTX-like_rpt1-3 cd23497
first, second and third ricin B-type lectin domains, beta-trefoil fold, found in ...
 2852-2950 1.77e-05

first, second and third ricin B-type lectin domains, beta-trefoil fold, found in Lysinibacillus sphaericus mosquitocidal toxin (MTX) and similar proteins; This subfamily includes Lysinibacillus sphaericus MTX and Pieris brassicae pierisin. MTX acts as an ADP-ribosyl transferase. Pierisin, also called NAD--DNA ADP-ribosyltransferase, pierisin-2, or pierisin-B, catalyzes the ADP ribosylation of double-stranded DNA by targeting the N2 amino group of dG residues. It induces apoptosis in a range of human cell lines. Members of this family contain four ricin B-type lectin domains with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The model corresponds to the first, second and third ricin B-type lectin domains. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467375 [Multi-domain]  Cd Length: 139  Bit Score: 46.97  E-value: 1.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2852 YSGKDTQIWHycrglF----KSKA--------SHTCLDVIGGRDTPGAKVALWTEHGQLRQKWRMSRNGT----ISSYLS 2915
Cdd:cd23497     31 NLGLDNQKWN-----FtydsSKKAykiksgknPNLLLSWDSNASSKEMVIRGYTGSGSDNQYWRIERTEDgyykLRNLAD 105

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1577429051 2916 DELVLDVKGGNYYDKTHVIVNQPlEGEETQKWDIE 2950
Cdd:cd23497    106 LKKVLDLANGNTNNGTRIQVYDN-NGTSAQKWIIK 139
beta-trefoil_Ricin_RSA cd23455
ricin B-type lectin domain, beta-trefoil fold, found in Rhizoctonia solani agglutinin (RSA) ...
 2868-2949 1.02e-04

ricin B-type lectin domain, beta-trefoil fold, found in Rhizoctonia solani agglutinin (RSA) and similar proteins; RSA is a 15.5-kDa lectin accumulated in the mycelium and sclerotia of the soil born plant pathogenic fungus R. solani. It may act as a storage protein implicated in fungal insecticidal activity. It displays high selectivity towards terminal non-reducing N-acetylgalactosamine residues. RSA reveals a domain-swapping dimeric assembly. Each monomer contains a ricin B-type lectin domain that adopts a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467333 [Multi-domain]  Cd Length: 131  Bit Score: 44.62  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2868 KSKASHTCLDVIGGRDTPGAKVALWTEHGQLRQKWRMSRNGTISSYlsdeLVLDVKGGNY-YDKTHVIVNQPLEGEETQK 2946
Cdd:cd23455      6 KNVATGTVLDLYLGSSAEGTPVQGYQPNGGDNQKWQLEWVGSGNGV----TLRNVASGTYaGFPAHADGGQVVGSNNPVL 81


                   ...
gi 1577429051 2947 WDI 2949
Cdd:cd23455     82 FTI 84
lectin_2 NF035930
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
 2837-2902 1.49e-04

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


Pssm-ID: 468267 [Multi-domain]  Cd Length: 238  Bit Score: 45.93  E-value: 1.49e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1577429051 2837 GNPAD-ARTMSVcisPYSGKDTQIWHYCRGLFKSKASHTCLDVIGGRDTPGAKVALWTEHGQLRQKW 2902
Cdd:NF035930   175 GNTRDgARVIAW---SCSGGPNQRWRWRGGQIRSRLSGKCLDIEGGRARPGQPVIVWSCNGGPNQRW 238
beta-trefoil_Ricin_RPI cd23452
ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine ...
 2848-2947 3.20e-04

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: 42.89  E-value: 3.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2848 CISPYSGKDT-----QIWHyCRGL------FKS----KASHTCLDVIGGRDTPGAKVALWTEHGQLRQKWRMSRNGTISS 2912
Cdd:cd23452     13 CIDVPNSSTTdgaplQLWD-CNGTnaqkwtFASdgtlRALGKCLDVAWGGTDNGTAVQLWTCSGNPAQQFVLSGAGDLVN 91

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1577429051 2913 YLSDELVlDVKGGNYYDKTHVivnQPLE--GEETQKW 2947
Cdd:cd23452     92 PQANKCV-DVSGGNSGNGTRL---QLWEcsGNANQKW 124
beta-trefoil_Ricin_MPL_CNL cd23422
ricin B-type lectin domain, beta-trefoil fold, found in Macrolepiota procera ricin B-like ...
 2824-2903 1.44e-03

ricin B-type lectin domain, beta-trefoil fold, found in Macrolepiota procera ricin B-like lectin (MPL), Clitocybe nebularis lectin (CNL), and similar proteins; MPL and CNL are a homodimeric ricin B-like lectins with a beta-trefoil fold that is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Their alpha subunit may harbor a sugar-binding pocket. MPL has the highest specificity for terminal N-acetyllactosamine and other beta-galactosides. CNL induces maturation and activation of dendritic cells via the toll-like receptor 4 pathway. It is specific for terminal, non-reducing N-acetylgalactosamine (Gal-NAc)-containing carbohydrates including N,N'-diacetyllactosediamine/LDN (GalNAcbeta1-4GlcNAc, LacdiNAc). It is also specific for carbohydrates containing N-acetylglucosamine (-GlcNAc) or N-acetyllactosamine (-Galbeta1-4GlcNAc) at the reducing end.


Pssm-ID: 467300 [Multi-domain]  Cd Length: 135  Bit Score: 41.15  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2824 IRNRAQDEYLTVTGNPADaRTMSVCISPYSGKDTQIWHYCRGLFKSKASHTC--LDVIGGRDTPGAKVALWTEHGQLRQK 2901
Cdd:cd23422     51 IQSVSTGKYLGIEGGPRD-GTRLVGSDQPFVWDIEPDEGDSGAFRIFVPGTNlvLDLDDGGSAPGTPVQLWERSEGPNQL 129


                   ..
gi 1577429051 2902 WR 2903
Cdd:cd23422    130 WR 131
beta-trefoil_Ricin_MOA-like cd23416
ricin B-type lectin domain, beta-trefoil fold, found in Marasmius oreades agglutinin (MOA) and ...
 2819-2950 1.45e-03

ricin B-type lectin domain, beta-trefoil fold, found in Marasmius oreades agglutinin (MOA) and similar proteins; The family includes Marasmius oreades agglutinin (MOA) and Polyporus squamosus Ricin B-related lectin (PSL). MOA is a lectin isolated from fruiting bodies of the mushroom M. oreades. It specifically binds non-reducing terminal Galalpha(1,3)Gal carbohydrates, such as that which occurs in the xenotransplantation epitope Galalpha(1,3)Galbeta(1,4)GlcNAc and the branched blood group B determinant Galalpha(1,3)[Fucalpha(1,2)]Gal. Polyporus squamosus Ricin B-related lectin (PSL) is a lectin specific for glycans terminating with the sequence Neu5Acalpha2-6Galbeta. Like MOA, PSL is a calcium-dependent cysteine protease. Both MOA and PSL contain an N-terminal ricin B-type lectin domain and a C-terminal agglutinin domain. The ricin B-type lectin domain is a beta-trefoil domain, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.


Pssm-ID: 467295 [Multi-domain]  Cd Length: 145  Bit Score: 41.56  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2819 AVYiRIRNRAQDEYLTVTGNPADARTmSVCISPYSGKDT---QIWHycrgLFKSK-----------ASHTCLDVIGGRDT 2884
Cdd:cd23416      1 GVY-HIRNAGTGTVLDLSGGSSANGT-PIQGWQKTGDTGsfnQLWL----LEPVPngsdtytiqnvRSGTYLDLAGGSSA 74

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2885 PGAKVALWTEHGQLRQKWRMSRNGTISSYL----SDELVLDVKGGNYYDKTHVIVNQPLEGEETQKWDIE 2950
Cdd:cd23416     75 NGTAIVGWQSTNNPNQQWVIKPANGGTYYKiqnkGTGTFLDLYGGDSANGTKIVGWTGHWGNPNQLWLFE 144
beta-trefoil_Ricin_AgaB34-like cd23458
ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 ...
 2867-2926 1.66e-03

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: 41.15  E-value: 1.66e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1577429051 2867 FKSKASHTCLDVIGGRDTPGAKVALWTEHGQLRQKWRMSRNG----TISSYLSDeLVLDVKGGN 2926
Cdd:cd23458     52 IKASHSGKCLDVAGGSTANGANIQQWDCVGGANQQWKLQDLGngyfELKARHSG-KCLDVAGGS 114
beta-trefoil_Ricin_1,3Gal43A cd23446
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and ...
 2870-2950 3.83e-03

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: 40.06  E-value: 3.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429051 2870 KASHTCLDVIGGRDTPGAKVALWTEHGQLRQKWRMSRNG----TISSYLSDeLVLDVKGGNYYDKTHVIvNQPLEGEETQ 2945
Cdd:cd23446      8 RNSGKALDVLSGSTTDGAQIEQWTDNGGTSQQWYFTDVGggyyKIVNRNSG-KALDVNGASTADGAAII-QWTSNGGDNQ 85


                   ....*
gi 1577429051 2946 KWDIE 2950
Cdd:cd23446     86 QWQIV 90
beta-trefoil_Ricin_AgaB34-like cd23458
ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 ...
 2868-2926 7.10e-03

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: 39.23  E-value: 7.10e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1577429051 2868 KSKASHTCLDVIGGRDTPGAKVALWTEHGQLRQKWRM--SRNG--TISSYLSDeLVLDVKGGN 2926
Cdd:cd23458      6 RNRNSGKCIDVAGGSTANGANIQQWDCGSGSNQQWTLveIDNGyyRIKASHSG-KCLDVAGGS 67
 
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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