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Conserved domains on  [gi|1176265075|ref|XP_020666038|]
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very large A-kinase anchor protein isoform X1 [Pogona vitticeps]

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 ...
 2334-2469 2.38e-72

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: 238.11  E-value: 2.38e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2334 QPAVYFRIKNRSQDKYLTVTGKLMDARATSVCLSPLNCKNTQIWRYSCGLIKSKANDACLDVIGGRDVSGAKVALWIEHG 2413
Cdd:cd23463      1 QPRVYLRIKNRAQGLYLTTEGNLADPRATSVCVSQYNGKDTQIWYYCRGLLKSKANDACLDVIGGKDNPGSKVALWTEHG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1176265075 2414 KARQKWTFNKDGTISSYLSDQLVLDVKGGYYYDRNHIVVNQADNNECSQKWDFEIL 2469
Cdd:cd23463     81 KTHQKWRINEDGTISSHLSDDLVLDLKGGNYYDKDHLIVNNPEEDQQTQKWDIELL 136
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 1979-2062 9.47e-29

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: 111.05  E-value: 9.47e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 1979 KMIIYEKSHFGGWCKEISENTDCVPMVlenaGDFQGVGSVRVIGGIWVAYEKERYKGQQYLLEEGEYEDWHSWGGTNNSL 2058
Cdd:pfam00030    1 KIVLYEKENFQGRSIELTDDCPSLQER----GFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDRI 76


                   ....
gi 1176265075 2059 MSLR 2062
Cdd:pfam00030   77 GSLR 80
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2089-2154 3.55e-23

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: 95.25  E-value: 3.55e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1176265075 2089 VNQEIPDLELAGFGLVTRSINVKSGVWVAYQQKYFCGEQYVLEKGKYKCFLDWGGSSDNIMSIRPV 2154
Cdd:pfam00030   17 LTDDCPSLQERGFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDRIGSLRPI 82
Crystall super family cl02528
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2253-2332 1.27e-15

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: 73.68  E-value: 1.27e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2253 ISLFALENYEGKELRLQEAVSSVLNKDLHFLTQSVWVRSGLWIAYEGCHFLGKQFLLEPTKISNWTQFSG-WKLIGSLRP 2331
Cdd:pfam00030    2 IVLYEKENFQGRSIELTDDCPSLQERGFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGApNDRIGSLRP 81


                   .
gi 1176265075 2332 V 2332
Cdd:pfam00030   82 I 82
Crystall super family cl02528
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2168-2244 6.95e-14

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: 68.67  E-value: 6.95e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2168 IKAFNKTHFQGTCIDFTEEATDLES--FTP--CSFKVLRGCWLLC----YQGETgdnwCVLEEDLYADLASCGCPAAAVK 2239
Cdd:pfam00030    2 IVLYEKENFQGRSIELTDDCPSLQErgFNSrvNSIRVLSGAWVLYehpnFRGRQ----YVLEPGEYPDWSDWGAPNDRIG 77


                   ....*
gi 1176265075 2240 SLKPV 2244
Cdd:pfam00030   78 SLRPI 82
Crystall super family cl02528
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 1830-1882 1.93e-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: 59.04  E-value: 1.93e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1176265075 1830 IRVVRGCWVLYEKPRYQGQKYILEEGE-KMLSDILNLHCeehqgniTIGSVRQI 1882
Cdd:pfam00030   36 IRVLSGAWVLYEHPNFRGRQYVLEPGEyPDWSDWGAPND-------RIGSLRPI 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 ...
 2334-2469 2.38e-72

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: 238.11  E-value: 2.38e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2334 QPAVYFRIKNRSQDKYLTVTGKLMDARATSVCLSPLNCKNTQIWRYSCGLIKSKANDACLDVIGGRDVSGAKVALWIEHG 2413
Cdd:cd23463      1 QPRVYLRIKNRAQGLYLTTEGNLADPRATSVCVSQYNGKDTQIWYYCRGLLKSKANDACLDVIGGKDNPGSKVALWTEHG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1176265075 2414 KARQKWTFNKDGTISSYLSDQLVLDVKGGYYYDRNHIVVNQADNNECSQKWDFEIL 2469
Cdd:cd23463     81 KTHQKWRINEDGTISSHLSDDLVLDLKGGNYYDKDHLIVNNPEEDQQTQKWDIELL 136
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 1979-2062 9.47e-29

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: 111.05  E-value: 9.47e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 1979 KMIIYEKSHFGGWCKEISENTDCVPMVlenaGDFQGVGSVRVIGGIWVAYEKERYKGQQYLLEEGEYEDWHSWGGTNNSL 2058
Cdd:pfam00030    1 KIVLYEKENFQGRSIELTDDCPSLQER----GFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDRI 76


                   ....
gi 1176265075 2059 MSLR 2062
Cdd:pfam00030   77 GSLR 80
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 1979-2064 3.48e-24

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 98.35  E-value: 3.48e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075  1979 KMIIYEKSHFGGWCKEISENTDCvpmvLENAGDFQGVGSVRVIGGIWVAYEKERYKGQQYLLEEGEYEDWHSWGGTNNSL 2058
Cdd:smart00247    1 KITLYEDENFQGRSYELSDDCPS----LQDYGSRDNVSSVRVESGCWVLYEQPNYRGRQYVLEPGEYPDYQEWGGFNDQI 76


                    ....*.
gi 1176265075  2059 MSLRFL 2064
Cdd:smart00247   77 SSIRRI 82
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2089-2154 3.55e-23

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: 95.25  E-value: 3.55e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1176265075 2089 VNQEIPDLELAGFGLVTRSINVKSGVWVAYQQKYFCGEQYVLEKGKYKCFLDWGGSSDNIMSIRPV 2154
Cdd:pfam00030   17 LTDDCPSLQERGFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDRIGSLRPI 82
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
2338-2464 1.25e-18

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 84.12  E-value: 1.25e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2338 YFRIKNRSQDKYLTVTGKlmDARATSVCLSPlnC---KNTQIWRYSC-GLIKSKANDACLDVigGRDVSGAKVALW-IEH 2412
Cdd:pfam00652    2 TGRIRNRASGKCLDVPGG--SSAGGPVGLYP--ChgsNGNQLWTLTGdGTIRSVASDLCLDV--GSTADGAKVVLWpCHP 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1176265075 2413 GKARQKWTFNKDGT-ISSYLSDqLVLDVKGGyYYDRNHIVVNQADNNECSQKW 2464
Cdd:pfam00652   76 GNGNQRWRYDEDGTqIRNPQSG-KCLDVSGA-GTSNGKVILWTCDSGNPNQQW 126
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 2094-2154 3.28e-17

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 78.32  E-value: 3.28e-17
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1176265075  2094 PDLELAGFGLVTRSINVKSGVWVAYQQKYFCGEQYVLEKGKYKCFLDWGGSSDNIMSIRPV 2154
Cdd:smart00247   22 PSLQDYGSRDNVSSVRVESGCWVLYEQPNYRGRQYVLEPGEYPDYQEWGGFNDQISSIRRI 82
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2253-2332 1.27e-15

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: 73.68  E-value: 1.27e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2253 ISLFALENYEGKELRLQEAVSSVLNKDLHFLTQSVWVRSGLWIAYEGCHFLGKQFLLEPTKISNWTQFSG-WKLIGSLRP 2331
Cdd:pfam00030    2 IVLYEKENFQGRSIELTDDCPSLQERGFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGApNDRIGSLRP 81


                   .
gi 1176265075 2332 V 2332
Cdd:pfam00030   82 I 82
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2168-2244 6.95e-14

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: 68.67  E-value: 6.95e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2168 IKAFNKTHFQGTCIDFTEEATDLES--FTP--CSFKVLRGCWLLC----YQGETgdnwCVLEEDLYADLASCGCPAAAVK 2239
Cdd:pfam00030    2 IVLYEKENFQGRSIELTDDCPSLQErgFNSrvNSIRVLSGAWVLYehpnFRGRQ----YVLEPGEYPDWSDWGAPNDRIG 77


                   ....*
gi 1176265075 2240 SLKPV 2244
Cdd:pfam00030   78 SLRPI 82
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 2361-2467 1.65e-11

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 63.30  E-value: 1.65e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075  2361 ATSVCLSPLN---------CKNT---QIWRY-SCGLIKSKANDACLDVIGGRDVsgaKVALWIEHGKA-RQKWTFNKDGT 2426
Cdd:smart00458    5 NTGKCLDVNGnknpvglfdCHGTggnQLWKLtSDGAIRIKDTDLCLTANGNTGS---TVTLYSCDGTNdNQYWEVNKDGT 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 1176265075  2427 ISSYLSDqLVLDVKGGyyYDRNHIVVNQADNNEcSQKWDFE 2467
Cdd:smart00458   82 IRNPDSG-KCLDVKDG--NTGTKVILWTCSGNP-NQKWIFE 118
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 1830-1882 1.93e-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: 59.04  E-value: 1.93e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1176265075 1830 IRVVRGCWVLYEKPRYQGQKYILEEGE-KMLSDILNLHCeehqgniTIGSVRQI 1882
Cdd:pfam00030   36 IRVLSGAWVLYEHPNFRGRQYVLEPGEyPDWSDWGAPND-------RIGSLRPI 82
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 1830-1856 2.68e-08

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 52.90  E-value: 2.68e-08
                            10        20
                    ....*....|....*....|....*..
gi 1176265075  1830 IRVVRGCWVLYEKPRYQGQKYILEEGE 1856
Cdd:smart00247   36 VRVESGCWVLYEQPNYRGRQYVLEPGE 62
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 2253-2332 2.76e-06

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 47.12  E-value: 2.76e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075  2253 ISLFALENYEGKELRLQEAVSSvLNKDLHF-LTQSVWVRSGLWIAYEGCHFLGKQFLLEP---TKISNWTQFSGWklIGS 2328
Cdd:smart00247    2 ITLYEDENFQGRSYELSDDCPS-LQDYGSRdNVSSVRVESGCWVLYEQPNYRGRQYVLEPgeyPDYQEWGGFNDQ--ISS 78


                    ....
gi 1176265075  2329 LRPV 2332
Cdd:smart00247   79 IRRI 82
lectin_2 NF035930
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
 2390-2464 8.13e-05

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: 46.70  E-value: 8.13e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1176265075 2390 DACLDVIGGRDVSGAKVALWIEHGKARQKWTFnKDGTISSYLSDQlVLDVKGGYYYDRNHIVVNQADNNEcSQKW 2464
Cdd:NF035930   167 DLCLDVADGNTRDGARVIAWSCSGGPNQRWRW-RGGQIRSRLSGK-CLDIEGGRARPGQPVIVWSCNGGP-NQRW 238
lectin_2 NF035930
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
 2371-2419 1.55e-03

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: 42.47  E-value: 1.55e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1176265075 2371 CKN--TQIWRYSCGLIKSKANDACLDVIGGRDVSGAKVALWIEHGKARQKW 2419
Cdd:NF035930   188 CSGgpNQRWRWRGGQIRSRLSGKCLDIEGGRARPGQPVIVWSCNGGPNQRW 238
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 2176-2244 1.93e-03

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 39.41  E-value: 1.93e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1176265075  2176 FQGTCIDFTEEATDL-ESFTPC---SFKVLRGCWLLcYQ--GETGDNWcVLEEDLYADLASCGCPAAAVKSLKPV 2244
Cdd:smart00247   10 FQGRSYELSDDCPSLqDYGSRDnvsSVRVESGCWVL-YEqpNYRGRQY-VLEPGEYPDYQEWGGFNDQISSIRRI 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 ...
 2334-2469 2.38e-72

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: 238.11  E-value: 2.38e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2334 QPAVYFRIKNRSQDKYLTVTGKLMDARATSVCLSPLNCKNTQIWRYSCGLIKSKANDACLDVIGGRDVSGAKVALWIEHG 2413
Cdd:cd23463      1 QPRVYLRIKNRAQGLYLTTEGNLADPRATSVCVSQYNGKDTQIWYYCRGLLKSKANDACLDVIGGKDNPGSKVALWTEHG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1176265075 2414 KARQKWTFNKDGTISSYLSDQLVLDVKGGYYYDRNHIVVNQADNNECSQKWDFEIL 2469
Cdd:cd23463     81 KTHQKWRINEDGTISSHLSDDLVLDLKGGNYYDKDHLIVNNPEEDQQTQKWDIELL 136
beta-trefoil_Ricin_CRYBG cd23430
ricin B-type lectin domain, beta-trefoil fold, found in the beta/gamma crystallin ...
 2337-2468 8.74e-56

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: 190.49  E-value: 8.74e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2337 VYFRIKNRSQDKYLTVTGKLMDARATSVCLSPLNCKNTQIWRYSCGLIKSK-ANDACLDVIGGRDVSGAKVALWIEHGKA 2415
Cdd:cd23430      1 VYFRLRNKATGLFLSVNGNLEDLKLLRVQVMPDVGADDQIWYYQEGLIKCRiAEDCCLTVIGSLVTPGSKVGLWLEQNAD 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1176265075 2416 RQKWTFNKDGTISSYLSDQLVLDVKGGYYYDRNHIVVNQADNNECSQKWDFEI 2468
Cdd:cd23430     81 RQFWSLKSDGRIYSKLKPNLVLDVKGGTQYDQNHVILNTPSEEKFTQVWEIMV 133
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 1979-2062 9.47e-29

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: 111.05  E-value: 9.47e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 1979 KMIIYEKSHFGGWCKEISENTDCVPMVlenaGDFQGVGSVRVIGGIWVAYEKERYKGQQYLLEEGEYEDWHSWGGTNNSL 2058
Cdd:pfam00030    1 KIVLYEKENFQGRSIELTDDCPSLQER----GFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDRI 76


                   ....
gi 1176265075 2059 MSLR 2062
Cdd:pfam00030   77 GSLR 80
beta-trefoil_Ricin_CRYBG1 cd23464
ricin B-type lectin domain, beta-trefoil fold, found in beta/gamma crystallin ...
 2334-2469 2.56e-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: 112.20  E-value: 2.56e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2334 QPAVYFRIKNRSQDKYLTVTGKLMDARATSVCLSPLNCKNTQIWRYSCGLIKSK-ANDACLDVIGGRDVSGAKVALWIEH 2412
Cdd:cd23464      1 QKRVYFRLRNKETGCFMSTNGNLDDLKLLRIQVLEDTGSDDQIWVYQDGLIRCRmAEDCCLETVGNLVTAGSKLGLSLEQ 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1176265075 2413 GKARQKWTFNKDGTISSYLSDQLVLDVKGGYYYDRNHIVVNQADNNECSQKWDFEIL 2469
Cdd:cd23464     81 GKDNQFWSITSDGRIYSKLKPDLVLDIKGGQQYDQNHVILNTFDEEKLTQRWEVEIL 137
beta-trefoil_Ricin_CRYBG2 cd23465
ricin B-type lectin domain, beta-trefoil fold, found in beta/gamma crystallin ...
 2334-2469 7.50e-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: 110.73  E-value: 7.50e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2334 QPAVYFRIKNRSQDKYLTVTGKLMDARATSVCLSPLNCKNTQIWRYSCGLIKSK-ANDACLDVIGGRDvSGAKVALWIEH 2412
Cdd:cd23465      1 QRRVYFRLRNRELGLYLAVPDGVEDMKAGRVVVTEQQEGMSHVWFYEDGLLKNQmAPTMSLQVIGPPD-NGAKVVLWSET 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1176265075 2413 GKARQKWTFNKDGTISSYLSDQLVLDVKGGYYYDRNHIVVNQADNNECSQKWDFEIL 2469
Cdd:cd23465     80 RQPRQTWSIQPSGHILSQMFEGMILDVKGGRTYDRDHVVLWEVSEERPSQIWDMEVL 136
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 1979-2064 3.48e-24

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 98.35  E-value: 3.48e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075  1979 KMIIYEKSHFGGWCKEISENTDCvpmvLENAGDFQGVGSVRVIGGIWVAYEKERYKGQQYLLEEGEYEDWHSWGGTNNSL 2058
Cdd:smart00247    1 KITLYEDENFQGRSYELSDDCPS----LQDYGSRDNVSSVRVESGCWVLYEQPNYRGRQYVLEPGEYPDYQEWGGFNDQI 76


                    ....*.
gi 1176265075  2059 MSLRFL 2064
Cdd:smart00247   77 SSIRRI 82
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2089-2154 3.55e-23

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: 95.25  E-value: 3.55e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1176265075 2089 VNQEIPDLELAGFGLVTRSINVKSGVWVAYQQKYFCGEQYVLEKGKYKCFLDWGGSSDNIMSIRPV 2154
Cdd:pfam00030   17 LTDDCPSLQERGFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDRIGSLRPI 82
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
2338-2464 1.25e-18

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 84.12  E-value: 1.25e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2338 YFRIKNRSQDKYLTVTGKlmDARATSVCLSPlnC---KNTQIWRYSC-GLIKSKANDACLDVigGRDVSGAKVALW-IEH 2412
Cdd:pfam00652    2 TGRIRNRASGKCLDVPGG--SSAGGPVGLYP--ChgsNGNQLWTLTGdGTIRSVASDLCLDV--GSTADGAKVVLWpCHP 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1176265075 2413 GKARQKWTFNKDGT-ISSYLSDqLVLDVKGGyYYDRNHIVVNQADNNECSQKW 2464
Cdd:pfam00652   76 GNGNQRWRYDEDGTqIRNPQSG-KCLDVSGA-GTSNGKVILWTCDSGNPNQQW 126
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 2338-2464 5.50e-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: 82.42  E-value: 5.50e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2338 YFRIKNRSQDKYLTVTGKLMDARATsVCLSPLNCKNTQIWRYS-----CGLIKSKANDACLDVIGGRDVSGAKVALWIEH 2412
Cdd:cd00161      2 TYRIVNAASGKCLDVAGGSTANGAP-VQQWTCNGGANQQWTLTpvgdgYYTIRNVASGKCLDVAGGSTANGANVQQWTCN 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1176265075 2413 GKARQKWTF----NKDGTISSYLSDqLVLDVKGGYYYDRNHIVVNQADNNEcSQKW 2464
Cdd:cd00161     81 GGDNQQWRLepvgDGYYRIVNKHSG-KCLDVSGGSTANGANVQQWTCNGGA-NQQW 134
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 2094-2154 3.28e-17

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 78.32  E-value: 3.28e-17
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1176265075  2094 PDLELAGFGLVTRSINVKSGVWVAYQQKYFCGEQYVLEKGKYKCFLDWGGSSDNIMSIRPV 2154
Cdd:smart00247   22 PSLQDYGSRDNVSSVRVESGCWVLYEQPNYRGRQYVLEPGEYPDYQEWGGFNDQISSIRRI 82
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2253-2332 1.27e-15

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: 73.68  E-value: 1.27e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2253 ISLFALENYEGKELRLQEAVSSVLNKDLHFLTQSVWVRSGLWIAYEGCHFLGKQFLLEPTKISNWTQFSG-WKLIGSLRP 2331
Cdd:pfam00030    2 IVLYEKENFQGRSIELTDDCPSLQERGFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGApNDRIGSLRP 81


                   .
gi 1176265075 2332 V 2332
Cdd:pfam00030   82 I 82
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2168-2244 6.95e-14

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: 68.67  E-value: 6.95e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2168 IKAFNKTHFQGTCIDFTEEATDLES--FTP--CSFKVLRGCWLLC----YQGETgdnwCVLEEDLYADLASCGCPAAAVK 2239
Cdd:pfam00030    2 IVLYEKENFQGRSIELTDDCPSLQErgFNSrvNSIRVLSGAWVLYehpnFRGRQ----YVLEPGEYPDWSDWGAPNDRIG 77


                   ....*
gi 1176265075 2240 SLKPV 2244
Cdd:pfam00030   78 SLRPI 82
beta-trefoil_Ricin_GllA-1 cd23454
GllA-1 domain, beta-trefoil fold, found in Mucor circinelloides Gellins and similar proteins; ...
 2338-2466 3.79e-13

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: 68.50  E-value: 3.79e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2338 YFRIKNRSQDKYLTVTGKLMDARATsVCLSPLNCKN--TQIWRYSCGLIKSKANDACLDVIGGRDVSGAKVALWIE-HGK 2414
Cdd:cd23454      2 WFFIKSSSNGLVLDVEHGSLKSGAK-VVLAPLKTKDyeSQLWRYDDGYLVNKASGLVLDIQGGVVKSGTRLVQSPKkPSK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1176265075 2415 AR--QKWTFNKDGTISSYLSDQLVLDVKGGYYYDRNHIVV----NQADNNEcsQKWDF 2466
Cdd:cd23454     81 DAnnQRWGLTADGYIYLLSNPSLVLGIKGNETREGARVILqerkLQKDALN--QRWTF 136
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 2384-2467 2.24e-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: 66.24  E-value: 2.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2384 IKSKANDACLDVIGGRDVSGAKVALWIEHGKARQKWTF----NKDGTISSYLSDqLVLDVKGGYYYDRNHIVVNQADNNE 2459
Cdd:cd00161      5 IVNAASGKCLDVAGGSTANGAPVQQWTCNGGANQQWTLtpvgDGYYTIRNVASG-KCLDVAGGSTANGANVQQWTCNGGD 83


                   ....*...
gi 1176265075 2460 cSQKWDFE 2467
Cdd:cd00161     84 -NQQWRLE 90
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 2361-2467 1.65e-11

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 63.30  E-value: 1.65e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075  2361 ATSVCLSPLN---------CKNT---QIWRY-SCGLIKSKANDACLDVIGGRDVsgaKVALWIEHGKA-RQKWTFNKDGT 2426
Cdd:smart00458    5 NTGKCLDVNGnknpvglfdCHGTggnQLWKLtSDGAIRIKDTDLCLTANGNTGS---TVTLYSCDGTNdNQYWEVNKDGT 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 1176265075  2427 ISSYLSDqLVLDVKGGyyYDRNHIVVNQADNNEcSQKWDFE 2467
Cdd:smart00458   82 IRNPDSG-KCLDVKDG--NTGTKVILWTCSGNP-NQKWIFE 118
beta-trefoil_Ricin_SCDase cd23456
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ...
 2338-2443 2.75e-11

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: 62.76  E-value: 2.75e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2338 YFRIKNRSQDKYLTVTGKLMDAraTSVCLSplNCKNT--QIWRY-SCGLIKSKANDA-CLDVIGGRdVSGAKVALWIEHG 2413
Cdd:cd23456      2 YFQLKSQASGLCLDVSGGATNG--ANVVVY--DCNNSnsQKWYYdATGRLHSKANPGkCLDAGGEN-SNGANVVLWACND 76

                           90       100       110
                   ....*....|....*....|....*....|
gi 1176265075 2414 KARQKWTFNkDGTISSYLSDQLVLDVKGGY 2443
Cdd:cd23456     77 SANQRWDFD-GNFIRSRNNTNLALDAYGSQ 105
beta-trefoil_Ricin_EW29-like cd23449
ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa ...
 2338-2467 4.91e-11

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: 62.31  E-value: 4.91e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2338 YFRIKNRSQDKYLTVTGKLMDArATSVCLSPLNCKNT--QIW--RYSCGLIKSKANDACLDVIGGRDVSGAKValwiEHG 2413
Cdd:cd23449      2 YFYIKSKLNGKVLDVEGANAKP-GAKVIMWEKKGGAEdnQLWyeDEVTGTIRSKLNDFCLDASGDKGLILNPY----DPS 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1176265075 2414 KARQKWTFNKDgTISSYLSDQLVLDVKGGYYYDRNHIVVnQADNNECSQKWDFE 2467
Cdd:cd23449     77 NPKQQWKISGN-KIQNRSNPDNVLDIKGGSKDDGARLCA-WEYNGGPNQLWDFE 128
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 2346-2442 1.13e-10

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


Pssm-ID: 467297 [Multi-domain]  Cd Length: 130  Bit Score: 61.21  E-value: 1.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2346 QDKYLTVTGKLmDARATSVCLSPLNCKNTQIWRY-SCGLIKSKAnDACLDVIGGRDVSGAKVALWIEHGKARQKWTFNKD 2424
Cdd:cd23418     13 SGRCLDVPGGS-TTNGTRLILWDCHGGANQQFTFtSAGELRVGG-DKCLDAAGGGTTNGTPVVIWPCNGGANQKWRFNSD 90

                           90
                   ....*....|....*...
gi 1176265075 2425 GTISSYLSDqLVLDVKGG 2442
Cdd:cd23418     91 GTIRNVNSG-LCLDVAGG 107
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 1830-1882 1.93e-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: 59.04  E-value: 1.93e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1176265075 1830 IRVVRGCWVLYEKPRYQGQKYILEEGE-KMLSDILNLHCeehqgniTIGSVRQI 1882
Cdd:pfam00030   36 IRVLSGAWVLYEHPNFRGRQYVLEPGEyPDWSDWGAPND-------RIGSLRPI 82
beta-trefoil_Ricin_SCDase_rpt2 cd23500
second ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ...
 2385-2465 4.95e-10

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: 59.40  E-value: 4.95e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2385 KSKANDACLDVIGGRDVSGAKVALWIEHGKARQKWTFN-KDGTISSYLSDQLVLDVKGGYYYDRNHIVVNQADNNECSQK 2463
Cdd:cd23500      6 RSKRSGKCLSAANGSQLNGSLVQLDACHASAGQLWYFDpKKGTIRSALDGNKCLAIPGGNTGNHTQLQLADCDASNPAQQ 85


                   ..
gi 1176265075 2464 WD 2465
Cdd:cd23500     86 FN 87
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 2382-2466 2.10e-09

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: 57.74  E-value: 2.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2382 GLIKSKANDACLDVIGGRDVSGAKVALWIEHGKARQKWTFNKDGTISSYlsDQLVLDVKGGYYYDRNHIVVNQAdNNECS 2461
Cdd:cd23418      6 GQIRGYGSGRCLDVPGGSTTNGTRLILWDCHGGANQQFTFTSAGELRVG--GDKCLDAAGGGTTNGTPVVIWPC-NGGAN 82


                   ....*
gi 1176265075 2462 QKWDF 2466
Cdd:cd23418     83 QKWRF 87
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
2382-2466 1.27e-08

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 55.23  E-value: 1.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2382 GLIKSKANDACLDViGGRDVSGAKVALWIEHG-KARQKWTFNKDGTISSYlSDQLVLDVkGGYYYDRNhIVVNQADNNEC 2460
Cdd:pfam00652    3 GRIRNRASGKCLDV-PGGSSAGGPVGLYPCHGsNGNQLWTLTGDGTIRSV-ASDLCLDV-GSTADGAK-VVLWPCHPGNG 78


                   ....*.
gi 1176265075 2461 SQKWDF 2466
Cdd:pfam00652   79 NQRWRY 84
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 1830-1856 2.68e-08

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 52.90  E-value: 2.68e-08
                            10        20
                    ....*....|....*....|....*..
gi 1176265075  1830 IRVVRGCWVLYEKPRYQGQKYILEEGE 1856
Cdd:smart00247   36 VRVESGCWVLYEQPNYRGRQYVLEPGE 62
beta-trefoil_Ricin_SCDase cd23456
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ...
 2384-2467 2.74e-07

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: 51.59  E-value: 2.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2384 IKSKANDACLDVIGGrDVSGAKVALWIEHGKARQKWTFNKDGTISSYLSDQLVLDVKGGYYYdrNHIVVNQADNNECSQK 2463
Cdd:cd23456      5 LKSQASGLCLDVSGG-ATNGANVVVYDCNNSNSQKWYYDATGRLHSKANPGKCLDAGGENSN--GANVVLWACNDSANQR 81


                   ....
gi 1176265075 2464 WDFE 2467
Cdd:cd23456     82 WDFD 85
RicinB_lectin_2 pfam14200
Ricin-type beta-trefoil lectin domain-like;
2384-2442 1.81e-06

Ricin-type beta-trefoil lectin domain-like;


Pssm-ID: 464102 [Multi-domain]  Cd Length: 89  Bit Score: 48.14  E-value: 1.81e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1176265075 2384 IKSKANDACLDVIGGRDVSGAKVALWIEHGKARQKWTFNKDG----TISSYLSDqLVLDVKGG 2442
Cdd:pfam14200   18 IVNVASGKYLDVAGGSTANGANVQQWTDNGNDNQQWRIVDAGdgyyRIVNKASG-KVLDVAGS 79
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 2341-2466 1.91e-06

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 7 (GALNT7) and similar proteins; GALNT7 (EC 2.4.1.41), also called polypeptide GalNAc transferase 7, GalNAc-T7, pp-GaNTase 7, protein-UDP acetylgalactosaminyltransferase 7, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7, acts as glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Its appropriate peptide substrate remains unidentified. GALNT7 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467315 [Multi-domain]  Cd Length: 124  Bit Score: 49.22  E-value: 1.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2341 IKNRSQDKYLTVTGKLMDARatsVCLSPlnCK---NTQIWRYSC-GLIKSkaNDACLDVIGgrdvSGAKVALWIEHGKAR 2416
Cdd:cd23437      8 IRNLGTGLCLDTMGHQNGGP---VGLYP--CHgmgGNQLFRLNEaGQLAV--GEQCLTASG----SGGKVKLRKCNLGET 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1176265075 2417 QKWTFNK-DGTISsYLSDQLVLDVKGgyyyDRNHIVVNQADNNECSQKWDF 2466
Cdd:cd23437     77 GKWEYDEaTGQIR-HKGTGKCLDLNE----GTNKLILQPCDSSSPSQKWEF 122
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 2253-2332 2.76e-06

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 47.12  E-value: 2.76e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075  2253 ISLFALENYEGKELRLQEAVSSvLNKDLHF-LTQSVWVRSGLWIAYEGCHFLGKQFLLEP---TKISNWTQFSGWklIGS 2328
Cdd:smart00247    2 ITLYEDENFQGRSYELSDDCPS-LQDYGSRdNVSSVRVESGCWVLYEQPNYRGRQYVLEPgeyPDYQEWGGFNDQ--ISS 78


                    ....
gi 1176265075  2329 LRPV 2332
Cdd:smart00247   79 IRRI 82
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 2347-2421 3.27e-06

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


Pssm-ID: 467297 [Multi-domain]  Cd Length: 130  Bit Score: 48.50  E-value: 3.27e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1176265075 2347 DKYLTVTGkLMDARATSVCLSPLNCKNTQIWRYSC-GLIKSKANDACLDVIGGRDVSGAKVALWIEHGKARQKWTF 2421
Cdd:cd23418     56 DKCLDAAG-GGTTNGTPVVIWPCNGGANQKWRFNSdGTIRNVNSGLCLDVAGGGTANGTRLILWSCNGGSNQRWRR 130
beta-trefoil_Ricin_SCDase_rpt1 cd23499
first ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ...
 2384-2466 4.42e-05

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


Pssm-ID: 467377 [Multi-domain]  Cd Length: 131  Bit Score: 45.52  E-value: 4.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2384 IKSKANDACLDvIGGRD---VSGAKVALW-IEHGKARQKWTFNKD-GTISSYLSDQLVLDVKGGYYydRNHIVVNQADNN 2458
Cdd:cd23499      5 IVNRASGKCLD-IPGNDndvVNGANVILWdCADKSADQRWIYDAAsGMLRNKANPSYCLDNRGQAY--NGGEVVLWQCED 81


                   ....*...
gi 1176265075 2459 ECSQKWDF 2466
Cdd:cd23499     82 SDNLRWTY 89
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
 2387-2464 4.47e-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: 45.02  E-value: 4.47e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1176265075 2387 KANDACLDVIGGRDVSGAKVALWIEHGKARQKWTFNKDGTISSYLSdQLVLDVKGGYYYDRNHIVVnqAD-NNECSQKW 2464
Cdd:cd23451     49 RVLGKCLDVSGGGTANGTLVQLWDCNGTGAQKWVPRADGTLYNPQS-GKCLDAPGGSTTDGTQLQL--YTcNGTAAQQW 124
lectin_2 NF035930
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
 2390-2464 8.13e-05

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: 46.70  E-value: 8.13e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1176265075 2390 DACLDVIGGRDVSGAKVALWIEHGKARQKWTFnKDGTISSYLSDQlVLDVKGGYYYDRNHIVVNQADNNEcSQKW 2464
Cdd:NF035930   167 DLCLDVADGNTRDGARVIAWSCSGGPNQRWRW-RGGQIRSRLSGK-CLDIEGGRARPGQPVIVWSCNGGP-NQRW 238
beta-trefoil_Ricin_AgaB34-like cd23458
ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 ...
 2338-2464 1.29e-04

ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 and similar proteins; Beta-agarase (EC 3.2.1.81), also called endo-beta-agarase, is a glycosyl hydrolase family 16 (GH16) member that catalyzes the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea (marine red algae), giving the tetramer as the predominant product. Beta-agarase contains a ricin B-type lectin domain that adopts a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467336 [Multi-domain]  Cd Length: 135  Bit Score: 44.24  E-value: 1.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2338 YFRIKNRSQDKYLTVTGKLMdARATSVCLSPLNCKNTQIWR--------YScglIKSKANDACLDVIGGRDVSGAKVALW 2409
Cdd:cd23458      2 TYRIRNRNSGKCIDVAGGST-ANGANIQQWDCGSGSNQQWTlveidngyYR---IKASHSGKCLDVAGGSTANGANIQQW 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1176265075 2410 IEHGKARQKWTFNKDG----TISSYLSDQlVLDVKGGYYYDRNHIVVNQADNNECsQKW 2464
Cdd:cd23458     78 DCVGGANQQWKLQDLGngyfELKARHSGK-CLDVAGGSTANGASIQQWTCNGNDN-QRF 134
RicinB_lectin_2 pfam14200
Ricin-type beta-trefoil lectin domain-like;
2338-2409 1.52e-04

Ricin-type beta-trefoil lectin domain-like;


Pssm-ID: 464102 [Multi-domain]  Cd Length: 89  Bit Score: 42.75  E-value: 1.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2338 YFRIKNRSQDKYLTVTGKLmDARATSVCLSPLNCKNTQIWR--------YScglIKSKANDACLDVIGGRDvSGAKVALW 2409
Cdd:pfam14200   15 YYTIVNVASGKYLDVAGGS-TANGANVQQWTDNGNDNQQWRivdagdgyYR---IVNKASGKVLDVAGSTA-NGTNVQQW 89
beta-trefoil_Ricin_SCDase_rpt1 cd23499
first ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ...
 2338-2466 1.53e-04

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


Pssm-ID: 467377 [Multi-domain]  Cd Length: 131  Bit Score: 43.98  E-value: 1.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2338 YFRIKNRSQDKYLTVTGKLMD-ARATSVCLSPlnCKNT---QIWRY--SCGLIKSKAN-DACLDViGGRDVSGAKVALWI 2410
Cdd:cd23499      2 FVRIVNRASGKCLDIPGNDNDvVNGANVILWD--CADKsadQRWIYdaASGMLRNKANpSYCLDN-RGQAYNGGEVVLWQ 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1176265075 2411 EHGKARQKWTFNkDGTISSYLSDQLVLDvkgGYYYDRNHIVVNQADNNECSQKWDF 2466
Cdd:cd23499     79 CEDSDNLRWTYD-NGVLRSKHNPNIVLD---AYGRDNNSQVGQWEYHGGANQQWEL 130
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
 2382-2464 1.54e-04

ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and similar proteins; Glucan endo-1,3-beta-glucosidase (EC 3.2.1.39), also called (1->3)-beta-glucan endohydrolase, or (1->3)-beta-glucanase, or laminarinase, belongs to the glycosyl hydrolase 64 (GH64) family. It catalyzes hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans. It has been implicated in the defense against fungal pathogens. Glucan endo-1,3-beta-glucosidase contains a C-terminal ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467329 [Multi-domain]  Cd Length: 125  Bit Score: 43.47  E-value: 1.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2382 GLIKSKANDACLDVIGGRDVSGAKVALWIEHGKARQKWTFNKDGTISSYlsdQLVLDVKGGYYYDRNHIVVnqAD-NNEC 2460
Cdd:cd23451      3 GPVRLANAGKCLDVPGSSTADGNPVQIYTCNGTAAQKWTLGTDGTLRVL---GKCLDVSGGGTANGTLVQL--WDcNGTG 77


                   ....
gi 1176265075 2461 SQKW 2464
Cdd:cd23451     78 AQKW 81
beta-trefoil_Ricin_RPI cd23452
ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine ...
 2370-2464 2.30e-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: 43.27  E-value: 2.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2370 NCKNTQIWRY-SCGLIKSkaNDACLDVIGGRDVSGAKVALWIEHGKARQKWTFNKDGTISSYLSDQLVlDVKGGyyydrn 2448
Cdd:cd23452     33 NGTNAQKWTFaSDGTLRA--LGKCLDVAWGGTDNGTAVQLWTCSGNPAQQFVLSGAGDLVNPQANKCV-DVSGG------ 103

                           90       100
                   ....*....|....*....|....*
gi 1176265075 2449 hivvNQADNN-----ECS----QKW 2464
Cdd:cd23452    104 ----NSGNGTrlqlwECSgnanQKW 124
beta-trefoil_Ricin_RPI cd23452
ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine ...
 2392-2442 2.44e-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: 2.44e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1176265075 2392 CLDVIGGRDVSGAKVALWIEHGKARQKWTFNKDGTISSYlsdQLVLDVKGG 2442
Cdd:cd23452     13 CIDVPNSSTTDGAPLQLWDCNGTNAQKWTFASDGTLRAL---GKCLDVAWG 60
beta-trefoil_Ricin_RIPs_II_rpt2 cd23444
second ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating ...
 2370-2466 4.66e-04

second ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating proteins (RIPs); Type II ribosome-inactivating proteins (RIPs) inhibit translation in eukaryotes by irreversibly inactivating the 28S rRNA and preventing the binding of elongation factor II to the ribosome. They consist of a catalytic A-chain which has rRNA N-glycosidase activity and a lectin B-chain containing two ricin B-type lectin domains with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The lectin chain facilitates the internalization of the catalytic chain on binding to the cell surface. The two chains are connected by a disulfide bridge. This model corresponds to the second ricin B-type lectin domain. Members of this family includes Ricinus communis ricin, bitter gourd (Momordica charantia) seed lectin (BGSL), snake gourd (Trichosanthes anguina) seed lectin (SGSL), Sambucus ebulus ebulin I, Sambucus nigra nigrin b (also known as agglutinin V or SNAV), SNAI (also known as agglutinin I), SNAI' and SNAIf, Abrus precatorius abrin (ABR) and agglutinin-I (AAG), and Viscum album beta-galactoside-specific lectins 1-4 (also known as mistletoe lectins or MLs).


Pssm-ID: 467322 [Multi-domain]  Cd Length: 122  Bit Score: 42.26  E-value: 4.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2370 NCKNT---QIWR-YSCGLIKSKAN-DACLDviGGRDVSGAKVALWIEHGKARQKWTFNKDGTISSyLSDQLVLDVKGGYY 2444
Cdd:cd23444     26 ECVSNkkeQKWAlYPDGTIRPNQNrNLCLT--SSSDVQGSIIVVLSCSGSSGQRWVFRNDGTILN-LYTGLVMDVKESDP 102

                           90       100
                   ....*....|....*....|..
gi 1176265075 2445 YDRNhIVVNQAdNNECSQKWDF 2466
Cdd:cd23444    103 SLKQ-IILWPA-TGGPNQQWTL 122
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 1838-1965 4.75e-04

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: 40.94  E-value: 4.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 1838 VLYEKPRYQGQKYILEEgekmlsDILNLHCEEHqgnitigsvrqiMKDCSvpeiqlypqdgsdcfaiSIQsavtdvgelr 1917
Cdd:pfam00030    3 VLYEKENFQGRSIELTD------DCPSLQERGF------------NSRVN-----------------SIR---------- 37

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1176265075 1918 vrnpalsVKAGVWLAYSDVNYKGTMMVLEE----NHGSCETSAADIKSLRPL 1965
Cdd:pfam00030   38 -------VLSGAWVLYEHPNFRGRQYVLEPgeypDWSDWGAPNDRIGSLRPI 82
beta-trefoil_Ricin_1,3Gal43A cd23446
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and ...
 2338-2421 1.29e-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: 41.21  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2338 YFRIKNRSQDKYLTVTGKLMDARATSVcLSPLNCKNTQIWRY-SCGL----IKSKANDACLDVIGGRDVSGAKVALWIEH 2412
Cdd:cd23446     49 YYKIVNRNSGKALDVNGASTADGAAII-QWTSNGGDNQQWQIvDTGDgyykIVNRNSGKLLDVNGWSTADGADIIQWSDN 127


                   ....*....
gi 1176265075 2413 GKARQKWTF 2421
Cdd:cd23446    128 GGTNQQWQL 136
lectin_2 NF035930
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
 2371-2419 1.55e-03

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: 42.47  E-value: 1.55e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1176265075 2371 CKN--TQIWRYSCGLIKSKANDACLDVIGGRDVSGAKVALWIEHGKARQKW 2419
Cdd:NF035930   188 CSGgpNQRWRWRGGQIRSRLSGKCLDIEGGRARPGQPVIVWSCNGGPNQRW 238
beta-trefoil_Ricin_ebulin-like_rpt1 cd23483
first ricin B-type lectin domain, beta-trefoil fold, found in Sambucus ebulus ebulin I and ...
 2392-2429 1.67e-03

first ricin B-type lectin domain, beta-trefoil fold, found in Sambucus ebulus ebulin I and similar proteins; The family includes Sambucus ebulus ebulin I and Sambucus nigra nigrin b (also known as agglutinin V or SNAV), SNAI (also known as agglutinin I), SNAI' and SNAIf. Ebulin l is a type II ribosome-inactivating protein (RIP) isolated from the leaves of Sambucus ebulus. It is a disulfide-linked heterodimer composed of a toxic A chain and a galactoside-specific lectin B chain. It is considered a nontoxic type II RIP due to a reduced cytotoxicity on whole cells and animals as compared with other toxic type II RIP like ricins. Ebulin l binds an A-chain substrate analogue, pteroic acid. It binds bind galactose and lactose in subdomain 1alpha in a similar manner to that of ricin. In contrast, it binds only the monosaccharide galactose, and not the disaccharide lactose in subdomain 2gamma. SNAV is a non-toxic GalNAc-specific type II RIP which strongly inhibits mammalian protein synthesis but does not affect plant nor bacterial protein synthesis. SNAI is a Neu5Ac(alpha2-6)Gal/GalNAc-specific agglutinin. It also acts as a type II RIP that strongly inhibits mammalian but not plant ribosomes. SNAI' is another NeuAc(alpha2,6)Gal/GalNAc binding type II RIP from elderberry (Sambucus nigra) bark. It is a minor bark protein which closely resembles the major Neu5Ac(alpha2,6)Gal/GalNAc binding type II RIP, SNAI, with respect to its carbohydrate-binding specificity and ribosome-inactivating activity but has a different molecular structure due to a single cysteine residue present in the B chain of SNAI but absent from SNAI'. SNAIf is a fruit-specific SNAI. It functions as a fetuin-binding fruit lectin. Like Ebulin l, SNAV, SNAI, SNAI' and SNAIf consist of a sugar-binding B chain linked via a disulfide bond to the catalytically active A chain. The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain. It may also be responsible for cell agglutination (lectin activity). The B chain contains two ricin B-type lectin domains with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. This model corresponds to the first ricin B-type lectin domain.


Pssm-ID: 467361 [Multi-domain]  Cd Length: 127  Bit Score: 40.57  E-value: 1.67e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1176265075 2392 CLDVIGGRDVSGAKVALWIEHGKARQKWTFNKDGTISS 2429
Cdd:cd23483     13 CVDVRNGYDTDGTPVQLWPCGTQRNQQWTFDTDGTIRS 50
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 2176-2244 1.93e-03

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 39.41  E-value: 1.93e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1176265075  2176 FQGTCIDFTEEATDL-ESFTPC---SFKVLRGCWLLcYQ--GETGDNWcVLEEDLYADLASCGCPAAAVKSLKPV 2244
Cdd:smart00247   10 FQGRSYELSDDCPSLqDYGSRDnvsSVRVESGCWVL-YEqpNYRGRQY-VLEPGEYPDYQEWGGFNDQISSIRRI 82
beta-trefoil_Ricin_RIPs_II_rpt1 cd23443
first ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating ...
 2392-2429 2.46e-03

first ricin B-type lectin domain, beta-trefoil fold, found in type II ribosome-inactivating proteins (RIPs); Type II ribosome-inactivating proteins (RIPs) inhibit translation in eukaryotes by irreversibly inactivating the 28S rRNA and preventing the binding of elongation factor II to the ribosome. They consist of a catalytic A-chain which has rRNA N-glycosidase activity and a lectin B-chain containing two ricin B-type lectin domains with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The lectin chain facilitates the internalization of the catalytic chain on binding to the cell surface. The two chains are connected by a disulfide bridge. This model corresponds to the first ricin B-type lectin domain. Members of this subfamily includes Ricinus communis ricin, bitter gourd (Momordica charantia) seed lectin (BGSL), snake gourd (Trichosanthes anguina) seed lectin (SGSL), Sambucus ebulus ebulin I, Sambucus nigra nigrin b (also known as agglutinin V or SNAV), SNAI (also known as agglutinin I), SNAI' and SNAIf, Abrus precatorius abrin (ABR) and agglutinin-I (AAG), and Viscum album beta-galactoside-specific lectins 1-4 (also known as mistletoe lectins or MLs).


Pssm-ID: 467321 [Multi-domain]  Cd Length: 123  Bit Score: 39.97  E-value: 2.46e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1176265075 2392 CLDVIGGRDVSGAKVALW-IEHGKARQKWTFNKDGTISS 2429
Cdd:cd23443     12 CVDVKDGYYSDGNPVILWpCKSQDANQLWTFKRDGTIRS 50
beta-trefoil_Ricin_ebulin-like_rpt2 cd23490
second ricin B-type lectin domain, beta-trefoil fold, found in Sambucus ebulus ebulin I and ...
 2413-2468 5.22e-03

second ricin B-type lectin domain, beta-trefoil fold, found in Sambucus ebulus ebulin I and similar proteins; This subfamily includes Sambucus ebulus ebulin I and Sambucus nigra nigrin b (also known as agglutinin V or SNAV), SNAI (also known as agglutinin I), SNAI' and SNAIf. Ebulin l is a type II ribosome-inactivating protein (RIP) isolated from the leaves of Sambucus ebulus. It is a disulfide-linked heterodimer composed of a toxic A chain and a galactoside-specific lectin B chain. It is considered a nontoxic type II RIP due to a reduced cytotoxicity on whole cells and animals as compared with other toxic type II RIP like ricin. Ebulin l binds an A-chain substrate analogue, pteroic acid. It binds bind galactose and lactose in subdomain 1alpha in a similar manner to that of ricin. In contrast, it binds only the monosaccharide galactose, and not the disaccharide lactose in subdomain 2gamma. SNAV is a non-toxic GalNAc-specific type II RIP which strongly inhibits mammalian protein synthesis but does not affect plant nor bacterial protein synthesis. SNAI is Neu5Ac(alpha2-6)Gal/GalNAc specific agglutinin. It also acts as a type II RIP that strongly inhibits mammalian but not plant ribosomes. SNAI' is another NeuAc(alpha2,6)Gal/GalNAc binding type II RIP from elderberry (Sambucus nigra) bark. It is a minor bark protein which closely resembles the major Neu5Ac(alpha2,6)Gal/GalNAc binding type II RIP, SNAI, with respect to its carbohydrate-binding specificity and ribosome-inactivating activity but has a different molecular structure due to a single cysteine residue present in the B chain of SNAI but absent from SNAI'. SNAIf is fruit specific SNAI. It functions as fetuin-binding fruit lectin. Like Ebulin l, SNAV, SNAI, SNAI' and SNAIf consist of a sugar-binding B chain linked via a disulfide bond to the catalytically active A chain. The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain. It may also be responsible for cell agglutination (lectin activity). The B chain contains two ricin B-type lectin domains with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The model corresponds to the second ricin B-type lectin domain.


Pssm-ID: 467368 [Multi-domain]  Cd Length: 125  Bit Score: 39.36  E-value: 5.22e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1176265075 2413 GKARQKWTFNKDGTISSyLSDQLVLDVKGGYYYDRnHIVVNQADNNEcSQKWDFEI 2468
Cdd:cd23490     73 GLPNQRWVFNTDGTIVN-PNSKLVMDVKQSDVSLR-EIILFPPTGNP-NQQWITQT 125
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 2382-2467 6.24e-03

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 9 (Pgant9) and similar proteins; The subfamily includes Pgant9 (also called pp-GaNTase 9, protein-UDP acetylgalactosaminyltransferase 9, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9), Pgant4 (also called pp-GaNTase 4, N-acetylgalactosaminyltransferase 4, protein-UDP acetylgalactosaminyltransferase 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4) and Pgant6 (also called pp-GaNTase 6, N-acetylgalactosaminyltransferase 6, protein-UDP acetylgalactosaminyltransferase 6, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6). They function as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant9 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Pgant4 and Pgant6 do not act as a peptide transferase, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. They prefer the diglycosylated Muc5AC-3/13 as a substrate. Pgant6 may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467340 [Multi-domain]  Cd Length: 126  Bit Score: 38.89  E-value: 6.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2382 GLIKSKANDACLDVIGGRDVSGAKVALWIEHGKAR-QKWTFNKDGTI--------SSYLSDQLVL----DVKGGY--YYD 2446
Cdd:cd23462      6 GEIRNLAGKLCLDAPGRKKELNKPVGLYPCHGQGGnQYWMLTKDGEIrrddlcldYAGGSGDVTLypchGMKGNQfwIYD 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1176265075 2447 RN--------------------HIVVNQADNNECSQKWDFE 2467
Cdd:cd23462     86 EEtkqivhgtskkclelsddssKLVMEPCNGSSPRQQWEFE 126
beta-trefoil_Ricin_laminarinase cd23451
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...
 2344-2420 6.97e-03

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: 38.85  E-value: 6.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2344 RSQDKYLTVTGKLMdARATSVCLSplNCKNT--QIWRYSC-GLIKSKANDACLDVIGGRDVSGAKVALWIEHGKARQKWT 2420
Cdd:cd23451     49 RVLGKCLDVSGGGT-ANGTLVQLW--DCNGTgaQKWVPRAdGTLYNPQSGKCLDAPGGSTTDGTQLQLYTCNGTAAQQWT 125
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 2382-2466 7.04e-03

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


Pssm-ID: 467338 [Multi-domain]  Cd Length: 121  Bit Score: 38.58  E-value: 7.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176265075 2382 GLIKSKANDACLDVIgGRDVSGAKVALWIEHGKAR-QKWTFNKDGTISsylSDQLVLDvkggyYYDRNHIVVNQADNNEC 2460
Cdd:cd23460      3 GQIKHTESGLCLDWA-GESNGDKTVALKPCHGGGGnQFWMYTGDGQIR---QDHLCLT-----ADEGNKVTLRECADQLP 73


                   ....*.
gi 1176265075 2461 SQKWDF 2466
Cdd:cd23460     74 SQEWSY 79
 
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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