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Conserved domains on  [gi|334184536|ref|NP_001189624|]
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beta-galactosidase 8 [Arabidopsis thaliana]

Protein Classification

beta-galactosidase( domain architecture ID 1000425)

beta-galactosidase catalyzes the hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides

CATH:  3.20.20.80
CAZY:  GH35
EC:  3.2.1.23
Gene Ontology:  GO:0004565|GO:0005975
PubMed:  8535779|7624375|21639842|31731209|20552664

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03059 super family cl31552
beta-galactosidase; Provisional
 24-846 0e+00

beta-galactosidase; Provisional


The actual alignment was detected with superfamily member PLN03059:

Pssm-ID: 166698 [Multi-domain]  Cd Length: 840  Bit Score: 1102.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536  24 ANVTYDHRALVIDGKRKVLISGSIHYPRSTPEMWPELIQKSKDGGLDVIETYVFWSGHEPEKNKYNFEGRYDLVKFVKLA 103
Cdd:PLN03059  28 ASVSYDHRAFIINGQRRILISGSIHYPRSTPEMWPDLIQKAKDGGLDVIQTYVFWNGHEPSPGNYYFEDRYDLVKFIKVV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 104 AKAGLYVHLRIGPYVCAEWNYGGFPVWLHFVPGIKFRTDNEPFKEEMQRFTTKIVDLMKQEKLYASQGGPIILSQIENEY 183
Cdd:PLN03059 108 QAAGLYVHLRIGPYICAEWNFGGFPVWLKYVPGIEFRTDNGPFKAAMQKFTEKIVDMMKSEKLFEPQGGPIILSQIENEY 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 184 GNIDSAYGAAAKSYIKWSASMALSLDTGVPWNMCQQTDAPDPMINTCNGFYCDQFTPNSNNKPKMWTENWSGWFLGFGDP 263
Cdd:PLN03059 188 GPVEWEIGAPGKAYTKWAADMAVKLGTGVPWVMCKQEDAPDPVIDTCNGFYCENFKPNKDYKPKMWTEAWTGWYTEFGGA 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 264 SPYRPVEDLAFAVARFYQRGGTFQNYYMYHGGTNFDRTSGGPLISTSYDYDAPIDEYGLLRQPKWGHLRDLHKAIKLCED 343
Cdd:PLN03059 268 VPNRPAEDLAFSVARFIQNGGSFINYYMYHGGTNFGRTAGGPFIATSYDYDAPLDEYGLPREPKWGHLRDLHKAIKLCEP 347

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 344 ALIATDPTITSLGSNLEAAVYKTESgSCAAFLANVDTKSDATVTFNGKSYNLPAWSVSILPDCKNVAFNTAKINSATest 423
Cdd:PLN03059 348 ALVSVDPTVTSLGSNQEAHVFKSKS-ACAAFLANYDTKYSVKVTFGNGQYDLPPWSVSILPDCKTAVFNTARLGAQS--- 423

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 424 afARQSLKPDGGSSaelgSQWSYIKEPIGISKADAFLKPGLLEQINTTADKSDYLWYSLRTDIKGDETFLDEGSKAVLHI 503
Cdd:PLN03059 424 --SQMKMNPVGSTF----SWQSYNEETASAYTDDTTTMDGLWEQINVTRDATDYLWYMTEVHIDPDEGFLKTGQYPVLTI 497

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 504 ESLGQVVYAFINGKLAGSGHGK---QKISLDIPINLVTGTNTIDLLSVTVGLANYGAFFDLVGAGITGPVTLKSAKGGsS 580
Cdd:PLN03059 498 FSAGHALHVFINGQLAGTVYGElsnPKLTFSQNVKLTVGINKISLLSVAVGLPNVGLHFETWNAGVLGPVTLKGLNEG-T 576

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 581 IDLASQQWTYQVGLKGEDTGLATV---DSSEWVSKSPLPTKQPLIWYKTTFDAPSGSEPVAIDFTGTGKGIAWVNGQSIG 657
Cdd:PLN03059 577 RDLSGWKWSYKIGLKGEALSLHTItgsSSVEWVEGSLLAQKQPLTWYKTTFDAPGGNDPLALDMSSMGKGQIWINGQSIG 656

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 658 RYWPTSIAgNGGCTeSCDYRGSYRANKCLKNCGKPSQTLYHVPRSWLKPSGNILVLFEEMGGDPTQISFATKQTGSnLCL 737
Cdd:PLN03059 657 RHWPAYTA-HGSCN-GCNYAGTFDDKKCRTNCGEPSQRWYHVPRSWLKPSGNLLIVFEEWGGNPAGISLVKRTTDS-VCA 733

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 738 TVSQSHpPPVDTWTSDSkISNRNRTRPVLSLKCPiSTQVIFSIKFASFGTPKGTCGSFTQGHCNSSRSLSLVQKACIGLR 817
Cdd:PLN03059 734 DIFEGQ-PALKNWQIIA-SGKVNSLQPKAHLWCP-PGQKISKIKFASFGVPQGTCGSFREGSCHAHKSYDAFERNCIGKQ 810

                        810       820       830
                 ....*....|....*....|....*....|
gi 334184536 818 SCNVEVSTRVF-GEPCRGVVKSLAVEASCS 846
Cdd:PLN03059 811 SCSVTVAPEVFgGDPCPDSMKKLSVEAVCS 840
 
Name Accession Description Interval E-value
PLN03059 PLN03059
beta-galactosidase; Provisional
 24-846 0e+00

beta-galactosidase; Provisional


Pssm-ID: 166698 [Multi-domain]  Cd Length: 840  Bit Score: 1102.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536  24 ANVTYDHRALVIDGKRKVLISGSIHYPRSTPEMWPELIQKSKDGGLDVIETYVFWSGHEPEKNKYNFEGRYDLVKFVKLA 103
Cdd:PLN03059  28 ASVSYDHRAFIINGQRRILISGSIHYPRSTPEMWPDLIQKAKDGGLDVIQTYVFWNGHEPSPGNYYFEDRYDLVKFIKVV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 104 AKAGLYVHLRIGPYVCAEWNYGGFPVWLHFVPGIKFRTDNEPFKEEMQRFTTKIVDLMKQEKLYASQGGPIILSQIENEY 183
Cdd:PLN03059 108 QAAGLYVHLRIGPYICAEWNFGGFPVWLKYVPGIEFRTDNGPFKAAMQKFTEKIVDMMKSEKLFEPQGGPIILSQIENEY 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 184 GNIDSAYGAAAKSYIKWSASMALSLDTGVPWNMCQQTDAPDPMINTCNGFYCDQFTPNSNNKPKMWTENWSGWFLGFGDP 263
Cdd:PLN03059 188 GPVEWEIGAPGKAYTKWAADMAVKLGTGVPWVMCKQEDAPDPVIDTCNGFYCENFKPNKDYKPKMWTEAWTGWYTEFGGA 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 264 SPYRPVEDLAFAVARFYQRGGTFQNYYMYHGGTNFDRTSGGPLISTSYDYDAPIDEYGLLRQPKWGHLRDLHKAIKLCED 343
Cdd:PLN03059 268 VPNRPAEDLAFSVARFIQNGGSFINYYMYHGGTNFGRTAGGPFIATSYDYDAPLDEYGLPREPKWGHLRDLHKAIKLCEP 347

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 344 ALIATDPTITSLGSNLEAAVYKTESgSCAAFLANVDTKSDATVTFNGKSYNLPAWSVSILPDCKNVAFNTAKINSATest 423
Cdd:PLN03059 348 ALVSVDPTVTSLGSNQEAHVFKSKS-ACAAFLANYDTKYSVKVTFGNGQYDLPPWSVSILPDCKTAVFNTARLGAQS--- 423

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 424 afARQSLKPDGGSSaelgSQWSYIKEPIGISKADAFLKPGLLEQINTTADKSDYLWYSLRTDIKGDETFLDEGSKAVLHI 503
Cdd:PLN03059 424 --SQMKMNPVGSTF----SWQSYNEETASAYTDDTTTMDGLWEQINVTRDATDYLWYMTEVHIDPDEGFLKTGQYPVLTI 497

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 504 ESLGQVVYAFINGKLAGSGHGK---QKISLDIPINLVTGTNTIDLLSVTVGLANYGAFFDLVGAGITGPVTLKSAKGGsS 580
Cdd:PLN03059 498 FSAGHALHVFINGQLAGTVYGElsnPKLTFSQNVKLTVGINKISLLSVAVGLPNVGLHFETWNAGVLGPVTLKGLNEG-T 576

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 581 IDLASQQWTYQVGLKGEDTGLATV---DSSEWVSKSPLPTKQPLIWYKTTFDAPSGSEPVAIDFTGTGKGIAWVNGQSIG 657
Cdd:PLN03059 577 RDLSGWKWSYKIGLKGEALSLHTItgsSSVEWVEGSLLAQKQPLTWYKTTFDAPGGNDPLALDMSSMGKGQIWINGQSIG 656

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 658 RYWPTSIAgNGGCTeSCDYRGSYRANKCLKNCGKPSQTLYHVPRSWLKPSGNILVLFEEMGGDPTQISFATKQTGSnLCL 737
Cdd:PLN03059 657 RHWPAYTA-HGSCN-GCNYAGTFDDKKCRTNCGEPSQRWYHVPRSWLKPSGNLLIVFEEWGGNPAGISLVKRTTDS-VCA 733

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 738 TVSQSHpPPVDTWTSDSkISNRNRTRPVLSLKCPiSTQVIFSIKFASFGTPKGTCGSFTQGHCNSSRSLSLVQKACIGLR 817
Cdd:PLN03059 734 DIFEGQ-PALKNWQIIA-SGKVNSLQPKAHLWCP-PGQKISKIKFASFGVPQGTCGSFREGSCHAHKSYDAFERNCIGKQ 810

                        810       820       830
                 ....*....|....*....|....*....|
gi 334184536 818 SCNVEVSTRVF-GEPCRGVVKSLAVEASCS 846
Cdd:PLN03059 811 SCSVTVAPEVFgGDPCPDSMKKLSVEAVCS 840
Glyco_hydro_35 pfam01301
Glycosyl hydrolases family 35;
32-336 6.48e-171

Glycosyl hydrolases family 35;


Pssm-ID: 396048 [Multi-domain]  Cd Length: 316  Bit Score: 496.39  E-value: 6.48e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536   32 ALVIDGKRKVLISGSIHYPRSTPEMWPELIQKSKDGGLDVIETYVFWSGHEPEKNKYNFEGRYDLVKFVKLAAKAGLYVH 111
Cdd:pfam01301   1 SFLIDGKRFRLISGSIHYFRIPPEMWPDRLQKAKALGLNAIETYVFWNLHEPEPGQYDFSGILDLVKFIKLAQEAGLYVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536  112 LRIGPYVCAEWNYGGFPVWLHFVPGIKFRTDNEPFKEEMQRFTTKIVDLMKqeKLYASQGGPIILSQIENEYG--NIDSA 189
Cdd:pfam01301  81 LRPGPYICAEWDFGGLPAWLLTVPGIRLRTSDPPFLEAVERYLTALLPKMK--PLQATNGGPIIMVQVENEYGsyGVDKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536  190 YGAA-AKSYIKWSASMALSLDTGVPWNMCQQ-TDAPDPMINTCNGFYCDQFT--------PNSNNKPKMWTENWSGWFLG 259
Cdd:pfam01301 159 YLRAlRKAYKEWGADMALLFTTDGPWGMCLQcGDLPGPDIYATNGFGCGANPpsnfkllrPFSPNKPLMWSEFWTGWFDH 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536  260 FGDPSPYRPVEDLAFAVARFYQRgGTFQNYYMYHGGTNFDRTSGGPLIS---TSYDYDAPIDEYGLLRqPKWGHLRDLHK 336
Cdd:pfam01301 239 WGGPHAIRPAEDIAFEVARFLAK-NSSVNLYMFHGGTNFGFTNGANFYGpqtTSYDYDAPIDEAGDPT-PKYGHLKDLIT 316
Gal_Rha_Lectin_BGal cd22842
galactose/rhamnose binding lectin domain found in plant beta-galactosidases and similar ...
 758-845 5.56e-35

galactose/rhamnose binding lectin domain found in plant beta-galactosidases and similar proteins; The family represents a group of plant beta-galactosidases (BGals), which belong to glycoside hydrolase family 35. They have a C-terminal domain homologous to animal galactose and rhamnose-binding lectins. BGals (EC 3.2.1.23), also called Exo-(1->4)-beta-D-galactanase, or lactase, catalyze hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Some family members contain more than one galactose/rhamnose binding lectin domain. Due to the lack of rhamnose-binding key residues, the galactose/rhamnose-binding lectin domains of BGals do not form a binding pocket for rhamnose. Therefore, BGals are unlikely to act as rhamnose-binding lectins.


Pssm-ID: 438699 [Multi-domain]  Cd Length: 91  Bit Score: 127.78  E-value: 5.56e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 758 NRNRTRPVLSLKCPiSTQVIFSIKFASFGTPKGTCGSFTQGHCNSSRSLSLVQKACIGLRSCNVEVSTRV-FGEPCRGVV 836
Cdd:cd22842    4 NEGGPGSTLTLSCP-AGQVISSIDFASYGTPTGTCGSFSKGSCHAPNSLSVVEKACLGKNSCSIPASNSVfFGDPCPGTT 82


                 ....*....
gi 334184536 837 KSLAVEASC 845
Cdd:cd22842   83 KRLAVQATC 91
GanA COG1874
Beta-galactosidase GanA [Carbohydrate transport and metabolism];
38-194 1.50e-22

Beta-galactosidase GanA [Carbohydrate transport and metabolism];


Pssm-ID: 441478 [Multi-domain]  Cd Length: 609  Bit Score: 103.08  E-value: 1.50e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536  38 KRKVLISGSIHYPRSTPEMWPELIQKSKDGGLDVIET-YVFWSGHEPEKNKYNFEGrydLVKFVKLAAKAGLYVHLRIGP 116
Cdd:COG1874    7 KPFLILGGDYHPERWPPEVWAEDIRLMKAAGLNTVRIgYFAWNLHEPEEGVFDFDW---LDRFIDLLHEAGLKVILRTPT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 117 YVcaewnyggFPVWLH---------------FVPGI--KFRTDNEPFKEEMQRFTTKivdLMKQeklYAsQGGPIILSQI 179
Cdd:COG1874   84 AA--------PPAWLLkkypeilpvdadgrrRGFGSrrHYCPSSPVYREAARRIVRA---LAER---YG-DHPAVIMWQV 148

                        170
                 ....*....|....*
gi 334184536 180 ENEYGNIDSAYGAAA 194
Cdd:COG1874  149 DNEYGSYDYCDACAA 163
 
Name Accession Description Interval E-value
PLN03059 PLN03059
beta-galactosidase; Provisional
 24-846 0e+00

beta-galactosidase; Provisional


Pssm-ID: 166698 [Multi-domain]  Cd Length: 840  Bit Score: 1102.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536  24 ANVTYDHRALVIDGKRKVLISGSIHYPRSTPEMWPELIQKSKDGGLDVIETYVFWSGHEPEKNKYNFEGRYDLVKFVKLA 103
Cdd:PLN03059  28 ASVSYDHRAFIINGQRRILISGSIHYPRSTPEMWPDLIQKAKDGGLDVIQTYVFWNGHEPSPGNYYFEDRYDLVKFIKVV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 104 AKAGLYVHLRIGPYVCAEWNYGGFPVWLHFVPGIKFRTDNEPFKEEMQRFTTKIVDLMKQEKLYASQGGPIILSQIENEY 183
Cdd:PLN03059 108 QAAGLYVHLRIGPYICAEWNFGGFPVWLKYVPGIEFRTDNGPFKAAMQKFTEKIVDMMKSEKLFEPQGGPIILSQIENEY 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 184 GNIDSAYGAAAKSYIKWSASMALSLDTGVPWNMCQQTDAPDPMINTCNGFYCDQFTPNSNNKPKMWTENWSGWFLGFGDP 263
Cdd:PLN03059 188 GPVEWEIGAPGKAYTKWAADMAVKLGTGVPWVMCKQEDAPDPVIDTCNGFYCENFKPNKDYKPKMWTEAWTGWYTEFGGA 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 264 SPYRPVEDLAFAVARFYQRGGTFQNYYMYHGGTNFDRTSGGPLISTSYDYDAPIDEYGLLRQPKWGHLRDLHKAIKLCED 343
Cdd:PLN03059 268 VPNRPAEDLAFSVARFIQNGGSFINYYMYHGGTNFGRTAGGPFIATSYDYDAPLDEYGLPREPKWGHLRDLHKAIKLCEP 347

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 344 ALIATDPTITSLGSNLEAAVYKTESgSCAAFLANVDTKSDATVTFNGKSYNLPAWSVSILPDCKNVAFNTAKINSATest 423
Cdd:PLN03059 348 ALVSVDPTVTSLGSNQEAHVFKSKS-ACAAFLANYDTKYSVKVTFGNGQYDLPPWSVSILPDCKTAVFNTARLGAQS--- 423

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 424 afARQSLKPDGGSSaelgSQWSYIKEPIGISKADAFLKPGLLEQINTTADKSDYLWYSLRTDIKGDETFLDEGSKAVLHI 503
Cdd:PLN03059 424 --SQMKMNPVGSTF----SWQSYNEETASAYTDDTTTMDGLWEQINVTRDATDYLWYMTEVHIDPDEGFLKTGQYPVLTI 497

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 504 ESLGQVVYAFINGKLAGSGHGK---QKISLDIPINLVTGTNTIDLLSVTVGLANYGAFFDLVGAGITGPVTLKSAKGGsS 580
Cdd:PLN03059 498 FSAGHALHVFINGQLAGTVYGElsnPKLTFSQNVKLTVGINKISLLSVAVGLPNVGLHFETWNAGVLGPVTLKGLNEG-T 576

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 581 IDLASQQWTYQVGLKGEDTGLATV---DSSEWVSKSPLPTKQPLIWYKTTFDAPSGSEPVAIDFTGTGKGIAWVNGQSIG 657
Cdd:PLN03059 577 RDLSGWKWSYKIGLKGEALSLHTItgsSSVEWVEGSLLAQKQPLTWYKTTFDAPGGNDPLALDMSSMGKGQIWINGQSIG 656

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 658 RYWPTSIAgNGGCTeSCDYRGSYRANKCLKNCGKPSQTLYHVPRSWLKPSGNILVLFEEMGGDPTQISFATKQTGSnLCL 737
Cdd:PLN03059 657 RHWPAYTA-HGSCN-GCNYAGTFDDKKCRTNCGEPSQRWYHVPRSWLKPSGNLLIVFEEWGGNPAGISLVKRTTDS-VCA 733

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 738 TVSQSHpPPVDTWTSDSkISNRNRTRPVLSLKCPiSTQVIFSIKFASFGTPKGTCGSFTQGHCNSSRSLSLVQKACIGLR 817
Cdd:PLN03059 734 DIFEGQ-PALKNWQIIA-SGKVNSLQPKAHLWCP-PGQKISKIKFASFGVPQGTCGSFREGSCHAHKSYDAFERNCIGKQ 810

                        810       820       830
                 ....*....|....*....|....*....|
gi 334184536 818 SCNVEVSTRVF-GEPCRGVVKSLAVEASCS 846
Cdd:PLN03059 811 SCSVTVAPEVFgGDPCPDSMKKLSVEAVCS 840
Glyco_hydro_35 pfam01301
Glycosyl hydrolases family 35;
32-336 6.48e-171

Glycosyl hydrolases family 35;


Pssm-ID: 396048 [Multi-domain]  Cd Length: 316  Bit Score: 496.39  E-value: 6.48e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536   32 ALVIDGKRKVLISGSIHYPRSTPEMWPELIQKSKDGGLDVIETYVFWSGHEPEKNKYNFEGRYDLVKFVKLAAKAGLYVH 111
Cdd:pfam01301   1 SFLIDGKRFRLISGSIHYFRIPPEMWPDRLQKAKALGLNAIETYVFWNLHEPEPGQYDFSGILDLVKFIKLAQEAGLYVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536  112 LRIGPYVCAEWNYGGFPVWLHFVPGIKFRTDNEPFKEEMQRFTTKIVDLMKqeKLYASQGGPIILSQIENEYG--NIDSA 189
Cdd:pfam01301  81 LRPGPYICAEWDFGGLPAWLLTVPGIRLRTSDPPFLEAVERYLTALLPKMK--PLQATNGGPIIMVQVENEYGsyGVDKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536  190 YGAA-AKSYIKWSASMALSLDTGVPWNMCQQ-TDAPDPMINTCNGFYCDQFT--------PNSNNKPKMWTENWSGWFLG 259
Cdd:pfam01301 159 YLRAlRKAYKEWGADMALLFTTDGPWGMCLQcGDLPGPDIYATNGFGCGANPpsnfkllrPFSPNKPLMWSEFWTGWFDH 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536  260 FGDPSPYRPVEDLAFAVARFYQRgGTFQNYYMYHGGTNFDRTSGGPLIS---TSYDYDAPIDEYGLLRqPKWGHLRDLHK 336
Cdd:pfam01301 239 WGGPHAIRPAEDIAFEVARFLAK-NSSVNLYMFHGGTNFGFTNGANFYGpqtTSYDYDAPIDEAGDPT-PKYGHLKDLIT 316
Gal_Rha_Lectin_BGal cd22842
galactose/rhamnose binding lectin domain found in plant beta-galactosidases and similar ...
 758-845 5.56e-35

galactose/rhamnose binding lectin domain found in plant beta-galactosidases and similar proteins; The family represents a group of plant beta-galactosidases (BGals), which belong to glycoside hydrolase family 35. They have a C-terminal domain homologous to animal galactose and rhamnose-binding lectins. BGals (EC 3.2.1.23), also called Exo-(1->4)-beta-D-galactanase, or lactase, catalyze hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Some family members contain more than one galactose/rhamnose binding lectin domain. Due to the lack of rhamnose-binding key residues, the galactose/rhamnose-binding lectin domains of BGals do not form a binding pocket for rhamnose. Therefore, BGals are unlikely to act as rhamnose-binding lectins.


Pssm-ID: 438699 [Multi-domain]  Cd Length: 91  Bit Score: 127.78  E-value: 5.56e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 758 NRNRTRPVLSLKCPiSTQVIFSIKFASFGTPKGTCGSFTQGHCNSSRSLSLVQKACIGLRSCNVEVSTRV-FGEPCRGVV 836
Cdd:cd22842    4 NEGGPGSTLTLSCP-AGQVISSIDFASYGTPTGTCGSFSKGSCHAPNSLSVVEKACLGKNSCSIPASNSVfFGDPCPGTT 82


                 ....*....
gi 334184536 837 KSLAVEASC 845
Cdd:cd22842   83 KRLAVQATC 91
GHD pfam17834
Beta-sandwich domain in beta galactosidase; This entry corresponds to a beta sandwich like ...
 345-416 7.90e-30

Beta-sandwich domain in beta galactosidase; This entry corresponds to a beta sandwich like domain found in glycosyl hydrolase family 35 beta galactosidase enzymes.


Pssm-ID: 436079  Cd Length: 72  Bit Score: 112.78  E-value: 7.90e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334184536  345 LIATDPTITSLGSNLEAAVYKTESGSCAAFLANVDTKSDATVTFNGKSYNLPAWSVSILPDCKNVAFNTAKI 416
Cdd:pfam17834   1 LLSGQYTTTNLGKLQTATVFEKDKGSCVAFLVNIDDKKDANVTFRGSDYFLPAWSISILPDCKTVVFNTAKV 72
Gal_Lectin pfam02140
Galactose binding lectin domain;
768-845 3.08e-25

Galactose binding lectin domain;


Pssm-ID: 460460 [Multi-domain]  Cd Length: 79  Bit Score: 99.67  E-value: 3.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536  768 LKCPiSTQVIfSIKFASFGTPKG-TCGSFTQG-HCNSSRSLSLVQKACIGLRSCNVEVSTRVFG-EPCRGVVKSLAVEAS 844
Cdd:pfam02140   1 LSCP-PGKVI-SILFASYGRPDGtTCPSFIQGtNCHSPNSLAIVSKACQGKNSCSVPASNSVFGgDPCPGTYKYLEVEYK 78


                  .
gi 334184536  845 C 845
Cdd:pfam02140  79 C 79
GanA COG1874
Beta-galactosidase GanA [Carbohydrate transport and metabolism];
38-194 1.50e-22

Beta-galactosidase GanA [Carbohydrate transport and metabolism];


Pssm-ID: 441478 [Multi-domain]  Cd Length: 609  Bit Score: 103.08  E-value: 1.50e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536  38 KRKVLISGSIHYPRSTPEMWPELIQKSKDGGLDVIET-YVFWSGHEPEKNKYNFEGrydLVKFVKLAAKAGLYVHLRIGP 116
Cdd:COG1874    7 KPFLILGGDYHPERWPPEVWAEDIRLMKAAGLNTVRIgYFAWNLHEPEEGVFDFDW---LDRFIDLLHEAGLKVILRTPT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 117 YVcaewnyggFPVWLH---------------FVPGI--KFRTDNEPFKEEMQRFTTKivdLMKQeklYAsQGGPIILSQI 179
Cdd:COG1874   84 AA--------PPAWLLkkypeilpvdadgrrRGFGSrrHYCPSSPVYREAARRIVRA---LAER---YG-DHPAVIMWQV 148

                        170
                 ....*....|....*
gi 334184536 180 ENEYGNIDSAYGAAA 194
Cdd:COG1874  149 DNEYGSYDYCDACAA 163
Gal_Rha_Lectin_SUL-I-like cd22827
galactose/rhamnose binding lectin domain found in Toxopneustes pileolus rhamnose-binding ...
 766-845 2.03e-16

galactose/rhamnose binding lectin domain found in Toxopneustes pileolus rhamnose-binding lectin SUL-I and similar proteins; SUL-I is a galactose/rhamnose-binding lectin with mitogenic, chemotactic, and cytotoxic activity. These activities can be triggered by binding of the lectin to specific carbohydrate chains on target cells. SUL-I may be involved in self-defense against invading microorganisms. SUL-I is composed of three distinctive domains with a folding structure similar to galactose/rhamnose-binding lectin domain found in proteins such as mammalian latrophilins, Oncorhynchus keta L-rhamnose-binding lectins (CSLs), and Silurus asotus rhamnose-binding lectin (SAL). The family also includes Heliocidaris crassispina D-galactoside-specific lectin, also known as sea urchin egg lectin or SUEL, and Echinometra lucunter L-rhamnose-binding lectin ELEL-1, both of which contain only one galactose/rhamnose-binding lectin domain. SUEL binds D-galactoside. It may play an important role in the activation of eggs triggered by fertilization, or in their subsequent differentiation. The dimeric form is essential for hemagglutination activity of SUEL. ELEL-1 is a rhamnose-binding lectin that also binds alpha-D-melibiose, alpha-D-lactose, beta-D-lactose, methyl-alpha-D-galactopyranoside, methyl-beta-D--galactopyranoside and D-galactose, but not D-arabinose, L-fucose, D-glucose, D-mannose, D-maltose, D-sucrose, N-acetyl-D-galactosamine, N-acetyl-D-glucosamine, N-acetyl-D-mannosamine-D-xylose, or by glycoproteins orosomucoid, thyroglobulin, ovomucoid and porcine stomach mucin. It shows cation-independent hemagglutinating activity against rabbit and human erythrocytes. ELEL-1 agglutinates cells of Gram-positive bacterial species S. aureus but not those of Gram-negative E. coli.


Pssm-ID: 438684 [Multi-domain]  Cd Length: 89  Bit Score: 74.93  E-value: 2.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 766 LSLKCPiSTQVIfSIKFASFG-TPKGTCGSFTQ--GHCNSSRSLSLVQKACIGLRSCNVEVSTRVFGEPCRGVVKSLAVE 842
Cdd:cd22827    9 LTISCP-AGKVI-DIVSANYGrTDSSTCPSGGIknTNCRASNSLSIVRNRCNGKRSCSVKASNSVFGDPCVGTYKYLEVR 86


                 ...
gi 334184536 843 ASC 845
Cdd:cd22827   87 YRC 89
Gal_Rha_Lectin cd22823
Galactose/rhamnose-binding lectin domain; Galactose/rhamnose-binding lectin domain is formed ...
 765-845 4.40e-14

Galactose/rhamnose-binding lectin domain; Galactose/rhamnose-binding lectin domain is formed from a four-stranded antiparallel beta-sheet which packs against an alpha-helix. It was originally described as galactose-binding lectin domain since it was found in a galactose-binding sea urchin egg lectin (SUEL). SUEL was first isolated as a D-galactoside binding lectin, it was later shown that it binds to L-rhamnose preferentially. Galactose/rhamnose-binding lectin domain is also found in many rhamnose-binding lectins, such as Oncorhynchus keta L-rhamnose-binding lectins (CSLs) and Silurus asotus rhamnose-binding lectin (SAL). In addition, the superfamily includes many SUEL/CSLs/SAL homologous proteins, such as plant beta-galactosidases, mammalian latrophilins, Caenorhabditis elegans protein EVA-1 and its homolog, human protein EVA-1 homolog C (also known as C21orf63). Due to the lack of galactose/rhamnose-binding key residues, some superfamily members may not form a binding pocket for galactose/rhamnose. Therefore, they are unlikely to act as galactose/rhamnose-binding lectins.


Pssm-ID: 438682 [Multi-domain]  Cd Length: 91  Bit Score: 68.30  E-value: 4.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 765 VLSLKCPiSTQVIfSIKFASFG-TPKGTC----GSFTQGHCNSSRSLSLVQKACIGLRSCNVEVSTRVFGEPCRGVVKSL 839
Cdd:cd22823    8 TLTLSCP-SGQVI-KILSAFYGrTDGTTCccgpNNTSDTNCCSPDVLDIVKELCDGKQSCSVPASNSVFGDPCPGTSKYL 85


                 ....*.
gi 334184536 840 AVEASC 845
Cdd:cd22823   86 EVTYTC 91
Gal_Rha_Lectin_RBL_rpt2 cd22836
second galactose/rhamnose binding lectin domain found in Silurus asotus rhamnose-binding ...
 768-845 8.18e-11

second galactose/rhamnose binding lectin domain found in Silurus asotus rhamnose-binding lectin (RBL) and similar proteins; RBL, also known as Silurus asotus (catfish) roe lectin (SAL), is a lectin that binds L-rhamnose. It also binds monosaccharides possessing steric similarity to the hydroxyl group orientation at C2 and C4 of the pyranose ring structure of L-rhamnose, such as L-mannose and L-lyxose. RBL does not require a Ca2+ ion or free thiol group for its agglutination activity. RBL contains three galactose/rhamnose-binding lectin domains. This model corresponds to the second one.


Pssm-ID: 438693 [Multi-domain]  Cd Length: 95  Bit Score: 59.22  E-value: 8.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 768 LKCPISTQVIFSikfASFG-TPKGTCGS------FTQGHCNSSRSLSLVQKACIGLRSCNVEVSTRVFGEPCRGVVKSLA 840
Cdd:cd22836   14 LKCGSGVIQIIS---ANYGrTDSTTCSAgrpasqVQNTNCYASNSLAIVSQSCNGKKSCTVSASNSVFSDPCVGTYKYLY 90


                 ....*
gi 334184536 841 VEASC 845
Cdd:cd22836   91 VTYSC 95
Gal_Rha_Lectin_EVA1_EVA1C_rpt2 cd22829
second galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
 766-845 3.92e-10

second galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, human protein EVA-1 homolog C and similar proteins; The family includes Caenorhabditis elegans protein EVA-1 and its homologs, such as human protein EVA-1 homolog C (also known as C21orf63). EVA-1 functions as an UNC-40 coreceptor to enhance attraction to the MADD-4 guidance cue in C. elegans. It also acts as a receptor for slt-1 and is required for the guidance of the AVM pioneer axon to the ventral nerve cord. Human C21orf63 is a type-1 transmembrane heparin-binding protein. Members in this family contain two tandem galactose/rhamnose-binding lectin domains. This model corresponds to the second one. Due to the lack of rhamnose-binding key residues, the second galactose/rhamnose-binding domains of EVA-1 does not form a binding pocket for rhamnose.


Pssm-ID: 438686 [Multi-domain]  Cd Length: 99  Bit Score: 57.27  E-value: 3.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 766 LSLKCPISTQ-VIFSikfASFG-TPKGT--CGSFTQGH----CNSSRSLSLVQKACIGLRSCNVEVSTRVFGEPCR-GVV 836
Cdd:cd22829   12 LRLSCKPSSRlAIYS---ASYGrTLEGSveCPSTPKGDpdeeCLSDVALETVMKRCHGKRRCSLTADSETFGDPCPpGVR 88


                 ....*....
gi 334184536 837 KSLAVEASC 845
Cdd:cd22829   89 KYLKVVYTC 97
Gal_Rha_Lectin_dCirl cd22830
galactose/rhamnose binding lectin domain found in Drosophila melanogaster Latrophilin Cirl and ...
 765-845 1.59e-09

galactose/rhamnose binding lectin domain found in Drosophila melanogaster Latrophilin Cirl and similar proteins; Latrophilin Cirl (calcium-independent receptor for latrotoxin) is an adhesion-type G-protein-coupled receptor (aGPCR) that acts as a molecular sensor and signal transducer that detects and converts mechanical stimuli into a metabotropic response. It functions in mechanosensory neurons by modulating ionotropic receptor currents, the initiating step of cellular mechanosensation. The model corresponds to a galactose/rhamnose-binding lectin domain found at the N-terminus of Latrophilin Cirl.


Pssm-ID: 438687 [Multi-domain]  Cd Length: 92  Bit Score: 55.32  E-value: 1.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 765 VLSLKCPiSTQVIfSIKFASFGTPKGT-CGSFTQG----HCNSSRSLSLVQKACIGLRSCNVEVSTRVFGEPCRGVVKSL 839
Cdd:cd22830    9 QLTLECE-DGTVI-RIIRANYGRFSIAiCNDHGNTdwsvNCMSPRSLRVVQERCDGKRSCSIPASSSVFGDPCPGTPKYL 86


                 ....*.
gi 334184536 840 AVEASC 845
Cdd:cd22830   87 EVHYQC 92
Glyco_hydro_42 pfam02449
Beta-galactosidase; This group of beta-galactosidase enzymes belong to the glycosyl hydrolase ...
 48-200 3.96e-09

Beta-galactosidase; This group of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. The enzyme catalyzes the hydrolysis of terminal, non-reducing terminal beta-D-galactosidase residues.


Pssm-ID: 396834  Cd Length: 376  Bit Score: 59.59  E-value: 3.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536   48 HYPRSTpemWPELIQKSKDGGLDVIETYVF-WSGHEPEKNKYNFEGrydLVKFVKLAAKAGLYVHLRIGPyvcaewnyGG 126
Cdd:pfam02449   6 QWPEET---WEEDIRLMKEAGVNVVRIGIFaWAKLEPEEGKYDFEW---LDEVIDLLAKAGIKVILATPT--------AA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536  127 FPVWL-HFVPGIkFRTDNE-------------PFKEEMQRFTTKIVDLMkqEKLYASQGGpIILSQIENEYGNIDSA-YG 191
Cdd:pfam02449  72 PPAWLvKKHPEI-LPVDADgrrrgfgsrhhycPSSPVYREYAARIVEAL--AERYGDHPA-LIGWHIDNEYGCHVSEcYC 147

                         170
                  ....*....|
gi 334184536  192 A-AAKSYIKW 200
Cdd:pfam02449 148 EtCERAFRKW 157
Gal_Rha_Lectin_EVA1_EVA1C_rpt1 cd22828
first galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
 766-845 4.40e-09

first galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, human protein EVA-1 homolog C and similar proteins; The family includes Caenorhabditis elegans protein EVA-1 and its homologs, such as human protein EVA-1 homolog C (also known as C21orf63). EVA-1 functions as an UNC-40 coreceptor to enhance attraction to the MADD-4 guidance cue in C. elegans. It also acts as a receptor for slt-1 and is required for the guidance of the AVM pioneer axon to the ventral nerve cord. Human C21orf63 is a type-1 transmembrane heparin-binding protein. Both human C21orf63 is a type-1 transmembrane heparin-binding protein. Members in this family contain two tandem galactose/rhamnose-binding lectin domains. This model corresponds to the first one.


Pssm-ID: 438685 [Multi-domain]  Cd Length: 105  Bit Score: 54.59  E-value: 4.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 766 LSLKCPISTQVifSIKFASFG------------TPKGTCGSFTQGHCNSSRSLSLVQKACIGLRSCNVEVSTRVFGE-PC 832
Cdd:cd22828   13 LTLRCPPNTTI--SIQSAFYGrsvpsaqlcpsqSGPASSTSLEDTNCLAPTALQKVVEECQKKRSCRLLVSSRTFGLdPC 90

                         90
                 ....*....|...
gi 334184536 833 RGVVKSLAVEASC 845
Cdd:cd22828   91 PGTSKYLEVAYKC 103
Gal_Rha_Lectin_LAT2 cd22840
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ...
 765-845 2.07e-08

galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like protein 2 (LAT2) and similar proteins; LAT2 may have a role in pharyngeal pumping during feeding. It contains a galactose/rhamnose binding lectin domain at the N-terminal region. Due to the lack of rhamnose-binding key residues, the galactose/rhamnose-binding domains of LAT2 does not form a binding pocket for rhamnose. Therefore, LAT2 is unlikely to act as a rhamnose-binding lectin.


Pssm-ID: 438697 [Multi-domain]  Cd Length: 96  Bit Score: 52.41  E-value: 2.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 765 VLSLKCPIStQVIfSIKFASFGT--PKGTCGSFTQG---HCNSSRSLSLVQKACIGLRSCNVEVSTRVFGE-PCRGVV-K 837
Cdd:cd22840   11 PFEISCPSG-QRI-KVDYASYGAigTRSTCGDSVSPageTCSAPNSLQTMRQRCQGRQSCEIRVLNSLFPNdPCPGTSkK 88


                 ....*...
gi 334184536 838 SLAVEASC 845
Cdd:cd22840   89 YLEYRYRC 96
Gal_Rha_Lectin_SML_rpt2 cd22835
second galactose/rhamnose binding lectin domain found in Scomberomorus niphonius ...
 765-845 9.53e-08

second galactose/rhamnose binding lectin domain found in Scomberomorus niphonius L-rhamnose-binding lectin (SML) and similar proteins; SML is a rhamnose-binding lectin that also binds melibiose, raffinose, D-galactose, L-arabinose, D-fucose, maltose and D-glucose with decreasing affinity. It does not bind D-arabinose, L-fucose, lactose, xylose or 2-deoxy-D-galactose. SML shows strong hemagglutinating activity against rabbit erythrocytes. SML contains two tandem galactose/rhamnose-binding lectin domains. This model corresponds to the second one.


Pssm-ID: 438692 [Multi-domain]  Cd Length: 92  Bit Score: 50.38  E-value: 9.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 765 VLSLKCPIStQVIFSIKfASFG-TPKGTCgSFTQ-----GHCNSSRSLSLVQKACIGLRSCNVEVSTRVFGEPCRGVVKS 838
Cdd:cd22835    9 LAHLKCDEG-QVISVYG-ADYGrRDKTTC-SFGRppsqiQNVECSNPTDKVAERCNGKNSCSIKASNSVFGDPCVGTYKY 85


                 ....*..
gi 334184536 839 LAVEASC 845
Cdd:cd22835   86 LEVAYTC 92
Gal_Rha_Lectin_LPHNs cd22826
galactose/rhamnose binding lectin domain found in latrophilins; Latrophilins, also called ...
 768-845 1.15e-07

galactose/rhamnose binding lectin domain found in latrophilins; Latrophilins, also called lectomedins or latrotoxin receptors, belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: latrophilin-1 (LPHN1), Latrophilin-2 (LPHN2), and Latrophilin-3 (LPHN3). The LPHN1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. LPHN2 and LPHN3, although sharing strong sequence homology to LPHN1, do not bind alpha-latrotoxin. While LPHN3 is also brain specific, LPHN2, is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. All members in this family contain a galactose/rhamnose-binding lectin domain at N-terminus.


Pssm-ID: 438683 [Multi-domain]  Cd Length: 92  Bit Score: 50.39  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 768 LKCPiSTQVIFsIKFASFG-TPKGTCGSFTQ---GHCNSSRSLSLVQKACIGLRSCNVEVSTRVFGEPCRGVVKSLAVEA 843
Cdd:cd22826   13 LRCP-GSDVIM-IESANYGrTDSSTCPSDPNmtdTNCYLPDALAIVSQRCNNRTRCNVRADSSFFPDPCPGTFKYLEVIY 90


                 ..
gi 334184536 844 SC 845
Cdd:cd22826   91 EC 92
Gal_Rha_Lectin_LAT1 cd22839
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ...
 768-845 2.10e-07

galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like protein 1 (LAT1) and similar proteins; LAT1 plays a role in the establishment of anterior-posterior polarity in tissues during embryogenesis. It is required for the alignment of the mitotic spindles and division planes. It may have a role in cell death events and play an essential role in normal defection and oocyte fertilization. LAT1 is involved in sperm function. it operates in pharyngeal pumping during feeding. LAT1 contains a galactose/rhamnose binding lectin domain at the N-terminus.


Pssm-ID: 438696 [Multi-domain]  Cd Length: 95  Bit Score: 49.73  E-value: 2.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 768 LKCPISTqvIFSIKFASFGtpkgtcgSFTQGHCNSS------------RSLSLVQKACIGLRSCNVEVSTRVFGE-PCRG 834
Cdd:cd22839   14 LSCPEGK--YISIRLANYG-------RFSLGVCNPSnnidlsttcqndKTLPILQKSCDGKSECSFVVSNKFFFEdPCPG 84

                         90
                 ....*....|.
gi 334184536 835 VVKSLAVEASC 845
Cdd:cd22839   85 TPKYLEATYSC 95
Gal_Rha_Lectin_REJ3 cd22841
galactose/rhamnose binding lectin domain found in Strongylocentrotus purpuratus receptor for ...
 777-845 3.16e-07

galactose/rhamnose binding lectin domain found in Strongylocentrotus purpuratus receptor for egg jelly 3 protein (REJ3) and similar proteins; REJ3 is a polycystin-1 protein (components of non-selective cation channels) that is cleaved at the GPS (G-protein-coupled receptor proteolytic site) domain and localizes to the acrosomal region of sea urchin sperm. REJ3 is a multidomain protein containing only one galactose/rhamnose-binding lectin domain at its N-terminus.


Pssm-ID: 438698 [Multi-domain]  Cd Length: 92  Bit Score: 49.01  E-value: 3.16e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334184536 777 IFSIKFASFG-TPKGTCG---SFTQGHCNSSRSLSLVQKACIGLRSCNVEVSTRVFGEPCRGVVKSLAVEASC 845
Cdd:cd22841   20 VINIHSAVYGrTDSTTCShdqSVSNTNCHSDDSVNILSACCNGQSQCTVTATNSIFGDPCPGTYKYLNVTYTC 92
Gal_Rha_Lectin-like_P113 cd22843
galactose/rhamnose binding lectin-like domain found in Plasmodium falciparum P113 and similar ...
 766-845 4.60e-06

galactose/rhamnose binding lectin-like domain found in Plasmodium falciparum P113 and similar proteins; P113 is an abundant glycosylphosphatidylinositol (GPI)-anchored merozoite surface protein that tethers the RH5:CyRPA:RIPR complex to the merozoite surface. The N-terminal region of P113 contains two closely interacting domains, which resemble the galactose/rhamnose-binding lectin domains found in proteins such as sea urchin egg lectin (SUEL), plant beta-galactosidases, mammalian latrophilins, and catfish rhamnose-binding lectin (SAL) eggs. Due to the lack of rhamnose-binding key residues, the galactose/rhamnose binding lectin-like domains of P113 do not form a binding pocket for rhamnose. Therefore, P113 is unlikely to act as a rhamnose-binding lectin. This model corresponds to galactose/rhamnose binding lectin-like domain of P113.


Pssm-ID: 438700 [Multi-domain]  Cd Length: 89  Bit Score: 45.51  E-value: 4.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 766 LSLKCPISTQVifSIKFASFGTPKGTCGSFTQGHCNSSRSLSLVQKACIGLRSCNVEVSTRVFGEPCRGVVKSLAVEASC 845
Cdd:cd22843   12 VTIHCPGDGNI--SIKSATYGYNNSNVCIYCNSFNCDKDITSPVNKKCCGKNTCVLTVSDILEGNPCGIGNSYIRVVYTC 89
Gal_Rha_Lectin_CSL3_rpt1_rpt2-like cd22832
first and second galactose/rhamnose binding lectin domain found in Oncorhynchus keta ...
 800-845 6.82e-06

first and second galactose/rhamnose binding lectin domain found in Oncorhynchus keta L-rhamnose-binding lectin CSL3 and similar proteins; The family includes a group of L-rhamnose-binding lectins, such as Oncorhynchus keta CSL1-3. CSL1 has hemagglutinating activity towards rabbit erythrocytes, but not human type B erythrocytes. CSL2 has hemagglutinating activity towards rabbit erythrocytes and human type B erythrocytes. CSL3 has hemagglutinating activity towards rabbit erythrocytes, human type A erythrocytes, human type B erythrocytes, human type O erythrocytes, and sheep erythrocytes. Their hemagglutinating activities are inhibited by smooth-type lipopolysaccharide (LPS) from different bacterial species. Members in this family contain two tandem galactose-binding lectin domains. This model corresponds to the first and second galactose/rhamnose-binding lectin domains found in Oncorhynchus keta CSL3, as well as the second galactose/rhamnose-binding lectin domain found in Oncorhynchus keta CSL2.


Pssm-ID: 438689 [Multi-domain]  Cd Length: 94  Bit Score: 45.17  E-value: 6.82e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 334184536 800 CNSSRSLSLVQKACIGLRSCNVEVSTRVFGEPCRGVVKSLAVEASC 845
Cdd:cd22832   49 CLSQSTTSKMAERCDGKSQCIVPASNSVFGDPCVGTYKYLDVAYTC 94
Gal_Rha_Lectin_RBL_rpt3 cd22837
third galactose/rhamnose binding lectin domain found in Silurus asotus rhamnose-binding lectin ...
 767-845 2.07e-04

third galactose/rhamnose binding lectin domain found in Silurus asotus rhamnose-binding lectin (RBL) and similar proteins; RBL, also known as Silurus asotus (catfish) roe lectin (SAL), is a lectin that binds L-rhamnose. It also binds monosaccharides possessing steric similarity to the hydroxyl group orientation at C2 and C4 of the pyranose ring structure of L-rhamnose, such as L-mannose and L-lyxose. RBL does not require a Ca2+ ion or free thiol group for its agglutination activity. RBL contains three galactose/rhamnose-binding lectin domains. This model corresponds to the third one.


Pssm-ID: 438694 [Multi-domain]  Cd Length: 87  Bit Score: 40.87  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 767 SLKCPISTQVIFSIKFASFGTPkgTC--GSFTQGHCNSSrSLSLVQKACIGLRSCNVEVSTRVFGEPCRGVVKSLAVEAS 844
Cdd:cd22837   10 TITCSPETINVISAFYGRTDST--TCshGRPSTTNCSSD-TLAYIRALCQGKQTCTLQASNSVFGDPCPGTYKYLRITYS 86


                 .
gi 334184536 845 C 845
Cdd:cd22837   87 C 87
LacZ COG3250
Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism];
427-572 3.72e-03

Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism];


Pssm-ID: 442481 [Multi-domain]  Cd Length: 638  Bit Score: 40.90  E-value: 3.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184536 427 RQSLKPDGGSSAELGSQWSYIKEP-----IGISKADAFLKPGLLEqiNTTAdksdylWYslRTDIKGDETflDEGSKAVL 501
Cdd:COG3250    6 RLGDAPEGAKPDFDDSGWDPITVPgdwelDLYGLPDPFVGPWYLY--NGVG------WY--RRTFTVPAS--WKGKRVFL 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334184536 502 HIESLGQVVYAFINGKLAGSgH--GKQKISLDIPINLVTGTNTidlLSVTV---GLANYGAFFD-LVGAGITGPVTL 572
Cdd:COG3250   74 HFEGVDTAAEVWVNGKKVGY-HegGFTPFEFDITDYLKPGENV---LAVRVdnpSDGSYLEGQDwWRTSGIYRDVWL 146
 
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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