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Conserved domains on  [gi|1590550131|ref|XP_028244398|]
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beta-galactosidase 1-like [Glycine soja]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03059 super family cl31552
beta-galactosidase; Provisional
 13-843 0e+00

beta-galactosidase; Provisional


The actual alignment was detected with superfamily member PLN03059:

Pssm-ID: 166698 [Multi-domain]  Cd Length: 840  Bit Score: 1513.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131  13 LLLVVFACSLLGQASASVSYDHKAIIINGQRRILLSGSIHYPRSTPEMWPDLIQKAKEGGLDVIQTYVFWNGHEPSPGKY 92
Cdd:PLN03059   13 FLLFLLSSSWVSHGSASVSYDHRAFIINGQRRILISGSIHYPRSTPEMWPDLIQKAKDGGLDVIQTYVFWNGHEPSPGNY 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131  93 YFGGNYDLVRFIKLVQQAGLYVNLRIGPYVCAEWNFGGFPVWLKYIPGISFRTDNGPFKFQMEKFTKKIVDMMKAERLFE 172
Cdd:PLN03059   93 YFEDRYDLVKFIKVVQAAGLYVHLRIGPYICAEWNFGGFPVWLKYVPGIEFRTDNGPFKAAMQKFTEKIVDMMKSEKLFE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 173 SQGGPIILSQIENEYGPMEYEIGAPGRSYTQWAAHMAVGLGTGVPWIMCKQDDAPDPIINTCNGFYCDYFSPNKAYKPKM 252
Cdd:PLN03059  173 PQGGPIILSQIENEYGPVEWEIGAPGKAYTKWAADMAVKLGTGVPWVMCKQEDAPDPVIDTCNGFYCENFKPNKDYKPKM 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 253 WTEAWTGWFTEFGGAVPHRPAEDLAFSIARFIQKGGSFVNYYMYHGGTNFGRTAGGPFIATSYDYDAPLDEYGLARQPKW 332
Cdd:PLN03059  253 WTEAWTGWYTEFGGAVPNRPAEDLAFSVARFIQNGGSFINYYMYHGGTNFGRTAGGPFIATSYDYDAPLDEYGLPREPKW 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 333 GHLKDLHRAIKLCEPALVSGDSTVQRLGNYEEAHVFRSKSgACAAFLANYNPQSYATVAFGNQHYNLPPWSISILPNCKH 412
Cdd:PLN03059  333 GHLRDLHKAIKLCEPALVSVDPTVTSLGSNQEAHVFKSKS-ACAAFLANYDTKYSVKVTFGNGQYDLPPWSVSILPDCKT 411

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 413 TVYNTARVGSQSTTMKMTrvPIHGGLSWKAFNEETTTTDDS-SFTVTGLLEQINATRDLSDYLWYSTDVVINSNEGFLRN 491
Cdd:PLN03059  412 AVFNTARLGAQSSQMKMN--PVGSTFSWQSYNEETASAYTDdTTTMDGLWEQINVTRDATDYLWYMTEVHIDPDEGFLKT 489

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 492 GKNPVLTVLSAGHALHVFINNQLSGTAYGSLEAPKLTFSESVRLRAGVNKISLLSVAVGLPNVGPHFERWNAGVLGPITL 571
Cdd:PLN03059  490 GQYPVLTIFSAGHALHVFINGQLAGTVYGELSNPKLTFSQNVKLTVGINKISLLSVAVGLPNVGLHFETWNAGVLGPVTL 569

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 572 SGLNEGRRDLTWQKWSYKVGLKGEALNLHSLSGSSSVEWLQGFLVSRRQPLTWYKTTFDAPAGVAPLALDMGSMGKGQVW 651
Cdd:PLN03059  570 KGLNEGTRDLSGWKWSYKIGLKGEALSLHTITGSSSVEWVEGSLLAQKQPLTWYKTTFDAPGGNDPLALDMSSMGKGQIW 649

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 652 INGQSLGRYWPAYKASGSCGYCNYAGTYNEKKCGSNCGEASQRWYHVPHSWLKPSGNLLVVFEELGGDPNGIFLVRRDID 731
Cdd:PLN03059  650 INGQSIGRHWPAYTAHGSCNGCNYAGTFDDKKCRTNCGEPSQRWYHVPRSWLKPSGNLLIVFEEWGGNPAGISLVKRTTD 729

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 732 SVCADIYEWQPNLVSYEMQASGKVRSPvRPKAHLSCGPGQKISSIKFASFGTPVGSCGSYREGSCHAHKSYDAFLKNCVG 811
Cdd:PLN03059  730 SVCADIFEGQPALKNWQIIASGKVNSL-QPKAHLWCPPGQKISKIKFASFGVPQGTCGSFREGSCHAHKSYDAFERNCIG 808

                         810       820       830
                  ....*....|....*....|....*....|..
gi 1590550131 812 QSWCTVTVSPEIFGGDPCPRVMKKLSVEAICT 843
Cdd:PLN03059  809 KQSCSVTVAPEVFGGDPCPDSMKKLSVEAVCS 840
 
Name Accession Description Interval E-value
PLN03059 PLN03059
beta-galactosidase; Provisional
 13-843 0e+00

beta-galactosidase; Provisional


Pssm-ID: 166698 [Multi-domain]  Cd Length: 840  Bit Score: 1513.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131  13 LLLVVFACSLLGQASASVSYDHKAIIINGQRRILLSGSIHYPRSTPEMWPDLIQKAKEGGLDVIQTYVFWNGHEPSPGKY 92
Cdd:PLN03059   13 FLLFLLSSSWVSHGSASVSYDHRAFIINGQRRILISGSIHYPRSTPEMWPDLIQKAKDGGLDVIQTYVFWNGHEPSPGNY 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131  93 YFGGNYDLVRFIKLVQQAGLYVNLRIGPYVCAEWNFGGFPVWLKYIPGISFRTDNGPFKFQMEKFTKKIVDMMKAERLFE 172
Cdd:PLN03059   93 YFEDRYDLVKFIKVVQAAGLYVHLRIGPYICAEWNFGGFPVWLKYVPGIEFRTDNGPFKAAMQKFTEKIVDMMKSEKLFE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 173 SQGGPIILSQIENEYGPMEYEIGAPGRSYTQWAAHMAVGLGTGVPWIMCKQDDAPDPIINTCNGFYCDYFSPNKAYKPKM 252
Cdd:PLN03059  173 PQGGPIILSQIENEYGPVEWEIGAPGKAYTKWAADMAVKLGTGVPWVMCKQEDAPDPVIDTCNGFYCENFKPNKDYKPKM 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 253 WTEAWTGWFTEFGGAVPHRPAEDLAFSIARFIQKGGSFVNYYMYHGGTNFGRTAGGPFIATSYDYDAPLDEYGLARQPKW 332
Cdd:PLN03059  253 WTEAWTGWYTEFGGAVPNRPAEDLAFSVARFIQNGGSFINYYMYHGGTNFGRTAGGPFIATSYDYDAPLDEYGLPREPKW 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 333 GHLKDLHRAIKLCEPALVSGDSTVQRLGNYEEAHVFRSKSgACAAFLANYNPQSYATVAFGNQHYNLPPWSISILPNCKH 412
Cdd:PLN03059  333 GHLRDLHKAIKLCEPALVSVDPTVTSLGSNQEAHVFKSKS-ACAAFLANYDTKYSVKVTFGNGQYDLPPWSVSILPDCKT 411

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 413 TVYNTARVGSQSTTMKMTrvPIHGGLSWKAFNEETTTTDDS-SFTVTGLLEQINATRDLSDYLWYSTDVVINSNEGFLRN 491
Cdd:PLN03059  412 AVFNTARLGAQSSQMKMN--PVGSTFSWQSYNEETASAYTDdTTTMDGLWEQINVTRDATDYLWYMTEVHIDPDEGFLKT 489

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 492 GKNPVLTVLSAGHALHVFINNQLSGTAYGSLEAPKLTFSESVRLRAGVNKISLLSVAVGLPNVGPHFERWNAGVLGPITL 571
Cdd:PLN03059  490 GQYPVLTIFSAGHALHVFINGQLAGTVYGELSNPKLTFSQNVKLTVGINKISLLSVAVGLPNVGLHFETWNAGVLGPVTL 569

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 572 SGLNEGRRDLTWQKWSYKVGLKGEALNLHSLSGSSSVEWLQGFLVSRRQPLTWYKTTFDAPAGVAPLALDMGSMGKGQVW 651
Cdd:PLN03059  570 KGLNEGTRDLSGWKWSYKIGLKGEALSLHTITGSSSVEWVEGSLLAQKQPLTWYKTTFDAPGGNDPLALDMSSMGKGQIW 649

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 652 INGQSLGRYWPAYKASGSCGYCNYAGTYNEKKCGSNCGEASQRWYHVPHSWLKPSGNLLVVFEELGGDPNGIFLVRRDID 731
Cdd:PLN03059  650 INGQSIGRHWPAYTAHGSCNGCNYAGTFDDKKCRTNCGEPSQRWYHVPRSWLKPSGNLLIVFEEWGGNPAGISLVKRTTD 729

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 732 SVCADIYEWQPNLVSYEMQASGKVRSPvRPKAHLSCGPGQKISSIKFASFGTPVGSCGSYREGSCHAHKSYDAFLKNCVG 811
Cdd:PLN03059  730 SVCADIFEGQPALKNWQIIASGKVNSL-QPKAHLWCPPGQKISKIKFASFGVPQGTCGSFREGSCHAHKSYDAFERNCIG 808

                         810       820       830
                  ....*....|....*....|....*....|..
gi 1590550131 812 QSWCTVTVSPEIFGGDPCPRVMKKLSVEAICT 843
Cdd:PLN03059  809 KQSCSVTVAPEVFGGDPCPDSMKKLSVEAVCS 840
Glyco_hydro_35 pfam01301
Glycosyl hydrolases family 35;
36-340 8.07e-163

Glycosyl hydrolases family 35;


Pssm-ID: 396048 [Multi-domain]  Cd Length: 316  Bit Score: 475.59  E-value: 8.07e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131  36 AIIINGQRRILLSGSIHYPRSTPEMWPDLIQKAKEGGLDVIQTYVFWNGHEPSPGKYYFGGNYDLVRFIKLVQQAGLYVN 115
Cdd:pfam01301   1 SFLIDGKRFRLISGSIHYFRIPPEMWPDRLQKAKALGLNAIETYVFWNLHEPEPGQYDFSGILDLVKFIKLAQEAGLYVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 116 LRIGPYVCAEWNFGGFPVWLKYIPGISFRTDNGPFKFQMEKFTKKIVDMMKaeRLFESQGGPIILSQIENEYGP--MEYE 193
Cdd:pfam01301  81 LRPGPYICAEWDFGGLPAWLLTVPGIRLRTSDPPFLEAVERYLTALLPKMK--PLQATNGGPIIMVQVENEYGSygVDKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 194 IGAPGR-SYTQWAAHMAVGLGTGVPWIMCKQD-DAPDPIINTCNGFYCDYF--------SPNKAYKPKMWTEAWTGWFTE 263
Cdd:pfam01301 159 YLRALRkAYKEWGADMALLFTTDGPWGMCLQCgDLPGPDIYATNGFGCGANppsnfkllRPFSPNKPLMWSEFWTGWFDH 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 264 FGGAVPHRPAEDLAFSIARFIQKGGSfVNYYMYHGGTNFGRTAGGPFIA---TSYDYDAPLDEYGLARqPKWGHLKDLHR 340
Cdd:pfam01301 239 WGGPHAIRPAEDIAFEVARFLAKNSS-VNLYMFHGGTNFGFTNGANFYGpqtTSYDYDAPIDEAGDPT-PKYGHLKDLIT 316
Gal_Rha_Lectin_BGal cd22842
galactose/rhamnose binding lectin domain found in plant beta-galactosidases and similar ...
 757-842 1.74e-39

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: 140.88  E-value: 1.74e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 757 SPVRPKAHLSCGPGQKISSIKFASFGTPVGSCGSYREGSCHAHKSYDAFLKNCVGQSWCTVTVSPEIFGGDPCPRVMKKL 836
Cdd:cd22842     6 GGPGSTLTLSCPAGQVISSIDFASYGTPTGTCGSFSKGSCHAPNSLSVVEKACLGKNSCSIPASNSVFFGDPCPGTTKRL 85


                  ....*.
gi 1590550131 837 SVEAIC 842
Cdd:cd22842    86 AVQATC 91
GanA COG1874
Beta-galactosidase GanA [Carbohydrate transport and metabolism];
44-338 2.34e-27

Beta-galactosidase GanA [Carbohydrate transport and metabolism];


Pssm-ID: 441478 [Multi-domain]  Cd Length: 609  Bit Score: 118.11  E-value: 2.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131  44 RILLSGSIHYPRSTPEMWPDLIQKAKEGGLDVIQT-YVFWNGHEPSPGKYYFGGnydLVRFIKLVQQAGLYVNLRIGPYV 122
Cdd:COG1874     9 FLILGGDYHPERWPPEVWAEDIRLMKAAGLNTVRIgYFAWNLHEPEEGVFDFDW---LDRFIDLLHEAGLKVILRTPTAA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 123 caewnfggFPVWL--KYiPGISFRTDNG-PFKF---QMEKFT--------KKIVDMMkAERLfeSQGGPIILSQIENEYG 188
Cdd:COG1874    86 --------PPAWLlkKY-PEILPVDADGrRRGFgsrRHYCPSspvyreaaRRIVRAL-AERY--GDHPAVIMWQVDNEYG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 189 P-----------------------------------MEY----EIGAPGRS----------------------------- 200
Cdd:COG1874   154 SydycdacaaafrdwlrerygtldalneawgtafwsQRYtdwdEIEPPRLTpttanpslrldfrrfssdqvleylraqrd 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 201 -----------------------YTQWAAHMAVglgtgVPWIMCKQDDAPDPIIntcNGFYCDYFSPNKAYKPKMWTEAW 257
Cdd:COG1874   234 ilreagpdvpvttnfmgpfpgldYWKLARDLDV-----VSWDNYPDGSAADPDE---IAFAHDLMRGLKGGGPFMVMEQW 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 258 TGWFTeFGGAVPHRPAEDLAFSIARFIQKGGSFVNYYMYHggtnfgRTAGGpfiaTSYDYDAPLDEYGlARQPKWGHLKD 337
Cdd:COG1874   306 PGWVN-WGPYNPAKRPGQLRLWSLQALAHGADGVNYFQWR------PSRGG----TEYDHDAPLDHAG-RPTRKFREVRE 373


                  .
gi 1590550131 338 L 338
Cdd:COG1874   374 L 374
 
Name Accession Description Interval E-value
PLN03059 PLN03059
beta-galactosidase; Provisional
 13-843 0e+00

beta-galactosidase; Provisional


Pssm-ID: 166698 [Multi-domain]  Cd Length: 840  Bit Score: 1513.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131  13 LLLVVFACSLLGQASASVSYDHKAIIINGQRRILLSGSIHYPRSTPEMWPDLIQKAKEGGLDVIQTYVFWNGHEPSPGKY 92
Cdd:PLN03059   13 FLLFLLSSSWVSHGSASVSYDHRAFIINGQRRILISGSIHYPRSTPEMWPDLIQKAKDGGLDVIQTYVFWNGHEPSPGNY 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131  93 YFGGNYDLVRFIKLVQQAGLYVNLRIGPYVCAEWNFGGFPVWLKYIPGISFRTDNGPFKFQMEKFTKKIVDMMKAERLFE 172
Cdd:PLN03059   93 YFEDRYDLVKFIKVVQAAGLYVHLRIGPYICAEWNFGGFPVWLKYVPGIEFRTDNGPFKAAMQKFTEKIVDMMKSEKLFE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 173 SQGGPIILSQIENEYGPMEYEIGAPGRSYTQWAAHMAVGLGTGVPWIMCKQDDAPDPIINTCNGFYCDYFSPNKAYKPKM 252
Cdd:PLN03059  173 PQGGPIILSQIENEYGPVEWEIGAPGKAYTKWAADMAVKLGTGVPWVMCKQEDAPDPVIDTCNGFYCENFKPNKDYKPKM 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 253 WTEAWTGWFTEFGGAVPHRPAEDLAFSIARFIQKGGSFVNYYMYHGGTNFGRTAGGPFIATSYDYDAPLDEYGLARQPKW 332
Cdd:PLN03059  253 WTEAWTGWYTEFGGAVPNRPAEDLAFSVARFIQNGGSFINYYMYHGGTNFGRTAGGPFIATSYDYDAPLDEYGLPREPKW 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 333 GHLKDLHRAIKLCEPALVSGDSTVQRLGNYEEAHVFRSKSgACAAFLANYNPQSYATVAFGNQHYNLPPWSISILPNCKH 412
Cdd:PLN03059  333 GHLRDLHKAIKLCEPALVSVDPTVTSLGSNQEAHVFKSKS-ACAAFLANYDTKYSVKVTFGNGQYDLPPWSVSILPDCKT 411

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 413 TVYNTARVGSQSTTMKMTrvPIHGGLSWKAFNEETTTTDDS-SFTVTGLLEQINATRDLSDYLWYSTDVVINSNEGFLRN 491
Cdd:PLN03059  412 AVFNTARLGAQSSQMKMN--PVGSTFSWQSYNEETASAYTDdTTTMDGLWEQINVTRDATDYLWYMTEVHIDPDEGFLKT 489

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 492 GKNPVLTVLSAGHALHVFINNQLSGTAYGSLEAPKLTFSESVRLRAGVNKISLLSVAVGLPNVGPHFERWNAGVLGPITL 571
Cdd:PLN03059  490 GQYPVLTIFSAGHALHVFINGQLAGTVYGELSNPKLTFSQNVKLTVGINKISLLSVAVGLPNVGLHFETWNAGVLGPVTL 569

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 572 SGLNEGRRDLTWQKWSYKVGLKGEALNLHSLSGSSSVEWLQGFLVSRRQPLTWYKTTFDAPAGVAPLALDMGSMGKGQVW 651
Cdd:PLN03059  570 KGLNEGTRDLSGWKWSYKIGLKGEALSLHTITGSSSVEWVEGSLLAQKQPLTWYKTTFDAPGGNDPLALDMSSMGKGQIW 649

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 652 INGQSLGRYWPAYKASGSCGYCNYAGTYNEKKCGSNCGEASQRWYHVPHSWLKPSGNLLVVFEELGGDPNGIFLVRRDID 731
Cdd:PLN03059  650 INGQSIGRHWPAYTAHGSCNGCNYAGTFDDKKCRTNCGEPSQRWYHVPRSWLKPSGNLLIVFEEWGGNPAGISLVKRTTD 729

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 732 SVCADIYEWQPNLVSYEMQASGKVRSPvRPKAHLSCGPGQKISSIKFASFGTPVGSCGSYREGSCHAHKSYDAFLKNCVG 811
Cdd:PLN03059  730 SVCADIFEGQPALKNWQIIASGKVNSL-QPKAHLWCPPGQKISKIKFASFGVPQGTCGSFREGSCHAHKSYDAFERNCIG 808

                         810       820       830
                  ....*....|....*....|....*....|..
gi 1590550131 812 QSWCTVTVSPEIFGGDPCPRVMKKLSVEAICT 843
Cdd:PLN03059  809 KQSCSVTVAPEVFGGDPCPDSMKKLSVEAVCS 840
Glyco_hydro_35 pfam01301
Glycosyl hydrolases family 35;
36-340 8.07e-163

Glycosyl hydrolases family 35;


Pssm-ID: 396048 [Multi-domain]  Cd Length: 316  Bit Score: 475.59  E-value: 8.07e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131  36 AIIINGQRRILLSGSIHYPRSTPEMWPDLIQKAKEGGLDVIQTYVFWNGHEPSPGKYYFGGNYDLVRFIKLVQQAGLYVN 115
Cdd:pfam01301   1 SFLIDGKRFRLISGSIHYFRIPPEMWPDRLQKAKALGLNAIETYVFWNLHEPEPGQYDFSGILDLVKFIKLAQEAGLYVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 116 LRIGPYVCAEWNFGGFPVWLKYIPGISFRTDNGPFKFQMEKFTKKIVDMMKaeRLFESQGGPIILSQIENEYGP--MEYE 193
Cdd:pfam01301  81 LRPGPYICAEWDFGGLPAWLLTVPGIRLRTSDPPFLEAVERYLTALLPKMK--PLQATNGGPIIMVQVENEYGSygVDKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 194 IGAPGR-SYTQWAAHMAVGLGTGVPWIMCKQD-DAPDPIINTCNGFYCDYF--------SPNKAYKPKMWTEAWTGWFTE 263
Cdd:pfam01301 159 YLRALRkAYKEWGADMALLFTTDGPWGMCLQCgDLPGPDIYATNGFGCGANppsnfkllRPFSPNKPLMWSEFWTGWFDH 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 264 FGGAVPHRPAEDLAFSIARFIQKGGSfVNYYMYHGGTNFGRTAGGPFIA---TSYDYDAPLDEYGLARqPKWGHLKDLHR 340
Cdd:pfam01301 239 WGGPHAIRPAEDIAFEVARFLAKNSS-VNLYMFHGGTNFGFTNGANFYGpqtTSYDYDAPIDEAGDPT-PKYGHLKDLIT 316
Gal_Rha_Lectin_BGal cd22842
galactose/rhamnose binding lectin domain found in plant beta-galactosidases and similar ...
 757-842 1.74e-39

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: 140.88  E-value: 1.74e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 757 SPVRPKAHLSCGPGQKISSIKFASFGTPVGSCGSYREGSCHAHKSYDAFLKNCVGQSWCTVTVSPEIFGGDPCPRVMKKL 836
Cdd:cd22842     6 GGPGSTLTLSCPAGQVISSIDFASYGTPTGTCGSFSKGSCHAPNSLSVVEKACLGKNSCSIPASNSVFFGDPCPGTTKRL 85


                  ....*.
gi 1590550131 837 SVEAIC 842
Cdd:cd22842    86 AVQATC 91
Gal_Lectin pfam02140
Galactose binding lectin domain;
765-842 5.63e-28

Galactose binding lectin domain;


Pssm-ID: 460460 [Multi-domain]  Cd Length: 79  Bit Score: 107.38  E-value: 5.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 765 LSCGPGQKISsIKFASFGTPVGS-CGSYREGS-CHAHKSYDAFLKNCVGQSWCTVTVSPEIFGGDPCPRVMKKLSVEAIC 842
Cdd:pfam02140   1 LSCPPGKVIS-ILFASYGRPDGTtCPSFIQGTnCHSPNSLAIVSKACQGKNSCSVPASNSVFGGDPCPGTYKYLEVEYKC 79
GanA COG1874
Beta-galactosidase GanA [Carbohydrate transport and metabolism];
44-338 2.34e-27

Beta-galactosidase GanA [Carbohydrate transport and metabolism];


Pssm-ID: 441478 [Multi-domain]  Cd Length: 609  Bit Score: 118.11  E-value: 2.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131  44 RILLSGSIHYPRSTPEMWPDLIQKAKEGGLDVIQT-YVFWNGHEPSPGKYYFGGnydLVRFIKLVQQAGLYVNLRIGPYV 122
Cdd:COG1874     9 FLILGGDYHPERWPPEVWAEDIRLMKAAGLNTVRIgYFAWNLHEPEEGVFDFDW---LDRFIDLLHEAGLKVILRTPTAA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 123 caewnfggFPVWL--KYiPGISFRTDNG-PFKF---QMEKFT--------KKIVDMMkAERLfeSQGGPIILSQIENEYG 188
Cdd:COG1874    86 --------PPAWLlkKY-PEILPVDADGrRRGFgsrRHYCPSspvyreaaRRIVRAL-AERY--GDHPAVIMWQVDNEYG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 189 P-----------------------------------MEY----EIGAPGRS----------------------------- 200
Cdd:COG1874   154 SydycdacaaafrdwlrerygtldalneawgtafwsQRYtdwdEIEPPRLTpttanpslrldfrrfssdqvleylraqrd 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 201 -----------------------YTQWAAHMAVglgtgVPWIMCKQDDAPDPIIntcNGFYCDYFSPNKAYKPKMWTEAW 257
Cdd:COG1874   234 ilreagpdvpvttnfmgpfpgldYWKLARDLDV-----VSWDNYPDGSAADPDE---IAFAHDLMRGLKGGGPFMVMEQW 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 258 TGWFTeFGGAVPHRPAEDLAFSIARFIQKGGSFVNYYMYHggtnfgRTAGGpfiaTSYDYDAPLDEYGlARQPKWGHLKD 337
Cdd:COG1874   306 PGWVN-WGPYNPAKRPGQLRLWSLQALAHGADGVNYFQWR------PSRGG----TEYDHDAPLDHAG-RPTRKFREVRE 373


                  .
gi 1590550131 338 L 338
Cdd:COG1874   374 L 374
GHD pfam17834
Beta-sandwich domain in beta galactosidase; This entry corresponds to a beta sandwich like ...
 349-420 8.09e-26

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: 101.22  E-value: 8.09e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1590550131 349 LVSGDSTVQRLGNYEEAHVFRSKSGACAAFLANYNPQSYATVAFGNQHYNLPPWSISILPNCKHTVYNTARV 420
Cdd:pfam17834   1 LLSGQYTTTNLGKLQTATVFEKDKGSCVAFLVNIDDKKDANVTFRGSDYFLPAWSISILPDCKTVVFNTAKV 72
Gal_Rha_Lectin cd22823
Galactose/rhamnose-binding lectin domain; Galactose/rhamnose-binding lectin domain is formed ...
 762-842 1.26e-12

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: 64.45  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 762 KAHLSCGPGQKISsIKFASFG-TPVGSCGSYREGS----CHAHKSYDAFLKNCVGQSWCTVTVSPEIFgGDPCPRVMKKL 836
Cdd:cd22823     8 TLTLSCPSGQVIK-ILSAFYGrTDGTTCCCGPNNTsdtnCCSPDVLDIVKELCDGKQSCSVPASNSVF-GDPCPGTSKYL 85


                  ....*.
gi 1590550131 837 SVEAIC 842
Cdd:cd22823    86 EVTYTC 91
Gal_Rha_Lectin_SUL-I-like cd22827
galactose/rhamnose binding lectin domain found in Toxopneustes pileolus rhamnose-binding ...
 762-842 2.67e-10

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: 57.60  E-value: 2.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 762 KAHLSCGPGQKISsIKFASFG-TPVGSCGS--YREGSCHAHKSYDAFLKNCVGQSWCTVTVSPEIFgGDPCPRVMKKLSV 838
Cdd:cd22827     8 TLTISCPAGKVID-IVSANYGrTDSSTCPSggIKNTNCRASNSLSIVRNRCNGKRSCSVKASNSVF-GDPCVGTYKYLEV 85


                  ....
gi 1590550131 839 EAIC 842
Cdd:cd22827    86 RYRC 89
Gal_Rha_Lectin_REJ3 cd22841
galactose/rhamnose binding lectin domain found in Strongylocentrotus purpuratus receptor for ...
 765-842 3.75e-10

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: 57.10  E-value: 3.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 765 LSCGPGqkISSIKFASFG-TPVGSCGSYREGS---CHAHKSYDAFLKNCVGQSWCTVTVSPEIFgGDPCPRVMKKLSVEA 840
Cdd:cd22841    14 IDCGNG--VINIHSAVYGrTDSTTCSHDQSVSntnCHSDDSVNILSACCNGQSQCTVTATNSIF-GDPCPGTYKYLNVTY 90


                  ..
gi 1590550131 841 IC 842
Cdd:cd22841    91 TC 92
Glyco_hydro_42 pfam02449
Beta-galactosidase; This group of beta-galactosidase enzymes belong to the glycosyl hydrolase ...
 52-188 2.07e-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: 60.36  E-value: 2.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131  52 HYPRSTpemWPDLIQKAKEGGLDVIQTYVF-WNGHEPSPGKYYFGGnydLVRFIKLVQQAGLYVNLRIGPyvcaewnfGG 130
Cdd:pfam02449   6 QWPEET---WEEDIRLMKEAGVNVVRIGIFaWAKLEPEEGKYDFEW---LDEVIDLLAKAGIKVILATPT--------AA 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1590550131 131 FPVWL--KYiPGISFRTDNG---------PFKFQMEKF---TKKIVDMMkAERLfeSQGGPIILSQIENEYG 188
Cdd:pfam02449  72 PPAWLvkKH-PEILPVDADGrrrgfgsrhHYCPSSPVYreyAARIVEAL-AERY--GDHPALIGWHIDNEYG 139
Gal_Rha_Lectin_LAT1 cd22839
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ...
 763-842 1.68e-08

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: 52.81  E-value: 1.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 763 AHLSCGPGQKISsIKFASFGT-PVGSCG-SYR---EGSCHAHKSYDAFLKNCVGQSWCTVTVSPEIFGGDPCPRVMKKLS 837
Cdd:cd22839    12 ANLSCPEGKYIS-IRLANYGRfSLGVCNpSNNidlSTTCQNDKTLPILQKSCDGKSECSFVVSNKFFFEDPCPGTPKYLE 90


                  ....*
gi 1590550131 838 VEAIC 842
Cdd:cd22839    91 ATYSC 95
Gal_Rha_Lectin_EVA1_EVA1C_rpt1 cd22828
first galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
 762-838 2.78e-08

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: 52.28  E-value: 2.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 762 KAHLSCGPGQKISsIKFASFGTPVGS---CGSYREG---------SCHAHKSYDAFLKNCVGQSWCTVTVSPEIFGGDPC 829
Cdd:cd22828    12 ELTLRCPPNTTIS-IQSAFYGRSVPSaqlCPSQSGPasstsledtNCLAPTALQKVVEECQKKRSCRLLVSSRTFGLDPC 90


                  ....*....
gi 1590550131 830 PRVMKKLSV 838
Cdd:cd22828    91 PGTSKYLEV 99
Gal_Rha_Lectin_dCirl cd22830
galactose/rhamnose binding lectin domain found in Drosophila melanogaster Latrophilin Cirl and ...
 764-842 2.79e-07

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: 49.16  E-value: 2.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 764 HLSCGPGQKISSIKfASFGT-PVGSCGSYREG----SCHAHKSYDAFLKNCVGQSWCTVTVSPEIFgGDPCPRVMKKLSV 838
Cdd:cd22830    11 TLECEDGTVIRIIR-ANYGRfSIAICNDHGNTdwsvNCMSPRSLRVVQERCDGKRSCSIPASSSVF-GDPCPGTPKYLEV 88


                  ....
gi 1590550131 839 EAIC 842
Cdd:cd22830    89 HYQC 92
Gal_Rha_Lectin_EVA1_EVA1C_rpt2 cd22829
second galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
 762-842 7.79e-07

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: 48.02  E-value: 7.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 762 KAHLSCGPGQKISsIKFASFG-TPVGS--CGSYREG----SCHAHKSYDAFLKNCVGQSWCTVTVSPEIFgGDPCPRVMK 834
Cdd:cd22829    11 KLRLSCKPSSRLA-IYSASYGrTLEGSveCPSTPKGdpdeECLSDVALETVMKRCHGKRRCSLTADSETF-GDPCPPGVR 88


                  ....*....
gi 1590550131 835 K-LSVEAIC 842
Cdd:cd22829    89 KyLKVVYTC 97
Gal_Rha_Lectin_SML_rpt2 cd22835
second galactose/rhamnose binding lectin domain found in Scomberomorus niphonius ...
 763-842 1.42e-06

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: 46.91  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 763 AHLSCGPGQKISSIKfASFGTPVGSCGSYR---------EGSCHAHKSYDaflkNCVGQSWCTVTVSPEIFgGDPCPRVM 833
Cdd:cd22835    10 AHLKCDEGQVISVYG-ADYGRRDKTTCSFGrppsqiqnvECSNPTDKVAE----RCNGKNSCSIKASNSVF-GDPCVGTY 83


                  ....*....
gi 1590550131 834 KKLSVEAIC 842
Cdd:cd22835    84 KYLEVAYTC 92
Gal_Rha_Lectin_LAT2 cd22840
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ...
 764-842 1.02e-05

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: 44.71  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 764 HLSCGPGQKISsIKFASFGT-PVGS-CGSYREGSCHAHKSYDAF--LKN-CVGQSWCTVTVSPEIFGGDPCPRVMKK-LS 837
Cdd:cd22840    13 EISCPSGQRIK-VDYASYGAiGTRStCGDSVSPAGETCSAPNSLqtMRQrCQGRQSCEIRVLNSLFPNDPCPGTSKKyLE 91


                  ....*
gi 1590550131 838 VEAIC 842
Cdd:cd22840    92 YRYRC 96
Gal_Rha_Lectin_RBL_rpt2 cd22836
second galactose/rhamnose binding lectin domain found in Silurus asotus rhamnose-binding ...
 763-842 1.73e-05

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: 44.20  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 763 AHLSCGPGQ-KISSikfASFG-TPVGSCGSYREGS------CHAHKSYDAFLKNCVGQSWCTVTVSPEIFgGDPCPRVMK 834
Cdd:cd22836    12 AVLKCGSGViQIIS---ANYGrTDSTTCSAGRPASqvqntnCYASNSLAIVSQSCNGKKSCTVSASNSVF-SDPCVGTYK 87


                  ....*...
gi 1590550131 835 KLSVEAIC 842
Cdd:cd22836    88 YLYVTYSC 95
Gal_Rha_Lectin-like_P113 cd22843
galactose/rhamnose binding lectin-like domain found in Plasmodium falciparum P113 and similar ...
 764-830 1.26e-04

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: 41.66  E-value: 1.26e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590550131 764 HLSCGPGQKISsIKFASFGTPVGSCGSYREGSCHAHKSYDAFLKNCVGQSWCTVTVSpEIFGGDPCP 830
Cdd:cd22843    13 TIHCPGDGNIS-IKSATYGYNNSNVCIYCNSFNCDKDITSPVNKKCCGKNTCVLTVS-DILEGNPCG 77
Gal_Rha_Lectin_LPHNs cd22826
galactose/rhamnose binding lectin domain found in latrophilins; Latrophilins, also called ...
 762-842 4.45e-04

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: 39.99  E-value: 4.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590550131 762 KAHLSCgPGQKISSIKFASFG-TPVGSCGSY---REGSCHAHKSYDAFLKNCVGQSWCTVTVSPEIFGgDPCPRVMKKLS 837
Cdd:cd22826    10 KIRLRC-PGSDVIMIESANYGrTDSSTCPSDpnmTDTNCYLPDALAIVSQRCNNRTRCNVRADSSFFP-DPCPGTFKYLE 87


                  ....*
gi 1590550131 838 VEAIC 842
Cdd:cd22826    88 VIYEC 92
 
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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