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Conserved domains on  [gi|18418558|ref|NP_567973|]
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beta-galactosidase 11 [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

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PLN03059 super family cl31552
beta-galactosidase; Provisional
 41-839 0e+00

beta-galactosidase; Provisional


The actual alignment was detected with superfamily member PLN03059:

Pssm-ID: 166698 [Multi-domain]  Cd Length: 840  Bit Score: 756.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558   41 VTYDGTSLIIDGKRELLYSGSIHYPRSTPEMWPSIIKRAKQGGLNTIQTYVFWNVHEPQQGKFNFSGRADLVKFIKLIQK 120
Cdd:PLN03059  30 VSYDHRAFIINGQRRILISGSIHYPRSTPEMWPDLIQKAKDGGLDVIQTYVFWNGHEPSPGNYYFEDRYDLVKFIKVVQA 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  121 NGMYVTLRLGPFIQAEWTHGGLPYWLREVPGIFFRTDNKQFKEHTERYVRMILDKMKEERLFASQGGPIILGQIENEYSA 200
Cdd:PLN03059 110 AGLYVHLRIGPYICAEWNFGGFPVWLKYVPGIEFRTDNGPFKAAMQKFTEKIVDMMKSEKLFEPQGGPIILSQIENEYGP 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  201 VQRAYKQDGLNYIKWASNLVDSMKLGIPWVMCKQNDAPDPMINACNGRHCGDTFpgPNRENKPSLWTENWTTQFRVFGDP 280
Cdd:PLN03059 190 VEWEIGAPGKAYTKWAADMAVKLGTGVPWVMCKQEDAPDPVIDTCNGFYCENFK--PNKDYKPKMWTEAWTGWYTEFGGA 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  281 PTQRSVEDIAYSVARFFSKNGTHVNYYMYHGGTNFGRTSAH-YVTTRYYDDAPLDEYGLEKEPKYGHLKHLHNALNLCKK 359
Cdd:PLN03059 268 VPNRPAEDLAFSVARFIQNGGSFINYYMYHGGTNFGRTAGGpFIATSYDYDAPLDEYGLPREPKWGHLRDLHKAIKLCEP 347

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  360 PLLWGQPKTEKPGKDTEIRYYEqpGTKTCAAFLANNNTEAAETIKFKGREYVIAPRSISILPDCKTVVYNTAQIVSQHTS 439
Cdd:PLN03059 348 ALVSVDPTVTSLGSNQEAHVFK--SKSACAAFLANYDTKYSVKVTFGNGQYDLPPWSVSILPDCKTAVFNTARLGAQSSQ 425

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  440 rnfMKSKKANKKFDFKVFTETLPSKLEGNSYIP---VELYGLTKDKTDYGWYTTSFKVHKNHLPTKKGVKTFVRIASLGH 516
Cdd:PLN03059 426 ---MKMNPVGSTFSWQSYNEETASAYTDDTTTMdglWEQINVTRDATDYLWYMTEVHIDPDEGFLKTGQYPVLTIFSAGH 502

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  517 ALHAWLNGEYLGSGHGSHEEKSFVFQKQVTLKAGENHLVMLGVLTGFPDSGSYMEHRYTGPRG-ISILGLTSGTLDLTeS 595
Cdd:PLN03059 503 ALHVFINGQLAGTVYGELSNPKLTFSQNVKLTVGINKISLLSVAVGLPNVGLHFETWNAGVLGpVTLKGLNEGTRDLS-G 581

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  596 SKWGNKIGMEGEKLGIHTEEGLKKVEWKK--FTGKAPGLTWYQTYFDAPESVSAATIRMHGMGKGLIWVNGEGVGRYWQS 673
Cdd:PLN03059 582 WKWSYKIGLKGEALSLHTITGSSSVEWVEgsLLAQKQPLTWYKTTFDAPGGNDPLALDMSSMGKGQIWINGQSIGRHWPA 661

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  674 FL--------------------SPLGQPTQIEYHIPRSFLKPKKNLLVIFEEEPNvKPELMDFAIVNRDTVCSYVGENyT 733
Cdd:PLN03059 662 YTahgscngcnyagtfddkkcrTNCGEPSQRWYHVPRSWLKPSGNLLIVFEEWGG-NPAGISLVKRTTDSVCADIFEG-Q 739

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  734 PSVRHWtrkkdqvQAI----TDNVSLTATLKCSGTKKIAAVEFASFGNPIGVCGNFTLGTCNAPVSKQVIEKHCLGKAEC 809
Cdd:PLN03059 740 PALKNW-------QIIasgkVNSLQPKAHLWCPPGQKISKIKFASFGVPQGTCGSFREGSCHAHKSYDAFERNCIGKQSC 812

                        810       820       830
                 ....*....|....*....|....*....|
gi 18418558  810 VIPVNKSTFqqdKKDSCKNVVKMLAVQVKC 839
Cdd:PLN03059 813 SVTVAPEVF---GGDPCPDSMKKLSVEAVC 839
 
Name Accession Description Interval E-value
PLN03059 PLN03059
beta-galactosidase; Provisional
 41-839 0e+00

beta-galactosidase; Provisional


Pssm-ID: 166698 [Multi-domain]  Cd Length: 840  Bit Score: 756.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558   41 VTYDGTSLIIDGKRELLYSGSIHYPRSTPEMWPSIIKRAKQGGLNTIQTYVFWNVHEPQQGKFNFSGRADLVKFIKLIQK 120
Cdd:PLN03059  30 VSYDHRAFIINGQRRILISGSIHYPRSTPEMWPDLIQKAKDGGLDVIQTYVFWNGHEPSPGNYYFEDRYDLVKFIKVVQA 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  121 NGMYVTLRLGPFIQAEWTHGGLPYWLREVPGIFFRTDNKQFKEHTERYVRMILDKMKEERLFASQGGPIILGQIENEYSA 200
Cdd:PLN03059 110 AGLYVHLRIGPYICAEWNFGGFPVWLKYVPGIEFRTDNGPFKAAMQKFTEKIVDMMKSEKLFEPQGGPIILSQIENEYGP 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  201 VQRAYKQDGLNYIKWASNLVDSMKLGIPWVMCKQNDAPDPMINACNGRHCGDTFpgPNRENKPSLWTENWTTQFRVFGDP 280
Cdd:PLN03059 190 VEWEIGAPGKAYTKWAADMAVKLGTGVPWVMCKQEDAPDPVIDTCNGFYCENFK--PNKDYKPKMWTEAWTGWYTEFGGA 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  281 PTQRSVEDIAYSVARFFSKNGTHVNYYMYHGGTNFGRTSAH-YVTTRYYDDAPLDEYGLEKEPKYGHLKHLHNALNLCKK 359
Cdd:PLN03059 268 VPNRPAEDLAFSVARFIQNGGSFINYYMYHGGTNFGRTAGGpFIATSYDYDAPLDEYGLPREPKWGHLRDLHKAIKLCEP 347

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  360 PLLWGQPKTEKPGKDTEIRYYEqpGTKTCAAFLANNNTEAAETIKFKGREYVIAPRSISILPDCKTVVYNTAQIVSQHTS 439
Cdd:PLN03059 348 ALVSVDPTVTSLGSNQEAHVFK--SKSACAAFLANYDTKYSVKVTFGNGQYDLPPWSVSILPDCKTAVFNTARLGAQSSQ 425

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  440 rnfMKSKKANKKFDFKVFTETLPSKLEGNSYIP---VELYGLTKDKTDYGWYTTSFKVHKNHLPTKKGVKTFVRIASLGH 516
Cdd:PLN03059 426 ---MKMNPVGSTFSWQSYNEETASAYTDDTTTMdglWEQINVTRDATDYLWYMTEVHIDPDEGFLKTGQYPVLTIFSAGH 502

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  517 ALHAWLNGEYLGSGHGSHEEKSFVFQKQVTLKAGENHLVMLGVLTGFPDSGSYMEHRYTGPRG-ISILGLTSGTLDLTeS 595
Cdd:PLN03059 503 ALHVFINGQLAGTVYGELSNPKLTFSQNVKLTVGINKISLLSVAVGLPNVGLHFETWNAGVLGpVTLKGLNEGTRDLS-G 581

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  596 SKWGNKIGMEGEKLGIHTEEGLKKVEWKK--FTGKAPGLTWYQTYFDAPESVSAATIRMHGMGKGLIWVNGEGVGRYWQS 673
Cdd:PLN03059 582 WKWSYKIGLKGEALSLHTITGSSSVEWVEgsLLAQKQPLTWYKTTFDAPGGNDPLALDMSSMGKGQIWINGQSIGRHWPA 661

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  674 FL--------------------SPLGQPTQIEYHIPRSFLKPKKNLLVIFEEEPNvKPELMDFAIVNRDTVCSYVGENyT 733
Cdd:PLN03059 662 YTahgscngcnyagtfddkkcrTNCGEPSQRWYHVPRSWLKPSGNLLIVFEEWGG-NPAGISLVKRTTDSVCADIFEG-Q 739

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  734 PSVRHWtrkkdqvQAI----TDNVSLTATLKCSGTKKIAAVEFASFGNPIGVCGNFTLGTCNAPVSKQVIEKHCLGKAEC 809
Cdd:PLN03059 740 PALKNW-------QIIasgkVNSLQPKAHLWCPPGQKISKIKFASFGVPQGTCGSFREGSCHAHKSYDAFERNCIGKQSC 812

                        810       820       830
                 ....*....|....*....|....*....|
gi 18418558  810 VIPVNKSTFqqdKKDSCKNVVKMLAVQVKC 839
Cdd:PLN03059 813 SVTVAPEVF---GGDPCPDSMKKLSVEAVC 839
Glyco_hydro_35 pfam01301
Glycosyl hydrolases family 35;
47-352 2.15e-153

Glycosyl hydrolases family 35;


Pssm-ID: 396048 [Multi-domain]  Cd Length: 316  Bit Score: 451.71  E-value: 2.15e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558    47 SLIIDGKRELLYSGSIHYPRSTPEMWPSIIKRAKQGGLNTIQTYVFWNVHEPQQGKFNFSGRADLVKFIKLIQKNGMYVT 126
Cdd:pfam01301   1 SFLIDGKRFRLISGSIHYFRIPPEMWPDRLQKAKALGLNAIETYVFWNLHEPEPGQYDFSGILDLVKFIKLAQEAGLYVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558   127 LRLGPFIQAEWTHGGLPYWLREVPGIFFRTDNKQFKEHTERYVRMILDKMKEerLFASQGGPIILGQIENEYS--AVQRA 204
Cdd:pfam01301  81 LRPGPYICAEWDFGGLPAWLLTVPGIRLRTSDPPFLEAVERYLTALLPKMKP--LQATNGGPIIMVQVENEYGsyGVDKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558   205 YKQD-GLNYIKWASNLVDSMKLGIPWVMCKQN-DAPDPMINACNGRHCGDTFP------GPNRENKPSLWTENWTTQFRV 276
Cdd:pfam01301 159 YLRAlRKAYKEWGADMALLFTTDGPWGMCLQCgDLPGPDIYATNGFGCGANPPsnfkllRPFSPNKPLMWSEFWTGWFDH 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558   277 FGDPPTQRSVEDIAYSVARFFSKNgTHVNYYMYHGGTNFGRTS-AHYVT---TRYYDDAPLDEYGLEKePKYGHLKHLHN 352
Cdd:pfam01301 239 WGGPHAIRPAEDIAFEVARFLAKN-SSVNLYMFHGGTNFGFTNgANFYGpqtTSYDYDAPIDEAGDPT-PKYGHLKDLIT 316
Gal_Rha_Lectin_BGal cd22842
galactose/rhamnose binding lectin domain found in plant beta-galactosidases and similar ...
 756-839 6.25e-34

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: 125.09  E-value: 6.25e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558 756 TATLKCSGTKKIAAVEFASFGNPIGVCGNFTLGTCNAPVSKQVIEKHCLGKAECVIPVNKSTFQqdkKDSCKNVVKMLAV 835
Cdd:cd22842  11 TLTLSCPAGQVISSIDFASYGTPTGTCGSFSKGSCHAPNSLSVVEKACLGKNSCSIPASNSVFF---GDPCPGTTKRLAV 87


                ....
gi 18418558 836 QVKC 839
Cdd:cd22842  88 QATC 91
GanA COG1874
Beta-galactosidase GanA [Carbohydrate transport and metabolism];
53-198 1.00e-24

Beta-galactosidase GanA [Carbohydrate transport and metabolism];


Pssm-ID: 441478 [Multi-domain]  Cd Length: 609  Bit Score: 110.02  E-value: 1.00e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  53 KRELLYSGSIHYPRSTPEMWPSIIKRAKQGGLNTIQT-YVFWNVHEPQQGKFNFSGradLVKFIKLIQKNGMYVTLRLGP 131
Cdd:COG1874   7 KPFLILGGDYHPERWPPEVWAEDIRLMKAAGLNTVRIgYFAWNLHEPEEGVFDFDW---LDRFIDLLHEAGLKVILRTPT 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558 132 FIqaewthggLPYWL-REVPGIF----------------FRTDNKQFKEHTERYVRMILdkmkeERlfASQGGPIILGQI 194
Cdd:COG1874  84 AA--------PPAWLlKKYPEILpvdadgrrrgfgsrrhYCPSSPVYREAARRIVRALA-----ER--YGDHPAVIMWQV 148


                ....
gi 18418558 195 ENEY 198
Cdd:COG1874 149 DNEY 152
 
Name Accession Description Interval E-value
PLN03059 PLN03059
beta-galactosidase; Provisional
 41-839 0e+00

beta-galactosidase; Provisional


Pssm-ID: 166698 [Multi-domain]  Cd Length: 840  Bit Score: 756.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558   41 VTYDGTSLIIDGKRELLYSGSIHYPRSTPEMWPSIIKRAKQGGLNTIQTYVFWNVHEPQQGKFNFSGRADLVKFIKLIQK 120
Cdd:PLN03059  30 VSYDHRAFIINGQRRILISGSIHYPRSTPEMWPDLIQKAKDGGLDVIQTYVFWNGHEPSPGNYYFEDRYDLVKFIKVVQA 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  121 NGMYVTLRLGPFIQAEWTHGGLPYWLREVPGIFFRTDNKQFKEHTERYVRMILDKMKEERLFASQGGPIILGQIENEYSA 200
Cdd:PLN03059 110 AGLYVHLRIGPYICAEWNFGGFPVWLKYVPGIEFRTDNGPFKAAMQKFTEKIVDMMKSEKLFEPQGGPIILSQIENEYGP 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  201 VQRAYKQDGLNYIKWASNLVDSMKLGIPWVMCKQNDAPDPMINACNGRHCGDTFpgPNRENKPSLWTENWTTQFRVFGDP 280
Cdd:PLN03059 190 VEWEIGAPGKAYTKWAADMAVKLGTGVPWVMCKQEDAPDPVIDTCNGFYCENFK--PNKDYKPKMWTEAWTGWYTEFGGA 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  281 PTQRSVEDIAYSVARFFSKNGTHVNYYMYHGGTNFGRTSAH-YVTTRYYDDAPLDEYGLEKEPKYGHLKHLHNALNLCKK 359
Cdd:PLN03059 268 VPNRPAEDLAFSVARFIQNGGSFINYYMYHGGTNFGRTAGGpFIATSYDYDAPLDEYGLPREPKWGHLRDLHKAIKLCEP 347

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  360 PLLWGQPKTEKPGKDTEIRYYEqpGTKTCAAFLANNNTEAAETIKFKGREYVIAPRSISILPDCKTVVYNTAQIVSQHTS 439
Cdd:PLN03059 348 ALVSVDPTVTSLGSNQEAHVFK--SKSACAAFLANYDTKYSVKVTFGNGQYDLPPWSVSILPDCKTAVFNTARLGAQSSQ 425

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  440 rnfMKSKKANKKFDFKVFTETLPSKLEGNSYIP---VELYGLTKDKTDYGWYTTSFKVHKNHLPTKKGVKTFVRIASLGH 516
Cdd:PLN03059 426 ---MKMNPVGSTFSWQSYNEETASAYTDDTTTMdglWEQINVTRDATDYLWYMTEVHIDPDEGFLKTGQYPVLTIFSAGH 502

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  517 ALHAWLNGEYLGSGHGSHEEKSFVFQKQVTLKAGENHLVMLGVLTGFPDSGSYMEHRYTGPRG-ISILGLTSGTLDLTeS 595
Cdd:PLN03059 503 ALHVFINGQLAGTVYGELSNPKLTFSQNVKLTVGINKISLLSVAVGLPNVGLHFETWNAGVLGpVTLKGLNEGTRDLS-G 581

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  596 SKWGNKIGMEGEKLGIHTEEGLKKVEWKK--FTGKAPGLTWYQTYFDAPESVSAATIRMHGMGKGLIWVNGEGVGRYWQS 673
Cdd:PLN03059 582 WKWSYKIGLKGEALSLHTITGSSSVEWVEgsLLAQKQPLTWYKTTFDAPGGNDPLALDMSSMGKGQIWINGQSIGRHWPA 661

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  674 FL--------------------SPLGQPTQIEYHIPRSFLKPKKNLLVIFEEEPNvKPELMDFAIVNRDTVCSYVGENyT 733
Cdd:PLN03059 662 YTahgscngcnyagtfddkkcrTNCGEPSQRWYHVPRSWLKPSGNLLIVFEEWGG-NPAGISLVKRTTDSVCADIFEG-Q 739

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  734 PSVRHWtrkkdqvQAI----TDNVSLTATLKCSGTKKIAAVEFASFGNPIGVCGNFTLGTCNAPVSKQVIEKHCLGKAEC 809
Cdd:PLN03059 740 PALKNW-------QIIasgkVNSLQPKAHLWCPPGQKISKIKFASFGVPQGTCGSFREGSCHAHKSYDAFERNCIGKQSC 812

                        810       820       830
                 ....*....|....*....|....*....|
gi 18418558  810 VIPVNKSTFqqdKKDSCKNVVKMLAVQVKC 839
Cdd:PLN03059 813 SVTVAPEVF---GGDPCPDSMKKLSVEAVC 839
Glyco_hydro_35 pfam01301
Glycosyl hydrolases family 35;
47-352 2.15e-153

Glycosyl hydrolases family 35;


Pssm-ID: 396048 [Multi-domain]  Cd Length: 316  Bit Score: 451.71  E-value: 2.15e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558    47 SLIIDGKRELLYSGSIHYPRSTPEMWPSIIKRAKQGGLNTIQTYVFWNVHEPQQGKFNFSGRADLVKFIKLIQKNGMYVT 126
Cdd:pfam01301   1 SFLIDGKRFRLISGSIHYFRIPPEMWPDRLQKAKALGLNAIETYVFWNLHEPEPGQYDFSGILDLVKFIKLAQEAGLYVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558   127 LRLGPFIQAEWTHGGLPYWLREVPGIFFRTDNKQFKEHTERYVRMILDKMKEerLFASQGGPIILGQIENEYS--AVQRA 204
Cdd:pfam01301  81 LRPGPYICAEWDFGGLPAWLLTVPGIRLRTSDPPFLEAVERYLTALLPKMKP--LQATNGGPIIMVQVENEYGsyGVDKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558   205 YKQD-GLNYIKWASNLVDSMKLGIPWVMCKQN-DAPDPMINACNGRHCGDTFP------GPNRENKPSLWTENWTTQFRV 276
Cdd:pfam01301 159 YLRAlRKAYKEWGADMALLFTTDGPWGMCLQCgDLPGPDIYATNGFGCGANPPsnfkllRPFSPNKPLMWSEFWTGWFDH 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558   277 FGDPPTQRSVEDIAYSVARFFSKNgTHVNYYMYHGGTNFGRTS-AHYVT---TRYYDDAPLDEYGLEKePKYGHLKHLHN 352
Cdd:pfam01301 239 WGGPHAIRPAEDIAFEVARFLAKN-SSVNLYMFHGGTNFGFTNgANFYGpqtTSYDYDAPIDEAGDPT-PKYGHLKDLIT 316
Gal_Rha_Lectin_BGal cd22842
galactose/rhamnose binding lectin domain found in plant beta-galactosidases and similar ...
 756-839 6.25e-34

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: 125.09  E-value: 6.25e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558 756 TATLKCSGTKKIAAVEFASFGNPIGVCGNFTLGTCNAPVSKQVIEKHCLGKAECVIPVNKSTFQqdkKDSCKNVVKMLAV 835
Cdd:cd22842  11 TLTLSCPAGQVISSIDFASYGTPTGTCGSFSKGSCHAPNSLSVVEKACLGKNSCSIPASNSVFF---GDPCPGTTKRLAV 87


                ....
gi 18418558 836 QVKC 839
Cdd:cd22842  88 QATC 91
GanA COG1874
Beta-galactosidase GanA [Carbohydrate transport and metabolism];
53-198 1.00e-24

Beta-galactosidase GanA [Carbohydrate transport and metabolism];


Pssm-ID: 441478 [Multi-domain]  Cd Length: 609  Bit Score: 110.02  E-value: 1.00e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558  53 KRELLYSGSIHYPRSTPEMWPSIIKRAKQGGLNTIQT-YVFWNVHEPQQGKFNFSGradLVKFIKLIQKNGMYVTLRLGP 131
Cdd:COG1874   7 KPFLILGGDYHPERWPPEVWAEDIRLMKAAGLNTVRIgYFAWNLHEPEEGVFDFDW---LDRFIDLLHEAGLKVILRTPT 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558 132 FIqaewthggLPYWL-REVPGIF----------------FRTDNKQFKEHTERYVRMILdkmkeERlfASQGGPIILGQI 194
Cdd:COG1874  84 AA--------PPAWLlKKYPEILpvdadgrrrgfgsrrhYCPSSPVYREAARRIVRALA-----ER--YGDHPAVIMWQV 148


                ....
gi 18418558 195 ENEY 198
Cdd:COG1874 149 DNEY 152
Gal_Lectin pfam02140
Galactose binding lectin domain;
759-839 5.23e-23

Galactose binding lectin domain;


Pssm-ID: 460460 [Multi-domain]  Cd Length: 79  Bit Score: 93.51  E-value: 5.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558   759 LKCSGTKKIAaVEFASFGNPIG-VCGNFTLGT-CNAPVSKQVIEKHCLGKAECVIPVNKSTFQqdkKDSCKNVVKMLAVQ 836
Cdd:pfam02140   1 LSCPPGKVIS-ILFASYGRPDGtTCPSFIQGTnCHSPNSLAIVSKACQGKNSCSVPASNSVFG---GDPCPGTYKYLEVE 76


                  ...
gi 18418558   837 VKC 839
Cdd:pfam02140  77 YKC 79
GHD pfam17834
Beta-sandwich domain in beta galactosidase; This entry corresponds to a beta sandwich like ...
 361-433 4.08e-22

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: 90.44  E-value: 4.08e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18418558   361 LLWGQPKTEKPGKDTEIRYYEQPGTKtCAAFLANNNTEAAETIKFKGREYVIAPRSISILPDCKTVVYNTAQI 433
Cdd:pfam17834   1 LLSGQYTTTNLGKLQTATVFEKDKGS-CVAFLVNIDDKKDANVTFRGSDYFLPAWSISILPDCKTVVFNTAKV 72
Gal_Rha_Lectin cd22823
Galactose/rhamnose-binding lectin domain; Galactose/rhamnose-binding lectin domain is formed ...
 756-839 8.97e-10

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: 56.36  E-value: 8.97e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558 756 TATLKCSGTKKIAaVEFASFG-NPIGVC----GNFTLGTCNAPVSKQVIEKHCLGKAECVIPVNKSTFqqdkKDSCKNVV 830
Cdd:cd22823   8 TLTLSCPSGQVIK-ILSAFYGrTDGTTCccgpNNTSDTNCCSPDVLDIVKELCDGKQSCSVPASNSVF----GDPCPGTS 82


                ....*....
gi 18418558 831 KMLAVQVKC 839
Cdd:cd22823  83 KYLEVTYTC 91
Glyco_hydro_42 pfam02449
Beta-galactosidase; This group of beta-galactosidase enzymes belong to the glycosyl hydrolase ...
 63-198 1.10e-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: 61.13  E-value: 1.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558    63 HYPRSTpemWPSIIKRAKQGGLNTIQTYVF-WNVHEPQQGKFNFSGradLVKFIKLIQKNGMYVTLRLGPfiqaewthGG 141
Cdd:pfam02449   6 QWPEET---WEEDIRLMKEAGVNVVRIGIFaWAKLEPEEGKYDFEW---LDEVIDLLAKAGIKVILATPT--------AA 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18418558   142 LPYWL-------------REVPGI----FFRTDNKQFKEHTERYVRMIldkmkEERLfaSQGGPIILGQIENEY 198
Cdd:pfam02449  72 PPAWLvkkhpeilpvdadGRRRGFgsrhHYCPSSPVYREYAARIVEAL-----AERY--GDHPALIGWHIDNEY 138
Gal_Rha_Lectin_SUL-I-like cd22827
galactose/rhamnose binding lectin domain found in Toxopneustes pileolus rhamnose-binding ...
 756-839 7.09e-09

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: 53.36  E-value: 7.09e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558 756 TATLKCSGTKKIAaVEFASFG--NPIgVCGNFTLGT--CNAPVSKQVIEKHCLGKAECVIPVNKSTFqqdkKDSCKNVVK 831
Cdd:cd22827   8 TLTISCPAGKVID-IVSANYGrtDSS-TCPSGGIKNtnCRASNSLSIVRNRCNGKRSCSVKASNSVF----GDPCVGTYK 81


                ....*...
gi 18418558 832 MLAVQVKC 839
Cdd:cd22827  82 YLEVRYRC 89
Gal_Rha_Lectin_LAT2 cd22840
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ...
 758-839 9.67e-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: 50.49  E-value: 9.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558 758 TLKCSGTKKIAaVEFASFGNpIG---VCGNFTLG---TCNAPVSKQVIEKHCLGKAECVIPVNKSTFQqdkKDSC-KNVV 830
Cdd:cd22840  13 EISCPSGQRIK-VDYASYGA-IGtrsTCGDSVSPageTCSAPNSLQTMRQRCQGRQSCEIRVLNSLFP---NDPCpGTSK 87


                ....*....
gi 18418558 831 KMLAVQVKC 839
Cdd:cd22840  88 KYLEYRYRC 96
Gal_Rha_Lectin_dCirl cd22830
galactose/rhamnose binding lectin domain found in Drosophila melanogaster Latrophilin Cirl and ...
 756-839 2.37e-06

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: 46.46  E-value: 2.37e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558 756 TATLKCSGTKKIAAVEfASFGNpigvcgnFTLGTCN------------APVSKQVIEKHCLGKAECVIPVNKSTFqqdkK 823
Cdd:cd22830   9 QLTLECEDGTVIRIIR-ANYGR-------FSIAICNdhgntdwsvncmSPRSLRVVQERCDGKRSCSIPASSSVF----G 76

                        90
                ....*....|....*.
gi 18418558 824 DSCKNVVKMLAVQVKC 839
Cdd:cd22830  77 DPCPGTPKYLEVHYQC 92
Gal_Rha_Lectin_LAT1 cd22839
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ...
 755-839 5.51e-06

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: 45.49  E-value: 5.51e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558 755 LTATLKCSGTKKIAaVEFASFGN-PIGVC---GNFTLGT-CNAPVSKQVIEKHCLGKAECVIPVNKSTFQQdkkDSCKNV 829
Cdd:cd22839  10 DVANLSCPEGKYIS-IRLANYGRfSLGVCnpsNNIDLSTtCQNDKTLPILQKSCDGKSECSFVVSNKFFFE---DPCPGT 85

                        90
                ....*....|
gi 18418558 830 VKMLAVQVKC 839
Cdd:cd22839  86 PKYLEATYSC 95
LacZ COG3250
Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism];
476-555 7.98e-05

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


Pssm-ID: 442481 [Multi-domain]  Cd Length: 638  Bit Score: 46.29  E-value: 7.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558 476 YGLTKDKTDYGWYTTSFKVHKNhlptKKGVKTFVRIASLGHALHAWLNGEYLGSGHGSHEekSFVFqkQVT--LKAGENH 553
Cdd:COG3250  44 VGPWYLYNGVGWYRRTFTVPAS----WKGKRVFLHFEGVDTAAEVWVNGKKVGYHEGGFT--PFEF--DITdyLKPGENV 115


                ..
gi 18418558 554 LV 555
Cdd:COG3250 116 LA 117
Gal_Rha_Lectin_EVA1_EVA1C_rpt1 cd22828
first galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
 789-839 1.37e-04

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: 41.88  E-value: 1.37e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 18418558 789 TCNAPVSKQVIEKHCLGKAECVIPVNKSTFQQdkkDSCKNVVKMLAVQVKC 839
Cdd:cd22828  56 NCLAPTALQKVVEECQKKRSCRLLVSSRTFGL---DPCPGTSKYLEVAYKC 103
Glyco_hydro_2_N pfam02837
Glycosyl hydrolases family 2, sugar binding domain; This family contains beta-galactosidase, ...
 486-556 2.18e-03

Glycosyl hydrolases family 2, sugar binding domain; This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities and has a jelly-roll fold. The domain binds the sugar moiety during the sugar-hydrolysis reaction.


Pssm-ID: 397120 [Multi-domain]  Cd Length: 169  Bit Score: 39.92  E-value: 2.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18418558   486 GWYTTSFKVhknhlPTK-KGVKTFVRIASLGHALHAWLNGEYLGSGHGSHeeKSFVFQKQVTLKAGENHLVM 556
Cdd:pfam02837  67 GWYQRTFFI-----PSKwAGQRIRLRFDGVTHYGEVWVNGQWVGEHQGGY--TPFEFDLTPYVIAGKNRIAV 131
Gal_Rha_Lectin-like_P113 cd22843
galactose/rhamnose binding lectin-like domain found in Plasmodium falciparum P113 and similar ...
 756-839 4.39e-03

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: 37.04  E-value: 4.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418558 756 TATLKCSGTKKIAaVEFASFG-NPIGVCGNFTLGTCNAPVSKQViEKHCLGKAECVIPVNKSTFqqdkKDSCKNVVKMLA 834
Cdd:cd22843  11 EVTIHCPGDGNIS-IKSATYGyNNSNVCIYCNSFNCDKDITSPV-NKKCCGKNTCVLTVSDILE----GNPCGIGNSYIR 84


                ....*
gi 18418558 835 VQVKC 839
Cdd:cd22843  85 VVYTC 89
 
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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