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Conserved domains on  [gi|1039007969|gb|ANM58139|]
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beta-galactosidase 16 [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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN03059 super family cl31552
beta-galactosidase; Provisional
19-709 0e+00

beta-galactosidase; Provisional


The actual alignment was detected with superfamily member PLN03059:

Pssm-ID: 166698 [Multi-domain]  Cd Length: 840  Bit Score: 704.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969  19 GLPFWLHNVQGIVFRTDNEPFKYHMKRYAKMIVKLMKSENLYASQGGPIILSQIENEYGMVGRAFRQEGKSYVKWTAKLA 98
Cdd:PLN03059  130 GFPVWLKYVPGIEFRTDNGPFKAAMQKFTEKIVDMMKSEKLFEPQGGPIILSQIENEYGPVEWEIGAPGKAYTKWAADMA 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969  99 VELDTGVPWVMCKQDDAPDPLVNACNGRQCgETFKgPNSPNKPAIWTENWTSFYQTYGEEPLIRSAEDIAFHVALFIAKN 178
Cdd:PLN03059  210 VKLGTGVPWVMCKQEDAPDPVIDTCNGFYC-ENFK-PNKDYKPKMWTEAWTGWYTEFGGAVPNRPAEDLAFSVARFIQNG 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 179 GSFVNYYMYHGGTNFGRNAS-QFVITSYYDQAPLDEYGLLRQPKWGHLKELHAAVKLCEEPLLSGLQTTISLGKLQTAFV 257
Cdd:PLN03059  288 GSFINYYMYHGGTNFGRTAGgPFIATSYDYDAPLDEYGLPREPKWGHLRDLHKAIKLCEPALVSVDPTVTSLGSNQEAHV 367
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 258 FGKKAnLCAAILVNQD-KCESTVQFRNSSYRLSPKSVSVLPDCKNVAFNTAKVNAQyntRTRKARQNLSSPQMWEEFT-E 335
Cdd:PLN03059  368 FKSKS-ACAAFLANYDtKYSVKVTFGNGQYDLPPWSVSILPDCKTAVFNTARLGAQ---SSQMKMNPVGSTFSWQSYNeE 443
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 336 TVPSFSETSIRSESLLEHMNTTQDTSDYLWQTTR--------FQQSEGAPsVLKVNHLGHALHAFVNGRFIGSMHGTFKA 407
Cdd:PLN03059  444 TASAYTDDTTTMDGLWEQINVTRDATDYLWYMTEvhidpdegFLKTGQYP-VLTIFSAGHALHVFINGQLAGTVYGELSN 522
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 408 HRFLLEKNMSLNNGTNNLALLSVMVGLPNSGAHLER---RVVGSRSVKIWN-GRYQLyfNNYSWGYQVGLKGEKFHVYTE 483
Cdd:PLN03059  523 PKLTFSQNVKLTVGINKISLLSVAVGLPNVGLHFETwnaGVLGPVTLKGLNeGTRDL--SGWKWSYKIGLKGEALSLHTI 600
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 484 DGSAKVQWKQYR-DSKSQPLTWYKASFDTPEGEDPVALNLGSMGKGEAWVNGQSIGRYWVSF------------------ 544
Cdd:PLN03059  601 TGSSSVEWVEGSlLAQKQPLTWYKTTFDAPGGNDPLALDMSSMGKGQIWINGQSIGRHWPAYtahgscngcnyagtfddk 680
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 545 --HTYKGNPSQIWYHIPRSFLKPNSNLLVILeEEREGNPLGITIDTVSVTEVCGHVSNTNPhPVISPRKKGLNRKNltyr 622
Cdd:PLN03059  681 kcRTNCGEPSQRWYHVPRSWLKPSGNLLIVF-EEWGGNPAGISLVKRTTDSVCADIFEGQP-ALKNWQIIASGKVN---- 754
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 623 yDRKPKVQLQCPTGRKISKILFASFGTPNGSCGSYSIGSCHSPNSLAVVQKACLKKSRCSVPVWSKTFGGDSCPHTVKSL 702
Cdd:PLN03059  755 -SLQPKAHLWCPPGQKISKIKFASFGVPQGTCGSFREGSCHAHKSYDAFERNCIGKQSCSVTVAPEVFGGDPCPDSMKKL 833

                  ....*..
gi 1039007969 703 LVRAQCS 709
Cdd:PLN03059  834 SVEAVCS 840
 
Name Accession Description Interval E-value
PLN03059 PLN03059
beta-galactosidase; Provisional
19-709 0e+00

beta-galactosidase; Provisional


Pssm-ID: 166698 [Multi-domain]  Cd Length: 840  Bit Score: 704.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969  19 GLPFWLHNVQGIVFRTDNEPFKYHMKRYAKMIVKLMKSENLYASQGGPIILSQIENEYGMVGRAFRQEGKSYVKWTAKLA 98
Cdd:PLN03059  130 GFPVWLKYVPGIEFRTDNGPFKAAMQKFTEKIVDMMKSEKLFEPQGGPIILSQIENEYGPVEWEIGAPGKAYTKWAADMA 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969  99 VELDTGVPWVMCKQDDAPDPLVNACNGRQCgETFKgPNSPNKPAIWTENWTSFYQTYGEEPLIRSAEDIAFHVALFIAKN 178
Cdd:PLN03059  210 VKLGTGVPWVMCKQEDAPDPVIDTCNGFYC-ENFK-PNKDYKPKMWTEAWTGWYTEFGGAVPNRPAEDLAFSVARFIQNG 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 179 GSFVNYYMYHGGTNFGRNAS-QFVITSYYDQAPLDEYGLLRQPKWGHLKELHAAVKLCEEPLLSGLQTTISLGKLQTAFV 257
Cdd:PLN03059  288 GSFINYYMYHGGTNFGRTAGgPFIATSYDYDAPLDEYGLPREPKWGHLRDLHKAIKLCEPALVSVDPTVTSLGSNQEAHV 367
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 258 FGKKAnLCAAILVNQD-KCESTVQFRNSSYRLSPKSVSVLPDCKNVAFNTAKVNAQyntRTRKARQNLSSPQMWEEFT-E 335
Cdd:PLN03059  368 FKSKS-ACAAFLANYDtKYSVKVTFGNGQYDLPPWSVSILPDCKTAVFNTARLGAQ---SSQMKMNPVGSTFSWQSYNeE 443
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 336 TVPSFSETSIRSESLLEHMNTTQDTSDYLWQTTR--------FQQSEGAPsVLKVNHLGHALHAFVNGRFIGSMHGTFKA 407
Cdd:PLN03059  444 TASAYTDDTTTMDGLWEQINVTRDATDYLWYMTEvhidpdegFLKTGQYP-VLTIFSAGHALHVFINGQLAGTVYGELSN 522
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 408 HRFLLEKNMSLNNGTNNLALLSVMVGLPNSGAHLER---RVVGSRSVKIWN-GRYQLyfNNYSWGYQVGLKGEKFHVYTE 483
Cdd:PLN03059  523 PKLTFSQNVKLTVGINKISLLSVAVGLPNVGLHFETwnaGVLGPVTLKGLNeGTRDL--SGWKWSYKIGLKGEALSLHTI 600
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 484 DGSAKVQWKQYR-DSKSQPLTWYKASFDTPEGEDPVALNLGSMGKGEAWVNGQSIGRYWVSF------------------ 544
Cdd:PLN03059  601 TGSSSVEWVEGSlLAQKQPLTWYKTTFDAPGGNDPLALDMSSMGKGQIWINGQSIGRHWPAYtahgscngcnyagtfddk 680
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 545 --HTYKGNPSQIWYHIPRSFLKPNSNLLVILeEEREGNPLGITIDTVSVTEVCGHVSNTNPhPVISPRKKGLNRKNltyr 622
Cdd:PLN03059  681 kcRTNCGEPSQRWYHVPRSWLKPSGNLLIVF-EEWGGNPAGISLVKRTTDSVCADIFEGQP-ALKNWQIIASGKVN---- 754
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 623 yDRKPKVQLQCPTGRKISKILFASFGTPNGSCGSYSIGSCHSPNSLAVVQKACLKKSRCSVPVWSKTFGGDSCPHTVKSL 702
Cdd:PLN03059  755 -SLQPKAHLWCPPGQKISKIKFASFGVPQGTCGSFREGSCHAHKSYDAFERNCIGKQSCSVTVAPEVFGGDPCPDSMKKL 833

                  ....*..
gi 1039007969 703 LVRAQCS 709
Cdd:PLN03059  834 SVEAVCS 840
Glyco_hydro_35 pfam01301
Glycosyl hydrolases family 35;
19-230 5.09e-93

Glycosyl hydrolases family 35;


Pssm-ID: 396048 [Multi-domain]  Cd Length: 316  Bit Score: 291.85  E-value: 5.09e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969  19 GLPFWLHNVQGIVFRTDNEPFKYHMKRYAKMIVKLMKSenLYASQGGPIILSQIENEYG--MVGRAF-RQEGKSYVKWTA 95
Cdd:pfam01301  95 GLPAWLLTVPGIRLRTSDPPFLEAVERYLTALLPKMKP--LQATNGGPIIMVQVENEYGsyGVDKAYlRALRKAYKEWGA 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969  96 KLAVELDTGVPWVMCKQD-DAPDPLVNACNGRQCGETFK------GPNSPNKPAIWTENWTSFYQTYGEEPLIRSAEDIA 168
Cdd:pfam01301 173 DMALLFTTDGPWGMCLQCgDLPGPDIYATNGFGCGANPPsnfkllRPFSPNKPLMWSEFWTGWFDHWGGPHAIRPAEDIA 252
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039007969 169 FHVALFIAKNGSfVNYYMYHGGTNFGR-NASQFV---ITSYYDQAPLDEYGLLRqPKWGHLKELHA 230
Cdd:pfam01301 253 FEVARFLAKNSS-VNLYMFHGGTNFGFtNGANFYgpqTTSYDYDAPIDEAGDPT-PKYGHLKDLIT 316
Gal_Rha_Lectin_BGal cd22842
galactose/rhamnose binding lectin domain found in plant beta-galactosidases and similar ...
626-708 1.47e-42

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: 148.97  E-value: 1.47e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 626 KPKVQLQCPTGRKISKILFASFGTPNGSCGSYSIGSCHSPNSLAVVQKACLKKSRCSVPVWSKTFGGDSCPHTVKSLLVR 705
Cdd:cd22842     9 GSTLTLSCPAGQVISSIDFASYGTPTGTCGSFSKGSCHAPNSLSVVEKACLGKNSCSIPASNSVFFGDPCPGTTKRLAVQ 88

                  ...
gi 1039007969 706 AQC 708
Cdd:cd22842    89 ATC 91
 
Name Accession Description Interval E-value
PLN03059 PLN03059
beta-galactosidase; Provisional
19-709 0e+00

beta-galactosidase; Provisional


Pssm-ID: 166698 [Multi-domain]  Cd Length: 840  Bit Score: 704.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969  19 GLPFWLHNVQGIVFRTDNEPFKYHMKRYAKMIVKLMKSENLYASQGGPIILSQIENEYGMVGRAFRQEGKSYVKWTAKLA 98
Cdd:PLN03059  130 GFPVWLKYVPGIEFRTDNGPFKAAMQKFTEKIVDMMKSEKLFEPQGGPIILSQIENEYGPVEWEIGAPGKAYTKWAADMA 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969  99 VELDTGVPWVMCKQDDAPDPLVNACNGRQCgETFKgPNSPNKPAIWTENWTSFYQTYGEEPLIRSAEDIAFHVALFIAKN 178
Cdd:PLN03059  210 VKLGTGVPWVMCKQEDAPDPVIDTCNGFYC-ENFK-PNKDYKPKMWTEAWTGWYTEFGGAVPNRPAEDLAFSVARFIQNG 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 179 GSFVNYYMYHGGTNFGRNAS-QFVITSYYDQAPLDEYGLLRQPKWGHLKELHAAVKLCEEPLLSGLQTTISLGKLQTAFV 257
Cdd:PLN03059  288 GSFINYYMYHGGTNFGRTAGgPFIATSYDYDAPLDEYGLPREPKWGHLRDLHKAIKLCEPALVSVDPTVTSLGSNQEAHV 367
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 258 FGKKAnLCAAILVNQD-KCESTVQFRNSSYRLSPKSVSVLPDCKNVAFNTAKVNAQyntRTRKARQNLSSPQMWEEFT-E 335
Cdd:PLN03059  368 FKSKS-ACAAFLANYDtKYSVKVTFGNGQYDLPPWSVSILPDCKTAVFNTARLGAQ---SSQMKMNPVGSTFSWQSYNeE 443
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 336 TVPSFSETSIRSESLLEHMNTTQDTSDYLWQTTR--------FQQSEGAPsVLKVNHLGHALHAFVNGRFIGSMHGTFKA 407
Cdd:PLN03059  444 TASAYTDDTTTMDGLWEQINVTRDATDYLWYMTEvhidpdegFLKTGQYP-VLTIFSAGHALHVFINGQLAGTVYGELSN 522
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 408 HRFLLEKNMSLNNGTNNLALLSVMVGLPNSGAHLER---RVVGSRSVKIWN-GRYQLyfNNYSWGYQVGLKGEKFHVYTE 483
Cdd:PLN03059  523 PKLTFSQNVKLTVGINKISLLSVAVGLPNVGLHFETwnaGVLGPVTLKGLNeGTRDL--SGWKWSYKIGLKGEALSLHTI 600
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 484 DGSAKVQWKQYR-DSKSQPLTWYKASFDTPEGEDPVALNLGSMGKGEAWVNGQSIGRYWVSF------------------ 544
Cdd:PLN03059  601 TGSSSVEWVEGSlLAQKQPLTWYKTTFDAPGGNDPLALDMSSMGKGQIWINGQSIGRHWPAYtahgscngcnyagtfddk 680
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 545 --HTYKGNPSQIWYHIPRSFLKPNSNLLVILeEEREGNPLGITIDTVSVTEVCGHVSNTNPhPVISPRKKGLNRKNltyr 622
Cdd:PLN03059  681 kcRTNCGEPSQRWYHVPRSWLKPSGNLLIVF-EEWGGNPAGISLVKRTTDSVCADIFEGQP-ALKNWQIIASGKVN---- 754
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 623 yDRKPKVQLQCPTGRKISKILFASFGTPNGSCGSYSIGSCHSPNSLAVVQKACLKKSRCSVPVWSKTFGGDSCPHTVKSL 702
Cdd:PLN03059  755 -SLQPKAHLWCPPGQKISKIKFASFGVPQGTCGSFREGSCHAHKSYDAFERNCIGKQSCSVTVAPEVFGGDPCPDSMKKL 833

                  ....*..
gi 1039007969 703 LVRAQCS 709
Cdd:PLN03059  834 SVEAVCS 840
Glyco_hydro_35 pfam01301
Glycosyl hydrolases family 35;
19-230 5.09e-93

Glycosyl hydrolases family 35;


Pssm-ID: 396048 [Multi-domain]  Cd Length: 316  Bit Score: 291.85  E-value: 5.09e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969  19 GLPFWLHNVQGIVFRTDNEPFKYHMKRYAKMIVKLMKSenLYASQGGPIILSQIENEYG--MVGRAF-RQEGKSYVKWTA 95
Cdd:pfam01301  95 GLPAWLLTVPGIRLRTSDPPFLEAVERYLTALLPKMKP--LQATNGGPIIMVQVENEYGsyGVDKAYlRALRKAYKEWGA 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969  96 KLAVELDTGVPWVMCKQD-DAPDPLVNACNGRQCGETFK------GPNSPNKPAIWTENWTSFYQTYGEEPLIRSAEDIA 168
Cdd:pfam01301 173 DMALLFTTDGPWGMCLQCgDLPGPDIYATNGFGCGANPPsnfkllRPFSPNKPLMWSEFWTGWFDHWGGPHAIRPAEDIA 252
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039007969 169 FHVALFIAKNGSfVNYYMYHGGTNFGR-NASQFV---ITSYYDQAPLDEYGLLRqPKWGHLKELHA 230
Cdd:pfam01301 253 FEVARFLAKNSS-VNLYMFHGGTNFGFtNGANFYgpqTTSYDYDAPIDEAGDPT-PKYGHLKDLIT 316
Gal_Rha_Lectin_BGal cd22842
galactose/rhamnose binding lectin domain found in plant beta-galactosidases and similar ...
626-708 1.47e-42

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: 148.97  E-value: 1.47e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 626 KPKVQLQCPTGRKISKILFASFGTPNGSCGSYSIGSCHSPNSLAVVQKACLKKSRCSVPVWSKTFGGDSCPHTVKSLLVR 705
Cdd:cd22842     9 GSTLTLSCPAGQVISSIDFASYGTPTGTCGSFSKGSCHAPNSLSVVEKACLGKNSCSIPASNSVFFGDPCPGTTKRLAVQ 88

                  ...
gi 1039007969 706 AQC 708
Cdd:cd22842    89 ATC 91
Gal_Lectin pfam02140
Galactose binding lectin domain;
631-708 2.39e-30

Galactose binding lectin domain;


Pssm-ID: 460460 [Multi-domain]  Cd Length: 79  Bit Score: 113.92  E-value: 2.39e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 631 LQCPTGRKISkILFASFGTPNGS-CGSYSIGS-CHSPNSLAVVQKACLKKSRCSVPVWSKTFGGDSCPHTVKSLLVRAQC 708
Cdd:pfam02140   1 LSCPPGKVIS-ILFASYGRPDGTtCPSFIQGTnCHSPNSLAIVSKACQGKNSCSVPASNSVFGGDPCPGTYKYLEVEYKC 79
GHD pfam17834
Beta-sandwich domain in beta galactosidase; This entry corresponds to a beta sandwich like ...
239-309 8.34e-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: 112.39  E-value: 8.34e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039007969 239 LLSGLQTTISLGKLQTAFVFGKKANLCAAILVNQDKCES-TVQFRNSSYRLSPKSVSVLPDCKNVAFNTAKV 309
Cdd:pfam17834   1 LLSGQYTTTNLGKLQTATVFEKDKGSCVAFLVNIDDKKDaNVTFRGSDYFLPAWSISILPDCKTVVFNTAKV 72
Gal_Rha_Lectin_SUL-I-like cd22827
galactose/rhamnose binding lectin domain found in Toxopneustes pileolus rhamnose-binding ...
630-708 6.56e-15

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: 70.31  E-value: 6.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 630 QLQCPTGRKIsKILFASFG-TPNGSCGSYSI--GSCHSPNSLAVVQKACLKKSRCSVPVwSKTFGGDSCPHTVKSLLVRA 706
Cdd:cd22827    10 TISCPAGKVI-DIVSANYGrTDSSTCPSGGIknTNCRASNSLSIVRNRCNGKRSCSVKA-SNSVFGDPCVGTYKYLEVRY 87

                  ..
gi 1039007969 707 QC 708
Cdd:cd22827    88 RC 89
Gal_Rha_Lectin_EVA1_EVA1C_rpt1 cd22828
first galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
628-708 1.62e-14

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: 70.00  E-value: 1.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 628 KVQLQCPTGRKISkILFASFG------------TPNGSCGSYSIGSCHSPNSLAVVQKACLKKSRCSVPVWSKTFGGDSC 695
Cdd:cd22828    12 ELTLRCPPNTTIS-IQSAFYGrsvpsaqlcpsqSGPASSTSLEDTNCLAPTALQKVVEECQKKRSCRLLVSSRTFGLDPC 90
                          90
                  ....*....|...
gi 1039007969 696 PHTVKSLLVRAQC 708
Cdd:cd22828    91 PGTSKYLEVAYKC 103
Gal_Rha_Lectin cd22823
Galactose/rhamnose-binding lectin domain; Galactose/rhamnose-binding lectin domain is formed ...
628-708 3.69e-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: 3.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 628 KVQLQCPTGRKIsKILFASFG-TPNGSCGSYSIGS----CHSPNSLAVVQKACLKKSRCSVPVwSKTFGGDSCPHTVKSL 702
Cdd:cd22823     8 TLTLSCPSGQVI-KILSAFYGrTDGTTCCCGPNNTsdtnCCSPDVLDIVKELCDGKQSCSVPA-SNSVFGDPCPGTSKYL 85

                  ....*.
gi 1039007969 703 LVRAQC 708
Cdd:cd22823    86 EVTYTC 91
Gal_Rha_Lectin_LAT1 cd22839
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ...
629-708 4.63e-12

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: 62.44  E-value: 4.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 629 VQLQCPTGRKISkILFASFGtpngscgSYSIG------------SCHSPNSLAVVQKACLKKSRCSVPVWSKTFGGDSCP 696
Cdd:cd22839    12 ANLSCPEGKYIS-IRLANYG-------RFSLGvcnpsnnidlstTCQNDKTLPILQKSCDGKSECSFVVSNKFFFEDPCP 83
                          90
                  ....*....|..
gi 1039007969 697 HTVKSLLVRAQC 708
Cdd:cd22839    84 GTPKYLEATYSC 95
Gal_Rha_Lectin_LAT2 cd22840
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ...
628-708 1.30e-10

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: 58.58  E-value: 1.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 628 KVQLQCPTGRKIsKILFASFGTPNGS--CGSYSIG---SCHSPNSLAVVQKACLKKSRCSVPVWSKTFGGDSCPHTV-KS 701
Cdd:cd22840    11 PFEISCPSGQRI-KVDYASYGAIGTRstCGDSVSPageTCSAPNSLQTMRQRCQGRQSCEIRVLNSLFPNDPCPGTSkKY 89

                  ....*..
gi 1039007969 702 LLVRAQC 708
Cdd:cd22840    90 LEYRYRC 96
Gal_Rha_Lectin_dCirl cd22830
galactose/rhamnose binding lectin domain found in Drosophila melanogaster Latrophilin Cirl and ...
631-708 1.13e-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: 55.71  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 631 LQCPTGRKISkILFASFG-------TPNGSCGsYSIgSCHSPNSLAVVQKACLKKSRCSVPVwSKTFGGDSCPHTVKSLL 703
Cdd:cd22830    12 LECEDGTVIR-IIRANYGrfsiaicNDHGNTD-WSV-NCMSPRSLRVVQERCDGKRSCSIPA-SSSVFGDPCPGTPKYLE 87

                  ....*
gi 1039007969 704 VRAQC 708
Cdd:cd22830    88 VHYQC 92
Gal_Rha_Lectin_EVA1_EVA1C_rpt2 cd22829
second galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
628-700 8.08e-09

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: 53.42  E-value: 8.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 628 KVQLQCPTGRKISkILFASFG-TPNGS--CGSYSIG----SCHSPNSLAVVQKACLKKSRCSVPVWSKTFgGDSCPHTVK 700
Cdd:cd22829    11 KLRLSCKPSSRLA-IYSASYGrTLEGSveCPSTPKGdpdeECLSDVALETVMKRCHGKRRCSLTADSETF-GDPCPPGVR 88
Gal_Rha_Lectin_RBL_rpt2 cd22836
second galactose/rhamnose binding lectin domain found in Silurus asotus rhamnose-binding ...
662-708 1.79e-06

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: 46.51  E-value: 1.79e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1039007969 662 CHSPNSLAVVQKACLKKSRCSVPVWSKTFgGDSCPHTVKSLLVRAQC 708
Cdd:cd22836    50 CYASNSLAIVSQSCNGKKSCTVSASNSVF-SDPCVGTYKYLYVTYSC 95
Gal_Rha_Lectin-like_P113 cd22843
galactose/rhamnose binding lectin-like domain found in Plasmodium falciparum P113 and similar ...
631-708 1.22e-05

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: 43.97  E-value: 1.22e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039007969 631 LQCPTGRKISkILFASFGTPNGSCGSYSIGSCHSPNSLAVVQKACLKKSRCSVPVWSKTFgGDSCPHTVKSLLVRAQC 708
Cdd:cd22843    14 IHCPGDGNIS-IKSATYGYNNSNVCIYCNSFNCDKDITSPVNKKCCGKNTCVLTVSDILE-GNPCGIGNSYIRVVYTC 89
Gal_Rha_Lectin_REJ3 cd22841
galactose/rhamnose binding lectin domain found in Strongylocentrotus purpuratus receptor for ...
631-708 1.90e-05

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: 43.62  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039007969 631 LQCPTGRKIskILFASFGTPNGS----CGSYSIGSCHSPNSLAVVQKACLKKSRCSVPVwSKTFGGDSCPHTVKSLLVRA 706
Cdd:cd22841    14 IDCGNGVIN--IHSAVYGRTDSTtcshDQSVSNTNCHSDDSVNILSACCNGQSQCTVTA-TNSIFGDPCPGTYKYLNVTY 90

                  ..
gi 1039007969 707 QC 708
Cdd:cd22841    91 TC 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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