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Conserved domains on  [gi|238481152|ref|NP_001154292|]
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beta-galactosidase 14 [Arabidopsis thaliana]

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
 65-831 0e+00

beta-galactosidase; Provisional


The actual alignment was detected with superfamily member PLN03059:

Pssm-ID: 166698 [Multi-domain]  Cd Length: 840  Bit Score: 727.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152   65 SRKHMWPSIIDKARIGGLNTIQTYVFWNVHEPEQGKYDFKGRFDLVKFIKLIHEKGLYVTLRLGPFIQAEWNHGGLPYWL 144
Cdd:PLN03059   56 STPEMWPDLIQKAKDGGLDVIQTYVFWNGHEPSPGNYYFEDRYDLVKFIKVVQAAGLYVHLRIGPYICAEWNFGGFPVWL 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  145 REVPDVYFRTNNEPFKEHTERYVRKILGMMKEEKLFASQGGPIILGQIENEYNAVQLAYKENGEKYIKWAANLVESMNLG 224
Cdd:PLN03059  136 KYVPGIEFRTDNGPFKAAMQKFTEKIVDMMKSEKLFEPQGGPIILSQIENEYGPVEWEIGAPGKAYTKWAADMAVKLGTG 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  225 IPWVMCKQNDAPGNLINACNGRHCGDTFpgPNRHDKPSLWTENWTTQFRVFGDPPTQRTVEDIAFSVARYFSKNGSHVNY 304
Cdd:PLN03059  216 VPWVMCKQEDAPDPVIDTCNGFYCENFK--PNKDYKPKMWTEAWTGWYTEFGGAVPNRPAEDLAFSVARFIQNGGSFINY 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  305 YMYHGGTNFGRTSAH-FVTTRYYDDAPLDEFGLEKAPKYGHLKHVHRALRLCKKALFWGQLRAQTLGPDTEVRYYEqpGT 383
Cdd:PLN03059  294 YMYHGGTNFGRTAGGpFIATSYDYDAPLDEYGLPREPKWGHLRDLHKAIKLCEPALVSVDPTVTSLGSNQEAHVFK--SK 371

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  384 KVCAAFLSNNNTRDTNTIKFKGQDYVLPSRSISILPDCKTVVYNTAQIVAQHSWrdfVKSEKTSKGLKFEMFSENIPSLL 463
Cdd:PLN03059  372 SACAAFLANYDTKYSVKVTFGNGQYDLPPWSVSILPDCKTAVFNTARLGAQSSQ---MKMNPVGSTFSWQSYNEETASAY 448

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  464 DGDSLIPGELYY---LTKDKTDY----ACVKIDEDDFPDQKGLKTILRVASLGHALIVYVNGEYAGKAHGRHEMKSFEFA 536
Cdd:PLN03059  449 TDDTTTMDGLWEqinVTRDATDYlwymTEVHIDPDEGFLKTGQYPVLTIFSAGHALHVFINGQLAGTVYGELSNPKLTFS 528

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  537 KPVNFKTGDNRISILGVLTGLPDSGSYMEHRFAGPRA-ISIIGLKSGTRDLTeNNEWGHLAGLEGEKKEVYTEEGSKKVK 615
Cdd:PLN03059  529 QNVKLTVGINKISLLSVAVGLPNVGLHFETWNAGVLGpVTLKGLNEGTRDLS-GWKWSYKIGLKGEALSLHTITGSSSVE 607

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  616 WEKD---GKRKPLTWYKTYFETPEGVNAVAIRMKAMGKGLIWVNGIGVGRYWMSFL--------------------SPLG 672
Cdd:PLN03059  608 WVEGsllAQKQPLTWYKTTFDAPGGNDPLALDMSSMGKGQIWINGQSIGRHWPAYTahgscngcnyagtfddkkcrTNCG 687

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  673 EPTQTEYHIPRSFMKgeKKKNMLVILEEEPGvKLESIDFVLVNRDTICSNVGEDYPvSVKSWKREGpkiVSRSKDMRLKA 752
Cdd:PLN03059  688 EPSQRWYHVPRSWLK--PSGNLLIVFEEWGG-NPAGISLVKRTTDSVCADIFEGQP-ALKNWQIIA---SGKVNSLQPKA 760

                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238481152  753 VMRCPPEKQMVEVQFASFGDPTGTCGNFTMGKCSASKSKEVVEKECLGRNYCSIVVARETFGDKGCPEIVKTLAVQVKC 831
Cdd:PLN03059  761 HLWCPPGQKISKIKFASFGVPQGTCGSFREGSCHAHKSYDAFERNCIGKQSCSVTVAPEVFGGDPCPDSMKKLSVEAVC 839
PRP1_N pfam06424
PRP1 splicing factor, N-terminal; This domain is specific to the N-terminal part of the prp1 ...
 921-1050 2.65e-58

PRP1 splicing factor, N-terminal; This domain is specific to the N-terminal part of the prp1 splicing factor, which is involved in mRNA splicing (and possibly also poly(A)+ RNA nuclear export and cell cycle progression). This domain is specific to the N terminus of the RNA splicing factor encoded by prp1. It is involved in mRNA splicing and possibly also poly(A)and RNA nuclear export and cell cycle progression.


:

Pssm-ID: 461908  Cd Length: 109  Bit Score: 195.44  E-value: 2.65e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152   921 PPSNYVAGLGRGAAGFTTrsdigparangdgnadvnhkfDDFEGHDAGLFANAESDDQDKEADAIWDAIDRRMDSRRKDR 1000
Cdd:pfam06424    1 APPGYVAGLGRGATGFTT---------------------DEFEGYDGGLFAGGPYDKDDEEADRIYEAIDERMDERRKKR 59

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 238481152  1001 REAKLKQEIENYRASNPKVSGQFVDLTRKLHTLSEDEWDSIPEIGNYSHR 1050
Cdd:pfam06424   60 REAREKEELEKYRAERPKIQQQFADLKRGLATVSEEEWANIPEVGDLTRK 109
 
Name Accession Description Interval E-value
PLN03059 PLN03059
beta-galactosidase; Provisional
 65-831 0e+00

beta-galactosidase; Provisional


Pssm-ID: 166698 [Multi-domain]  Cd Length: 840  Bit Score: 727.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152   65 SRKHMWPSIIDKARIGGLNTIQTYVFWNVHEPEQGKYDFKGRFDLVKFIKLIHEKGLYVTLRLGPFIQAEWNHGGLPYWL 144
Cdd:PLN03059   56 STPEMWPDLIQKAKDGGLDVIQTYVFWNGHEPSPGNYYFEDRYDLVKFIKVVQAAGLYVHLRIGPYICAEWNFGGFPVWL 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  145 REVPDVYFRTNNEPFKEHTERYVRKILGMMKEEKLFASQGGPIILGQIENEYNAVQLAYKENGEKYIKWAANLVESMNLG 224
Cdd:PLN03059  136 KYVPGIEFRTDNGPFKAAMQKFTEKIVDMMKSEKLFEPQGGPIILSQIENEYGPVEWEIGAPGKAYTKWAADMAVKLGTG 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  225 IPWVMCKQNDAPGNLINACNGRHCGDTFpgPNRHDKPSLWTENWTTQFRVFGDPPTQRTVEDIAFSVARYFSKNGSHVNY 304
Cdd:PLN03059  216 VPWVMCKQEDAPDPVIDTCNGFYCENFK--PNKDYKPKMWTEAWTGWYTEFGGAVPNRPAEDLAFSVARFIQNGGSFINY 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  305 YMYHGGTNFGRTSAH-FVTTRYYDDAPLDEFGLEKAPKYGHLKHVHRALRLCKKALFWGQLRAQTLGPDTEVRYYEqpGT 383
Cdd:PLN03059  294 YMYHGGTNFGRTAGGpFIATSYDYDAPLDEYGLPREPKWGHLRDLHKAIKLCEPALVSVDPTVTSLGSNQEAHVFK--SK 371

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  384 KVCAAFLSNNNTRDTNTIKFKGQDYVLPSRSISILPDCKTVVYNTAQIVAQHSWrdfVKSEKTSKGLKFEMFSENIPSLL 463
Cdd:PLN03059  372 SACAAFLANYDTKYSVKVTFGNGQYDLPPWSVSILPDCKTAVFNTARLGAQSSQ---MKMNPVGSTFSWQSYNEETASAY 448

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  464 DGDSLIPGELYY---LTKDKTDY----ACVKIDEDDFPDQKGLKTILRVASLGHALIVYVNGEYAGKAHGRHEMKSFEFA 536
Cdd:PLN03059  449 TDDTTTMDGLWEqinVTRDATDYlwymTEVHIDPDEGFLKTGQYPVLTIFSAGHALHVFINGQLAGTVYGELSNPKLTFS 528

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  537 KPVNFKTGDNRISILGVLTGLPDSGSYMEHRFAGPRA-ISIIGLKSGTRDLTeNNEWGHLAGLEGEKKEVYTEEGSKKVK 615
Cdd:PLN03059  529 QNVKLTVGINKISLLSVAVGLPNVGLHFETWNAGVLGpVTLKGLNEGTRDLS-GWKWSYKIGLKGEALSLHTITGSSSVE 607

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  616 WEKD---GKRKPLTWYKTYFETPEGVNAVAIRMKAMGKGLIWVNGIGVGRYWMSFL--------------------SPLG 672
Cdd:PLN03059  608 WVEGsllAQKQPLTWYKTTFDAPGGNDPLALDMSSMGKGQIWINGQSIGRHWPAYTahgscngcnyagtfddkkcrTNCG 687

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  673 EPTQTEYHIPRSFMKgeKKKNMLVILEEEPGvKLESIDFVLVNRDTICSNVGEDYPvSVKSWKREGpkiVSRSKDMRLKA 752
Cdd:PLN03059  688 EPSQRWYHVPRSWLK--PSGNLLIVFEEWGG-NPAGISLVKRTTDSVCADIFEGQP-ALKNWQIIA---SGKVNSLQPKA 760

                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238481152  753 VMRCPPEKQMVEVQFASFGDPTGTCGNFTMGKCSASKSKEVVEKECLGRNYCSIVVARETFGDKGCPEIVKTLAVQVKC 831
Cdd:PLN03059  761 HLWCPPGQKISKIKFASFGVPQGTCGSFREGSCHAHKSYDAFERNCIGKQSCSVTVAPEVFGGDPCPDSMKKLSVEAVC 839
Glyco_hydro_35 pfam01301
Glycosyl hydrolases family 35;
67-350 3.48e-139

Glycosyl hydrolases family 35;


Pssm-ID: 396048 [Multi-domain]  Cd Length: 316  Bit Score: 420.89  E-value: 3.48e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152    67 KHMWPSIIDKARIGGLNTIQTYVFWNVHEPEQGKYDFKGRFDLVKFIKLIHEKGLYVTLRLGPFIQAEWNHGGLPYWLRE 146
Cdd:pfam01301   23 PEMWPDRLQKAKALGLNAIETYVFWNLHEPEPGQYDFSGILDLVKFIKLAQEAGLYVILRPGPYICAEWDFGGLPAWLLT 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152   147 VPDVYFRTNNEPFKEHTERYVRKILGMMKeeKLFASQGGPIILGQIENEYN--AVQLAY-KENGEKYIKWAANLVESMNL 223
Cdd:pfam01301  103 VPGIRLRTSDPPFLEAVERYLTALLPKMK--PLQATNGGPIIMVQVENEYGsyGVDKAYlRALRKAYKEWGADMALLFTT 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152   224 GIPWVMCKQN-DAPGNLINACNGRHCGDTFP------GPNRHDKPSLWTENWTTQFRVFGDPPTQRTVEDIAFSVARYFS 296
Cdd:pfam01301  181 DGPWGMCLQCgDLPGPDIYATNGFGCGANPPsnfkllRPFSPNKPLMWSEFWTGWFDHWGGPHAIRPAEDIAFEVARFLA 260

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 238481152   297 KNGShVNYYMYHGGTNFGRTS-AHFVT---TRYYDDAPLDEFGLEKaPKYGHLKHVHR 350
Cdd:pfam01301  261 KNSS-VNLYMFHGGTNFGFTNgANFYGpqtTSYDYDAPIDEAGDPT-PKYGHLKDLIT 316
PRP1_N pfam06424
PRP1 splicing factor, N-terminal; This domain is specific to the N-terminal part of the prp1 ...
 921-1050 2.65e-58

PRP1 splicing factor, N-terminal; This domain is specific to the N-terminal part of the prp1 splicing factor, which is involved in mRNA splicing (and possibly also poly(A)+ RNA nuclear export and cell cycle progression). This domain is specific to the N terminus of the RNA splicing factor encoded by prp1. It is involved in mRNA splicing and possibly also poly(A)and RNA nuclear export and cell cycle progression.


Pssm-ID: 461908  Cd Length: 109  Bit Score: 195.44  E-value: 2.65e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152   921 PPSNYVAGLGRGAAGFTTrsdigparangdgnadvnhkfDDFEGHDAGLFANAESDDQDKEADAIWDAIDRRMDSRRKDR 1000
Cdd:pfam06424    1 APPGYVAGLGRGATGFTT---------------------DEFEGYDGGLFAGGPYDKDDEEADRIYEAIDERMDERRKKR 59

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 238481152  1001 REAKLKQEIENYRASNPKVSGQFVDLTRKLHTLSEDEWDSIPEIGNYSHR 1050
Cdd:pfam06424   60 REAREKEELEKYRAERPKIQQQFADLKRGLATVSEEEWANIPEVGDLTRK 109
Gal_Rha_Lectin_BGal cd22842
galactose/rhamnose binding lectin domain found in plant beta-galactosidases and similar ...
 751-831 1.62e-33

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: 123.93  E-value: 1.62e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  751 KAVMRCPPEKQMVEVQFASFGDPTGTCGNFTMGKCSASKSKEVVEKECLGRNYCSIVVARETFGDKGCPEIVKTLAVQVK 830
Cdd:cd22842    11 TLTLSCPAGQVISSIDFASYGTPTGTCGSFSKGSCHAPNSLSVVEKACLGKNSCSIPASNSVFFGDPCPGTTKRLAVQAT 90


                  .
gi 238481152  831 C 831
Cdd:cd22842    91 C 91
GanA COG1874
Beta-galactosidase GanA [Carbohydrate transport and metabolism];
67-196 1.54e-19

Beta-galactosidase GanA [Carbohydrate transport and metabolism];


Pssm-ID: 441478 [Multi-domain]  Cd Length: 609  Bit Score: 93.84  E-value: 1.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152   67 KHMWPSIIDKARIGGLNTIQT-YVFWNVHEPEQGKYDFKGrfdLVKFIKLIHEKGLYVTLRLGPFIqaewnhggLPYWL- 144
Cdd:COG1874    23 PEVWAEDIRLMKAAGLNTVRIgYFAWNLHEPEEGVFDFDW---LDRFIDLLHEAGLKVILRTPTAA--------PPAWLl 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238481152  145 REVPDV----------------YFRTNNEPFKEHTERYVRKilgMMKEeklfASQGGPIILGQIENEY 196
Cdd:COG1874    92 KKYPEIlpvdadgrrrgfgsrrHYCPSSPVYREAARRIVRA---LAER----YGDHPAVIMWQVDNEY 152
 
Name Accession Description Interval E-value
PLN03059 PLN03059
beta-galactosidase; Provisional
 65-831 0e+00

beta-galactosidase; Provisional


Pssm-ID: 166698 [Multi-domain]  Cd Length: 840  Bit Score: 727.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152   65 SRKHMWPSIIDKARIGGLNTIQTYVFWNVHEPEQGKYDFKGRFDLVKFIKLIHEKGLYVTLRLGPFIQAEWNHGGLPYWL 144
Cdd:PLN03059   56 STPEMWPDLIQKAKDGGLDVIQTYVFWNGHEPSPGNYYFEDRYDLVKFIKVVQAAGLYVHLRIGPYICAEWNFGGFPVWL 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  145 REVPDVYFRTNNEPFKEHTERYVRKILGMMKEEKLFASQGGPIILGQIENEYNAVQLAYKENGEKYIKWAANLVESMNLG 224
Cdd:PLN03059  136 KYVPGIEFRTDNGPFKAAMQKFTEKIVDMMKSEKLFEPQGGPIILSQIENEYGPVEWEIGAPGKAYTKWAADMAVKLGTG 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  225 IPWVMCKQNDAPGNLINACNGRHCGDTFpgPNRHDKPSLWTENWTTQFRVFGDPPTQRTVEDIAFSVARYFSKNGSHVNY 304
Cdd:PLN03059  216 VPWVMCKQEDAPDPVIDTCNGFYCENFK--PNKDYKPKMWTEAWTGWYTEFGGAVPNRPAEDLAFSVARFIQNGGSFINY 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  305 YMYHGGTNFGRTSAH-FVTTRYYDDAPLDEFGLEKAPKYGHLKHVHRALRLCKKALFWGQLRAQTLGPDTEVRYYEqpGT 383
Cdd:PLN03059  294 YMYHGGTNFGRTAGGpFIATSYDYDAPLDEYGLPREPKWGHLRDLHKAIKLCEPALVSVDPTVTSLGSNQEAHVFK--SK 371

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  384 KVCAAFLSNNNTRDTNTIKFKGQDYVLPSRSISILPDCKTVVYNTAQIVAQHSWrdfVKSEKTSKGLKFEMFSENIPSLL 463
Cdd:PLN03059  372 SACAAFLANYDTKYSVKVTFGNGQYDLPPWSVSILPDCKTAVFNTARLGAQSSQ---MKMNPVGSTFSWQSYNEETASAY 448

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  464 DGDSLIPGELYY---LTKDKTDY----ACVKIDEDDFPDQKGLKTILRVASLGHALIVYVNGEYAGKAHGRHEMKSFEFA 536
Cdd:PLN03059  449 TDDTTTMDGLWEqinVTRDATDYlwymTEVHIDPDEGFLKTGQYPVLTIFSAGHALHVFINGQLAGTVYGELSNPKLTFS 528

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  537 KPVNFKTGDNRISILGVLTGLPDSGSYMEHRFAGPRA-ISIIGLKSGTRDLTeNNEWGHLAGLEGEKKEVYTEEGSKKVK 615
Cdd:PLN03059  529 QNVKLTVGINKISLLSVAVGLPNVGLHFETWNAGVLGpVTLKGLNEGTRDLS-GWKWSYKIGLKGEALSLHTITGSSSVE 607

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  616 WEKD---GKRKPLTWYKTYFETPEGVNAVAIRMKAMGKGLIWVNGIGVGRYWMSFL--------------------SPLG 672
Cdd:PLN03059  608 WVEGsllAQKQPLTWYKTTFDAPGGNDPLALDMSSMGKGQIWINGQSIGRHWPAYTahgscngcnyagtfddkkcrTNCG 687

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  673 EPTQTEYHIPRSFMKgeKKKNMLVILEEEPGvKLESIDFVLVNRDTICSNVGEDYPvSVKSWKREGpkiVSRSKDMRLKA 752
Cdd:PLN03059  688 EPSQRWYHVPRSWLK--PSGNLLIVFEEWGG-NPAGISLVKRTTDSVCADIFEGQP-ALKNWQIIA---SGKVNSLQPKA 760

                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238481152  753 VMRCPPEKQMVEVQFASFGDPTGTCGNFTMGKCSASKSKEVVEKECLGRNYCSIVVARETFGDKGCPEIVKTLAVQVKC 831
Cdd:PLN03059  761 HLWCPPGQKISKIKFASFGVPQGTCGSFREGSCHAHKSYDAFERNCIGKQSCSVTVAPEVFGGDPCPDSMKKLSVEAVC 839
Glyco_hydro_35 pfam01301
Glycosyl hydrolases family 35;
67-350 3.48e-139

Glycosyl hydrolases family 35;


Pssm-ID: 396048 [Multi-domain]  Cd Length: 316  Bit Score: 420.89  E-value: 3.48e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152    67 KHMWPSIIDKARIGGLNTIQTYVFWNVHEPEQGKYDFKGRFDLVKFIKLIHEKGLYVTLRLGPFIQAEWNHGGLPYWLRE 146
Cdd:pfam01301   23 PEMWPDRLQKAKALGLNAIETYVFWNLHEPEPGQYDFSGILDLVKFIKLAQEAGLYVILRPGPYICAEWDFGGLPAWLLT 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152   147 VPDVYFRTNNEPFKEHTERYVRKILGMMKeeKLFASQGGPIILGQIENEYN--AVQLAY-KENGEKYIKWAANLVESMNL 223
Cdd:pfam01301  103 VPGIRLRTSDPPFLEAVERYLTALLPKMK--PLQATNGGPIIMVQVENEYGsyGVDKAYlRALRKAYKEWGADMALLFTT 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152   224 GIPWVMCKQN-DAPGNLINACNGRHCGDTFP------GPNRHDKPSLWTENWTTQFRVFGDPPTQRTVEDIAFSVARYFS 296
Cdd:pfam01301  181 DGPWGMCLQCgDLPGPDIYATNGFGCGANPPsnfkllRPFSPNKPLMWSEFWTGWFDHWGGPHAIRPAEDIAFEVARFLA 260

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 238481152   297 KNGShVNYYMYHGGTNFGRTS-AHFVT---TRYYDDAPLDEFGLEKaPKYGHLKHVHR 350
Cdd:pfam01301  261 KNSS-VNLYMFHGGTNFGFTNgANFYGpqtTSYDYDAPIDEAGDPT-PKYGHLKDLIT 316
PRP1_N pfam06424
PRP1 splicing factor, N-terminal; This domain is specific to the N-terminal part of the prp1 ...
 921-1050 2.65e-58

PRP1 splicing factor, N-terminal; This domain is specific to the N-terminal part of the prp1 splicing factor, which is involved in mRNA splicing (and possibly also poly(A)+ RNA nuclear export and cell cycle progression). This domain is specific to the N terminus of the RNA splicing factor encoded by prp1. It is involved in mRNA splicing and possibly also poly(A)and RNA nuclear export and cell cycle progression.


Pssm-ID: 461908  Cd Length: 109  Bit Score: 195.44  E-value: 2.65e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152   921 PPSNYVAGLGRGAAGFTTrsdigparangdgnadvnhkfDDFEGHDAGLFANAESDDQDKEADAIWDAIDRRMDSRRKDR 1000
Cdd:pfam06424    1 APPGYVAGLGRGATGFTT---------------------DEFEGYDGGLFAGGPYDKDDEEADRIYEAIDERMDERRKKR 59

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 238481152  1001 REAKLKQEIENYRASNPKVSGQFVDLTRKLHTLSEDEWDSIPEIGNYSHR 1050
Cdd:pfam06424   60 REAREKEELEKYRAERPKIQQQFADLKRGLATVSEEEWANIPEVGDLTRK 109
Gal_Rha_Lectin_BGal cd22842
galactose/rhamnose binding lectin domain found in plant beta-galactosidases and similar ...
 751-831 1.62e-33

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: 123.93  E-value: 1.62e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  751 KAVMRCPPEKQMVEVQFASFGDPTGTCGNFTMGKCSASKSKEVVEKECLGRNYCSIVVARETFGDKGCPEIVKTLAVQVK 830
Cdd:cd22842    11 TLTLSCPAGQVISSIDFASYGTPTGTCGSFSKGSCHAPNSLSVVEKACLGKNSCSIPASNSVFFGDPCPGTTKRLAVQAT 90


                  .
gi 238481152  831 C 831
Cdd:cd22842    91 C 91
Gal_Lectin pfam02140
Galactose binding lectin domain;
754-831 1.75e-25

Galactose binding lectin domain;


Pssm-ID: 460460 [Multi-domain]  Cd Length: 79  Bit Score: 100.83  E-value: 1.75e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152   754 MRCPPeKQMVEVQFASFGDPTG-TCGNFTMGK-CSASKSKEVVEKECLGRNYCSIVVARETFGDKGCPEIVKTLAVQVKC 831
Cdd:pfam02140    1 LSCPP-GKVISILFASYGRPDGtTCPSFIQGTnCHSPNSLAIVSKACQGKNSCSVPASNSVFGGDPCPGTYKYLEVEYKC 79
GHD pfam17834
Beta-sandwich domain in beta galactosidase; This entry corresponds to a beta sandwich like ...
 359-431 7.18e-24

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: 95.83  E-value: 7.18e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 238481152   359 LFWGQLRAQTLGPDTEVRYYEQPGTKvCAAFLSNNNTRDTNTIKFKGQDYVLPSRSISILPDCKTVVYNTAQI 431
Cdd:pfam17834    1 LLSGQYTTTNLGKLQTATVFEKDKGS-CVAFLVNIDDKKDANVTFRGSDYFLPAWSISILPDCKTVVFNTAKV 72
GanA COG1874
Beta-galactosidase GanA [Carbohydrate transport and metabolism];
67-196 1.54e-19

Beta-galactosidase GanA [Carbohydrate transport and metabolism];


Pssm-ID: 441478 [Multi-domain]  Cd Length: 609  Bit Score: 93.84  E-value: 1.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152   67 KHMWPSIIDKARIGGLNTIQT-YVFWNVHEPEQGKYDFKGrfdLVKFIKLIHEKGLYVTLRLGPFIqaewnhggLPYWL- 144
Cdd:COG1874    23 PEVWAEDIRLMKAAGLNTVRIgYFAWNLHEPEEGVFDFDW---LDRFIDLLHEAGLKVILRTPTAA--------PPAWLl 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238481152  145 REVPDV----------------YFRTNNEPFKEHTERYVRKilgMMKEeklfASQGGPIILGQIENEY 196
Cdd:COG1874    92 KKYPEIlpvdadgrrrgfgsrrHYCPSSPVYREAARRIVRA---LAER----YGDHPAVIMWQVDNEY 152
Gal_Rha_Lectin cd22823
Galactose/rhamnose-binding lectin domain; Galactose/rhamnose-binding lectin domain is formed ...
 751-831 2.01e-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: 58.28  E-value: 2.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  751 KAVMRCPPEkQMVEVQFASFG-DPTGTC----GNFTMGKCSASKSKEVVEKECLGRNYCSIVVARETFGDKgCPEIVKTL 825
Cdd:cd22823     8 TLTLSCPSG-QVIKILSAFYGrTDGTTCccgpNNTSDTNCCSPDVLDIVKELCDGKQSCSVPASNSVFGDP-CPGTSKYL 85


                  ....*.
gi 238481152  826 AVQVKC 831
Cdd:cd22823    86 EVTYTC 91
Glyco_hydro_42 pfam02449
Beta-galactosidase; This group of beta-galactosidase enzymes belong to the glycosyl hydrolase ...
 70-196 5.50e-10

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: 62.67  E-value: 5.50e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152    70 WPSIIDKARIGGLNTIQTYVF-WNVHEPEQGKYDFKGrfdLVKFIKLIHEKGLYVTLRLGPfiqaewnhGGLPYWL-REV 147
Cdd:pfam02449   12 WEEDIRLMKEAGVNVVRIGIFaWAKLEPEEGKYDFEW---LDEVIDLLAKAGIKVILATPT--------AAPPAWLvKKH 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 238481152   148 PDV----------------YFRTNNEPFKEHTERYVRKIlgmmkeEKLFASQGGpIILGQIENEY 196
Cdd:pfam02449   81 PEIlpvdadgrrrgfgsrhHYCPSSPVYREYAARIVEAL------AERYGDHPA-LIGWHIDNEY 138
Gal_Rha_Lectin_LPHNs cd22826
galactose/rhamnose binding lectin domain found in latrophilins; Latrophilins, also called ...
 751-831 2.88e-07

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


Pssm-ID: 438683 [Multi-domain]  Cd Length: 92  Bit Score: 49.24  E-value: 2.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  751 KAVMRCPPEKqMVEVQFASFG-DPTGTC---GNFTMGKCSASKSKEVVEKECLGRNYCSIVVARETFGDKgCPEIVKTLA 826
Cdd:cd22826    10 KIRLRCPGSD-VIMIESANYGrTDSSTCpsdPNMTDTNCYLPDALAIVSQRCNNRTRCNVRADSSFFPDP-CPGTFKYLE 87


                  ....*
gi 238481152  827 VQVKC 831
Cdd:cd22826    88 VIYEC 92
Gal_Rha_Lectin_SUL-I-like cd22827
galactose/rhamnose binding lectin domain found in Toxopneustes pileolus rhamnose-binding ...
 751-831 7.64e-07

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: 47.97  E-value: 7.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  751 KAVMRCPPEKQMvEVQFASFG--DPTgTCGNFTM--GKCSASKSKEVVEKECLGRNYCSIVVARETFGDKgCPEIVKTLA 826
Cdd:cd22827     8 TLTISCPAGKVI-DIVSANYGrtDSS-TCPSGGIknTNCRASNSLSIVRNRCNGKRSCSVKASNSVFGDP-CVGTYKYLE 84


                  ....*
gi 238481152  827 VQVKC 831
Cdd:cd22827    85 VRYRC 89
Gal_Rha_Lectin_EVA1_EVA1C_rpt1 cd22828
first galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
 754-831 8.58e-06

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: 45.73  E-value: 8.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  754 MRCPPEKQmVEVQFASFG----------DPTGTCGNFTMGK--CSASKSKEVVEKECLGRNYCSIVVARETFGDKGCPEI 821
Cdd:cd22828    15 LRCPPNTT-ISIQSAFYGrsvpsaqlcpSQSGPASSTSLEDtnCLAPTALQKVVEECQKKRSCRLLVSSRTFGLDPCPGT 93

                          90
                  ....*....|
gi 238481152  822 VKTLAVQVKC 831
Cdd:cd22828    94 SKYLEVAYKC 103
Gal_Rha_Lectin_LAT2 cd22840
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ...
 756-831 1.46e-04

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: 41.63  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  756 CPPEkQMVEVQFASFG-DPTG-TCGNFTMGK---CSASKSKEVVEKECLGRNYCSIVVARETFGDKGCPEIVKT-LAVQV 829
Cdd:cd22840    16 CPSG-QRIKVDYASYGaIGTRsTCGDSVSPAgetCSAPNSLQTMRQRCQGRQSCEIRVLNSLFPNDPCPGTSKKyLEYRY 94


                  ..
gi 238481152  830 KC 831
Cdd:cd22840    95 RC 96
Gal_Rha_Lectin_dCirl cd22830
galactose/rhamnose binding lectin domain found in Drosophila melanogaster Latrophilin Cirl and ...
 785-831 4.92e-04

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: 40.30  E-value: 4.92e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 238481152  785 CSASKSKEVVEKECLGRNYCSIVVARETFGDkGCPEIVKTLAVQVKC 831
Cdd:cd22830    47 CMSPRSLRVVQERCDGKRSCSIPASSSVFGD-PCPGTPKYLEVHYQC 92
Gal_Rha_Lectin_LAT1 cd22839
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ...
 778-831 6.29e-04

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: 40.10  E-value: 6.29e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 238481152  778 GNFTMGKCSAS------------KSKEVVEKECLGRNYCSIVVARETFGDKGCPEIVKTLAVQVKC 831
Cdd:cd22839    30 GRFSLGVCNPSnnidlsttcqndKTLPILQKSCDGKSECSFVVSNKFFFEDPCPGTPKYLEATYSC 95
Gal_Rha_Lectin_EVA1_EVA1C_rpt2 cd22829
second galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
 748-823 7.42e-04

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: 39.94  E-value: 7.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238481152  748 MRLkavmRCPPEKQMVeVQFASFG-DPTGT--CGNFTMG----KCSASKSKEVVEKECLGRNYCSIVVARETFGDkGCPE 820
Cdd:cd22829    12 LRL----SCKPSSRLA-IYSASYGrTLEGSveCPSTPKGdpdeECLSDVALETVMKRCHGKRRCSLTADSETFGD-PCPP 85


                  ...
gi 238481152  821 IVK 823
Cdd:cd22829    86 GVR 88
Gal_Rha_Lectin_SML_rpt2 cd22835
second galactose/rhamnose binding lectin domain found in Scomberomorus niphonius ...
 769-831 9.00e-03

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: 36.51  E-value: 9.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 238481152  769 SFGDPTGTCGNFtmgKCSASKSKevVEKECLGRNYCSIVVARETFGDKgCPEIVKTLAVQVKC 831
Cdd:cd22835    36 SFGRPPSQIQNV---ECSNPTDK--VAERCNGKNSCSIKASNSVFGDP-CVGTYKYLEVAYTC 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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