GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and beta-strands that is found in cell-adhesion GPCRs and precedes the GPS motif where the autoproteolysis occurs, family, pfam01825. The full GAIN domain, comprises the GPS and the GAIN, in cell-adhesion GPCRs, and is the functional unit for autoproteolysis. The GPS motif at the end of the GAIN domain is an ancient domain that exists in primitive ancestor organizms, and the full GAIN + GPS is conserved in all cell-adhesion GPCRs and all PKD1-related proteins.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622917   451 SLISIANDMSEVTSSKTLYGGDMLVTTKIIQTVSEKMmhdketfpdQRQREAMIMELLHCVVKTGSNLLDESQLSSWLDL 530
Cdd:pfam16489    1 GAKELARELRNATRHGPLYGGDVLTAVELLSQLFDLL---------ATQDATLSNAFLENFVQTVSNLLDPENRESWEDL 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622917   531 NPEDQMRVATSLLTGLEYNAFLLADTIIRERSVVQKVKNILLSVRVLETKTIQSSVV--FPDSDQWPLSSDRIELPRAAL 608
Cdd:pfam16489   72 QQTERGTAATKLLRTLEEYALLLAQNMKYLTPFTIVTPNIVLSVDRLDTHNFKGARFprFPMKGERPKDEDSVKLPPKAF 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622917   609 IDNSEGGLVRIVFAAFDRLESILKPsydhfdlksSRSYAILSNDSDVNAgeiqqrlRILNSKVISASLGK 678
Cdd:pfam16489  152 KPPDSNGTVVVVFILYRNLGSLLPP---------SSRYDPDRRSLRLPR-------RVVNSPVVSASVHS 205

seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary model represents the seven-transmembrane (7TM) receptors, often referred to as G protein-coupled receptors (GPCRs), which transmit physiological signals from the outside of the cell to the inside via G proteins. GPCRs constitute the largest known superfamily of transmembrane receptors across the three kingdoms of life that respond to a wide variety of extracellular stimuli including peptides, lipids, neurotransmitters, amino acids, hormones, and sensory stimuli such as light, smell and taste. All GPCRs share a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes. However, some 7TM receptors, such as the type 1 microbial rhodopsins, do not activate G proteins. Based on sequence similarity, GPCRs can be divided into six major classes: class A (the rhodopsin-like family), class B (the Methuselah-like, adhesion and secretin-like receptor family), class C (the metabotropic glutamate receptor family), class D (the fungal mating pheromone receptors), class E (the cAMP receptor family), and class F (the frizzled/smoothened receptor family). Nearly 800 human GPCR genes have been identified and are involved essentially in all major physiological processes. Approximately 40% of clinically marketed drugs mediate their effects through modulation of GPCR function for the treatment of a variety of human diseases including bacterial infections.

                          10        20        30
                  ....*....|....*....|....*....|...
gi 442622917  759 DGNMRIFIYISIGICVVFIVIALLTLKLFNGVF 791
Cdd:cd15441     1 VLLLKIVTYIGIGISLVLLVIAFLVLSCLRGLQ 33

GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and beta-strands that is found in cell-adhesion GPCRs and precedes the GPS motif where the autoproteolysis occurs, family, pfam01825. The full GAIN domain, comprises the GPS and the GAIN, in cell-adhesion GPCRs, and is the functional unit for autoproteolysis. The GPS motif at the end of the GAIN domain is an ancient domain that exists in primitive ancestor organizms, and the full GAIN + GPS is conserved in all cell-adhesion GPCRs and all PKD1-related proteins.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622917   451 SLISIANDMSEVTSSKTLYGGDMLVTTKIIQTVSEKMmhdketfpdQRQREAMIMELLHCVVKTGSNLLDESQLSSWLDL 530
Cdd:pfam16489    1 GAKELARELRNATRHGPLYGGDVLTAVELLSQLFDLL---------ATQDATLSNAFLENFVQTVSNLLDPENRESWEDL 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622917   531 NPEDQMRVATSLLTGLEYNAFLLADTIIRERSVVQKVKNILLSVRVLETKTIQSSVV--FPDSDQWPLSSDRIELPRAAL 608
Cdd:pfam16489   72 QQTERGTAATKLLRTLEEYALLLAQNMKYLTPFTIVTPNIVLSVDRLDTHNFKGARFprFPMKGERPKDEDSVKLPPKAF 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622917   609 IDNSEGGLVRIVFAAFDRLESILKPsydhfdlksSRSYAILSNDSDVNAgeiqqrlRILNSKVISASLGK 678
Cdd:pfam16489  152 KPPDSNGTVVVVFILYRNLGSLLPP---------SSRYDPDRRSLRLPR-------RVVNSPVVSASVHS 205

G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin REJ and polycystin.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 442622917    701 TNPTCVFWNYIDHAWSANGCSLESTNRTHSVCSCNHLTNFAILMDVVD 748
Cdd:smart00303    1 FNPICVFWDESSGEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPP 48

cadherin EGF LAG seven-pass G-type receptors, group IV adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors; The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. Celsr3 is expressed in both the developing and adult mouse brain. It has been functionally implicated in proper neuron migration and axon guidance in the CNS.

                          10        20        30
                  ....*....|....*....|....*....|...
gi 442622917  759 DGNMRIFIYISIGICVVFIVIALLTLKLFNGVF 791
Cdd:cd15441     1 VLLLKIVTYIGIGISLVLLVIAFLVLSCLRGLQ 33

GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and beta-strands that is found in cell-adhesion GPCRs and precedes the GPS motif where the autoproteolysis occurs, family, pfam01825. The full GAIN domain, comprises the GPS and the GAIN, in cell-adhesion GPCRs, and is the functional unit for autoproteolysis. The GPS motif at the end of the GAIN domain is an ancient domain that exists in primitive ancestor organizms, and the full GAIN + GPS is conserved in all cell-adhesion GPCRs and all PKD1-related proteins.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622917   451 SLISIANDMSEVTSSKTLYGGDMLVTTKIIQTVSEKMmhdketfpdQRQREAMIMELLHCVVKTGSNLLDESQLSSWLDL 530
Cdd:pfam16489    1 GAKELARELRNATRHGPLYGGDVLTAVELLSQLFDLL---------ATQDATLSNAFLENFVQTVSNLLDPENRESWEDL 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622917   531 NPEDQMRVATSLLTGLEYNAFLLADTIIRERSVVQKVKNILLSVRVLETKTIQSSVV--FPDSDQWPLSSDRIELPRAAL 608
Cdd:pfam16489   72 QQTERGTAATKLLRTLEEYALLLAQNMKYLTPFTIVTPNIVLSVDRLDTHNFKGARFprFPMKGERPKDEDSVKLPPKAF 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622917   609 IDNSEGGLVRIVFAAFDRLESILKPsydhfdlksSRSYAILSNDSDVNAgeiqqrlRILNSKVISASLGK 678
Cdd:pfam16489  152 KPPDSNGTVVVVFILYRNLGSLLPP---------SSRYDPDRRSLRLPR-------RVVNSPVVSASVHS 205

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622917   23 AYACEGKKLTIECDPGDVINLIRANYGRFSITICNDHGNVEWSVNCMFPKSLSVLNSRCAHKQSCGVLAATSMFGDPCPG 102
Cdd:cd22823     1 ATACEGETLTLSCPSGQVIKILSAFYGRTDGTTCCCGPNNTSDTNCCSPDVLDIVKELCDGKQSCSVPASNSVFGDPCPG 80

                          90
                  ....*....|.
gi 442622917  103 THKYLEAHYQC 113
Cdd:cd22823    81 TSKYLEVTYTC 91

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622917   26 CEGKKLTIECDPGDVINLIRANYGRFSITICNDHGNVEWSVNCMFPKSLSVLNSRCAHKQSCGVLAATSMF-GDPCPGTH 104
Cdd:cd22839     7 CEGDVANLSCPEGKYISIRLANYGRFSLGVCNPSNNIDLSTTCQNDKTLPILQKSCDGKSECSFVVSNKFFfEDPCPGTP 86

                  ....*....
gi 442622917  105 KYLEAHYQC 113
Cdd:cd22839    87 KYLEATYSC 95

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622917   22 TAYACEGKKLTIECDPGDVINLIRANYGRFSIT--ICNDHGNVEW-----SVNCMFPKSLSVLNSRCAHKQSCGVLAATS 94
Cdd:cd22828     4 QRHACDGEELTLRCPPNTTISIQSAFYGRSVPSaqLCPSQSGPASstsleDTNCLAPTALQKVVEECQKKRSCRLLVSSR 83

                          90       100
                  ....*....|....*....|
gi 442622917   95 MFG-DPCPGTHKYLEAHYQC 113
Cdd:cd22828    84 TFGlDPCPGTSKYLEVAYKC 103

second galactose/rhamnose binding lectin domain found in Oncorhynchus keta CSL1 and similar proteins; The family includes a group of L-rhamnose-binding lectins, such as Oncorhynchus keta CSL1. CSL1 has hemagglutinating activity towards rabbit erythrocytes, but not human type B erythrocytes. Its hemagglutinating activity is inhibited by smooth-type lipopolysaccharide (LPS) from Klebsiella pneumoniae, Escherichia coli K-235, Shigella flexneri 1A, Aeromonas salmonicida and Salmonella minnesota and rough-type LPS from S. flexneri, but not by rough-type LPS from E. coli K12 and E. coli EH100. CSL1 agglutinates E. coli K12 and Bacillus subtilis. CSL1 contains two tandem galactose-binding lectin domains. This model corresponds to the second one.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622917   22 TAYACEGKKLTIECDPgDVINLIRANYGRFSITICNdHGNVE---WSVNCMFPKSLSVLNSRCAHKQSCGVLAaTSMFGD 98
Cdd:cd22834     4 TSITCEGSPVSLDCGP-DVIKIYDANYGRRDSTTCS-HGRPEsqlTNTNCYLPETTKVMSERCNGKSLCDLLA-SNVVTD 80

                          90
                  ....*....|....*
gi 442622917   99 PCPGTHKYLEAHYQC 113
Cdd:cd22834    81 PCYGTYKYLEVSYSC 95

galactose/rhamnose binding lectin domain found in latrophilin-1 and similar proteins; Latrophilin-1 (LPHN1), also called adhesion G protein-coupled receptor L1 (ADGRL1), or calcium-independent alpha-latrotoxin receptor 1 (CIRL-1), or lectomedin-2, is a brain-specific calcium-independent receptor that mediates the effect 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. This model corresponds to a galactose/rhamnose-binding lectin domain found at the N-terminus of LPHN1.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622917   25 ACEGKKLTIECDPGDVINLIRANYGRFSITICNDHGNVEWSVNCMFPKSLSVLNSRCAHKQSCGVLAATSMFGDPCPGTH 104
Cdd:cd22844     6 ACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCPGTY 85

                          90
                  ....*....|
gi 442622917  105 KYLEAHYQCI 114
Cdd:cd22844    86 KYLEVQYDCV 95

galactose/rhamnose binding lectin domain found in latrophilin-3 and similar proteins; Latrophilin-3 (LPHN3), also called adhesion G protein-coupled receptor L3 (ADGRL3), or calcium-independent alpha-latrotoxin receptor 3 (CIRL-3), or lectomedin-3, is a brain-specific calcium-independent receptor that plays a role in cell-cell adhesion and neuron guidance via its interactions with FLRT2 and FLRT3 that are expressed at the surface of adjacent cells. It is involved in the development of glutamatergic synapses in the cortex. This model corresponds to a galactose/rhamnose-binding lectin domain found at the N-terminus of LPHN3.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622917   25 ACEGKKLTIECDPGDVINLIRANYGRFSITICNDHGNVEWSVNCMFPKSLSVLNSRCAHKQSCGVLAATSMFGDPCPGTH 104
Cdd:cd22846     7 SCESYPIELRCPGTDVIMIESANYGRTDDKICDSDPAQMENIRCYLPDAYKIMSQRCNNRTQCAVVAGPDVFPDPCPGTY 86

                          90
                  ....*....|
gi 442622917  105 KYLEAHYQCI 114
Cdd:cd22846    87 KYLEVQYECV 96

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622917   26 CEGKKLTIECdPGDVINLIRANYGRFSITIC-NDHGNVewSVNCMFPKSLSVLNSRCAHKQSCGVLAATSMFGDPCPGTH 104
Cdd:cd22841     7 CEGDTDVIDC-GNGVINIHSAVYGRTDSTTCsHDQSVS--NTNCHSDDSVNILSACCNGQSQCTVTATNSIFGDPCPGTY 83

                  ....*....
gi 442622917  105 KYLEAHYQC 113
Cdd:cd22841    84 KYLNVTYTC 92

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622917   20 YQTAYACEGKKLTIECDPGDVINLIRANYGRFS--ITICNDHGNVEWSVNCMFPKSLSVLNSRCAHKQSCGVLAATSMFG 97
Cdd:cd22829     1 FKSKVVCEGEKLRLSCKPSSRLAIYSASYGRTLegSVECPSTPKGDPDEECLSDVALETVMKRCHGKRRCSLTADSETFG 80

                          90
                  ....*....|....*....
gi 442622917   98 DPC-PGTHKYLEAHYQCIS 115
Cdd:cd22829    81 DPCpPGVRKYLKVVYTCVP 99

GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for auto-proteolysis, so is thus named, GPS. The GPS motif is a conserved sequence of ~40 amino acids containing canonical cysteine and tryptophan residues, and is the most highly conserved part of the domain. In most, if not all, cell-adhesion GPCRs these undergo autoproteolysis in the GPS between a conserved aliphatic residue (usually a leucine) and a threonine, serine, or cysteine residue. In higher eukaryotes this motif is found embedded in the C-terminal beta-stranded part of a GAIN domain - GPCR-Autoproteolysis INducing (GAIN). The GAIN-GPS domain adopts a fold in which the GPS motif, at the C-terminus, forms five beta-strands that are tightly integrated into the overall GAIN domain. The GPS motif, evolutionarily conserved from tetrahymena to mammals, is the only extracellular domain shared by all human cell-adhesion GPCRs and PKD proteins, and is the locus of multiple human disease mutations. The GAIN-GPS domain is both necessary and sufficient functionally for autoproteolysis, suggesting an autoproteolytic mechanism whereby the overall GAIN domain fine-tunes the chemical environment in the GPS to catalyze peptide bond hydrolysis. In the cell-adhesion GPCRs and PKD proteins, the GPS motif is always located at the end of their long N-terminal extracellular regions, immediately before the first transmembrane helix of the respective protein.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 442622917   703 PTCVFWNYIDH---AWSANGCSLESTNRTHSVCSCNHLTNFAIL 743
Cdd:pfam01825    1 PQCVFWDFTNSttgRWSTEGCTTVSLNDTHTVCSCNHLTSFAVL 44

galactose/rhamnose binding lectin domain found in Hydra vulgaris nematogalectin and similar proteins; Nematogalectin, also called nemgal, is a nematocyst protein with an N-terminal GlyXY domain and a galactose/rhamnose binding lectin domain. There are two nematogalectins, A and B, in Hydra, and they are the products of alternative splicing. They are major components of the nematocyst tubule. Nematogalectin functions as a trimer that could bind to multiple chondroitin glycosaminoglycan molecules and stabilize the chondroitin proteoglycan layer.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622917   20 YQTAYACEGKKLTIECDPGDVINLIRANYGRFSITIC-NDHGNVEWSVNCMFPKSLSV--LNSRCAHKQSCGVLAATSMF 96
Cdd:cd22838     1 PNTAIACEGEKLWLQCPQYELIKIKSAFWGRDDKKTCpHPPPGLPSNKMCETDEENVKkkVNDQCQGEQACEVVASNIFF 80

                          90
                  ....*....|....*....
gi 442622917   97 GDP-CPGTHKYLEAHYQCI 114
Cdd:cd22838    81 DDTiCPDVYKYLKVKYECI 99

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622917   28 GKKLTIECDPGDVINLIR-ANYGR-------FSITICNDhgnvewsvncmfPKSLSVLNSRCAHKQSCGVLAATSM-FGD 98
Cdd:cd22842     9 GSTLTLSCPAGQVISSIDfASYGTptgtcgsFSKGSCHA------------PNSLSVVEKACLGKNSCSIPASNSVfFGD 76

                          90
                  ....*....|....*
gi 442622917   99 PCPGTHKYL--EAHY 111
Cdd:cd22842    77 PCPGTTKRLavQATC 91

galactose binding lectin domain found in polycystic kidney disease protein 1-like 2 (polycystin-1L2) and similar proteins; Polycystin-1L2 is a novel G-protein-coupled receptor that may function as an ion-channel regulator. This model corresponds to a galactose/rhamnose-binding lectin domain found at the N-terminal region of polycystin-1L2. Due to the lack of rhamnose-binding key residues, the galactose/rhamnose-binding domains of Polycystin-1L2 does not form a binding pocket for rhamnose. Therefore, Polycystin-1L2 is unlikely to act as a rhamnose-binding lectin.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622917   25 ACEGKKLTIECDPGDVINLIRANYGRFSITICNdhgnvewSVNCMFPKSL-------SVLNS---RCAHKQSCGVLAATS 94
Cdd:cd22831     5 ACEDYNATLQCGSGQVIEIDDSFYGRNTPHYCR-------SENPSPPTDSqercswvDVRDLvaaQCHGLQVCQIPADPS 77

                          90       100
                  ....*....|....*....|
gi 442622917   95 MFGDPCPGTHKYLEAHYQCI 114
Cdd:cd22831    78 SFGEPCPELGSYLSVEYHCK 97

beta-galactosidase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622917   35 CDPGDVINLIR-ANYG-------RFSITICNDHgnvewsvncmfpKSLSVLNSRCAHKQSCGVLAATSMF-GDPCPGTHK 105
Cdd:PLN03059  764 CPPGQKISKIKfASFGvpqgtcgSFREGSCHAH------------KSYDAFERNCIGKQSCSVTVAPEVFgGDPCPDSMK 831

                  ....*...
gi 442622917  106 YLEAHYQC 113
Cdd:PLN03059  832 KLSVEAVC 839