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Conserved domains on  [gi|2462563787|ref|XP_054176198|]
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adhesion G protein-coupled receptor L1 isoform X13 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OLF super family cl02549
Olfactomedin-like domain;
143-399 1.37e-121

Olfactomedin-like domain;


The actual alignment was detected with superfamily member smart00284:

Pssm-ID: 470611  Cd Length: 255  Bit Score: 368.01  E-value: 1.37e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  143 GTLQKVLEPTSTHESE-HQSGAWCKDPLQA---GDRIYVMPWIPYRTDTLTEYASWEDYVAARHTTTYRLPNRVDGTGFV 218
Cdd:smart00284   1 GGLAGISKPVTLQTSWkGKSGAWMKDPLWNttkKSLYWYMPLNTRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGTGVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  219 VYDGAVFYNKERTRNIVKYDLRTRIKSGETVINTANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEGNNGRLVVSQLNP 298
Cdd:smart00284  81 VYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  299 YTLRFEGTWETGYDKRSASNAFMVCGVLYVLRSVYvdddseAAGNRVDYAFNTNANREEPVSLTFPNPYQFISSVDYNPR 378
Cdd:smart00284 161 ATLTIENTWITTYNKRSASNAFMICGILYVTRSLG------SKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPN 234

                          250       260
                   ....*....|....*....|.
gi 2462563787  379 DNQLYVWNNYFVVRYSLEFGP 399
Cdd:smart00284 235 DRKLYAWNNGHLVHYDIALKP 255
Gal_Rha_Lectin_LPHN1 cd22844
galactose/rhamnose binding lectin domain found in latrophilin-1 and similar proteins; ...
 35-131 3.26e-67

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.


:

Pssm-ID: 438701 [Multi-domain]  Cd Length: 97  Bit Score: 218.38  E-value: 3.26e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  35 MRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDP 114
Cdd:cd22844     1 MRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDP 80

                          90
                  ....*....|....*..
gi 2462563787 115 CPGTYKYLEVQYDCVPY 131
Cdd:cd22844    81 CPGTYKYLEVQYDCVPY 97
GAIN pfam16489
GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and ...
 557-782 3.27e-57

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.


:

Pssm-ID: 465137  Cd Length: 205  Bit Score: 195.18  E-value: 3.27e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787 557 NAANIASELARHTR-GSIYAGDVSSSVKLMEQLLDILDAQLQALrpieresagknynkmhkrertCKDYIKAVVETVDNL 635
Cdd:pfam16489   1 GAKELARELRNATRhGPLYGGDVLTAVELLSQLFDLLATQDATL---------------------SNAFLENFVQTVSNL 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787 636 LRPEALESWKDMNATEQVHTATMLLDVLEEGAFLLADNVREPARFLAAKENVVLEVTVLNTEGQVQELV--FPQEEYPRK 713
Cdd:pfam16489  60 LDPENRESWEDLQQTERGTAATKLLRTLEEYALLLAQNMKYLTPFTIVTPNIVLSVDRLDTHNFKGARFprFPMKGERPK 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462563787 714 --NSIQLSAKTIKQNSRNGVVKVVFILYNNLGLFLSTENATvklagEAGPGGPGGASLVVNSQVIAASINK 782
Cdd:pfam16489 140 deDSVKLPPKAFKPPDSNGTVVVVFILYRNLGSLLPPSSRY-----DPDRRSLRLPRRVVNSPVVSASVHS 205
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
 806-858 2.49e-20

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


:

Pssm-ID: 197639  Cd Length: 49  Bit Score: 84.75  E-value: 2.49e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462563787  806 FNANCSFWNYSErsmlGYWSTQGCRLVESNKTHTTCACSHLTNFAVLMAHREI 858
Cdd:smart00303   1 FNPICVFWDESS----GEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPPI 49
HormR smart00008
Domain present in hormone receptors;
484-547 5.37e-18

Domain present in hormone receptors;


:

Pssm-ID: 214468  Cd Length: 70  Bit Score: 78.71  E-value: 5.37e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462563787  484 PELFCEPREVRRVQWPATQQGMLVERPCPKGTRGI-----ASFQCLPALGlWNPRGPDLSNCTSPWVNQ 547
Cdd:smart00008   1 TDLGCPATWDGIICWPQTPAGQLVEVPCPKYFSGFsyktgASRNCTENGG-WSPPFPNYSNCTSNDYEE 68
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 399-503 1.49e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 1.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  399 PPDPSAGED-DSLPGPATSPPLSTTTTARPTPLTSTASPAATTPLRRAPLTTHPVGAINQLGPDLPPATAPVPS---TRR 474
Cdd:PHA03247  2786 PAVASLSESrESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGgdvRRR 2865

                           90       100
                   ....*....|....*....|....*....
gi 2462563787  475 PPAPNLHVSPELFCEPReVRRVQWPATQQ 503
Cdd:PHA03247  2866 PPSRSPAAKPAAPARPP-VRRLARPAVSR 2893
 
Name Accession Description Interval E-value
OLF smart00284
Olfactomedin-like domains;
143-399 1.37e-121

Olfactomedin-like domains;


Pssm-ID: 128580  Cd Length: 255  Bit Score: 368.01  E-value: 1.37e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  143 GTLQKVLEPTSTHESE-HQSGAWCKDPLQA---GDRIYVMPWIPYRTDTLTEYASWEDYVAARHTTTYRLPNRVDGTGFV 218
Cdd:smart00284   1 GGLAGISKPVTLQTSWkGKSGAWMKDPLWNttkKSLYWYMPLNTRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGTGVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  219 VYDGAVFYNKERTRNIVKYDLRTRIKSGETVINTANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEGNNGRLVVSQLNP 298
Cdd:smart00284  81 VYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  299 YTLRFEGTWETGYDKRSASNAFMVCGVLYVLRSVYvdddseAAGNRVDYAFNTNANREEPVSLTFPNPYQFISSVDYNPR 378
Cdd:smart00284 161 ATLTIENTWITTYNKRSASNAFMICGILYVTRSLG------SKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPN 234

                          250       260
                   ....*....|....*....|.
gi 2462563787  379 DNQLYVWNNYFVVRYSLEFGP 399
Cdd:smart00284 235 DRKLYAWNNGHLVHYDIALKP 255
OLF pfam02191
Olfactomedin-like domain;
145-397 9.21e-120

Olfactomedin-like domain;


Pssm-ID: 460482  Cd Length: 246  Bit Score: 363.01  E-value: 9.21e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787 145 LQKVLEPTSTHESEHQSGAWCKDPLQAGDRIYVMPwIPYRTDTLTEYASWEDYVAARHTTTYRLPNRVDGTGFVVYDGAV 224
Cdd:pfam02191   1 LVSVSKPVTVKLSGGKYGAWMKDPLPPSDKIYVTD-RGTSGNTLREYASLDDFKNGSPSKKYKLPYPWQGTGHVVYNGSL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787 225 FYNKERTRNIVKYDLRTRIKSGETVINTANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEGNNGRLVVSQLNPYTLRFE 304
Cdd:pfam02191  80 YYNKYNSRNIVKYDLTTRTVAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLDPETLEVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787 305 GTWETGYDKRSASNAFMVCGVLYVLRSVYVDDdseaagNRVDYAFNTNANREEPVSLTFPNPYQFISSVDYNPRDNQLYV 384
Cdd:pfam02191 160 QTWNTSYPKRSAGNAFMVCGVLYAVRSVNTRR------EEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLYA 233

                         250
                  ....*....|...
gi 2462563787 385 WNNYFVVRYSLEF 397
Cdd:pfam02191 234 WDDGYQVTYPVTF 246
Gal_Rha_Lectin_LPHN1 cd22844
galactose/rhamnose binding lectin domain found in latrophilin-1 and similar proteins; ...
 35-131 3.26e-67

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.


Pssm-ID: 438701 [Multi-domain]  Cd Length: 97  Bit Score: 218.38  E-value: 3.26e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  35 MRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDP 114
Cdd:cd22844     1 MRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDP 80

                          90
                  ....*....|....*..
gi 2462563787 115 CPGTYKYLEVQYDCVPY 131
Cdd:cd22844    81 CPGTYKYLEVQYDCVPY 97
GAIN pfam16489
GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and ...
 557-782 3.27e-57

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.


Pssm-ID: 465137  Cd Length: 205  Bit Score: 195.18  E-value: 3.27e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787 557 NAANIASELARHTR-GSIYAGDVSSSVKLMEQLLDILDAQLQALrpieresagknynkmhkrertCKDYIKAVVETVDNL 635
Cdd:pfam16489   1 GAKELARELRNATRhGPLYGGDVLTAVELLSQLFDLLATQDATL---------------------SNAFLENFVQTVSNL 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787 636 LRPEALESWKDMNATEQVHTATMLLDVLEEGAFLLADNVREPARFLAAKENVVLEVTVLNTEGQVQELV--FPQEEYPRK 713
Cdd:pfam16489  60 LDPENRESWEDLQQTERGTAATKLLRTLEEYALLLAQNMKYLTPFTIVTPNIVLSVDRLDTHNFKGARFprFPMKGERPK 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462563787 714 --NSIQLSAKTIKQNSRNGVVKVVFILYNNLGLFLSTENATvklagEAGPGGPGGASLVVNSQVIAASINK 782
Cdd:pfam16489 140 deDSVKLPPKAFKPPDSNGTVVVVFILYRNLGSLLPPSSRY-----DPDRRSLRLPRRVVNSPVVSASVHS 205
Gal_Lectin pfam02140
Galactose binding lectin domain;
48-128 5.21e-32

Galactose binding lectin domain;


Pssm-ID: 460460 [Multi-domain]  Cd Length: 79  Bit Score: 118.93  E-value: 5.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  48 LRCPGSDVIMVENANYGRTDDKICdadPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAF-PDPCPGTYKYLEVQY 126
Cdd:pfam02140   1 LSCPPGKVISILFASYGRPDGTTC---PSFIQGTNCHSPNSLAIVSKACQGKNSCSVPASNSVFgGDPCPGTYKYLEVEY 77


                  ..
gi 2462563787 127 DC 128
Cdd:pfam02140  78 KC 79
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
 806-858 2.49e-20

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


Pssm-ID: 197639  Cd Length: 49  Bit Score: 84.75  E-value: 2.49e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462563787  806 FNANCSFWNYSErsmlGYWSTQGCRLVESNKTHTTCACSHLTNFAVLMAHREI 858
Cdd:smart00303   1 FNPICVFWDESS----GEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPPI 49
HormR smart00008
Domain present in hormone receptors;
484-547 5.37e-18

Domain present in hormone receptors;


Pssm-ID: 214468  Cd Length: 70  Bit Score: 78.71  E-value: 5.37e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462563787  484 PELFCEPREVRRVQWPATQQGMLVERPCPKGTRGI-----ASFQCLPALGlWNPRGPDLSNCTSPWVNQ 547
Cdd:smart00008   1 TDLGCPATWDGIICWPQTPAGQLVEVPCPKYFSGFsyktgASRNCTENGG-WSPPFPNYSNCTSNDYEE 68
GPS pfam01825
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
 810-852 3.57e-17

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.


Pssm-ID: 460350  Cd Length: 44  Bit Score: 75.81  E-value: 3.57e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2462563787 810 CSFWNYSERSMlGYWSTQGCRLVESNKTHTTCACSHLTNFAVL 852
Cdd:pfam01825   3 CVFWDFTNSTT-GRWSTEGCTTVSLNDTHTVCSCNHLTSFAVL 44
HRM pfam02793
Hormone receptor domain; This extracellular domain contains four conserved cysteines that ...
 485-543 7.36e-10

Hormone receptor domain; This extracellular domain contains four conserved cysteines that probably for disulphide bridges. The domain is found in a variety of hormone receptors. It may be a ligand binding domain.


Pssm-ID: 397086  Cd Length: 64  Bit Score: 55.45  E-value: 7.36e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462563787 485 ELFCEPREVRRVQWPATQQGMLVERPCPKGT-----RGIASFQCLPAlGLWNPRGP-DLSNCTSP 543
Cdd:pfam02793   1 GLGCPRTWDGILCWPRTPAGETVEVPCPDYFsgfdpRGNASRNCTED-GTWSEHPPsNYSNCTSN 64
PHA03247 PHA03247
large tegument protein UL36; Provisional
 399-503 1.49e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 1.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  399 PPDPSAGED-DSLPGPATSPPLSTTTTARPTPLTSTASPAATTPLRRAPLTTHPVGAINQLGPDLPPATAPVPS---TRR 474
Cdd:PHA03247  2786 PAVASLSESrESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGgdvRRR 2865

                           90       100
                   ....*....|....*....|....*....
gi 2462563787  475 PPAPNLHVSPELFCEPReVRRVQWPATQQ 503
Cdd:PHA03247  2866 PPSRSPAAKPAAPARPP-VRRLARPAVSR 2893
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 397-581 1.29e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 42.60  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787 397 FGPPDPSAGEDDS------LPGPATS-PPLSTTTTARPTP--LTSTASPAATTPLRR-------APLTTHPVGAINQLGP 460
Cdd:pfam05109 439 FAAPNTTTGLPSSthvptnLTAPASTgPTVSTADVTSPTPagTTSGASPVTPSPSPRdngteskAPDMTSPTSAVTTPTP 518

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787 461 DlppATAPVPSTrRPPAPNLhVSPEL-FCEPREVRRVQWP-ATQQGMLVERPCPKGTrgiasfqcLPALGLWNPRgpdlS 538
Cdd:pfam05109 519 N---ATSPTPAV-TTPTPNA-TSPTLgKTSPTSAVTTPTPnATSPTPAVTTPTPNAT--------IPTLGKTSPT----S 581

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462563787 539 NCTSPWVNQVAQKIKSGENAANIASelarHTRGSIYAGDVSSS 581
Cdd:pfam05109 582 AVTTPTPNATSPTVGETSPQANTTN----HTLGGTSSTPVVTS 620
 
Name Accession Description Interval E-value
OLF smart00284
Olfactomedin-like domains;
143-399 1.37e-121

Olfactomedin-like domains;


Pssm-ID: 128580  Cd Length: 255  Bit Score: 368.01  E-value: 1.37e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  143 GTLQKVLEPTSTHESE-HQSGAWCKDPLQA---GDRIYVMPWIPYRTDTLTEYASWEDYVAARHTTTYRLPNRVDGTGFV 218
Cdd:smart00284   1 GGLAGISKPVTLQTSWkGKSGAWMKDPLWNttkKSLYWYMPLNTRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGTGVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  219 VYDGAVFYNKERTRNIVKYDLRTRIKSGETVINTANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEGNNGRLVVSQLNP 298
Cdd:smart00284  81 VYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  299 YTLRFEGTWETGYDKRSASNAFMVCGVLYVLRSVYvdddseAAGNRVDYAFNTNANREEPVSLTFPNPYQFISSVDYNPR 378
Cdd:smart00284 161 ATLTIENTWITTYNKRSASNAFMICGILYVTRSLG------SKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPN 234

                          250       260
                   ....*....|....*....|.
gi 2462563787  379 DNQLYVWNNYFVVRYSLEFGP 399
Cdd:smart00284 235 DRKLYAWNNGHLVHYDIALKP 255
OLF pfam02191
Olfactomedin-like domain;
145-397 9.21e-120

Olfactomedin-like domain;


Pssm-ID: 460482  Cd Length: 246  Bit Score: 363.01  E-value: 9.21e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787 145 LQKVLEPTSTHESEHQSGAWCKDPLQAGDRIYVMPwIPYRTDTLTEYASWEDYVAARHTTTYRLPNRVDGTGFVVYDGAV 224
Cdd:pfam02191   1 LVSVSKPVTVKLSGGKYGAWMKDPLPPSDKIYVTD-RGTSGNTLREYASLDDFKNGSPSKKYKLPYPWQGTGHVVYNGSL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787 225 FYNKERTRNIVKYDLRTRIKSGETVINTANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEGNNGRLVVSQLNPYTLRFE 304
Cdd:pfam02191  80 YYNKYNSRNIVKYDLTTRTVAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLDPETLEVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787 305 GTWETGYDKRSASNAFMVCGVLYVLRSVYVDDdseaagNRVDYAFNTNANREEPVSLTFPNPYQFISSVDYNPRDNQLYV 384
Cdd:pfam02191 160 QTWNTSYPKRSAGNAFMVCGVLYAVRSVNTRR------EEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLYA 233

                         250
                  ....*....|...
gi 2462563787 385 WNNYFVVRYSLEF 397
Cdd:pfam02191 234 WDDGYQVTYPVTF 246
Gal_Rha_Lectin_LPHN1 cd22844
galactose/rhamnose binding lectin domain found in latrophilin-1 and similar proteins; ...
 35-131 3.26e-67

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.


Pssm-ID: 438701 [Multi-domain]  Cd Length: 97  Bit Score: 218.38  E-value: 3.26e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  35 MRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDP 114
Cdd:cd22844     1 MRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDP 80

                          90
                  ....*....|....*..
gi 2462563787 115 CPGTYKYLEVQYDCVPY 131
Cdd:cd22844    81 CPGTYKYLEVQYDCVPY 97
Gal_Rha_Lectin_LPHN2 cd22845
galactose/rhamnose binding lectin domain found in latrophilin-2 and similar proteins; ...
 35-131 1.24e-59

galactose/rhamnose binding lectin domain found in latrophilin-2 and similar proteins; Latrophilin-2 (LPHN2), also called adhesion G protein-coupled receptor L2 (ADGRL2), or calcium-independent alpha-latrotoxin receptor 2 (CIRL-2), or latrophilin homolog 1 (LPHH1), or lectomedin-1, is ubiquitously distributed calcium-independent receptor of low affinity for alpha-latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells. It is probably implicated in the regulation of exocytosis. This model corresponds to a galactose/rhamnose-binding lectin domain found at the N-terminus of LPHN2.


Pssm-ID: 438702 [Multi-domain]  Cd Length: 97  Bit Score: 197.54  E-value: 1.24e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  35 MRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDP 114
Cdd:cd22845     1 VRRELSCEGYPIDLRCPGSDVIMIESANYGRTDDKICDADPFQMENTDCYLPDAYKIMTQRCNNRTQCIVVTGSDVFPDP 80

                          90
                  ....*....|....*..
gi 2462563787 115 CPGTYKYLEVQYDCVPY 131
Cdd:cd22845    81 CPGTYKYLEVQYECVPY 97
Gal_Rha_Lectin_LPHN3 cd22846
galactose/rhamnose binding lectin domain found in latrophilin-3 and similar proteins; ...
 34-131 1.97e-59

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.


Pssm-ID: 438703 [Multi-domain]  Cd Length: 99  Bit Score: 197.25  E-value: 1.97e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  34 LMRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPD 113
Cdd:cd22846     1 VVRRELSCESYPIELRCPGTDVIMIESANYGRTDDKICDSDPAQMENIRCYLPDAYKIMSQRCNNRTQCAVVAGPDVFPD 80

                          90
                  ....*....|....*...
gi 2462563787 114 PCPGTYKYLEVQYDCVPY 131
Cdd:cd22846    81 PCPGTYKYLEVQYECVPY 98
GAIN pfam16489
GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and ...
 557-782 3.27e-57

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.


Pssm-ID: 465137  Cd Length: 205  Bit Score: 195.18  E-value: 3.27e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787 557 NAANIASELARHTR-GSIYAGDVSSSVKLMEQLLDILDAQLQALrpieresagknynkmhkrertCKDYIKAVVETVDNL 635
Cdd:pfam16489   1 GAKELARELRNATRhGPLYGGDVLTAVELLSQLFDLLATQDATL---------------------SNAFLENFVQTVSNL 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787 636 LRPEALESWKDMNATEQVHTATMLLDVLEEGAFLLADNVREPARFLAAKENVVLEVTVLNTEGQVQELV--FPQEEYPRK 713
Cdd:pfam16489  60 LDPENRESWEDLQQTERGTAATKLLRTLEEYALLLAQNMKYLTPFTIVTPNIVLSVDRLDTHNFKGARFprFPMKGERPK 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462563787 714 --NSIQLSAKTIKQNSRNGVVKVVFILYNNLGLFLSTENATvklagEAGPGGPGGASLVVNSQVIAASINK 782
Cdd:pfam16489 140 deDSVKLPPKAFKPPDSNGTVVVVFILYRNLGSLLPPSSRY-----DPDRRSLRLPRRVVNSPVVSASVHS 205
Gal_Rha_Lectin_LPHNs cd22826
galactose/rhamnose binding lectin domain found in latrophilins; Latrophilins, also called ...
 36-128 3.95e-56

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: 187.91  E-value: 3.95e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  36 RRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPfQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPC 115
Cdd:cd22826     1 KREIACEGYKIRLRCPGSDVIMIESANYGRTDSSTCPSDP-NMTDTNCYLPDALAIVSQRCNNRTRCNVRADSSFFPDPC 79

                          90
                  ....*....|...
gi 2462563787 116 PGTYKYLEVQYDC 128
Cdd:cd22826    80 PGTFKYLEVIYEC 92
Gal_Lectin pfam02140
Galactose binding lectin domain;
48-128 5.21e-32

Galactose binding lectin domain;


Pssm-ID: 460460 [Multi-domain]  Cd Length: 79  Bit Score: 118.93  E-value: 5.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  48 LRCPGSDVIMVENANYGRTDDKICdadPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAF-PDPCPGTYKYLEVQY 126
Cdd:pfam02140   1 LSCPPGKVISILFASYGRPDGTTC---PSFIQGTNCHSPNSLAIVSKACQGKNSCSVPASNSVFgGDPCPGTYKYLEVEY 77


                  ..
gi 2462563787 127 DC 128
Cdd:pfam02140  78 KC 79
Gal_Rha_Lectin_CSL1_rpt2 cd22834
second galactose/rhamnose binding lectin domain found in Oncorhynchus keta CSL1 and similar ...
 36-128 6.02e-32

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.


Pssm-ID: 438691 [Multi-domain]  Cd Length: 95  Bit Score: 119.48  E-value: 6.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  36 RRELACEGYPIELRCpGSDVIMVENANYGRTDDKICDAD--PFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAgSDAFPD 113
Cdd:cd22834     3 KTSITCEGSPVSLDC-GPDVIKIYDANYGRRDSTTCSHGrpESQLTNTNCYLPETTKVMSERCNGKSLCDLLA-SNVVTD 80

                          90
                  ....*....|....*
gi 2462563787 114 PCPGTYKYLEVQYDC 128
Cdd:cd22834    81 PCYGTYKYLEVSYSC 95
Gal_Rha_Lectin cd22823
Galactose/rhamnose-binding lectin domain; Galactose/rhamnose-binding lectin domain is formed ...
 40-128 1.90e-31

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: 117.99  E-value: 1.90e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  40 ACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCPGTY 119
Cdd:cd22823     3 ACEGETLTLSCPSGQVIKILSAFYGRTDGTTCCCGPNNTSDTNCCSPDVLDIVKELCDGKQSCSVPASNSVFGDPCPGTS 82


                  ....*....
gi 2462563787 120 KYLEVQYDC 128
Cdd:cd22823    83 KYLEVTYTC 91
Gal_Rha_Lectin_SUL-I-like cd22827
galactose/rhamnose binding lectin domain found in Toxopneustes pileolus rhamnose-binding ...
 38-128 4.53e-29

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: 111.14  E-value: 4.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  38 ELACEGYPIELRCPGSDVIMVENANYGRTDDKICdadP-FQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCP 116
Cdd:cd22827     1 KRVCEGQTLTISCPAGKVIDIVSANYGRTDSSTC---PsGGIKNTNCRASNSLSIVRNRCNGKRSCSVKASNSVFGDPCV 77

                          90
                  ....*....|..
gi 2462563787 117 GTYKYLEVQYDC 128
Cdd:cd22827    78 GTYKYLEVRYRC 89
Gal_Rha_Lectin_dCirl cd22830
galactose/rhamnose binding lectin domain found in Drosophila melanogaster Latrophilin Cirl and ...
 40-128 1.26e-28

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: 110.02  E-value: 1.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  40 ACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCPGTY 119
Cdd:cd22830     4 ACEGSQLTLECEDGTVIRIIRANYGRFSIAICNDHGNTDWSVNCMSPRSLRVVQERCDGKRSCSIPASSSVFGDPCPGTP 83


                  ....*....
gi 2462563787 120 KYLEVQYDC 128
Cdd:cd22830    84 KYLEVHYQC 92
Gal_Rha_Lectin_RBL_rpt2 cd22836
second galactose/rhamnose binding lectin domain found in Silurus asotus rhamnose-binding ...
 36-128 5.11e-28

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: 108.14  E-value: 5.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  36 RRELACEGYPIELRCpGSDVIMVENANYGRTDDKICDADP--FQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPD 113
Cdd:cd22836     2 RTSVTCEGGYAVLKC-GSGVIQIISANYGRTDSTTCSAGRpaSQVQNTNCYASNSLAIVSQSCNGKKSCTVSASNSVFSD 80

                          90
                  ....*....|....*
gi 2462563787 114 PCPGTYKYLEVQYDC 128
Cdd:cd22836    81 PCVGTYKYLYVTYSC 95
Gal_Rha_Lectin_SML_rpt2 cd22835
second galactose/rhamnose binding lectin domain found in Scomberomorus niphonius ...
 37-128 3.20e-26

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: 103.15  E-value: 3.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  37 RELACEGYPIELRCPGSDVIMVENANYGRTDDKICDA--DPFQMENVQCYLPdaFKIMSQRCNNRTQCVVVAGSDAFPDP 114
Cdd:cd22835     1 HLVACEGSLAHLKCDEGQVISVYGADYGRRDKTTCSFgrPPSQIQNVECSNP--TDKVAERCNGKNSCSIKASNSVFGDP 78

                          90
                  ....*....|....
gi 2462563787 115 CPGTYKYLEVQYDC 128
Cdd:cd22835    79 CVGTYKYLEVAYTC 92
Gal_Rha_Lectin_CSL3_rpt1_rpt2-like cd22832
first and second galactose/rhamnose binding lectin domain found in Oncorhynchus keta ...
 37-128 1.43e-23

first and second galactose/rhamnose binding lectin domain found in Oncorhynchus keta L-rhamnose-binding lectin CSL3 and similar proteins; The family includes a group of L-rhamnose-binding lectins, such as Oncorhynchus keta CSL1-3. CSL1 has hemagglutinating activity towards rabbit erythrocytes, but not human type B erythrocytes. CSL2 has hemagglutinating activity towards rabbit erythrocytes and human type B erythrocytes. CSL3 has hemagglutinating activity towards rabbit erythrocytes, human type A erythrocytes, human type B erythrocytes, human type O erythrocytes, and sheep erythrocytes. Their hemagglutinating activities are inhibited by smooth-type lipopolysaccharide (LPS) from different bacterial species. Members in this family contain two tandem galactose-binding lectin domains. This model corresponds to the first and second galactose/rhamnose-binding lectin domains found in Oncorhynchus keta CSL3, as well as the second galactose/rhamnose-binding lectin domain found in Oncorhynchus keta CSL2.


Pssm-ID: 438689 [Multi-domain]  Cd Length: 94  Bit Score: 95.64  E-value: 1.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  37 RELACEGYPIELRCpGSDVIMVENANYGRTDDKICDAD-PF-QMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDP 114
Cdd:cd22832     2 SSITCEGSDAQLDC-DGGKIRIQRANYGRRDHDVCSIGrPAnQLTNTNCLSQSTTSKMAERCDGKSQCIVPASNSVFGDP 80

                          90
                  ....*....|....
gi 2462563787 115 CPGTYKYLEVQYDC 128
Cdd:cd22832    81 CVGTYKYLDVAYTC 94
Gal_Rha_Lectin_EVA1_EVA1C_rpt2 cd22829
second galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
 36-130 1.61e-22

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: 92.71  E-value: 1.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  36 RRELACEGYPIELRCPGSDVIMVENANYGRT--DDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPD 113
Cdd:cd22829     2 KSKVVCEGEKLRLSCKPSSRLAIYSASYGRTleGSVECPSTPKGDPDEECLSDVALETVMKRCHGKRRCSLTADSETFGD 81

                          90
                  ....*....|....*...
gi 2462563787 114 PC-PGTYKYLEVQYDCVP 130
Cdd:cd22829    82 PCpPGVRKYLKVVYTCVP 99
Gal_Rha_Lectin_CSL1-2_RBL_SML_rpt1 cd22833
first galactose/rhamnose binding lectin domain found in Oncorhynchus keta CSL1-2, Silurus ...
 41-130 2.77e-22

first galactose/rhamnose binding lectin domain found in Oncorhynchus keta CSL1-2, Silurus asotus RBL, Scomberomorus niphonius SML and similar proteins; The family includes a group of L-rhamnose-binding lectins, such as Oncorhynchus keta CSL1 and CSL2. CSL1 has hemagglutinating activity towards rabbit erythrocytes, but not human type B erythrocytes. CSL2 has hemagglutinating activity towards rabbit erythrocytes and human type B erythrocytes. Their hemagglutinating activities are inhibited by smooth-type lipopolysaccharide (LPS) from different bacterial species. The family also includes Silurus asotus rhamnose-binding lectin (RBL) and Scomberomorus niphonius L-rhamnose-binding lectin (SML). 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. 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. CSL1-2 and SML contain two tandem galactose/rhamnose-binding lectin domains. RBL contains three galactose/rhamnose-binding lectin domains. This model corresponds to the first one.


Pssm-ID: 438690 [Multi-domain]  Cd Length: 97  Bit Score: 91.94  E-value: 2.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  41 CEGYPIE-LRCpGSDVIMVENANYGRTDDKICDA--DPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCPG 117
Cdd:cd22833     6 CDGNNVHrLSC-DTGVINVQSALYGRTDSETCSEgrPPEQLTNTQCSQSGTLDLLKNRCDGKKVCELNTNDFRTSDPCPG 84

                          90
                  ....*....|...
gi 2462563787 118 TYKYLEVQYDCVP 130
Cdd:cd22833    85 TYKYLQTNYTCLP 97
Gal_Rha_Lectin_REJ3 cd22841
galactose/rhamnose binding lectin domain found in Strongylocentrotus purpuratus receptor for ...
 38-128 2.23e-21

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: 89.45  E-value: 2.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  38 ELACEGYPIELRCpGSDVIMVENANYGRTDDKICDADPFqMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCPG 117
Cdd:cd22841     4 FIVCEGDTDVIDC-GNGVINIHSAVYGRTDSTTCSHDQS-VSNTNCHSDDSVNILSACCNGQSQCTVTATNSIFGDPCPG 81

                          90
                  ....*....|.
gi 2462563787 118 TYKYLEVQYDC 128
Cdd:cd22841    82 TYKYLNVTYTC 92
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
 806-858 2.49e-20

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


Pssm-ID: 197639  Cd Length: 49  Bit Score: 84.75  E-value: 2.49e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462563787  806 FNANCSFWNYSErsmlGYWSTQGCRLVESNKTHTTCACSHLTNFAVLMAHREI 858
Cdd:smart00303   1 FNPICVFWDESS----GEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPPI 49
Gal_Rha_Lectin_EVA1_EVA1C_rpt1 cd22828
first galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
 40-130 2.20e-19

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: 83.87  E-value: 2.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  40 ACEGYPIELRCPGSDVIMVENANYGRTD--DKIC-----DADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFP 112
Cdd:cd22828     7 ACDGEELTLRCPPNTTISIQSAFYGRSVpsAQLCpsqsgPASSTSLEDTNCLAPTALQKVVEECQKKRSCRLLVSSRTFG 86

                          90
                  ....*....|....*....
gi 2462563787 113 -DPCPGTYKYLEVQYDCVP 130
Cdd:cd22828    87 lDPCPGTSKYLEVAYKCRP 105
HormR smart00008
Domain present in hormone receptors;
484-547 5.37e-18

Domain present in hormone receptors;


Pssm-ID: 214468  Cd Length: 70  Bit Score: 78.71  E-value: 5.37e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462563787  484 PELFCEPREVRRVQWPATQQGMLVERPCPKGTRGI-----ASFQCLPALGlWNPRGPDLSNCTSPWVNQ 547
Cdd:smart00008   1 TDLGCPATWDGIICWPQTPAGQLVEVPCPKYFSGFsyktgASRNCTENGG-WSPPFPNYSNCTSNDYEE 68
Gal_Rha_Lectin_LAT1 cd22839
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ...
 38-128 8.07e-18

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: 79.39  E-value: 8.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  38 ELACEGYPIELRCPGSDVIMVENANYGRTDDKICDaDPFQME-NVQCYLPDAFKIMSQRCNNRTQCVVVAGSD-AFPDPC 115
Cdd:cd22839     4 VIICEGDVANLSCPEGKYISIRLANYGRFSLGVCN-PSNNIDlSTTCQNDKTLPILQKSCDGKSECSFVVSNKfFFEDPC 82

                          90
                  ....*....|...
gi 2462563787 116 PGTYKYLEVQYDC 128
Cdd:cd22839    83 PGTPKYLEATYSC 95
Gal_Rha_Lectin_RBL_rpt3 cd22837
third galactose/rhamnose binding lectin domain found in Silurus asotus rhamnose-binding lectin ...
 41-128 2.66e-17

third 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 third one.


Pssm-ID: 438694 [Multi-domain]  Cd Length: 87  Bit Score: 77.47  E-value: 2.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  41 CEGYPIELRCPGSdVIMVENANYGRTDDKICDADpfQMENVQCYLPDAFKIMSQrCNNRTQCVVVAGSDAFPDPCPGTYK 120
Cdd:cd22837     4 CENDSATITCSPE-TINVISAFYGRTDSTTCSHG--RPSTTNCSSDTLAYIRAL-CQGKQTCTLQASNSVFGDPCPGTYK 79


                  ....*...
gi 2462563787 121 YLEVQYDC 128
Cdd:cd22837    80 YLRITYSC 87
GPS pfam01825
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
 810-852 3.57e-17

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.


Pssm-ID: 460350  Cd Length: 44  Bit Score: 75.81  E-value: 3.57e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2462563787 810 CSFWNYSERSMlGYWSTQGCRLVESNKTHTTCACSHLTNFAVL 852
Cdd:pfam01825   3 CVFWDFTNSTT-GRWSTEGCTTVSLNDTHTVCSCNHLTSFAVL 44
Gal_Rha_Lectin_nemgal cd22838
galactose/rhamnose binding lectin domain found in Hydra vulgaris nematogalectin and similar ...
 39-130 3.85e-16

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.


Pssm-ID: 438695 [Multi-domain]  Cd Length: 100  Bit Score: 74.62  E-value: 3.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  39 LACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQME-NVQCYL--PDAFKIMSQRCNNRTQCVVVAGSDAFPDP- 114
Cdd:cd22838     5 IACEGEKLWLQCPQYELIKIKSAFWGRDDKKTCPHPPPGLPsNKMCETdeENVKKKVNDQCQGEQACEVVASNIFFDDTi 84

                          90
                  ....*....|....*.
gi 2462563787 115 CPGTYKYLEVQYDCVP 130
Cdd:cd22838    85 CPDVYKYLKVKYECIP 100
Gal_Rha_Lectin_LAT2 cd22840
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ...
 39-128 1.07e-14

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: 70.52  E-value: 1.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  39 LACEGYPIELRCPGSDVIMVENANYGRTDD-KICDaDPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFP-DPCP 116
Cdd:cd22840     5 VACEGDPFEISCPSGQRIKVDYASYGAIGTrSTCG-DSVSPAGETCSAPNSLQTMRQRCQGRQSCEIRVLNSLFPnDPCP 83

                          90
                  ....*....|...
gi 2462563787 117 GTY-KYLEVQYDC 128
Cdd:cd22840    84 GTSkKYLEYRYRC 96
Gal_Rha_Lectin_PKD1L2 cd22831
galactose binding lectin domain found in polycystic kidney disease protein 1-like 2 ...
 37-128 3.12e-10

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.


Pssm-ID: 438688 [Multi-domain]  Cd Length: 98  Bit Score: 57.75  E-value: 3.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  37 RELACEGYPIELRCPGSDVIMVENANYGRTDDKIC--DADPFQMENVQ-CYLPDAFKIMSQRCNNRTQCVVVAGSDAFPD 113
Cdd:cd22831     2 RSLACEDYNATLQCGSGQVIEIDDSFYGRNTPHYCrsENPSPPTDSQErCSWVDVRDLVAAQCHGLQVCQIPADPSSFGE 81

                          90
                  ....*....|....*
gi 2462563787 114 PCPGTYKYLEVQYDC 128
Cdd:cd22831    82 PCPELGSYLSVEYHC 96
HRM pfam02793
Hormone receptor domain; This extracellular domain contains four conserved cysteines that ...
 485-543 7.36e-10

Hormone receptor domain; This extracellular domain contains four conserved cysteines that probably for disulphide bridges. The domain is found in a variety of hormone receptors. It may be a ligand binding domain.


Pssm-ID: 397086  Cd Length: 64  Bit Score: 55.45  E-value: 7.36e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462563787 485 ELFCEPREVRRVQWPATQQGMLVERPCPKGT-----RGIASFQCLPAlGLWNPRGP-DLSNCTSP 543
Cdd:pfam02793   1 GLGCPRTWDGILCWPRTPAGETVEVPCPDYFsgfdpRGNASRNCTED-GTWSEHPPsNYSNCTSN 64
Gal_Rha_Lectin_BGal cd22842
galactose/rhamnose binding lectin domain found in plant beta-galactosidases and similar ...
 40-128 1.40e-09

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: 55.75  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  40 ACEGYP---IELRCPGSDVI-MVENANYGrTDDKICDAdpFQMENvqCYLPDAFKIMSQRCNNRTQCVVVAGSDA-FPDP 114
Cdd:cd22842     3 VNEGGPgstLTLSCPAGQVIsSIDFASYG-TPTGTCGS--FSKGS--CHAPNSLSVVEKACLGKNSCSIPASNSVfFGDP 77

                          90
                  ....*....|....
gi 2462563787 115 CPGTYKYLEVQYDC 128
Cdd:cd22842    78 CPGTTKRLAVQATC 91
Gal_Rha_Lectin-like_P113 cd22843
galactose/rhamnose binding lectin-like domain found in Plasmodium falciparum P113 and similar ...
 39-128 1.80e-06

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: 46.67  E-value: 1.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  39 LACEGYPIELRCPGSDVIMVENANYGR--TDDKICdadpFQMENVQCYLPDAFkimSQRCNNRTQCVVVAGSDAFPDPCP 116
Cdd:cd22843     5 FVCFGQEVTIHCPGDGNISIKSATYGYnnSNVCIY----CNSFNCDKDITSPV---NKKCCGKNTCVLTVSDILEGNPCG 77

                          90
                  ....*....|..
gi 2462563787 117 GTYKYLEVQYDC 128
Cdd:cd22843    78 IGNSYIRVVYTC 89
PHA03247 PHA03247
large tegument protein UL36; Provisional
 399-503 1.49e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 1.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  399 PPDPSAGED-DSLPGPATSPPLSTTTTARPTPLTSTASPAATTPLRRAPLTTHPVGAINQLGPDLPPATAPVPS---TRR 474
Cdd:PHA03247  2786 PAVASLSESrESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGgdvRRR 2865

                           90       100
                   ....*....|....*....|....*....
gi 2462563787  475 PPAPNLHVSPELFCEPReVRRVQWPATQQ 503
Cdd:PHA03247  2866 PPSRSPAAKPAAPARPP-VRRLARPAVSR 2893
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 397-581 1.29e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 42.60  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787 397 FGPPDPSAGEDDS------LPGPATS-PPLSTTTTARPTP--LTSTASPAATTPLRR-------APLTTHPVGAINQLGP 460
Cdd:pfam05109 439 FAAPNTTTGLPSSthvptnLTAPASTgPTVSTADVTSPTPagTTSGASPVTPSPSPRdngteskAPDMTSPTSAVTTPTP 518

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787 461 DlppATAPVPSTrRPPAPNLhVSPEL-FCEPREVRRVQWP-ATQQGMLVERPCPKGTrgiasfqcLPALGLWNPRgpdlS 538
Cdd:pfam05109 519 N---ATSPTPAV-TTPTPNA-TSPTLgKTSPTSAVTTPTPnATSPTPAVTTPTPNAT--------IPTLGKTSPT----S 581

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462563787 539 NCTSPWVNQVAQKIKSGENAANIASelarHTRGSIYAGDVSSS 581
Cdd:pfam05109 582 AVTTPTPNATSPTVGETSPQANTTN----HTLGGTSSTPVVTS 620
PHA03247 PHA03247
large tegument protein UL36; Provisional
 399-501 2.16e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 2.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787  399 PPDPSAGEDDSLPGPATSpplsttttARPTPLTSTASPAATTPLRRAPLTTHPVGAinqlGPDLPPATAPVPSTRRPPAP 478
Cdd:PHA03247  2722 PPGPAAARQASPALPAAP--------APPAVPAGPATPGGPARPARPPTTAGPPAP----APPAAPAAGPPRRLTRPAVA 2789

                           90       100
                   ....*....|....*....|...
gi 2462563787  479 NLHVSPELFCEPREVRRVQWPAT 501
Cdd:PHA03247  2790 SLSESRESLPSPWDPADPPAAVL 2812
PLN02550 PLN02550
threonine dehydratase
 427-509 7.71e-03

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 39.90  E-value: 7.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563787 427 PTPLTSTASPAATTPLRRAPlTTHPVGAINQLGPDLPPATAPVPSTRRPPAPNLHVSPElfceprevrRVQWPATQQGML 506
Cdd:PLN02550    7 PTAGSPLRSHIGSPSKPVVG-STPFSRSRIPAAVDSADETSMAPPPPPSPLPLLKVSPN---------SLQYPAGYLGAV 76


                  ...
gi 2462563787 507 VER 509
Cdd:PLN02550   77 PER 79
 
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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