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Conserved domains on  [gi|1034606781|ref|XP_016881964|]
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adhesion G protein-coupled receptor L1 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
7tmB2_Latrophilin-1 cd16007
Latrophilin-1, member of the class B2 family of seven-transmembrane G protein-coupled ...
865-1122 0e+00

Latrophilin-1, member of the class B2 family of seven-transmembrane G protein-coupled receptors; 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: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 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. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, 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.


:

Pssm-ID: 320673 [Multi-domain]  Cd Length: 258  Bit Score: 570.71  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  865 ELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLA 944
Cdd:cd16007      1 ELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLIGIDKTQYQIACPIFAGLLHFFFLA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  945 AFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIV 1024
Cdd:cd16007     81 AFSWLCLEGVQLYLMLVEVFESEYSRKKYYYLCGYCFPALVVGISAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1025 VNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFIFVF 1104
Cdd:cd16007    161 VNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAITLLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGMFIFIF 240
                          250
                   ....*....|....*...
gi 1034606781 1105 HCALQKKVHKEYSKCLRH 1122
Cdd:cd16007    241 HCALQKKVHKEYSKCLRH 258
Latrophilin pfam02354
Latrophilin Cytoplasmic C-terminal region; This family consists of the cytoplasmic C-terminal ...
1121-1506 6.01e-175

Latrophilin Cytoplasmic C-terminal region; This family consists of the cytoplasmic C-terminal region in latrophilin. Latrophilin is a synaptic Ca2+ independent alpha- latrotoxin (LTX) receptor and is a novel member of the secretin family of G-protein coupled receptors that are involved in secretion. Latrophilin mRNA is present only in neuronal tissue. Lactrophillin interacts with G-alpha O.


:

Pssm-ID: 460538  Cd Length: 378  Bit Score: 527.90  E-value: 6.01e-175
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1121 RHSYCCIRSPPGGTHGSLKTSAMRSNTRYYTGTQSRIRRMWNDTVRKQTESSFMAGDINSTPTLNRGTMGNHLLTNPVLQ 1200
Cdd:pfam02354    1 RHSHCCSGLSSEGSHGSAKTSASRTTARYSTGTQSRIRRMWNDTVRKQSESSFIAGDINSTPTLNRGTMGNHLLTNPLLR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1201 PRGGTSPYNTLIAESVGFNPSSPPVFNSPElepglafrahpclfsslfwlppagsyrepKHPLG-GREACGMDTLPLNGN 1279
Cdd:pfam02354   81 PHGTTNPYNTLLAESVVFNPPSPPVFNSPG-----------------------------KHSLSnSRDSSGMDTLPLNGN 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1280 FNNSYSLRSGDFPPGDGGPEPPRGRNLADaAAFEKMIISELVHNNLRGSSSAAKGPPPPEPPVPPVPGGG---------- 1349
Cdd:pfam02354  132 FNNSYSLRSGDYENPDGTATYGCRRNLDD-AAFEKMIISELVHNNLRGRGNPKGRDHTRTSDRALPPHTNsggaggggsg 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1350 ---------GEEEAGGPGGADRAEIELLYKALEEPLLLPRAQSVLYQS-----DLDESESCTAEDGATSRPLSSPPGRDS 1415
Cdd:pfam02354  211 eeddamvadAPFPSRGPGRGGNLGLELHYEALEAPLLPQRAQSLLYQSqkarlDQEESESFTADLTETLDDSHHSPNRDS 290
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1416 LYASGANLRDSPsYPDSSPEGPSEALpppPPAPPGPPEIYYTSRpPALVARNPLQGYYQVRRPSHEGYLAAPGLEGPGPD 1495
Cdd:pfam02354  291 LYTSMPNLRDSP-YPDSSPEEEEELS---PSAQSESEDVYYKSM-PALGSRNQLQSYYQIRRGSSDGYIAPPSKEDPSPE 365
                          410
                   ....*....|...
gi 1034606781 1496 G--DGQMQLVTSL 1506
Cdd:pfam02354  366 GepDGQMQLVTSL 378
OLF super family cl02549
Olfactomedin-like domain;
143-399 1.32e-117

Olfactomedin-like domain;


The actual alignment was detected with superfamily member smart00284:

Pssm-ID: 470611  Cd Length: 255  Bit Score: 369.55  E-value: 1.32e-117
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   143 GTLQKVLEPTSTHESE-HQSGAWCKDPLQA---GDRIYVMPWIPYRTDTLTEYASWEDYVAARHTTTYRLPNRVDGTGFV 218
Cdd:smart00284    1 GGLAGISKPVTLQTSWkGKSGAWMKDPLWNttkKSLYWYMPLNTRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGTGVV 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   219 VYDGAVFYNKERTRNIVKYDLRTRIKSGETVINTANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEGNNGRLVVSQLNP 298
Cdd:smart00284   81 VYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNP 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   299 YTLRFEGTWETGYDKRSASNAFMVCGVLYVLRSVYvdddseAAGNRVDYAFNTNANREEPVSLTFPNPYQFISSVDYNPR 378
Cdd:smart00284  161 ATLTIENTWITTYNKRSASNAFMICGILYVTRSLG------SKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPN 234
                           250       260
                    ....*....|....*....|.
gi 1034606781   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 3.80e-66

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: 218.00  E-value: 3.80e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   35 MRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDP 114
Cdd:cd22844      1 MRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDP 80
                           90
                   ....*....|....*..
gi 1034606781  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 6.92e-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: 195.95  E-value: 6.92e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  557 NAANIASELARHTR-GSIYAGDVSSSVKLMEQLLDILDAQLQALrpieresagknynkmhkrertCKDYIKAVVETVDNL 635
Cdd:pfam16489    1 GAKELARELRNATRhGPLYGGDVLTAVELLSQLFDLLATQDATL---------------------SNAFLENFVQTVSNL 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  636 LRPEALESWKDMNATEQVHTATMLLDVLEEGAFLLADNVREPARFLAAKENVVLEVTVLNTEGQVQELV--FPQEEYPRK 713
Cdd:pfam16489   60 LDPENRESWEDLQQTERGTAATKLLRTLEEYALLLAQNMKYLTPFTIVTPNIVLSVDRLDTHNFKGARFprFPMKGERPK 139
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034606781  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 3.66e-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: 85.13  E-value: 3.66e-20
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1034606781   806 FNANCSFWNYSErsmlGYWSTQGCRLVESNKTHTTCACSHLTNFAVLMAHREI 858
Cdd:smart00303    1 FNPICVFWDESS----GEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPPI 49
HormR smart00008
Domain present in hormone receptors;
484-547 3.21e-18

Domain present in hormone receptors;


:

Pssm-ID: 214468  Cd Length: 70  Bit Score: 80.25  E-value: 3.21e-18
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034606781   484 PELFCEPREVRRVQWPATQQGMLVERPCPKGTRGI-----ASFQCLPALGlWNPRGPDLSNCTSPWVNQ 547
Cdd:smart00008    1 TDLGCPATWDGIICWPQTPAGQLVEVPCPKYFSGFsyktgASRNCTENGG-WSPPFPNYSNCTSNDYEE 68
PHA03247 super family cl33720
large tegument protein UL36; Provisional
399-503 2.10e-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: 46.08  E-value: 2.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  399 PPDPSAGED-DSLPGPATSPPLSTTTTARPTPLTSTASPAATTPLRRAPLTTHPVGAINQLGPDLPPATAPVPS---TRR 474
Cdd:PHA03247  2786 PAVASLSESrESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGgdvRRR 2865
                           90       100
                   ....*....|....*....|....*....
gi 1034606781  475 PPAPNLHVSPELFCEPReVRRVQWPATQQ 503
Cdd:PHA03247  2866 PPSRSPAAKPAAPARPP-VRRLARPAVSR 2893
 
Name Accession Description Interval E-value
7tmB2_Latrophilin-1 cd16007
Latrophilin-1, member of the class B2 family of seven-transmembrane G protein-coupled ...
865-1122 0e+00

Latrophilin-1, member of the class B2 family of seven-transmembrane G protein-coupled receptors; 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: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 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. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, 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.


Pssm-ID: 320673 [Multi-domain]  Cd Length: 258  Bit Score: 570.71  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  865 ELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLA 944
Cdd:cd16007      1 ELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLIGIDKTQYQIACPIFAGLLHFFFLA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  945 AFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIV 1024
Cdd:cd16007     81 AFSWLCLEGVQLYLMLVEVFESEYSRKKYYYLCGYCFPALVVGISAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1025 VNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFIFVF 1104
Cdd:cd16007    161 VNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAITLLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGMFIFIF 240
                          250
                   ....*....|....*...
gi 1034606781 1105 HCALQKKVHKEYSKCLRH 1122
Cdd:cd16007    241 HCALQKKVHKEYSKCLRH 258
Latrophilin pfam02354
Latrophilin Cytoplasmic C-terminal region; This family consists of the cytoplasmic C-terminal ...
1121-1506 6.01e-175

Latrophilin Cytoplasmic C-terminal region; This family consists of the cytoplasmic C-terminal region in latrophilin. Latrophilin is a synaptic Ca2+ independent alpha- latrotoxin (LTX) receptor and is a novel member of the secretin family of G-protein coupled receptors that are involved in secretion. Latrophilin mRNA is present only in neuronal tissue. Lactrophillin interacts with G-alpha O.


Pssm-ID: 460538  Cd Length: 378  Bit Score: 527.90  E-value: 6.01e-175
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1121 RHSYCCIRSPPGGTHGSLKTSAMRSNTRYYTGTQSRIRRMWNDTVRKQTESSFMAGDINSTPTLNRGTMGNHLLTNPVLQ 1200
Cdd:pfam02354    1 RHSHCCSGLSSEGSHGSAKTSASRTTARYSTGTQSRIRRMWNDTVRKQSESSFIAGDINSTPTLNRGTMGNHLLTNPLLR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1201 PRGGTSPYNTLIAESVGFNPSSPPVFNSPElepglafrahpclfsslfwlppagsyrepKHPLG-GREACGMDTLPLNGN 1279
Cdd:pfam02354   81 PHGTTNPYNTLLAESVVFNPPSPPVFNSPG-----------------------------KHSLSnSRDSSGMDTLPLNGN 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1280 FNNSYSLRSGDFPPGDGGPEPPRGRNLADaAAFEKMIISELVHNNLRGSSSAAKGPPPPEPPVPPVPGGG---------- 1349
Cdd:pfam02354  132 FNNSYSLRSGDYENPDGTATYGCRRNLDD-AAFEKMIISELVHNNLRGRGNPKGRDHTRTSDRALPPHTNsggaggggsg 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1350 ---------GEEEAGGPGGADRAEIELLYKALEEPLLLPRAQSVLYQS-----DLDESESCTAEDGATSRPLSSPPGRDS 1415
Cdd:pfam02354  211 eeddamvadAPFPSRGPGRGGNLGLELHYEALEAPLLPQRAQSLLYQSqkarlDQEESESFTADLTETLDDSHHSPNRDS 290
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1416 LYASGANLRDSPsYPDSSPEGPSEALpppPPAPPGPPEIYYTSRpPALVARNPLQGYYQVRRPSHEGYLAAPGLEGPGPD 1495
Cdd:pfam02354  291 LYTSMPNLRDSP-YPDSSPEEEEELS---PSAQSESEDVYYKSM-PALGSRNQLQSYYQIRRGSSDGYIAPPSKEDPSPE 365
                          410
                   ....*....|...
gi 1034606781 1496 G--DGQMQLVTSL 1506
Cdd:pfam02354  366 GepDGQMQLVTSL 378
OLF smart00284
Olfactomedin-like domains;
143-399 1.32e-117

Olfactomedin-like domains;


Pssm-ID: 128580  Cd Length: 255  Bit Score: 369.55  E-value: 1.32e-117
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   143 GTLQKVLEPTSTHESE-HQSGAWCKDPLQA---GDRIYVMPWIPYRTDTLTEYASWEDYVAARHTTTYRLPNRVDGTGFV 218
Cdd:smart00284    1 GGLAGISKPVTLQTSWkGKSGAWMKDPLWNttkKSLYWYMPLNTRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGTGVV 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   219 VYDGAVFYNKERTRNIVKYDLRTRIKSGETVINTANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEGNNGRLVVSQLNP 298
Cdd:smart00284   81 VYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNP 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   299 YTLRFEGTWETGYDKRSASNAFMVCGVLYVLRSVYvdddseAAGNRVDYAFNTNANREEPVSLTFPNPYQFISSVDYNPR 378
Cdd:smart00284  161 ATLTIENTWITTYNKRSASNAFMICGILYVTRSLG------SKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPN 234
                           250       260
                    ....*....|....*....|.
gi 1034606781   379 DNQLYVWNNYFVVRYSLEFGP 399
Cdd:smart00284  235 DRKLYAWNNGHLVHYDIALKP 255
OLF pfam02191
Olfactomedin-like domain;
145-397 2.15e-115

Olfactomedin-like domain;


Pssm-ID: 460482  Cd Length: 246  Bit Score: 363.01  E-value: 2.15e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  145 LQKVLEPTSTHESEHQSGAWCKDPLQAGDRIYVMPwIPYRTDTLTEYASWEDYVAARHTTTYRLPNRVDGTGFVVYDGAV 224
Cdd:pfam02191    1 LVSVSKPVTVKLSGGKYGAWMKDPLPPSDKIYVTD-RGTSGNTLREYASLDDFKNGSPSKKYKLPYPWQGTGHVVYNGSL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  225 FYNKERTRNIVKYDLRTRIKSGETVINTANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEGNNGRLVVSQLNPYTLRFE 304
Cdd:pfam02191   80 YYNKYNSRNIVKYDLTTRTVAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLDPETLEVE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  305 GTWETGYDKRSASNAFMVCGVLYVLRSVYVDDdseaagNRVDYAFNTNANREEPVSLTFPNPYQFISSVDYNPRDNQLYV 384
Cdd:pfam02191  160 QTWNTSYPKRSAGNAFMVCGVLYAVRSVNTRR------EEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLYA 233
                          250
                   ....*....|...
gi 1034606781  385 WNNYFVVRYSLEF 397
Cdd:pfam02191  234 WDDGYQVTYPVTF 246
7tm_2 pfam00002
7 transmembrane receptor (Secretin family); This family is known as Family B, the ...
866-1101 3.27e-94

7 transmembrane receptor (Secretin family); This family is known as Family B, the secretin-receptor family or family 2 of the G-protein-coupled receptors (GCPRs). They have been described in many animal species, but not in plants, fungi or prokaryotes. Three distinct sub-families are recognized. Subfamily B1 contains classical hormone receptors, such as receptors for secretin and glucagon, that are all involved in cAMP-mediated signalling pathways. Subfamily B2 contains receptors with long extracellular N-termini, such as the leukocyte cell-surface antigen CD97; calcium-independent receptors for latrotoxin, and brain-specific angiogenesis inhibitors amongst others. Subfamily B3 includes Methuselah and other Drosophila proteins. Other than the typical seven-transmembrane region, characteriztic structural features include an amino-terminal extracellular domain involved in ligand binding, and an intracellular loop (IC3) required for specific G-protein coupling.


Pssm-ID: 459625 [Multi-domain]  Cd Length: 248  Bit Score: 304.20  E-value: 3.27e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  866 LLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYE--------IACPIFAGL 937
Cdd:pfam00002    2 LSLKVIYTVGYSLSLVALLLAIAIFLLFRKLHCTRNYIHLNLFASFILRALLFLVGDAVLFNKqdldhcswVGCKVVAVF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  938 LHYFFLAAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIG 1017
Cdd:pfam00002   82 LHYFFLANFFWMLVEGLYLYTLLVEVFFSERKYFWWYLLIGWGVPALVVGIWAGVDPKGYGEDDGCWLSNENGLWWIIRG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1018 PVSFVIVVNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKES---VVMAYLFTTFN 1094
Cdd:pfam00002  162 PILLIILVNFIIFINIVRILVQKLRETNMGKSDLKQYRRLAKSTLLLLPLLGITWVFGLFAFNPENtlrVVFLYLFLILN 241

                   ....*..
gi 1034606781 1095 AFQGVFI 1101
Cdd:pfam00002  242 SFQGFFV 248
Gal_Rha_Lectin_LPHN1 cd22844
galactose/rhamnose binding lectin domain found in latrophilin-1 and similar proteins; ...
35-131 3.80e-66

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: 218.00  E-value: 3.80e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   35 MRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDP 114
Cdd:cd22844      1 MRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDP 80
                           90
                   ....*....|....*..
gi 1034606781  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 6.92e-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: 195.95  E-value: 6.92e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  557 NAANIASELARHTR-GSIYAGDVSSSVKLMEQLLDILDAQLQALrpieresagknynkmhkrertCKDYIKAVVETVDNL 635
Cdd:pfam16489    1 GAKELARELRNATRhGPLYGGDVLTAVELLSQLFDLLATQDATL---------------------SNAFLENFVQTVSNL 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  636 LRPEALESWKDMNATEQVHTATMLLDVLEEGAFLLADNVREPARFLAAKENVVLEVTVLNTEGQVQELV--FPQEEYPRK 713
Cdd:pfam16489   60 LDPENRESWEDLQQTERGTAATKLLRTLEEYALLLAQNMKYLTPFTIVTPNIVLSVDRLDTHNFKGARFprFPMKGERPK 139
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034606781  714 --NSIQLSAKTIKQNSRNGVVKVVFILYNNLGLFLSTENATvklagEAGPGGPGGASLVVNSQVIAASINK 782
Cdd:pfam16489  140 deDSVKLPPKAFKPPDSNGTVVVVFILYRNLGSLLPPSSRY-----DPDRRSLRLPRRVVNSPVVSASVHS 205
Gal_Lectin pfam02140
Galactose binding lectin domain;
48-128 9.76e-32

Galactose binding lectin domain;


Pssm-ID: 460460 [Multi-domain]  Cd Length: 79  Bit Score: 118.93  E-value: 9.76e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   48 LRCPGSDVIMVENANYGRTDDKICdadPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAF-PDPCPGTYKYLEVQY 126
Cdd:pfam02140    1 LSCPPGKVISILFASYGRPDGTTC---PSFIQGTNCHSPNSLAIVSKACQGKNSCSVPASNSVFgGDPCPGTYKYLEVEY 77

                   ..
gi 1034606781  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 3.66e-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: 85.13  E-value: 3.66e-20
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1034606781   806 FNANCSFWNYSErsmlGYWSTQGCRLVESNKTHTTCACSHLTNFAVLMAHREI 858
Cdd:smart00303    1 FNPICVFWDESS----GEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPPI 49
HormR smart00008
Domain present in hormone receptors;
484-547 3.21e-18

Domain present in hormone receptors;


Pssm-ID: 214468  Cd Length: 70  Bit Score: 80.25  E-value: 3.21e-18
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034606781   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 5.71e-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: 5.71e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1034606781  810 CSFWNYSERSMlGYWSTQGCRLVESNKTHTTCACSHLTNFAVL 852
Cdd:pfam01825    3 CVFWDFTNSTT-GRWSTEGCTTVSLNDTHTVCSCNHLTSFAVL 44
HRM pfam02793
Hormone receptor domain; This extracellular domain contains four conserved cysteines that ...
485-543 6.94e-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: 56.22  E-value: 6.94e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034606781  485 ELFCEPREVRRVQWPATQQGMLVERPCPKGT-----RGIASFQCLPAlGLWNPRGP-DLSNCTSP 543
Cdd:pfam02793    1 GLGCPRTWDGILCWPRTPAGETVEVPCPDYFsgfdpRGNASRNCTED-GTWSEHPPsNYSNCTSN 64
PHA03247 PHA03247
large tegument protein UL36; Provisional
399-503 2.10e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 2.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  399 PPDPSAGED-DSLPGPATSPPLSTTTTARPTPLTSTASPAATTPLRRAPLTTHPVGAINQLGPDLPPATAPVPS---TRR 474
Cdd:PHA03247  2786 PAVASLSESrESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGgdvRRR 2865
                           90       100
                   ....*....|....*....|....*....
gi 1034606781  475 PPAPNLHVSPELFCEPReVRRVQWPATQQ 503
Cdd:PHA03247  2866 PPSRSPAAKPAAPARPP-VRRLARPAVSR 2893
 
Name Accession Description Interval E-value
7tmB2_Latrophilin-1 cd16007
Latrophilin-1, member of the class B2 family of seven-transmembrane G protein-coupled ...
865-1122 0e+00

Latrophilin-1, member of the class B2 family of seven-transmembrane G protein-coupled receptors; 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: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 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. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, 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.


Pssm-ID: 320673 [Multi-domain]  Cd Length: 258  Bit Score: 570.71  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  865 ELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLA 944
Cdd:cd16007      1 ELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLIGIDKTQYQIACPIFAGLLHFFFLA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  945 AFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIV 1024
Cdd:cd16007     81 AFSWLCLEGVQLYLMLVEVFESEYSRKKYYYLCGYCFPALVVGISAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1025 VNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFIFVF 1104
Cdd:cd16007    161 VNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAITLLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGMFIFIF 240
                          250
                   ....*....|....*...
gi 1034606781 1105 HCALQKKVHKEYSKCLRH 1122
Cdd:cd16007    241 HCALQKKVHKEYSKCLRH 258
Latrophilin pfam02354
Latrophilin Cytoplasmic C-terminal region; This family consists of the cytoplasmic C-terminal ...
1121-1506 6.01e-175

Latrophilin Cytoplasmic C-terminal region; This family consists of the cytoplasmic C-terminal region in latrophilin. Latrophilin is a synaptic Ca2+ independent alpha- latrotoxin (LTX) receptor and is a novel member of the secretin family of G-protein coupled receptors that are involved in secretion. Latrophilin mRNA is present only in neuronal tissue. Lactrophillin interacts with G-alpha O.


Pssm-ID: 460538  Cd Length: 378  Bit Score: 527.90  E-value: 6.01e-175
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1121 RHSYCCIRSPPGGTHGSLKTSAMRSNTRYYTGTQSRIRRMWNDTVRKQTESSFMAGDINSTPTLNRGTMGNHLLTNPVLQ 1200
Cdd:pfam02354    1 RHSHCCSGLSSEGSHGSAKTSASRTTARYSTGTQSRIRRMWNDTVRKQSESSFIAGDINSTPTLNRGTMGNHLLTNPLLR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1201 PRGGTSPYNTLIAESVGFNPSSPPVFNSPElepglafrahpclfsslfwlppagsyrepKHPLG-GREACGMDTLPLNGN 1279
Cdd:pfam02354   81 PHGTTNPYNTLLAESVVFNPPSPPVFNSPG-----------------------------KHSLSnSRDSSGMDTLPLNGN 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1280 FNNSYSLRSGDFPPGDGGPEPPRGRNLADaAAFEKMIISELVHNNLRGSSSAAKGPPPPEPPVPPVPGGG---------- 1349
Cdd:pfam02354  132 FNNSYSLRSGDYENPDGTATYGCRRNLDD-AAFEKMIISELVHNNLRGRGNPKGRDHTRTSDRALPPHTNsggaggggsg 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1350 ---------GEEEAGGPGGADRAEIELLYKALEEPLLLPRAQSVLYQS-----DLDESESCTAEDGATSRPLSSPPGRDS 1415
Cdd:pfam02354  211 eeddamvadAPFPSRGPGRGGNLGLELHYEALEAPLLPQRAQSLLYQSqkarlDQEESESFTADLTETLDDSHHSPNRDS 290
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1416 LYASGANLRDSPsYPDSSPEGPSEALpppPPAPPGPPEIYYTSRpPALVARNPLQGYYQVRRPSHEGYLAAPGLEGPGPD 1495
Cdd:pfam02354  291 LYTSMPNLRDSP-YPDSSPEEEEELS---PSAQSESEDVYYKSM-PALGSRNQLQSYYQIRRGSSDGYIAPPSKEDPSPE 365
                          410
                   ....*....|...
gi 1034606781 1496 G--DGQMQLVTSL 1506
Cdd:pfam02354  366 GepDGQMQLVTSL 378
7tmB2_Latrophilin cd15436
Latrophilins, member of the class B2 family of seven-transmembrane G protein-coupled receptors; ...
865-1122 1.21e-167

Latrophilins, member of the class B2 family of seven-transmembrane G protein-coupled receptors; 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: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 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. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, 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.


Pssm-ID: 320552 [Multi-domain]  Cd Length: 258  Bit Score: 503.56  E-value: 1.21e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  865 ELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLA 944
Cdd:cd15436      1 ELLLFVITWVGIVISLVCLLICIFTFCFFRGLQTDRNTIHKNLCINLFIAELLFLIGINRTQYTIACPIFAGLLHFFFLA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  945 AFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIV 1024
Cdd:cd15436     81 AFCWLCLEGVQLYLLLVEVFESEYSRRKYFYLCGYSFPALVVAVSAAIDYRSYGTEKACWLRVDNYFIWSFIGPVTFVIT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1025 VNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFIFVF 1104
Cdd:cd15436    161 LNLVFLVITLHKMVSHSDLLKPDSSRLDNIKSWALGAIALLFLLGLTWSFGLMFINEESVVMAYLFTIFNAFQGVFIFIF 240
                          250
                   ....*....|....*...
gi 1034606781 1105 HCALQKKVHKEYSKCLRH 1122
Cdd:cd15436    241 HCALQKKVRKEYSKCLRH 258
7tmB2_Latrophilin-2 cd16006
Latrophilin-2, member of the class B2 family of seven-transmembrane G protein-coupled ...
865-1122 9.07e-155

Latrophilin-2, member of the class B2 family of seven-transmembrane G protein-coupled receptors; 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: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 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. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, 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.


Pssm-ID: 320672 [Multi-domain]  Cd Length: 258  Bit Score: 469.40  E-value: 9.07e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  865 ELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLA 944
Cdd:cd16006      1 ELLLTVITWVGIVISLVCLAICIFTFCFFRGLQSDRNTIHKNLCINLFIAEFIFLIGIDKTEYKIACPIFAGLLHFFFLA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  945 AFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIV 1024
Cdd:cd16006     81 AFAWMCLEGVQLYLMLVEVFESEYSRKKYYYVAGYLFPATVVGVSAAIDYKSYGTEKACWLRVDNYFIWSFIGPVTFIIL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1025 VNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFIFVF 1104
Cdd:cd16006    161 LNLIFLVITLCKMVKHSNTLKPDSSRLENIKSWVLGAFALLCLLGLTWSFGLLFINEETIVMAYLFTIFNAFQGMFIFIF 240
                          250
                   ....*....|....*...
gi 1034606781 1105 HCALQKKVHKEYSKCLRH 1122
Cdd:cd16006    241 HCALQKKVRKEYSKCFRH 258
7tmB2_Latrophilin_Adhesion_I cd15252
Latrophilins and similar receptors, group I adhesion GPCRs, member of class B2 family of ...
865-1121 5.55e-137

Latrophilins and similar receptors, group I adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors; Group I adhesion GPCRs consist of latrophilins (also called lectomedins or latrotoxin receptors) and 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: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 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. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, 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.


Pssm-ID: 320380 [Multi-domain]  Cd Length: 257  Bit Score: 421.91  E-value: 5.55e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  865 ELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLA 944
Cdd:cd15252      1 YNILTRITQVGIIISLVCLAICIFTFWFFRGLQSDRTTIHKNLCISLFLAELVFLIGINTTTNKIFCSVIAGLLHYFFLA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  945 AFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIV 1024
Cdd:cd15252     81 AFAWMFIEGIQLYLMLVEVFENEGSRHKNFYIFGYGSPAVIVGVSAALGYRYYGTTKVCWLSTENYFIWSFIGPATLIIL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1025 VNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFIFVF 1104
Cdd:cd15252    161 LNLIFLGVAIYKMFRHTAGLKPEVSCLENIRSWARGAIALLFLLGLTWIFGVLHINHASVVMAYLFTVSNSLQGMFIFLF 240
                          250
                   ....*....|....*..
gi 1034606781 1105 HCALQKKVHKEYSKCLR 1121
Cdd:cd15252    241 HCVLSRKVRKEYYKLFR 257
7tmB2_latrophilin-like_invertebrate cd15440
invertebrate latrophilin-like receptors, member of the class B2 family of seven-transmembrane ...
865-1121 9.34e-129

invertebrate latrophilin-like receptors, member of the class B2 family of seven-transmembrane G protein-coupled receptors; This subgroup includes latrophilin-like proteins that are found in invertebrates such as insects and worms. 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 vertebrate latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 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. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, 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.


Pssm-ID: 320556 [Multi-domain]  Cd Length: 259  Bit Score: 399.72  E-value: 9.34e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  865 ELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLA 944
Cdd:cd15440      1 QSALTFITYIGCIISIVCLLLAFITFTCFRNLQCDRNTIHKNLCLCLLIAEIVFLLGIDQTENRTLCGVIAGLLHYFFLA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  945 AFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIV 1024
Cdd:cd15440     81 AFSWMLLEGFQLYVMLVEVFEPEKSRIKWYYLFGYGLPALIVAVSAGVDPTGYGTEDHCWLSTENGFIWSFVGPVIVVLL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1025 VNLVFLMVTLHKMIRSSSVL--KPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFIF 1102
Cdd:cd15440    161 ANLVFLGMAIYVMCRHSSRSasKKDASKLKNIRGWLKGSIVLVVLLGLTWTFGLLFINQESIVMAYIFTILNSLQGLFIF 240
                          250
                   ....*....|....*....
gi 1034606781 1103 VFHCALQKKVHKEYSKCLR 1121
Cdd:cd15440    241 IFHCVLNEKVRKELRRWLR 259
7tmB2_Latrophilin-3 cd16005
Latrophilin-3, member of the class B2 family of seven-transmembrane G protein-coupled ...
865-1121 2.94e-123

Latrophilin-3, member of the class B2 family of seven-transmembrane G protein-coupled receptors; 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: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 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. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, 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.


Pssm-ID: 320671 [Multi-domain]  Cd Length: 258  Bit Score: 385.07  E-value: 2.94e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  865 ELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLA 944
Cdd:cd16005      1 DLLLDVITWVGILLSLVCLLICIFTFCFFRGLQSDRNTIHKNLCISLFVAELLFLIGINRTDQPIACAVFAALLHFFFLA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  945 AFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIV 1024
Cdd:cd16005     81 AFTWMFLEGVQLYIMLVEVFESEHSRRKYFYLVGYGMPALIVAVSAAVDYRSYGTDKVCWLRLDTYFIWSFIGPATLIIM 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1025 VNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFIFVF 1104
Cdd:cd16005    161 LNVIFLGIALYKMFHHTAILKPESGCLDNIKSWVIGAIALLCLLGLTWAFGLMYINESTVIMAYLFTIFNSLQGMFIFIF 240
                          250
                   ....*....|....*..
gi 1034606781 1105 HCALQKKVHKEYSKCLR 1121
Cdd:cd16005    241 HCVLQKKVRKEYGKCLR 257
OLF smart00284
Olfactomedin-like domains;
143-399 1.32e-117

Olfactomedin-like domains;


Pssm-ID: 128580  Cd Length: 255  Bit Score: 369.55  E-value: 1.32e-117
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   143 GTLQKVLEPTSTHESE-HQSGAWCKDPLQA---GDRIYVMPWIPYRTDTLTEYASWEDYVAARHTTTYRLPNRVDGTGFV 218
Cdd:smart00284    1 GGLAGISKPVTLQTSWkGKSGAWMKDPLWNttkKSLYWYMPLNTRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGTGVV 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   219 VYDGAVFYNKERTRNIVKYDLRTRIKSGETVINTANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEGNNGRLVVSQLNP 298
Cdd:smart00284   81 VYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNP 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   299 YTLRFEGTWETGYDKRSASNAFMVCGVLYVLRSVYvdddseAAGNRVDYAFNTNANREEPVSLTFPNPYQFISSVDYNPR 378
Cdd:smart00284  161 ATLTIENTWITTYNKRSASNAFMICGILYVTRSLG------SKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPN 234
                           250       260
                    ....*....|....*....|.
gi 1034606781   379 DNQLYVWNNYFVVRYSLEFGP 399
Cdd:smart00284  235 DRKLYAWNNGHLVHYDIALKP 255
OLF pfam02191
Olfactomedin-like domain;
145-397 2.15e-115

Olfactomedin-like domain;


Pssm-ID: 460482  Cd Length: 246  Bit Score: 363.01  E-value: 2.15e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  145 LQKVLEPTSTHESEHQSGAWCKDPLQAGDRIYVMPwIPYRTDTLTEYASWEDYVAARHTTTYRLPNRVDGTGFVVYDGAV 224
Cdd:pfam02191    1 LVSVSKPVTVKLSGGKYGAWMKDPLPPSDKIYVTD-RGTSGNTLREYASLDDFKNGSPSKKYKLPYPWQGTGHVVYNGSL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  225 FYNKERTRNIVKYDLRTRIKSGETVINTANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEGNNGRLVVSQLNPYTLRFE 304
Cdd:pfam02191   80 YYNKYNSRNIVKYDLTTRTVAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLDPETLEVE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  305 GTWETGYDKRSASNAFMVCGVLYVLRSVYVDDdseaagNRVDYAFNTNANREEPVSLTFPNPYQFISSVDYNPRDNQLYV 384
Cdd:pfam02191  160 QTWNTSYPKRSAGNAFMVCGVLYAVRSVNTRR------EEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLYA 233
                          250
                   ....*....|...
gi 1034606781  385 WNNYFVVRYSLEF 397
Cdd:pfam02191  234 WDDGYQVTYPVTF 246
7tmB2_ETL cd15437
Epidermal Growth Factor, latrophilin and seven transmembrane domain-containing protein 1; ...
867-1116 2.98e-100

Epidermal Growth Factor, latrophilin and seven transmembrane domain-containing protein 1; member of the class B2 family of seven-transmembrane G protein-coupled receptors; ETL (EGF-TM7-latrophilin-related protein) belongs to Group I adhesion GPCRs, which also include latrophilins (also called lectomedins or latrotoxin receptors). All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. ETL, for instance, contains EGF-like repeats, which also present in other EGF-TM7 adhesion GPCRs, such as Cadherin EGF LAG seven-pass G-type receptors (CELSR1-3), EGF-like module receptors (EMR1-3), CD97, and Flamingo. ETL is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. Furthermore, 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.


Pssm-ID: 320553 [Multi-domain]  Cd Length: 258  Bit Score: 321.44  E-value: 2.98e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  867 LLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLAAF 946
Cdd:cd15437      3 VLTRITQLGIIISLICLSMCIFTFWFFSEIQSTRTTIHKNLCCSLFLAELIFLIGINMNANKLFCSIIAGLLHYFFLAAF 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  947 SWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIVVN 1026
Cdd:cd15437     83 AWMCIEGIHLYLIVVGVIYNKGFLHKNFYIFGYGSPAVVVGISAALGYKYYGTTKVCWLSTENNFIWSFIGPACLIILVN 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1027 LVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFIFVFHC 1106
Cdd:cd15437    163 LLAFGVIIYKVFRHTAMLKPEVSCYENIRSCARGALALLFLLGATWIFGVLHVVYGSVVTAYLFTISNAFQGMFIFIFLC 242
                          250
                   ....*....|
gi 1034606781 1107 ALQKKVHKEY 1116
Cdd:cd15437    243 VLSRKIQEEY 252
7tmB2_CD97 cd15438
CD97 antigen, member of the class B2 family of seven-transmembrane G protein-coupled receptors; ...
868-1120 3.86e-97

CD97 antigen, member of the class B2 family of seven-transmembrane G protein-coupled receptors; group II adhesion GPCRs, including the leukocyte cell-surface antigen CD97 and the epidermal growth factor (EGF)-module-containing, mucin-like hormone receptor (EMR1-4), are primarily expressed in cells of the immune system. All EGF-TM7 receptors, which belong to the B2 subfamily B2 of adhesion GPCRs, are members of group II, except for ETL (EGF-TM7-latrophilin related protein), which is classified into group I. Members of the EGF-TM7 receptors are characterized by the presence of varying numbers of N-terminal EGF-like domains, which play critical roles in ligand recognition and cell adhesion, linked by a stalk region to a class B seven-transmembrane domain. In the case of CD97, alternative splicing results in three isoforms possessing either three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. 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. For example, CD97, which is involved in angiogenesis and the migration and invasion of tumor cells, has been shown to promote cell aggregation in a GPS proteolysis-dependent manner. CD97 is widely expressed on lymphocytes, monocytes, macrophages, dendritic cells, granulocytes and smooth muscle cells as well as in a variety of human tumors including colorectal, gastric, esophageal pancreatic, and thyroid carcinoma. EMR2 shares strong sequence homology with CD97, differing by only six amino acids. However, unlike CD97, EMR2 is not found in those of CD97-positive tumor cells and is not expressed on lymphocytes but instead on monocytes, macrophages and granulocytes. CD97 has three known ligands: CD55, decay-accelerating factor for regulation of complement system; chondroitin sulfate, a glycosaminoglycan found in the extracellular matrix; and the integrin alpha5beta1, which play a role in angiogenesis. Although EMR2 does not effectively interact with CD55, the fourth EGF-like domain of this receptor binds to chondroitin sulfate to mediate cell attachment.


Pssm-ID: 320554 [Multi-domain]  Cd Length: 261  Bit Score: 312.85  E-value: 3.86e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  868 LSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLAAFS 947
Cdd:cd15438      4 LTLITKVGLSVSLFCLFLCILTFLFCRSIRGTRNTIHLHLCLSLFLAHLIFLLGINNTNNQVACAVVAGLLHYFFLAAFC 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  948 WLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIVVNL 1027
Cdd:cd15438     84 WMSLEGVELYLMVVQVFNTQSLKKRYLLLIGYGVPLVIVAISAAVNSKGYGTQRHCWLSLERGFLWSFLGPVCLIILVNA 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1028 VFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFIFVFHCA 1107
Cdd:cd15438    164 IIFVITVWKLAEKFSSINPDMEKLRKIRALTITAIAQLCILGCTWIFGFFQFSDSTLVMSYLFTILNSLQGLFIFLLHCL 243
                          250
                   ....*....|...
gi 1034606781 1108 LQKKVHKEYSKCL 1120
Cdd:cd15438    244 LSKQVREEYSRWL 256
7tmB2_EMR cd15439
epidermal growth factor-like module-containing mucin-like hormone receptors, member of the ...
865-1118 5.11e-95

epidermal growth factor-like module-containing mucin-like hormone receptors, member of the class B2 family of seven-transmembrane G protein-coupled receptors; group II adhesion GPCRs, including the epidermal growth factor (EGF)-module-containing, mucin-like hormone receptor (EMR1-4) and the leukocyte cell-surface antigen CD97, are primarily expressed in cells of the immune system. All EGF-TM7 receptors, which belong to the B2 subfamily of adhesion GPCRs, are members of group II, except for ETL (EGF-TM7-latrophilin related protein), which is classified into group I. Members of the EGF-TM7 receptors are characterized by the presence of varying number of N-terminal EGF-like domains, which play critical roles in ligand recognition and cell adhesion, linked by a stalk region to a class B seven-transmembrane domain. In the case of EMR2, alternative splicing results in four isoforms possessing either two (EGF1,2), three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. 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. EMR2 shares strong sequence homology with CD97, differing by only six amino acids. CD97 is widely expressed on lymphocytes, monocytes, macrophages, dendritic cells, granulocytes and smooth muscle cells as well as in a variety of human tumors including colorectal, gastric, esophageal pancreatic, and thyroid carcinoma. However, unlike CD97, EMR2 is not found in those of CD97-positive tumor cells and is not expressed on lymphocytes but instead on monocytes, macrophages and granulocytes. CD97 has three known ligands: CD55, decay-accelerating factor for regulation of complement system; chondroitin sulfate, a glycosaminoglycan found in the extracellular matrix; and the integrin alpha5beta1, which play a role in angiogenesis. Although EMR2 does not effectively interact with CD55, the fourth EGF-like domain of this receptor binds to chondroitin sulfate to mediate cell attachment.


Pssm-ID: 320555 [Multi-domain]  Cd Length: 263  Bit Score: 306.96  E-value: 5.11e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  865 ELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLA 944
Cdd:cd15439      1 DLALTVITYVGLIISLLCLFLAILTFLLCRSIRNTSTSLHLQLSLCLFLADLLFLVGIDRTDNKVLCSIIAGFLHYLFLA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  945 AFSWLCLEGVHLYLLL-----VEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPV 1019
Cdd:cd15439     81 CFAWMFLEAVHLFLTVrnlkvVNYFSSHRFKKRFMYPVGYGLPAVIVAISAAVNPQGYGTPKHCWLSMEKGFIWSFLGPV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1020 SFVIVVNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGV 1099
Cdd:cd15439    161 CVIIVINLVLFCLTLWILREKLSSLNAEVSTLKNTRLLTFKAIAQLFILGCTWILGLFQVGPVATVMAYLFTITNSLQGV 240
                          250
                   ....*....|....*....
gi 1034606781 1100 FIFVFHCALQKKVHKEYSK 1118
Cdd:cd15439    241 FIFLVHCLLNRQVREEYRR 259
7tm_2 pfam00002
7 transmembrane receptor (Secretin family); This family is known as Family B, the ...
866-1101 3.27e-94

7 transmembrane receptor (Secretin family); This family is known as Family B, the secretin-receptor family or family 2 of the G-protein-coupled receptors (GCPRs). They have been described in many animal species, but not in plants, fungi or prokaryotes. Three distinct sub-families are recognized. Subfamily B1 contains classical hormone receptors, such as receptors for secretin and glucagon, that are all involved in cAMP-mediated signalling pathways. Subfamily B2 contains receptors with long extracellular N-termini, such as the leukocyte cell-surface antigen CD97; calcium-independent receptors for latrotoxin, and brain-specific angiogenesis inhibitors amongst others. Subfamily B3 includes Methuselah and other Drosophila proteins. Other than the typical seven-transmembrane region, characteriztic structural features include an amino-terminal extracellular domain involved in ligand binding, and an intracellular loop (IC3) required for specific G-protein coupling.


Pssm-ID: 459625 [Multi-domain]  Cd Length: 248  Bit Score: 304.20  E-value: 3.27e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  866 LLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYE--------IACPIFAGL 937
Cdd:pfam00002    2 LSLKVIYTVGYSLSLVALLLAIAIFLLFRKLHCTRNYIHLNLFASFILRALLFLVGDAVLFNKqdldhcswVGCKVVAVF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  938 LHYFFLAAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIG 1017
Cdd:pfam00002   82 LHYFFLANFFWMLVEGLYLYTLLVEVFFSERKYFWWYLLIGWGVPALVVGIWAGVDPKGYGEDDGCWLSNENGLWWIIRG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1018 PVSFVIVVNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKES---VVMAYLFTTFN 1094
Cdd:pfam00002  162 PILLIILVNFIIFINIVRILVQKLRETNMGKSDLKQYRRLAKSTLLLLPLLGITWVFGLFAFNPENtlrVVFLYLFLILN 241

                   ....*..
gi 1034606781 1095 AFQGVFI 1101
Cdd:pfam00002  242 SFQGFFV 248
7tmB2_Adhesion cd15040
adhesion receptors, subfamily B2 of the class B family of seven-transmembrane G ...
865-1116 2.78e-90

adhesion receptors, subfamily B2 of the class B family of seven-transmembrane G protein-coupled receptors; The B2 subfamily of class B GPCRs consists of cell-adhesion receptors with 33 members in humans and vertebrates. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing a variety of structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, linked to a class B seven-transmembrane domain. These include, for example, EGF (epidermal growth factor)-like domains in CD97, Celsr1 (cadherin family member), Celsr2, Celsr3, EMR1 (EGF-module-containing mucin-like hormone receptor-like 1), EMR2, EMR3, and Flamingo; two laminin A G-type repeats and nine cadherin domains in Flamingo and its human orthologs Celsr1, Celsr2 and Celsr3; olfactomedin-like domains in the latrotoxin receptors; and five or four thrombospondin type 1 repeats in BAI1 (brain-specific angiogenesis inhibitor 1), BAI2 and BAI3. Furthermore, 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.


Pssm-ID: 320168 [Multi-domain]  Cd Length: 253  Bit Score: 293.33  E-value: 2.78e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  865 ELLLSVITWVGIVISLVCLAICISTFCFLRGLQTD-RNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFL 943
Cdd:cd15040      1 EKALSIITYIGCGLSLLGLLLTIITYILFRKLRKRkPTKILLNLCLALLLANLLFLFGINSTDNPVLCTAVAALLHYFLL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  944 AAFSWLCLEGVHLYLLLVEVFESEYSR-TKYYYLGGYCFPALVVGIAAAIDYRSYG-TEKACWLRVDNYFIWSFIGPVSF 1021
Cdd:cd15040     81 ASFMWMLVEALLLYLRLVKVFGTYPRHfILKYALIGWGLPLIIVIITLAVDPDSYGnSSGYCWLSNGNGLYYAFLGPVLL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1022 VIVVNLVFLMVTLHKMIRSSSVLkpDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFI 1101
Cdd:cd15040    161 IILVNLVIFVLVLRKLLRLSAKR--NKKKRKKTKAQLRAAVSLFFLLGLTWIFGILAIFGARVVFQYLFAIFNSLQGFFI 238
                          250
                   ....*....|....*
gi 1034606781 1102 FVFHCALQKKVHKEY 1116
Cdd:cd15040    239 FIFHCLRNKEVRKAW 253
7tmB2_GPR133-like_Adhesion_V cd15933
orphan GPR133 and related proteins, group V adhesion GPCRs, member of class B2 family of ...
865-1116 2.15e-87

orphan GPR133 and related proteins, group V adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors; group V adhesion GPCRs include orphan receptors GPR133, GPR144, and closely related proteins. The function of GPR144 has not yet been characterized, whereas GPR133 is highly expressed in the pituitary gland and is coupled to the G(s) protein, leading to activation of adenylate cyclase pathway. Moreover, genetic variations in the GPR133 have been reported to be associated with adult height and heart rate. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, 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. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320599 [Multi-domain]  Cd Length: 252  Bit Score: 284.99  E-value: 2.15e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  865 ELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLA 944
Cdd:cd15933      1 ERALSIISYIGCGISIACLALTLIIFLVLRVLSSDRFQIHKNLCVALLLAQILLLAGEWAEGNKVACKVVAILLHFFFMA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  945 AFSWLCLEGVHLYLLLVEVFeSEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIV 1024
Cdd:cd15933     81 AFSWMLVEGLHLYLMIVKVF-NYKSKMRYYYFIGWGLPAIIVAISLAILFDDYGSPNVCWLSLDDGLIWAFVGPVIFIIT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1025 VNLVFLMVTLHKMIRSSSV-LKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFIFV 1103
Cdd:cd15933    160 VNTVILILVVKITVSLSTNdAKKSQGTLAQIKSTAKASVVLLPILGLTWLFGVLVVNSQTIVFQYIFVILNSLQGLMIFL 239
                          250
                   ....*....|...
gi 1034606781 1104 FHCALQKKVHKEY 1116
Cdd:cd15933    240 FHCVLNSEVRSAF 252
7tmB2_CELSR_Adhesion_IV cd15441
cadherin EGF LAG seven-pass G-type receptors, group IV adhesion GPCRs, member of the class B2 ...
866-1121 2.39e-83

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.


Pssm-ID: 320557 [Multi-domain]  Cd Length: 254  Bit Score: 273.74  E-value: 2.39e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  866 LLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLAA 945
Cdd:cd15441      2 LLLKIVTYIGIGISLVLLVIAFLVLSCLRGLQSNSNSIHKNLVACLLLAELLFLLGINQTENLFPCKLIAILLHYFYLSA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  946 FSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIVV 1025
Cdd:cd15441     82 FSWLLVESLHLYRMLTEPRDINHGHMRFYYLLGYGIPAIIVGLSVGLRPDGYGNPDFCWLSVNETLIWSFAGPIAFVIVI 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1026 NLVFLMVTLHKMIRsssvLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFIFVFH 1105
Cdd:cd15441    162 TLIIFILALRASCT----LKRHVLEKASVRTDLRSSFLLLPLLGATWVFGLLAVNEDSELLHYLFAGLNFLQGLFIFLFY 237
                          250
                   ....*....|....*.
gi 1034606781 1106 CALQKKVHKEYSKCLR 1121
Cdd:cd15441    238 CIFNKKVRRELKNALL 253
7tm_classB cd13952
class B family of seven-transmembrane G protein-coupled receptors; The class B of ...
865-1116 7.04e-80

class B family of seven-transmembrane G protein-coupled receptors; The class B of seven-transmembrane GPCRs is classified into three major subfamilies: subfamily B1 (secretin-like receptor family), B2 (adhesion family), and B3 (Methuselah-like family). The class B receptors have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi or prokaryotes. The B1 subfamily comprises receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the subfamily B1 receptors preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. The subfamily B2 consists of cell-adhesion receptors with 33 members in humans and vertebrates. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing a variety of structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, linked to a class B seven-transmembrane domain. These include, for example, EGF (epidermal growth factor)-like domains in CD97, Celsr1 (cadherin family member), Celsr2, Celsr3, EMR1 (EGF-module-containing mucin-like hormone receptor-like 1), EMR2, EMR3, and Flamingo; two laminin A G-type repeats and nine cadherin domains in Flamingo and its human orthologs Celsr1, Celsr2 and Celsr3; olfactomedin-like domains in the latrotoxin receptors; and five or four thrombospondin type 1 repeats in BAI1 (brain-specific angiogenesis inhibitor 1), BAI2 and BAI3. 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. Furthermore, the subfamily B3 includes Methuselah (Mth) protein, which was originally identified in Drosophila as a GPCR affecting stress resistance and aging, and its closely related proteins.


Pssm-ID: 410627 [Multi-domain]  Cd Length: 260  Bit Score: 264.07  E-value: 7.04e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  865 ELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYE--IACPIFAGLLHYFF 942
Cdd:cd13952      1 DLALSIITYIGCSLSLVGLLLTIITYLLFPKLRNLRGKILINLCLSLLLAQLLFLIGQLLTSSDrpVLCKALAILLHYFL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  943 LAAFSWLCLEGVHLYLLLVEVF-ESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYG-----TEKACWLRVDNYFIWSFI 1016
Cdd:cd13952     81 LASFFWMLVEAFDLYRTFVKVFgSSERRRFLKYSLYGWGLPLLIVIITAIVDFSLYGpspgyGGEYCWLSNGNALLWAFY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1017 GPVSFVIVVNLVFLMVTLHKmIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLL-FINKESVVMAYLFTTFNA 1095
Cdd:cd13952    161 GPVLLILLVNLVFFILTVRI-LLRKLRETPKQSERKSDRKQLRAYLKLFPLMGLTWIFGILaPFVGGSLVFWYLFDILNS 239
                          250       260
                   ....*....|....*....|.
gi 1034606781 1096 FQGVFIFVFHCALQKKVHKEY 1116
Cdd:cd13952    240 LQGFFIFLIFCLKNKEVRRLL 260
7tmB2_EMR_Adhesion_II cd15931
EGF-like module receptors, group II adhesion GPCRs, member of class B2 family of ...
868-1118 4.79e-73

EGF-like module receptors, group II adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors; group II adhesion GPCRs, including the leukocyte cell-surface antigen CD97 and the epidermal growth factor (EGF)-module-containing, mucin-like hormone receptor (EMR1-4), are primarily expressed in cells of the immune system. All EGF-TM7 receptors, which belong to the B2 subfamily B2 of adhesion GPCRs, are members of group II, except for ETL (EGF-TM7-latrophilin related protein), which is classified into group I. Members of the EGF-TM7 receptors are characterized by the presence of varying numbers of N-terminal EGF-like domains, which play critical roles in ligand recognition and cell adhesion, linked by a stalk region to a class B seven-transmembrane domain. In the case of CD97, alternative splicing results in three isoforms possessing either three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. On the other hand, EMR2 generates four isoforms possessing either two (EGF1,2), three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. 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. For example, CD97, which is involved in angiogenesis and the migration and invasion of tumor cells, has been shown to promote cell aggregation in a GPS proteolysis-dependent manner. CD97 is widely expressed on lymphocytes, monocytes, macrophages, dendritic cells, granulocytes and smooth muscle cells as well as in a variety of human tumors including colorectal, gastric, esophageal pancreatic, and thyroid carcinoma. EMR2 shares strong sequence homology with CD97, differing by only six amino acids. However, unlike CD97, EMR2 is not found in those of CD97-positive tumor cells and is not expressed on lymphocytes but instead on monocytes, macrophages and granulocytes. CD97 has three known ligands: CD55, decay-accelerating factor for regulation of complement system; chondroitin sulfate, a glycosaminoglycan found in the extracellular matrix; and the integrin alpha5beta1, which play a role in angiogenesis. Although EMR2 does not effectively interact with CD55, the fourth EGF-like domain of this receptor binds to chondroitin sulfate to mediate cell attachment.


Pssm-ID: 320597 [Multi-domain]  Cd Length: 262  Bit Score: 244.73  E-value: 4.79e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  868 LSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLAAFS 947
Cdd:cd15931      4 LEWINRVGVIVSLFCLGLAIFTFLLCRWIPKINTTAHLHLCLCLSMSHTLFLAGIEYVENELACTVMAGLLHYLFLASFV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  948 WLCLEGVHLYLLLVEVFESEYSR-----TKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFV 1022
Cdd:cd15931     84 WMLLEALQLHLLVRRLTKVQVIQrdglpRPLLCLIGYGVPFLIVGVSALVYSDGYGEAKMCWLSQERGFNWSFLGPVIAI 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1023 IVVNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFIF 1102
Cdd:cd15931    164 IGINWILFCATLWCLRQTLSNMNSDISQLKDTRLLTFKAVAQLFILGCTWVLGLFQTNPVALVFQYLFTILNSLQGAFLF 243
                          250
                   ....*....|....*.
gi 1034606781 1103 VFHCALQKKVHKEYSK 1118
Cdd:cd15931    244 LVHCLLNKEVREEYIK 259
Gal_Rha_Lectin_LPHN1 cd22844
galactose/rhamnose binding lectin domain found in latrophilin-1 and similar proteins; ...
35-131 3.80e-66

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: 218.00  E-value: 3.80e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   35 MRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDP 114
Cdd:cd22844      1 MRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDP 80
                           90
                   ....*....|....*..
gi 1034606781  115 CPGTYKYLEVQYDCVPY 131
Cdd:cd22844     81 CPGTYKYLEVQYDCVPY 97
Gal_Rha_Lectin_LPHN3 cd22846
galactose/rhamnose binding lectin domain found in latrophilin-3 and similar proteins; ...
34-131 7.27e-60

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: 200.33  E-value: 7.27e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   34 LMRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPD 113
Cdd:cd22846      1 VVRRELSCESYPIELRCPGTDVIMIESANYGRTDDKICDSDPAQMENIRCYLPDAYKIMSQRCNNRTQCAVVAGPDVFPD 80
                           90
                   ....*....|....*...
gi 1034606781  114 PCPGTYKYLEVQYDCVPY 131
Cdd:cd22846     81 PCPGTYKYLEVQYECVPY 98
Gal_Rha_Lectin_LPHN2 cd22845
galactose/rhamnose binding lectin domain found in latrophilin-2 and similar proteins; ...
35-131 9.07e-60

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: 199.85  E-value: 9.07e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   35 MRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDP 114
Cdd:cd22845      1 VRRELSCEGYPIDLRCPGSDVIMIESANYGRTDDKICDADPFQMENTDCYLPDAYKIMTQRCNNRTQCIVVTGSDVFPDP 80
                           90
                   ....*....|....*..
gi 1034606781  115 CPGTYKYLEVQYDCVPY 131
Cdd:cd22845     81 CPGTYKYLEVQYECVPY 97
7tmB2_GPR133 cd15256
orphan adhesion receptor GPR133, member of the class B2 family of seven-transmembrane G ...
865-1116 7.05e-58

orphan adhesion receptor GPR133, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR133 is an orphan receptor that belongs to the group V adhesion-GPCRs together with GPR144. The function of GPR144 has not yet been characterized, whereas GPR133 is highly expressed in the pituitary gland and is coupled to the Gs protein, leading to activation of adenylyl cyclase pathway. Moreover, genetic variations in the GPR133 have been reported to be associated with adult height and heart rate. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, 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. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320384 [Multi-domain]  Cd Length: 260  Bit Score: 200.92  E-value: 7.05e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  865 ELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNT---IHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYF 941
Cdd:cd15256      1 QVALSSITYVGCSLSIFCLAITLVTFAVLSSVSTIRNQryhIHANLSFAVLVAQILLLISFRFEPGTLPCKIMAILLHFF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  942 FLAAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSF 1021
Cdd:cd15256     81 FLSAFAWMLVEGLHLYSMVIKVFGSEESKHFYYYGIGWGSPLLICIISLTSALDSYGESDNCWLSLENGAIWAFVAPALF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1022 VIVVNLVFLMVtlhkMIRSSSVLKPDSSRL----DNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQ 1097
Cdd:cd15256    161 VIVVNIGILIA----VTRVISRISADNYKVhgdaNAFKLTAKAVAVLLPILGSSWVFGVLAVNTHALVFQYMFAIFNSLQ 236
                          250
                   ....*....|....*....
gi 1034606781 1098 GVFIFVFHCALQKKVHKEY 1116
Cdd:cd15256    237 GFFIFLFHCLLNSEVRAAF 255
GAIN pfam16489
GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and ...
557-782 6.92e-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: 195.95  E-value: 6.92e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  557 NAANIASELARHTR-GSIYAGDVSSSVKLMEQLLDILDAQLQALrpieresagknynkmhkrertCKDYIKAVVETVDNL 635
Cdd:pfam16489    1 GAKELARELRNATRhGPLYGGDVLTAVELLSQLFDLLATQDATL---------------------SNAFLENFVQTVSNL 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  636 LRPEALESWKDMNATEQVHTATMLLDVLEEGAFLLADNVREPARFLAAKENVVLEVTVLNTEGQVQELV--FPQEEYPRK 713
Cdd:pfam16489   60 LDPENRESWEDLQQTERGTAATKLLRTLEEYALLLAQNMKYLTPFTIVTPNIVLSVDRLDTHNFKGARFprFPMKGERPK 139
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034606781  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 5.62e-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: 188.68  E-value: 5.62e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   36 RRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPfQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPC 115
Cdd:cd22826      1 KREIACEGYKIRLRCPGSDVIMIESANYGRTDSSTCPSDP-NMTDTNCYLPDALAIVSQRCNNRTRCNVRADSSFFPDPC 79
                           90
                   ....*....|...
gi 1034606781  116 PGTYKYLEVQYDC 128
Cdd:cd22826     80 PGTFKYLEVIYEC 92
7tmB2_CELSR1 cd15991
Cadherin EGF LAG seven-pass G-type receptor 1, member of the class B2 family of ...
866-1114 1.27e-55

Cadherin EGF LAG seven-pass G-type receptor 1, 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. 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. 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.


Pssm-ID: 320657 [Multi-domain]  Cd Length: 254  Bit Score: 194.29  E-value: 1.27e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  866 LLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLAA 945
Cdd:cd15991      2 LPLKIITYTTVSLSLVALLITFILLVLIRTLRSNLHSIHKNLVAALFFSELIFLIGINQTENPFVCTVVAILLHYFYMST 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  946 FSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIVV 1025
Cdd:cd15991     82 FAWMFVEGLHIYRMLTEVRNINTGHMRFYYVVGWGIPAIITGLAVGLDPQGYGNPDFCWLSVQDTLIWSFAGPIGIVVII 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1026 NLVFLMVTlhkmIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFIFVFH 1105
Cdd:cd15991    162 NTVIFVLA----AKASCGRRQRYFEKSGVISMLRTAFLLLLLISATWLLGLMAVNSDTLSFHYLFAIFSCLQGIFIFFFH 237

                   ....*....
gi 1034606781 1106 CALQKKVHK 1114
Cdd:cd15991    238 CIFNKEVRK 246
7tmB2_CELSR2 cd15992
Cadherin EGF LAG seven-pass G-type receptor 2, member of the class B2 family of ...
866-1119 1.00e-48

Cadherin EGF LAG seven-pass G-type receptor 2, 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. 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. 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.


Pssm-ID: 320658  Cd Length: 255  Bit Score: 174.24  E-value: 1.00e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  866 LLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLAA 945
Cdd:cd15992      2 LPLKTLTWSSVGVTLGFLLLTFLFLLCLRALRSNKTSIRKNGATALFLSELVFILGINQADNPFACTVIAILLHFFYLCT 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  946 FSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIVV 1025
Cdd:cd15992     82 FSWLFLEGLHIYRMLSEVRDINYGPMRFYYLIGWGVPAFITGLAVGLDPEGYGNPDFCWLSIYDTLIWSFAGPVAFAVSM 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1026 NlVFLMVTLHKMirSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFIFVFH 1105
Cdd:cd15992    162 N-VFLYILSSRA--SCSAQQQSFEKKKGPVSGLRTAFTVLLLVSVTCLLALLSVNSDVILFHYLFAGFNCLQGPFIFLSH 238
                          250
                   ....*....|....
gi 1034606781 1106 CALQKKVHKEYSKC 1119
Cdd:cd15992    239 VVLLKEVRKALKTL 252
7tmB2_CELSR3 cd15993
Cadherin EGF LAG seven-pass G-type receptor 3, member of the class B2 family of ...
867-1120 1.47e-48

Cadherin EGF LAG seven-pass G-type receptor 3, 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. 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 neuronal migration and axon guidance in the CNS. 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.


Pssm-ID: 320659 [Multi-domain]  Cd Length: 254  Bit Score: 173.87  E-value: 1.47e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  867 LLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLAAF 946
Cdd:cd15993      3 TLAIVTYSSVSASLAALVLTFSVLTCLRGLKSNTRGIHSNIAAALFLSELLFLLGINRTENQFLCTVVAILLHYFFLSTF 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  947 SWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIVVN 1026
Cdd:cd15993     83 AWLFVQGLHIYRMQTEARNVNFGAMRFYYAIGWGVPAIITGLAVGLDPEGYGNPDFCWISIHDKLVWSFAGPIVVVIVMN 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1027 -LVFLMV------TLHKMIRSSSVLKpdssrldNIKSwalgAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGV 1099
Cdd:cd15993    163 gVMFLLVarmscsPGQKETKKTSVLM-------TLRS----SFLLLLLISATWLFGLLAVNNSVLAFHYLHAILCCLQGL 231
                          250       260
                   ....*....|....*....|..
gi 1034606781 1100 FIFVFHCALQKKVHKEYS-KCL 1120
Cdd:cd15993    232 AVLLLFCVLNEEVQEAWKlACL 253
7tmB2_GPR112 cd15997
Probable G protein-coupled receptor 112, member of the class B2 family of seven-transmembrane ...
865-1116 8.95e-45

Probable G protein-coupled receptor 112, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR112 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include orphan GPCRs such as GPR56, GPR64, GPR97, GPR114, and GPR126. GPR112 is specifically expressed in normal enterochromatin cells and gastrointestinal neuroendocrine carcinoma cells, but its biological function is unknown. 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. Furthermore, 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.


Pssm-ID: 320663  Cd Length: 269  Bit Score: 163.68  E-value: 8.95e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  865 ELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDR-NTIHKNLCINLFLAELLFLVG--IDKTQYEIACPIFAGLLHYF 941
Cdd:cd15997      1 ERILTLITYLGCGISSIFLGITLVTYLAFEKLRRDYpSKILINLCTALLMLNLVFLLNswLSSFNNYGLCITVAAFLHYF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  942 FLAAFSWLCLEGVHLYLLLVEVFESeYSRtKY---YYLGGYCFPALVVGIAAAIDYRSYGTEKA----------CWLRVD 1008
Cdd:cd15997     81 LLASFTWMGLEAVHMYFALVKVFNI-YIP-NYilkFCIAGWGIPAVVVALVLAINKDFYGNELSsdslhpstpfCWIQDD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1009 NYFIWSFIGPVSFVIVVNL-VFLMVTLHkmIRSSSVLKPDSSR----LDNIKSwalgAIALLFLLGLTWAFGLLFINKES 1083
Cdd:cd15997    159 VVFYISVVAYFCLIFLCNIsMFITVLIQ--IRSMKAKKPSRNWkqgfLHDLKS----VASLTFLLGLTWGFAFFAWGPVR 232
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1034606781 1084 VVMAYLFTTFNAFQGVFIFVFHCALQKKVHKEY 1116
Cdd:cd15997    233 IFFLYLFSICNTLQGFFIFVFHCLMKENVRKQW 265
7tmB2_GPR126-like_Adhesion_VIII cd15258
orphan GPR126 and related proteins, group VIII adhesion GPCRs, member of the class B2 family ...
868-1117 1.40e-44

orphan GPR126 and related proteins, group VIII adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Group VIII adhesion GPCRs include orphan GPCRs such as GPR56, GPR64, GPR97, GPR112, GPR114, and GPR126. GPR56 is involved in the regulation of oligodendrocyte development and myelination in the central nervous system via coupling to G(12/13) proteins, which leads to the activation of RhoA GTPase. GPR126, on the other hand, is required for Schwann cells, but not oligodendrocyte myelination in the peripheral nervous system. Gpr64 is mainly expressed in the epididymis of male reproductive tract, and targeted deletion of GPR64 causes sperm stasis and efferent duct blockage due to abnormal fluid reabsorption, resulting in male infertility. GPR64 is also over-expressed in Ewing's sarcoma (ES), as well as upregulated in other carcinomas from kidney, prostate or lung, and promotes invasiveness and metastasis in ES via the upregulation of placental growth factor (PGF) and matrix metalloproteinase (MMP) 1. GPR97 is identified as a lymphatic adhesion receptor that is specifically expressed in lymphatic endothelium, but not in blood vascular endothelium, and is shown to regulate migration of lymphatic endothelial cells via the small GTPases RhoA and cdc42. GPR112 is specifically expressed in normal enterochromatin cells and gastrointestinal neuroendocrine carcinoma cells, but its biological function is unknown. GPR114 is mainly found in granulocytes (polymorphonuclear leukocytes), and GPR114-transfected cells induced an increase in cAMP levels via coupling to G(s) protein. 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. Furthermore, 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.


Pssm-ID: 320386 [Multi-domain]  Cd Length: 267  Bit Score: 162.97  E-value: 1.40e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  868 LSVITWVGIVISLVCLAICISTFCFLRGLQTDRNT-IHKNLCINLFLAELLFLV--GIDKTQYEIACPIFAGLLHYFFLA 944
Cdd:cd15258      4 LTFISYVGCGISAIFLAITILTYIAFRKLRRDYPSkIHMNLCAALLLLNLAFLLssWIASFGSDGLCIAVAVALHYFLLA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  945 AFSWLCLEGVHLYLLLVEVFESeYSRTKYYYLG--GYCFPALVVGIAAAIDYRSYGTEKA-----------CWLRVDNYF 1011
Cdd:cd15258     84 CLTWMGLEAFHLYLLLVKVFNT-YIRRYILKLClvGWGLPALLVTLVLSVRSDNYGPITIpngegfqndsfCWIRDPVVF 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1012 IWSFIGPVSFVIVVNLVFLMVTLHKMIRsssvLKPDSSRLDNIKSWA--LGAIALLFLLGLTWAFGLLFINKESVVMAYL 1089
Cdd:cd15258    163 YITVVGYFGLTFLFNMVMLATVLVQICR----LREKAQATPRKRALHdlLTLLGLTFLLGLTWGLAFFAWGPFNLPFLYL 238
                          250       260
                   ....*....|....*....|....*...
gi 1034606781 1090 FTTFNAFQGVFIFVFHCALQKKVHKEYS 1117
Cdd:cd15258    239 FAIFNSLQGFFIFIWYCSMKENVRKQWR 266
7tmB3_Methuselah-like cd15039
Methuselah-like subfamily B3, member of the class B family of seven-transmembrane G ...
865-1118 1.05e-43

Methuselah-like subfamily B3, member of the class B family of seven-transmembrane G protein-coupled receptors; The subfamily B3 of class B GPCRs consists of Methuselah (Mth) and its closely related proteins found in bilateria. Mth was originally identified in Drosophila as a GPCR affecting stress resistance and aging. In addition to the seven transmembrane helices, Mth contains an N-terminal extracellular domain involved in ligand binding, and a third intracellular loop (IC3) required for the specificity of G-protein coupling. Drosophila Mth mutants showed an increase in average lifespan by 35% and greater resistance to a variety of stress factors, including starvation, high temperature, and paraquat-induced oxidative toxicity. Moreover, mutations in two endogenous peptide ligands of Methuselah, Stunted A and B, showed an increased in lifespan and resistance to oxidative stress induced by dietary paraquat. These results strongly suggest that the Stunted-Methuselah system plays important roles in stress response and aging.


Pssm-ID: 410632 [Multi-domain]  Cd Length: 270  Bit Score: 160.47  E-value: 1.05e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  865 ELLLSVITWVGIVISLVCLAICISTFCFLRGLQT--DRNTIhkNLCINLFLAELLFLVGIDKT-QYEIACPIFAGLLHYF 941
Cdd:cd15039      1 SSILGILTLIGLIISLVFLLLTLAVYALLPELRNlhGKCLM--CLVLSLFVAYLLLLIGQLLSsGDSTLCVALGILLHFF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  942 FLAAFSWLCLEGVHLYLLL---VEVFESEYSRTKYYYLGGYCF--PALVVGIAAAIDY--------RSYGtEKACWLRVD 1008
Cdd:cd15039     79 FLAAFFWLNVMSFDIWRTFrgkRSSSSRSKERKRFLRYSLYAWgvPLLLVAVTIIVDFspntdslrPGYG-EGSCWISNP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1009 NYFIWSFIGPVSFVIVVNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLL-FINKESVVMA 1087
Cdd:cd15039    158 WALLLYFYGPVALLLLFNIILFILTAIRIRKVKKETAKVQSRLRSDKQRFRLYLKLFVIMGVTWILEIIsWFVGGSSVLW 237
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1034606781 1088 YLFTTFNAFQGVFIFV-FHCalQKKVHKEYSK 1118
Cdd:cd15039    238 YIFDILNGLQGVFIFLiFVC--KRRVLRLLKK 267
7tmB2_GPR144 cd15255
orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G ...
865-1112 1.67e-41

orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR144 is an orphan receptor that belongs to the group V adhesion-GPCRs together with GPR133. The function of GPR144 has not yet been characterized, whereas GPR133 is highly expressed in the pituitary gland and is coupled to the Gs protein, leading to activation of adenylyl cyclase pathway. Moreover, genetic variations in the GPR133 have been reported to be associated with adult height and heart rate. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, 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. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320383 [Multi-domain]  Cd Length: 263  Bit Score: 153.85  E-value: 1.67e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  865 ELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLA 944
Cdd:cd15255      1 EATLRTLSFIGCGVSLCALIVTFILFLAVGVPKSERTTVHKNLIFALAAAEFLLMFSEWAKGNQVACWAVTALLHLFFLA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  945 AFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIV 1024
Cdd:cd15255     81 AFSWMLVEGLLLWSKVVAVNMSEDRRMKFYYVTGWGLPVVIVAVTLATSFNKYVADQHCWLNVQTDIIWAFVGPVLFVLT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1025 VNLVFL----MVTLHKMIRSSSVLKPDSSRLDNI--KSWALG--AIALLFLLGLTWAFGLLFinKESVVMAYLFTTFNAF 1096
Cdd:cd15255    161 VNTFVLfrvvMVTVSSARRRAKMLTPSSDLEKQIgiQIWATAkpVLVLLPVLGLTWLCGVLV--HLSDVWAYVFITLNSF 238
                          250
                   ....*....|....*.
gi 1034606781 1097 QGVFIFVFHCALQKKV 1112
Cdd:cd15255    239 QGLYIFLVYAIYNSEV 254
7tmB2_GPR126 cd15996
orphan adhesion receptor GPR126, member of the class B2 family of seven-transmembrane G ...
867-1120 4.33e-37

orphan adhesion receptor GPR126, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR126 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include orphan GPCRs such as GPR56, GPR64, GPR97, GPR112, and GPR114. GPR126 is required in Schwann cells for proper differentiation and myelination via G-Protein Activation. GPR126 is believed to couple to G(s)-protein, which leads to activation of adenylate cyclase for cAMP production. 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. Furthermore, 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.


Pssm-ID: 320662  Cd Length: 271  Bit Score: 141.56  E-value: 4.33e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  867 LLSVITWVGIVISLVCLAICISTFCFLRGLQTDR-NTIHKNLCINLFLAELLFLVGIDKTQYEIA--CPIFAGLLHYFFL 943
Cdd:cd15996      3 VLTFITYIGCGISAIFSAATLLTYIAFEKLRRDYpSKILMNLSTALLFLNLVFLLDGWIASFEIDelCITVAVLLHFFLL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  944 AAFSWLCLEGVHLYLLLVEVFESEYSRTKYYY-LGGYCFPALVVGIAAAI------------DYRSYGTEKACWLRVDNY 1010
Cdd:cd15996     83 ATFTWMGLEAIHMYIALVKVFNTYIRRYILKFcIIGWGLPALIVSIVLAStndnygygyygkDKDGQGGDEFCWIKNPVV 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1011 FIWSFIGPVSFVIVVNLVFLMVTLHKMI-----RSSSVLKPDSSRldNIKSwalgAIALLFLLGLTWAFGLLFINKESVV 1085
Cdd:cd15996    163 FYVTCAAYFGIMFLMNVAMFIVVMVQICgrngkRSNRTLREEILR--NLRS----VVSLTFLLGMTWGFAFFAWGPVNLA 236
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1034606781 1086 MAYLFTTFNAFQGVFIFVFHCALQKKVHKEYSKCL 1120
Cdd:cd15996    237 FMYLFTIFNSLQGLFIFVFHCALKENVQKQWRRHL 271
7tmB1_hormone_R cd15041
The subfamily B1 of hormone receptors (secretin-like), member of the class B family ...
866-1122 8.74e-37

The subfamily B1 of hormone receptors (secretin-like), member of the class B family seven-transmembrane G protein-coupled receptors; The B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of this subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. Moreover, the B1 subfamily receptors play key roles in hormone homeostasis and are promising drug targets in various human diseases including diabetes, osteoporosis, obesity, neurodegenerative conditions (Alzheimer###s and Parkinson's), cardiovascular disease, migraine, and psychiatric disorders (anxiety, depression). Furthermore, the subfamilies B2 and B3 consist of receptors that are capable of interacting with epidermal growth factors (EGF) and the Drosophila melanogaster Methuselah gene product (Mth), respectively. The class B GPCRs have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi, or prokaryotes.


Pssm-ID: 341321 [Multi-domain]  Cd Length: 273  Bit Score: 140.44  E-value: 8.74e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  866 LLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCI-----NLFLAELLFLVGIDKT----------QYEIA 930
Cdd:cd15041      2 LVVYYIYLVGYSLSLVALLPAIVIFLYFRSLRCTRIRLHINLFLsfilrAVFWIIWDLLVVYDRLtssgvetvlmQNPVG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  931 CPIFAGLLHYFFLAAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIdyRSYGTEKACWL-RVDN 1009
Cdd:cd15041     82 CKLLSVLKRYFKSANYFWMLCEGLYLHRLIVVAFFSEPSSLKLYYAIGWGLPLVIVVIWAIV--RALLSNESCWIsYNNG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1010 YFIWSFIGPVSFVIVVNLVFLM----VTLHKMiRSSSVLKPdssrlDNIKSWALGAIALLFLLGLTWafgLLFI----NK 1081
Cdd:cd15041    160 HYEWILYGPNLLALLVNLFFLInilrILLTKL-RSHPNAEP-----SNYRKAVKATLILIPLFGIQY---LLTIyrppDG 230
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1034606781 1082 ESVVMAYLFTT--FNAFQGVFIFVFHCALQKKVHKEYSKCLRH 1122
Cdd:cd15041    231 SEGELVYEYFNaiLNSSQGFFVAVIYCFLNGEVQSELKRKWSR 273
7tmB2_GPR116-like_Adhesion_VI cd15932
orphan GPR116 and related proteins, group IV adhesion GPCRs, member of the class B2 family of ...
865-1112 3.39e-35

orphan GPR116 and related proteins, group IV adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors; group VI adhesion GPCRs consist of orphan receptors GPR110, GPR111, GPR113, GPR115, GPR116, and closely related proteins. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. GPR110 possesses a SEA box in the N-terminal has been identified as an oncogene over-expressed in lung and prostate cancer. GPR113 contains a hormone binding domain and one EGF (epidermal grown factor) domain. GPR112 has extremely long N-terminus (about 2,400 amino acids) containing a number of Ser/Thr-rich glycosylation sites and a pentraxin (PTX) domain. GPR116 has two C2-set immunoglobulin-like repeats, which is found in the members of the immunoglobulin superfamily of cell surface proteins, and a SEA (sea urchin sperm protein, enterokinase, and a grin)-box, which is present in the extracellular domain of the transmembrane mucin (MUC) family and known to enhance O-glycosylation. In addition, 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. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320598 [Multi-domain]  Cd Length: 268  Bit Score: 135.90  E-value: 3.39e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  865 ELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHK------NLCINLFLAELLFLVGI---DKTQYEIACPIFA 935
Cdd:cd15932      1 SPALDYITYVGLGISILSLVLCLIIEALVWKSVTKNKTSYMrhvclvNIALSLLIADIWFIIGAaisTPPNPSPACTAAT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  936 GLLHYFFLAAFSWLCLEGVHLYLLLVEVFeSEYSRTKYYYLG---GYCFPAL--VVGIAAAIDYRSYGTEKACWLRVD-N 1009
Cdd:cd15932     81 FFIHFFYLALFFWMLTLGLLLFYRLVLVF-HDMSKSTMMAIAfslGYGCPLIiaIITVAATAPQGGYTRKGVCWLNWDkT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1010 YFIWSFIGPVSFVIVVNLVFLMVTLHKMIRSS---SVLKPDSSRLDNI-KSWALgaiaLLFLLGLTWAFGL-LFINKESV 1084
Cdd:cd15932    160 KALLAFVIPALAIVVVNFIILIVVIFKLLRPSvgeRPSKDEKNALVQIgKSVAI----LTPLLGLTWGFGLgTMIDPKSL 235
                          250       260
                   ....*....|....*....|....*...
gi 1034606781 1085 VMAYLFTTFNAFQGVFIFVFHCALQKKV 1112
Cdd:cd15932    236 AFHIIFAILNSFQGFFILVFGTLLDSKV 263
7tmB2_GPR64 cd15444
orphan adhesion receptor GPR64 and related proteins, member of subfamily B2 of the class B ...
866-1120 1.32e-34

orphan adhesion receptor GPR64 and related proteins, member of subfamily B2 of the class B secretin-like receptors of seven-transmembrane G protein-coupled receptors; GPR64 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include orphan GPCRs such as GPR56, GPR97, GPR112, GPR114, and GPR126. GPR64 is mainly expressed in the epididymis of male reproductive tract, and targeted deletion of GPR64 causes sperm stasis and efferent duct blockage due to abnormal fluid reabsorption, resulting in male infertility. GPR64 is also over-expressed in Ewing's sarcoma (ES), as well as upregulated in other carcinomas from kidney, prostate or lung, and promotes invasiveness and metastasis in ES via the upregulation of placental growth factor (PGF) and matrix metalloproteinase (MMP) 1. 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. Furthermore, 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.


Pssm-ID: 320560 [Multi-domain]  Cd Length: 271  Bit Score: 134.18  E-value: 1.32e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  866 LLLSVITWVGIVISLVCLAICISTFCFLRGLQTDR-NTIHKNLCINLFLAELLFLVGIDKTQYEIA---CPIFAGLLHYF 941
Cdd:cd15444      2 LILTFITYIGCGLSAIFLSVTLVTYIAFEKIRRDYpSKILIQLCVALLLLNLVFLLDSWIALYKDIvglCISVAVFLHYF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  942 FLAAFSWLCLEGVHLYLLLVEVFESeYSRtKY---YYLGGYCFPALVVGIAAAIDYRSYG-----------TEKACWLRV 1007
Cdd:cd15444     82 LLVSFTWMGLEAFHMYLALVKVFNT-YIR-KYilkFCIVGWGVPAVVVAIVLAVSKDNYGlgsygkspngsTDDFCWINN 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1008 DNYFIWSFIGPVSFVIVVNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSwaLGAIA-LLFLLGLTWAFGLLFINKESVVM 1086
Cdd:cd15444    160 NIVFYITVVGYFCVIFLLNISMFIVVLVQLCRIKKQKQLGAQRKTSLQD--LRSVAgITFLLGITWGFAFFAWGPVNLAF 237
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1034606781 1087 AYLFTTFNAFQGVFIFVFHCALQKKVHKEYSKCL 1120
Cdd:cd15444    238 MYLFAIFNTLQGFFIFIFYCVAKENVRKQWRRYL 271
7tmB2_GPR128 cd15257
orphan adhesion receptor GPR128, member of the class B2 family of seven-transmembrane G ...
868-1120 1.09e-32

orphan adhesion receptor GPR128, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR128 is an orphan receptor of the adhesion family (subclass B2) that belongs to the class B GPCRs. Expression of GPR128 was detected in the mouse intestinal mucosa and is thought to be involved in energy balance, as its knockout mice showed a decrease in body weight gain and an increase in intestinal contraction frequency compared to wild-type controls. 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. These include, for example, EGF (epidermal growth factor)-like domains in CD97, Celsr1 (cadherin family member), Celsr2, Celsr3, EMR1 (EGF-module-containing mucin-like hormone receptor-like 1), EMR2, EMR3, and Flamingo; two laminin A G-type repeats and nine cadherin domains in Flamingo and its human orthologs Celsr1, Celsr2 and Celsr3; olfactomedin-like domains in the latrotoxin receptors; and five or four thrombospondin type 1 repeats in BAI1 (brain-specific angiogenesis inhibitor 1), BAI2 and BAI3. Furthermore, 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.


Pssm-ID: 320385 [Multi-domain]  Cd Length: 303  Bit Score: 129.61  E-value: 1.09e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  868 LSVITWVGIVISLVCLAICISTFCFLRGLQTDRNT-IHKNLCINLFLAELLFLVGIDKT--QYEIA-------------- 930
Cdd:cd15257      4 LDIISTIGCVLSIAGLVITIIFHLHTRKLRKSSVTwVLLNLCSSLLLFNIIFTSGVENTnnDYEIStvpdretntvllse 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  931 ---------CPIFAGLLHYFFLAAFSWLCLEGVHLYLLLVEVFES--EYSrTKYYYLGGYCFPALVVGIAAAIDYR---- 995
Cdd:cd15257     84 eyvepdtdvCTAVAALLHYFLLVTFMWNAVYSAQLYLLLIRMMKPlpEMF-ILQASAIGWGIPAVVVAITLGATYRfpts 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  996 ------SYGTEKACWLRV-DNYF------IWSFIGPVSFVIVVNLVFLMVTLHKMIRSSSVLKpdSSRLDNIKSWALGAI 1062
Cdd:cd15257    163 lpvftrTYRQEEFCWLAAlDKNFdikkplLWGFLLPVGLILITNVILFIMTSQKVLKKNNKKL--TTKKRSYMKKIYITV 240
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034606781 1063 ALLFLLGLTWAFG-LLFINKES--VVMAYLFTTFNAFQGVFIFVFHCALQKKVHKEYSKCL 1120
Cdd:cd15257    241 SVAVVFGITWILGyLMLVNNDLskLVFSYIFCITNTTQGVQIFILYTWRTPEFRKLVSKLS 301
7tmB2_GPR113 cd15253
orphan adhesion receptor GPR113, member of the class B2 family of seven-transmembrane G ...
865-1112 2.34e-32

orphan adhesion receptor GPR113, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR113 is an orphan receptor that belongs to group VI adhesion-GPCRs along with GPR110, GPR111, GPR115, and GPR116. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. GPR113 contains a hormone binding domain and one EGF (epidermal grown factor) domain, and is primarily expressed in a subset of taste receptor cells. In addition, 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. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320381 [Multi-domain]  Cd Length: 271  Bit Score: 127.57  E-value: 2.34e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  865 ELLLSVITWVGIVISLVCLAICISTFCFLRGLQTdRNTIHK-------NLCINLFLAELLFLVG--IDKTQYEIACPIFA 935
Cdd:cd15253      1 SFWLDFLSQVGLGASILALLLCLGIYRLVWRSVV-RNKISYfrhmtlvNIAFSLLLADTCFLGAtfLSAGHESPLCLAAA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  936 GLLHYFFLAAFSWLCLEGVHLYLLLVEVFE--SEYSRTKYYYLGGYCFPALVVGIAAAIDY--RSYGTEKACWLRVDNYF 1011
Cdd:cd15253     80 FLCHFFYLATFFWMLVQALMLFHQLLFVFHqlAKRSVLPLMVTLGYLCPLLIAAATVAYYYpkRQYLHEGACWLNGESGA 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1012 IWSFIGPVSFVIVVNLVFLMVTLHKMIRSSSVLKPDSSrldniKSWALGAI--ALLFL---LGLTWAFGL-LFINKESVV 1085
Cdd:cd15253    160 IYAFSIPVLAIVLVNLLVLFVVLMKLMRPSVSEGPPPE-----ERKALLSIfkALLVLtpvFGLTWGLGVaTLTGESSQV 234
                          250       260
                   ....*....|....*....|....*..
gi 1034606781 1086 MAYLFTTFNAFQGVFIFVFHCALQKKV 1112
Cdd:cd15253    235 SHYGFAILNAFQGVFILLFGCLMDKKV 261
7tmB2_BAI_Adhesion_VII cd15251
brain-specific angiogenesis inhibitors, group VII adhesion GPCRs, member of the class B2 ...
869-1119 3.25e-32

brain-specific angiogenesis inhibitors, group VII adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all 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. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediate direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions.


Pssm-ID: 320379  Cd Length: 253  Bit Score: 126.60  E-value: 3.25e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  869 SVITWVGIVIS-LVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLAAFS 947
Cdd:cd15251      5 SVTLIVGCGVScLALLTLLAIYAAFWRYIRSERSIILINFCLSIISSNILILVGQTQTLNKGVCTMTAAFLHFFFLSSFC 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  948 WLCLEGVHLYLLLVEVFESEYSRTKYYYLgGYCFPALVVGIAAAID-YRSYGTEKACWLRVDNYFIWSFIGPVSFVIVVN 1026
Cdd:cd15251     85 WVLTEAWQSYMAVTGRMRTRLIRKRFLCL-GWGLPALVVAVSVGFTrTKGYGTSSYCWLSLEGGLLYAFVGPAAAVVLVN 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1027 LVFLMVTLHKMIRSSSVlkpdssrLDNIKSWALGAIALLFLLGLTWAFGLLFI-NKESVVMAYLFTTFNAFQGVFIFVFH 1105
Cdd:cd15251    164 MVIGILVFNKLVSRDGI-------SDNAMASLWSSCVVLPLLALTWMSAVLAMtDRRSVLFQILFAVFDSLQGFVIVMVH 236
                          250
                   ....*....|....
gi 1034606781 1106 CALQKKVhKEYSKC 1119
Cdd:cd15251    237 CILRREV-QDAVKC 249
7tmB2_GPR97 cd15442
orphan adhesion receptor GPR97, member of the class B2 family of seven-transmembrane G ...
868-1104 3.65e-32

orphan adhesion receptor GPR97, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR97 is an orphan receptor that has been classified into the group VIII of adhesion GPCRs. Other members of the Group VII include GPR56, GPR64, GPR112, GPR114, and GPR126. GPR97 is identified as a lymphatic adhesion receptor that is specifically expressed in lymphatic endothelium, but not in blood vascular endothelium, and is shown to regulate migration of lymphatic endothelial cells via the small GTPases RhoA and cdc42. 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. Furthermore, 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.


Pssm-ID: 320558 [Multi-domain]  Cd Length: 277  Bit Score: 127.22  E-value: 3.65e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  868 LSVITWVGIVISLVCLAICISTFCFLR----GLQTDRNT-IHKNLCINLFLAELLFLV--GIDKTQYEIACPIFAGLLHY 940
Cdd:cd15442      4 LVTISSAGCGVSMVFLIFTIILYFFLRftyqKFKSEDAPkIHVNLSSSLLLLNLAFLLnsGVSSRAHPGLCKALGGVTHY 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  941 FFLAAFSWLCLEGVHLYLLLVEVFESEYSrtkYYY----LGGYCFPALVVGIAAAIDyrSYG-----------TEKACWL 1005
Cdd:cd15442     84 FLLCCFTWMAIEAFHLYLLAIKVFNTYIH---HYFaklcLVGWGFPALVVTITGSIN--SYGaytimdmanrtTLHLCWI 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1006 RVDN----------YFIWSFI-GPVSFVIVVNLVFlmvtlhkMIRSSSVLKpdssrlDNIKSW--ALGAIALLFLLGLTW 1072
Cdd:cd15442    159 NSKHltvhyitvcgYFGLTFLfNTVVLGLVAWKIF-------HLQSATAGK------EKCQAWkgGLTVLGLSCLLGVTW 225
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1034606781 1073 AFGLLFINKESVVMAYLFTTFNAFQGVFIFVF 1104
Cdd:cd15442    226 GLAFFTYGSMSVPTVYIFALLNSLQGLFIFIW 257
Gal_Lectin pfam02140
Galactose binding lectin domain;
48-128 9.76e-32

Galactose binding lectin domain;


Pssm-ID: 460460 [Multi-domain]  Cd Length: 79  Bit Score: 118.93  E-value: 9.76e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   48 LRCPGSDVIMVENANYGRTDDKICdadPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAF-PDPCPGTYKYLEVQY 126
Cdd:pfam02140    1 LSCPPGKVISILFASYGRPDGTTC---PSFIQGTNCHSPNSLAIVSKACQGKNSCSVPASNSVFgGDPCPGTYKYLEVEY 77

                   ..
gi 1034606781  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 1.87e-31

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: 118.71  E-value: 1.87e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   36 RRELACEGYPIELRCpGSDVIMVENANYGRTDDKICDAD--PFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAgSDAFPD 113
Cdd:cd22834      3 KTSITCEGSPVSLDC-GPDVIKIYDANYGRRDSTTCSHGrpESQLTNTNCYLPETTKVMSERCNGKSLCDLLA-SNVVTD 80
                           90
                   ....*....|....*
gi 1034606781  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 2.92e-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: 2.92e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   40 ACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCPGTY 119
Cdd:cd22823      3 ACEGETLTLSCPSGQVIKILSAFYGRTDGTTCCCGPNNTSDTNCCSPDVLDIVKELCDGKQSCSVPASNSVFGDPCPGTS 82

                   ....*....
gi 1034606781  120 KYLEVQYDC 128
Cdd:cd22823     83 KYLEVTYTC 91
7tmB2_BAI2 cd15988
brain-specific angiogenesis inhibitor 2, a group VII adhesion GPCR, member of the class B2 ...
869-1119 1.36e-30

brain-specific angiogenesis inhibitor 2, a group VII adhesion GPCR, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all 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. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediates direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions.


Pssm-ID: 320654 [Multi-domain]  Cd Length: 291  Bit Score: 123.14  E-value: 1.36e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  869 SVITWVGIVISLVCLAICISTFC-FLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLAAFS 947
Cdd:cd15988      5 SVPLMIGCAVSCMALLILLAIYAaFWRFIRSERSIILLNFCLSILASNILILVGQSQTLSKGVCTMTAAFLHFFFLSSFC 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  948 WLCLEGVHLYLLLVEVFESEYSRTKYYYLgGYCFPALVVGIAAAID-YRSYGTEKACWLRVDNYFIWSFIGPVSFVIVVN 1026
Cdd:cd15988     85 WVLTEAWQSYLAVIGRMRTRLVRKRFLCL-GWGLPALVVAVSVGFTrTKGYGTASYCWLSLEGGLLYAFVGPAAVIVLVN 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1027 LVFLMVTLHKMI------------RSSSVLKPDSSRLdnIKSWALGAIA---------------------LLFLLGLTWA 1073
Cdd:cd15988    164 MLIGIIVFNKLMsrdgisdkskkqRAGSEAEPCSSLL--LKCSKCGVVSsaamssatassamaslwsscvVLPLLALTWM 241
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1034606781 1074 FGLLFI-NKESVVMAYLFTTFNAFQGVFIFVFHCALQKKVhKEYSKC 1119
Cdd:cd15988    242 SAVLAMtDRRSILFQVLFAVFNSVQGFVIITVHCFLRREV-QDVVKC 287
7tmB1_CRF-R cd15264
corticotropin-releasing factor receptors, member of the class B family of seven-transmembrane ...
869-1114 6.15e-30

corticotropin-releasing factor receptors, member of the class B family of seven-transmembrane G protein-coupled receptors; The vertebrate corticotropin-releasing factor (CRF) receptors are predominantly expressed in central nervous system with high levels in cortex tissue, brain stem, and pituitary. They have two isoforms as a result of alternative splicing of the same receptor gene: CRF-R1 and CRF-R2, which differ in tissue distribution and ligand binding affinities. Recently, a third CRF receptor (CRF-R3) has been identified in catfish pituitary. The catfish CRF-R1 is highly homologous to CRF-R3. CRF is a 41-amino acid neuropeptide that plays a central role in coordinating neuroendocrine, behavioral, and autonomic responses to stress by acting as the primary neuroregulator of the hypothalamic-pituitary-adrenal axis, which controls the levels of cortisol and other stress related hormones. In addition, the CRF family of neuropeptides also includes structurally related peptides such as mammalian urocortin, fish urotensin I, and frog sauvagine. The actions of CRF and CRF-related peptides are mediated through specific binding to CRF-R1 and CRF-R2. CRF and urocortin 1 bind and activate mammalian CRF-R1 with similar high affinities. By contrast, urocortin 2 and urocortin 3 do not bind to CRF-R1 or stimulate CRF-R1-mediated cAMP formation. Urocortin 1 also shows high affinity for mammalian CRF-R2, whereas CRF has significantly lower affinity for this receptor. These evidence suggest that urocortin 1 is an endogenous ligand for CRF-R1 and CRF-R2. The CRF receptors are members of the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, and parathyroid hormone (PTH). These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on its cellular location and function, CRF receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320392 [Multi-domain]  Cd Length: 265  Bit Score: 120.60  E-value: 6.15e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  869 SVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLV------GIDKTQYEIACPIFAGLLHYFF 942
Cdd:cd15264      5 LIIYYLGFSISLVALAVALIIFLYFRSLRCLRNNIHCNLIVTFILRNVTWFImqntltEIHHQSNQWVCRLIVTVYNYFQ 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  943 LAAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVgIAAAIDYRSYGTEKaCWL--RVDNYFIWSFIGPVS 1020
Cdd:cd15264     85 VTNFFWMFVEGLYLHTMIVWAYSADKIRFWYYIVIGWCIPCPFV-LAWAIVKLLYENEH-CWLpkSENSYYDYIYQGPIL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1021 FVIVVNLVFL---MVTLHKMIRSSSVLKPDSSRlDNIKSwalgAIALLFLLGLTWAfgLLFINKESVVMAYL-FTTFNA- 1095
Cdd:cd15264    163 LVLLINFIFLfniVWVLITKLRASNTLETIQYR-KAVKA----TLVLLPLLGITYM--LFFINPGDDKTSRLvFIYFNTf 235
                          250       260       270
                   ....*....|....*....|....*....|
gi 1034606781 1096 ---FQGVFIFVFHC--------ALQKKVHK 1114
Cdd:cd15264    236 lqsFQGLFVAVFYCflngevrsAIRKKFSR 265
7tmB1_DH_R cd15263
insect diuretic hormone receptors, member of the class B family of seven-transmembrane G ...
869-1112 6.63e-29

insect diuretic hormone receptors, member of the class B family of seven-transmembrane G protein-coupled receptors; This group includes G protein-coupled receptors that specifically bind to insect diuretic hormones found in Manduca sexta (moth) and Acheta domesticus (the house cricket), among others. Insect diuretic hormone and their GPCRs play critical roles in the regulation of water and ion balance. Thus they are attractive targets for developing new insecticides. Activation of the diuretic hormone receptors stimulate adenylate cyclase, thereby increasing cAMP levels in Malpighian tube. They belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of Gs family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx.


Pssm-ID: 320391 [Multi-domain]  Cd Length: 272  Bit Score: 117.86  E-value: 6.63e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  869 SVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFL----VGIDKTQYEIACPIFAGLLHYFFLA 944
Cdd:cd15263      5 TTIYFIGYSLSLVALSLALWIFLYFKDLRCLRNTIHTNLMFTYILADLTWIltltLQVSIGEDQKSCIILVVLLHYFHLT 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  945 AFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVV---GIAAAI-------DYRSYGTEKAC-WLRVDNYfIW 1013
Cdd:cd15263     85 NFFWMFVEGLYLYMLVVETFSGENIKLRVYAFIGWGIPAVVIviwAIVKALaptapntALDPNGLLKHCpWMAEHIV-DW 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1014 SFIGPVSFVIVVNLVFL---MVTLHKMIRSSSVLKPDSSRldnikswaLGAIALLF---LLGLTWAfgLLFINKESVVMA 1087
Cdd:cd15263    164 IFQGPAILVLAVNLVFLvriMWVLITKLRSANTVETQQYR--------KAAKALLVlipLLGITYI--LVIAGPTEGIAA 233
                          250       260
                   ....*....|....*....|....*....
gi 1034606781 1088 YLFTTFNAF----QGVFIFVFHCALQKKV 1112
Cdd:cd15263    234 NIFEYVRAVllstQGFTVALFYCFLNTEV 262
Gal_Rha_Lectin_SUL-I-like cd22827
galactose/rhamnose binding lectin domain found in Toxopneustes pileolus rhamnose-binding ...
38-128 8.61e-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: 8.61e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   38 ELACEGYPIELRCPGSDVIMVENANYGRTDDKICdadP-FQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCP 116
Cdd:cd22827      1 KRVCEGQTLTISCPAGKVIDIVSANYGRTDSSTC---PsGGIKNTNCRASNSLSIVRNRCNGKRSCSVKASNSVFGDPCV 77
                           90
                   ....*....|..
gi 1034606781  117 GTYKYLEVQYDC 128
Cdd:cd22827     78 GTYKYLEVRYRC 89
7tmB2_GPR116_Ig-Hepta cd15254
The immunoglobulin-repeat-containing receptor Ig-hepta/GPR116, member of the class B2 family ...
867-1112 8.93e-29

The immunoglobulin-repeat-containing receptor Ig-hepta/GPR116, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR116 (also known as Ig-hepta) is an orphan receptor that belongs to group VI adhesion-GPCRs along with GPR110, GPR111, GPR113, and GPR115. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. GPR116 has four I-set immunoglobulin-like repeats, which is found in the members of the immunoglobulin superfamily of cell surface proteins, and a SEA (sea urchin sperm protein, enterokinase, and a grin)-box, which is present in the extracellular domain of the transmembrane mucin (MUC) family and known to enhance O-glycosylation. GPR116 is highly expressed in fetal and adult lung, and it has been shown to regulate lung surfactant levels as well as to stimulate breast cancer metastasis through a G(q)-p63-RhoGEF-Rho GTPase signaling pathway. In addition, 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. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320382 [Multi-domain]  Cd Length: 275  Bit Score: 117.60  E-value: 8.93e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  867 LLSVITWVGIVISLVCLAICISTFCFL-RGLQTDRNTIHKNLCI-----NLFLAELLFLV--GIDKTQYEI---ACPIFA 935
Cdd:cd15254      3 ELDYITYIGLSISILSLAICIVIESLVwKSVTKNRTSYMRHVCIlniavSLLIADIWFIVvaAIQDQNYAVngnVCVAAT 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  936 GLLHYFFLAAFSWLCLEGVHLYLLLVEVFEsEYSRTKYYYLG---GYCFPAL--VVGIAAAIDYRSYGTEKACWLR-VDN 1009
Cdd:cd15254     83 FFIHFFYLCVFFWMLALGLMLFYRLVFILH-DTSKTIQKAVAfclGYGCPLIisVITIAVTLPRDSYTRKKVCWLNwEDS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1010 YFIWSFIGPVSFVIVVNLVFLMVTLHKMIRSSSVLKP----DSSRLDNIKSWALgaiaLLFLLGLTWAFGLLFINKES-V 1084
Cdd:cd15254    162 KALLAFVIPALIIVAVNSIITVVVIVKILRPSIGEKPskqeRSSLFQIIKSIGV----LTPLLGLTWGFGLATVIKGSsI 237
                          250       260
                   ....*....|....*....|....*...
gi 1034606781 1085 VMAYLFTTFNAFQGVFIFVFHCALQKKV 1112
Cdd:cd15254    238 VFHILFTLLNAFQGLFILVFGTLWDKKV 265
7tmB1_NPR_B4_insect-like cd15260
insect neuropeptide receptor subgroup B4 and related proteins, member of the class B family of ...
874-1079 2.00e-28

insect neuropeptide receptor subgroup B4 and related proteins, member of the class B family of seven-transmembrane G protein-coupled receptors; This subgroup includes a neuropeptide receptor found in Nilaparvata lugens (brown planthopper) and its closely related proteins from mollusks and annelid worms. They belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. The class B GPCRs have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi, or prokaryotes.


Pssm-ID: 320388 [Multi-domain]  Cd Length: 267  Bit Score: 116.22  E-value: 2.00e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  874 VGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLV-------GIDKTQY-EIACPIFAGLLHYFFLAA 945
Cdd:cd15260     10 GGYSVSLIALIISLAIFFSFRSLRCTRITIHMNLFISFALNNLLWIVwyklvvdNPEVLLEnPIWCQALHVLLQYFMVCN 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  946 FSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFiWSFIGPVSFVIVV 1025
Cdd:cd15260     90 YFWMFCEGLYLHTVLVVAFISEKSLMRWFIAIGWGVPLVITAIYAGVRASLPDDTERCWMEESSYQ-WILIVPVVLSLLI 168
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034606781 1026 NLVFLM----VTLHKMIRSSSVLKPDSSRLdnikswALGAIALLFLLgltwaFGLLFI 1079
Cdd:cd15260    169 NLIFLInivrVLLTKLRATSPNPAPAGLRK------AVRATLILIPL-----LGLQFL 215
Gal_Rha_Lectin_dCirl cd22830
galactose/rhamnose binding lectin domain found in Drosophila melanogaster Latrophilin Cirl and ...
40-128 2.84e-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: 109.63  E-value: 2.84e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   40 ACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCPGTY 119
Cdd:cd22830      4 ACEGSQLTLECEDGTVIRIIRANYGRFSIAICNDHGNTDWSVNCMSPRSLRVVQERCDGKRSCSIPASSSVFGDPCPGTP 83

                   ....*....
gi 1034606781  120 KYLEVQYDC 128
Cdd:cd22830     84 KYLEVHYQC 92
7tmB2_BAI1 cd15990
brain-specific angiogenesis inhibitor 1, a group VII adhesion GPCR, member of the class B2 ...
866-1119 4.41e-28

brain-specific angiogenesis inhibitor 1, a group VII adhesion GPCR, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all 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. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediates direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions.


Pssm-ID: 320656  Cd Length: 267  Bit Score: 115.09  E-value: 4.41e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  866 LLLSVITWVGI-VISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLA 944
Cdd:cd15990      5 LLPSVTLIVGCgVSSLTLLLLIIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLS 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  945 AFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLgGYCFPALVVGIAAAI-DYRSYGTEKACWLRVDNYFIWSFIGPVSFVI 1023
Cdd:cd15990     85 SFCWVLTEAWQSYMAVTGRLRNRIIRKRFLCL-GWGLPALVVAISVGFtKAKGYGTVNYCWLSLEGGLLYAFVGPAAAVV 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1024 VVNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWAlgAIALLFLLGLTWAFGLLFI-NKESVVMAYLFTTFNAFQGVFIF 1102
Cdd:cd15990    164 LVNMVIGILVFNKLVSKDGITDKKLKERAGASLWS--SCVVLPLLALTWMSAVLAItDRRSALFQILFAVFDSLEGFVIV 241
                          250
                   ....*....|....*..
gi 1034606781 1103 VFHCALQKKVhKEYSKC 1119
Cdd:cd15990    242 MVHCILRREV-QDAVKC 257
Gal_Rha_Lectin_RBL_rpt2 cd22836
second galactose/rhamnose binding lectin domain found in Silurus asotus rhamnose-binding ...
36-128 8.58e-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: 108.53  E-value: 8.58e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   36 RRELACEGYPIELRCpGSDVIMVENANYGRTDDKICDADP--FQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPD 113
Cdd:cd22836      2 RTSVTCEGGYAVLKC-GSGVIQIISANYGRTDSTTCSAGRpaSQVQNTNCYASNSLAIVSQSCNGKKSCTVSASNSVFSD 80
                           90
                   ....*....|....*
gi 1034606781  114 PCPGTYKYLEVQYDC 128
Cdd:cd22836     81 PCVGTYKYLYVTYSC 95
7tmB2_GPR124-like_Adhesion_III cd15259
orphan GPR124 and related proteins, group III adhesion GPCRs, member of class B2 family of ...
867-1119 4.52e-27

orphan GPR124 and related proteins, group III adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors; group III adhesion GPCRs include orphan GPR123, GPR124, GPR125, and their closely related proteins. 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. Furthermore, 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. GPR123 is predominantly expressed in the CNS including thalamus, brain stem and regions containing large pyramidal cells. GPR124, also known as tumor endothelial marker 5 (TEM5), is highly expressed in tumor vessels and in the vasculature of the developing embryo. GPR124 is essentially required for proper angiogenic sprouting into neural tissue, CNS-specific vascularization, and formation of the blood-brain barrier. GPR124 also interacts with the PDZ domain of DLG1 (discs large homolog 1) through its PDZ-binding motif. Recently, studies of double-knockout mice showed that GPR124 functions as a co-activator of Wnt7a/Wnt7b-dependent beta-catenin signaling in brain endothelium. Furthermore, WNT7-stimulated beta-catenin signaling is regulated by GPR124's intracellular PDZ binding motif and leucine-rich repeats (LRR) in its N-terminal extracellular domain. GPR125 directly interacts with dishevelled (Dvl) via its intracellular C-terminus, and together, GPR125 and Dvl recruit a subset of planar cell polarity (PCP) components into membrane subdomains, a prerequisite for activation of Wnt/PCP signaling. Thus, GPR125 influences the noncanonical WNT/PCP pathway, which does not involve beta-catenin, through interacting with and modulating the distribution of Dvl.


Pssm-ID: 320387 [Multi-domain]  Cd Length: 260  Bit Score: 112.08  E-value: 4.52e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  867 LLSVITWVGIVISLVCLAICISTFC-FLRGLQTDRNTIHK--NLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFL 943
Cdd:cd15259      3 LLHPVVYAGAALCLLCLLATIITYIvFHRLIRISRKGRHMlvNLCLHLLLTCVVFVGGINRTANQLVCQAVGILLHYSTL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  944 AAFSWLCLEGVHLYLLLVEVFES---------EYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLrVDNYFIWS 1014
Cdd:cd15259     83 CTLLWVGVTARNMYKQVTKTAKPpqdedqpprPPKPMLRFYLIGWGIPLIICGITAAVNLDNYSTYDYCWL-AWDPSLGA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1015 FIGPVSFVIVVNLVFLmvtlhkmIRSSSVLKPDSSRldnIKSWALGAIALLFLLGLTWAFGLLFINKE---SVVMAYLFT 1091
Cdd:cd15259    162 FYGPAALIVLVNCIYF-------LRIYCQLKGAPVS---FQSQLRGAVITLFLYVAMWACGALAVSQRyflDLVFSCLYG 231
                          250       260
                   ....*....|....*....|....*...
gi 1034606781 1092 TFNAFQGVFIFVFHCALQKKVHKEYSKC 1119
Cdd:cd15259    232 ATCSSLGLFVLIHHCLSREDVRQSWRQC 259
Gal_Rha_Lectin_SML_rpt2 cd22835
second galactose/rhamnose binding lectin domain found in Scomberomorus niphonius ...
37-128 3.83e-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: 103.53  E-value: 3.83e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   37 RELACEGYPIELRCPGSDVIMVENANYGRTDDKICDA--DPFQMENVQCYLPdaFKIMSQRCNNRTQCVVVAGSDAFPDP 114
Cdd:cd22835      1 HLVACEGSLAHLKCDEGQVISVYGADYGRRDKTTCSFgrPPSQIQNVECSNP--TDKVAERCNGKNSCSIKASNSVFGDP 78
                           90
                   ....*....|....
gi 1034606781  115 CPGTYKYLEVQYDC 128
Cdd:cd22835     79 CVGTYKYLEVAYTC 92
7tmB2_BAI3 cd15989
brain-specific angiogenesis inhibitor 3, a group VII adhesion GPCR, member of the class B2 ...
878-1122 1.34e-25

brain-specific angiogenesis inhibitor 3, a group VII adhesion GPCR, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all 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. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediates direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions.


Pssm-ID: 320655 [Multi-domain]  Cd Length: 293  Bit Score: 108.62  E-value: 1.34e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  878 ISLVCLAICISTFcfLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLAAFSWLCLEGVHLY 957
Cdd:cd15989     19 LALITLAVVYAAL--WRYIRSERSIILINFCLSIISSNILILVGQTQTHNKGICTMTTAFLHFFFLASFCWVLTEAWQSY 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  958 LLLVEVFESEYSRTKYYYLgGYCFPALVVGIAAAID-YRSYGTEKACWLRVDNYFIWSFIGPVSFVIVVNLVFLMVTLHK 1036
Cdd:cd15989     97 MAVTGKIRTRLIRKRFLCL-GWGLPALVVAISMGFTkAKGYGTPHYCWLSLEGGLLYAFVGPAAAVVLVNMVIGILVFNK 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1037 MI------------RSSSVLKPDS------SRLDNIKSWALGAIA-------------LLFLLGLTWAFGLL-FINKESV 1084
Cdd:cd15989    176 LVsrdgildkklkhRAGQMSEPHSgltlkcAKCGVVSTTALSATTasnamaslwsscvVLPLLALTWMSAVLaMTDKRSI 255
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1034606781 1085 VMAYLFTTFNAFQGVFIFVFHCALQKKVHKEYSKCLRH 1122
Cdd:cd15989    256 LFQILFAVFDSLQGFVIVMVHCILRREVQDAFRCRLRN 293
7tmB1_PDFR cd15261
The pigment dispersing factor receptor, member of the class B seven-transmembrane G ...
874-1124 6.55e-24

The pigment dispersing factor receptor, member of the class B seven-transmembrane G protein-coupled receptors; The pigment dispersing factor receptor (PDFR) is a G protein-coupled receptor that binds the circadian clock neuropeptide PDF, a functional ortholog of the mammalian vasoactive intestinal peptide (VIP), on the pacemaker neurons. The PDFR is implicated in regulating flight circuit development and in modulating acute flight In Drosophila melanogaster. The PDFR activation stimulates adenylate cyclase, thereby increasing cAMP levels in many different pacemakers, and the receptor signaling has been shown to regulate behavioral circadian rhythms and geotaxis in Drosophila. The PDFR belongs to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. . These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. They play key roles in hormone homeostasis in mammals and are promising drug targets in various human diseases including diabetes, osteoporosis, obesity, neurodegenerative conditions (Alzheimer###s and Parkinson's), cardiovascular disease, migraine, and psychiatric disorders (anxiety, depression).


Pssm-ID: 320389 [Multi-domain]  Cd Length: 282  Bit Score: 103.60  E-value: 6.55e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  874 VGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLV-----------------------GIDKTQYeiA 930
Cdd:cd15261     10 VGLCLSLVSLIISLFIFSYFRTLRNHRTRIHKNLFLAILLQVIIRLVlyidqaitrsrgshtnaattegrTINSTPI--L 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  931 CPIFAGLLHYFFLAAFSWLCLEGVHLY-LLLVEVFESEYSRTKYYYLgGYCFPALVVGIAAAIDYRSYGTEKaCWLrvdN 1009
Cdd:cd15261     88 CEGFYVLLEYAKTVMFMWMFIEGLYLHnIIVVSVFSGKPNYLFYYIL-GWGIPIVHTSAWAIVTLIKMKVNR-CWF---G 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1010 YFI----WSFIGPVSFVIVVNLVFLMVTLHKMIrsSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVV 1085
Cdd:cd15261    163 YYLtpyyWILEGPRLAVILINLFFLLNIIRVLV--SKLRESHSREIEQVRKAVKAAIVLLPLLGITNILQMIPPPLTSVI 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1034606781 1086 M-----AYLFTTFNAFQGVFIFVFHCALQKKVhkeySKCLRHSY 1124
Cdd:cd15261    241 VgfavwSYSTHFLTSFQGFFVALIYCFLNGEV----KNVLKKFW 280
7tmB2_GPR114 cd15443
orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G ...
868-1115 7.44e-24

orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR114 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include GPR56, GPR64, GPR97, GPR112, and GPR126. GPR114 is mainly found in granulocytes (polymorphonuclear leukocytes), and GPR114-transfected cells induced an increase in cAMP levels via coupling to G(s) protein. 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. Furthermore, 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.


Pssm-ID: 320559 [Multi-domain]  Cd Length: 268  Bit Score: 102.91  E-value: 7.44e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  868 LSVITWVGIVISLVCLAICISTFCFLRGLQTDRNT-IHKNLCINLFLAELLFLVG--IDKTQYEIACPIFAGLLHYFFLA 944
Cdd:cd15443      4 LTYISIVGCSISAAASLLTILLHFFSRKQPKDSTTrIHMNLLGSLFLLNGSFLLSppLATSQSTWLCRAAAALLHYSLLC 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  945 AFSWLCLEGVHLYLLLVEVFESeYSRTKYYYLG--GYCFPALVVGIAAAIDYRSYG-----------TEKACWLR---VD 1008
Cdd:cd15443     84 CLTWMAIEGFHLYLLLVKVYNI-YIRRYVLKLCvlGWGLPALIVLLVLIFKREAYGphtiptgtgyqNASMCWITsskVH 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1009 NYFIWSFIGPVSFVIVVNLVFLMVTLHKmIRSSSVLKPDSSRLDNIKswALGaiaLLFLLGLTWAFGLLFINKESVVMAY 1088
Cdd:cd15443    163 YVLVLGYAGLTSLFNLVVLAWVVRMLRR-LRSRKQELGERARRDWVT--VLG---LTCLLGTTWALAFFSFGVFLIPQLF 236
                          250       260
                   ....*....|....*....|....*..
gi 1034606781 1089 LFTTFNAFQGVFIFVFHCALQKKVHKE 1115
Cdd:cd15443    237 LFTIINSLYGFFICLWYCTQRRRSDAS 263
Gal_Rha_Lectin_CSL3_rpt1_rpt2-like cd22832
first and second galactose/rhamnose binding lectin domain found in Oncorhynchus keta ...
37-128 1.48e-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: 96.41  E-value: 1.48e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   37 RELACEGYPIELRCpGSDVIMVENANYGRTDDKICDAD-PF-QMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDP 114
Cdd:cd22832      2 SSITCEGSDAQLDC-DGGKIRIQRANYGRRDHDVCSIGrPAnQLTNTNCLSQSTTSKMAERCDGKSQCIVPASNSVFGDP 80
                           90
                   ....*....|....
gi 1034606781  115 CPGTYKYLEVQYDC 128
Cdd:cd22832     81 CVGTYKYLDVAYTC 94
7tmB1_NPR_B7_insect-like cd15273
insect neuropeptide receptor subgroup B7 and related proteins, member of the class B family of ...
867-1121 4.98e-23

insect neuropeptide receptor subgroup B7 and related proteins, member of the class B family of seven-transmembrane G protein-coupled receptors; This subgroup includes a neuropeptide receptor found in Nilaparvata lugens (brown planthopper) and its closely related proteins from invertebrates. They belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. The class B GPCRs have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi, or prokaryotes.


Pssm-ID: 320401 [Multi-domain]  Cd Length: 285  Bit Score: 100.91  E-value: 4.98e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  867 LLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINL-------FLAELLFLVG-----------------I 922
Cdd:cd15273      3 IIKGISQIGYIVSLITLIIAFAIFLSFKKLHCARNKLHMHLFASFilrafmtLLKDSLFIDGlglladiverngggnevI 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  923 DKTQYEIACPIFAGLLHYFFLAAFSWLCLEGVHLY-LLLVEVFESEySRTKYYYLGGYCFPALVVG---IAAAIDYRSYg 998
Cdd:cd15273     83 ANIGSNWVCKAITSLWQYFIIANYSWILMEGLYLHnLIFLALFSDE-NNIILYILLGWGLPLIFVVpwiVARILFENSL- 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  999 tekaCWLRVDNYFIWSFI-GPVSFVIVVNLVFLM----VTLHKMirSSSVLKpDSSRLdniKSWALGAIALLFLLGLTWA 1073
Cdd:cd15273    161 ----CWTTNSNLLNFLIIrIPIMISVLINFILFLnivrVLLVKL--RSSVNE-DSRRY---KKWAKSTLVLVPLFGVHYT 230
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034606781 1074 --FGLLFINK--ESVVMAYLFT--TFNAFQGVFIFVFHCALQKKVHKEYSKCLR 1121
Cdd:cd15273    231 ifLILSYLDDtnEAVELIWLFCdqLFASFQGFFVALLYCFLNGEVRAEIQRKWR 284
7tmB2_GPR56 cd15995
orphan adhesion receptor GPR56, member of the class B2 family of seven-transmembrane G ...
868-1108 6.00e-23

orphan adhesion receptor GPR56, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR56 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include orphan GPCRs such as GPR64, GPR97, GPR112, GPR114, and GPR126. GPR56 is involved in the regulation of oligodendrocyte development and myelination in the central nervous system via coupling to G(12/13) proteins, which leads to the activation of RhoA GTPase. 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. Furthermore, 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.


Pssm-ID: 320661  Cd Length: 269  Bit Score: 100.29  E-value: 6.00e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  868 LSVITWVGIVISLVCLAICISTFCFLRGLQTDRNT-IHKNLCINLFLAELLFLVG--IDKTQYEIACPIFAGLLHYFFLA 944
Cdd:cd15995      4 LTILTYVGCIISALASVFTIAFYLCSRRKPRDYTIyVHMNLLLAIFLLDTSFLISepLALTGSEAACRAGGMFLHFSLLA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  945 AFSWLCLEGVHLYLLLVEVFEseySRTKYYYLG----GYCFPALVVGIAAAIDYRSYGT---------EKA-----CWLR 1006
Cdd:cd15995     84 CLTWMGIEGYNLYRLVVEVFN---TYVPHFLLKlcavGWGLPIFLVTLIFLVDQDNYGPiilavhrspEKVtyatiCWIT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1007 VDNYFIWSFIGPVSFVIVVNLVFLMVTLHKMIRsssvLKPDSSRLdnikSWALGAIALLFLLGLTWAfgLLFINKES--- 1083
Cdd:cd15995    161 DSLISNITNLGLFSLVFLFNMAMLATMVVEILR----LRPRTHKW----SHVLTLLGLSLVLGIPWA--LAFFSFASgtf 230
                          250       260
                   ....*....|....*....|....*.
gi 1034606781 1084 -VVMAYLFTTFNAFQGVFIFVFHCAL 1108
Cdd:cd15995    231 qLVIVYLFTIINSLQGFLIFLWYWSM 256
Gal_Rha_Lectin_CSL1-2_RBL_SML_rpt1 cd22833
first galactose/rhamnose binding lectin domain found in Oncorhynchus keta CSL1-2, Silurus ...
41-130 2.27e-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: 93.10  E-value: 2.27e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   41 CEGYPIE-LRCpGSDVIMVENANYGRTDDKICDA--DPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCPG 117
Cdd:cd22833      6 CDGNNVHrLSC-DTGVINVQSALYGRTDSETCSEgrPPEQLTNTQCSQSGTLDLLKNRCDGKKVCELNTNDFRTSDPCPG 84
                           90
                   ....*....|...
gi 1034606781  118 TYKYLEVQYDCVP 130
Cdd:cd22833     85 TYKYLQTNYTCLP 97
Gal_Rha_Lectin_EVA1_EVA1C_rpt2 cd22829
second galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
36-130 2.91e-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: 2.91e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   36 RRELACEGYPIELRCPGSDVIMVENANYGRT--DDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPD 113
Cdd:cd22829      2 KSKVVCEGEKLRLSCKPSSRLAIYSASYGRTleGSVECPSTPKGDPDEECLSDVALETVMKRCHGKRRCSLTADSETFGD 81
                           90
                   ....*....|....*...
gi 1034606781  114 PC-PGTYKYLEVQYDCVP 130
Cdd:cd22829     82 PCpPGVRKYLKVVYTCVP 99
7tmB1_GLP2R cd15266
glucagon-like peptide-2 receptor, member of the class B family of seven-transmembrane G ...
866-1118 4.56e-22

glucagon-like peptide-2 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; Glucagon-like peptide-2 receptor (GLP2R) is a member of the glucagon receptor family of G protein-coupled receptors, which also includes glucagon receptor (GCGR) and GLP1R. GLP2R is activated by glucagon-like peptide 2, which is derived from the large proglucagon precursor. Activation of GLP1R stimulates glucose-dependent insulin secretion from pancreatic beta cells, whereas activation of GLP2R stimulates intestinal epithelial proliferation and increases villus height in the small intestine. GCGR regulates blood glucose levels by control of hepatic glycogenolysis and gluconeogenesis and by regulation of insulin secretion from the pancreatic beta-cells. GLP2R belongs to the B1 (or secretin-like) subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on their cellular location, GCGR and GLP receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320394 [Multi-domain]  Cd Length: 280  Bit Score: 97.89  E-value: 4.56e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  866 LLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVG--IDKTQY---------------- 927
Cdd:cd15266      2 LTLQLIYTIGYSLSLISLSLALLILLLLRKLHCTRNYIHMNLFASFILRALAVLIKdiVLYSTYskrpddetgwisylse 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  928 --EIACPIFAGLLHYFFLAAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVV---GIAaaidyRSYGTEKA 1002
Cdd:cd15266     82 esSTSCRVAQVFMHYFVGANYFWLLVEGLYLHTLLVTAVLSERRLLKKYMLIGWGTPVLFVvpwGVA-----KILLENTG 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1003 CWLRVDNYFIWSFI-GPVSFVIVVNLVFLMVTLHKMIrssSVLKPDSSRLDNIK-SWALGAIALLFLLGLTwAFGLLFIN 1080
Cdd:cd15266    157 CWGRNENMGIWWIIrGPILLCITVNFYIFLKILKLLL---SKLKAQQMRFTDYKyRLARSTLVLIPLLGIH-EVVFSFIT 232
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1034606781 1081 KESV------VMAYLFTTFNAFQGVFIFVFHCALQKKVHKEYSK 1118
Cdd:cd15266    233 DEQVegfsrhIRLFIQLTLSSFQGFLVAVLYCFANGEVKAELKK 276
Gal_Rha_Lectin_REJ3 cd22841
galactose/rhamnose binding lectin domain found in Strongylocentrotus purpuratus receptor for ...
38-128 3.81e-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: 3.81e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   38 ELACEGYPIELRCpGSDVIMVENANYGRTDDKICDADPFqMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCPG 117
Cdd:cd22841      4 FIVCEGDTDVIDC-GNGVINIHSAVYGRTDSTTCSHDQS-VSNTNCHSDDSVNILSACCNGQSQCTVTATNSIFGDPCPG 81
                           90
                   ....*....|.
gi 1034606781  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 3.66e-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: 85.13  E-value: 3.66e-20
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1034606781   806 FNANCSFWNYSErsmlGYWSTQGCRLVESNKTHTTCACSHLTNFAVLMAHREI 858
Cdd:smart00303    1 FNPICVFWDESS----GEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPPI 49
7tmB1_Secretin_R-like cd15930
secretin receptor-like group of hormone receptors, member of the class B family of ...
866-1115 4.26e-20

secretin receptor-like group of hormone receptors, member of the class B family of seven-transmembrane G protein-coupled receptors; This group represents G protein-coupled receptors for structurally similar peptide hormones that include secretin, growth-hormone-releasing hormone (GHRH), pituitary adenylate cyclase activating polypeptide (PACAP), and vasoactive intestinal peptide (VIP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. Secretin, a polypeptide secreted by entero-endocrine S cells in the small intestine, is involved in maintaining body fluid balance. This polypeptide regulates the secretion of bile and bicarbonate into the duodenum from the pancreatic and biliary ducts, as well as regulates the duodenal pH by the control of gastric acid secretion. Studies with secretin receptor-null mice indicate that secretin plays a role in regulating renal water reabsorption. Secretin mediates its biological actions by elevating intracellular cAMP via G protein-coupled secretin receptors, which are expressed in the brain, pancreas, stomach, kidney, and liver. GHRHR is a specific receptor for the growth hormone-releasing hormone (GHRH) that controls the synthesis and release of growth hormone (GH) from the anterior pituitary somatotrophs. Mutations in the gene encoding GHRHR have been connected to isolated growth hormone deficiency (IGHD), a short-stature condition caused by deficient production of GH or lack of GH action. VIP and PACAP exert their effects through three G protein-coupled receptors, PACAP-R1, VIP-R1 (vasoactive intestinal receptor type 1, also known as VPAC1) and VIP-R2 (or VPAC2). PACAP-R1 binds only PACAP with high affinity, whereas VIP-R1 and -R2 specifically bind and respond to both VIP and PACAP. VIP and PACAP and their receptors are widely expressed in the brain and periphery. They are upregulated in neurons and immune cells in responses to CNS injury and/or inflammation and exert potent anti-inflammatory effects, as well as play important roles in the control of circadian rhythms and stress responses, among many others. All B1 subfamily GPCRs are able to increase intracellular cAMP levels by coupling to adenylate cyclase via a stimulatory Gs protein. However, depending on its cellular location, some members of subfamily B1 are also capable of coupling to additional G proteins such as G(i/o) and/or G(q) proteins, thereby leading to activation of phospholipase C and intracellular calcium influx.


Pssm-ID: 320596 [Multi-domain]  Cd Length: 268  Bit Score: 91.72  E-value: 4.26e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  866 LLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHknlcINLFLAELLFLVGI---DKTQYE-----------IAC 931
Cdd:cd15930      2 LTVKIIYTVGYSLSLTSLTTAMIILCLFRKLHCTRNYIH----MNLFVSFILRAIAVfikDAVLFSsedvdhcfvstVGC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  932 PIFAGLLHYFFLAAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIdyRSYGTEKACWLRVDNYF 1011
Cdd:cd15930     78 KASMVFFQYCVMANFFWLLVEGLYLHTLLVISFFSERRYFWWYVLIGWGAPTVFVTVWIVA--RLYFEDTGCWDINDESP 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1012 IWSFI-GPVSFVIVVNLVF---LMVTLHKMIRSSSVLKPDSSRLdniKSWALGAIALLFLLGLTW-AFGLLFINKESVVM 1086
Cdd:cd15930    156 YWWIIkGPILISILVNFVLfinIIRILLQKLRSPDIGGNESSQY---KRLARSTLLLIPLFGIHYiVFAFFPENISLGIR 232
                          250       260
                   ....*....|....*....|....*....
gi 1034606781 1087 AYLFTTFNAFQGVFIFVFHCALQKKVHKE 1115
Cdd:cd15930    233 LYFELCLGSFQGFVVAVLYCFLNGEVQAE 261
7tmB2_GPR111_115 cd15994
orphan adhesion receptors GPR111 and GPR115, member of the class B2 family of ...
865-1112 1.74e-19

orphan adhesion receptors GPR111 and GPR115, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR111 and GPR115 are highly homologous orphan receptors that belong to group VI adhesion-GPCRs along with GPR110, GPR113, and GPR116. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, 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. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS. Both GPR111 and GPR5 are present only in land-living animals and are predominantly expressed in the developing skin.


Pssm-ID: 320660 [Multi-domain]  Cd Length: 267  Bit Score: 90.28  E-value: 1.74e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  865 ELLLSVITWVGIVISLVCLAIC--ISTFCFLRGLQTD----RNTIHKNLCINLFLAELLFLVGI---DKTQYEIACPIFA 935
Cdd:cd15994      1 NAVLDYITRIGLGLSIFSLALCltIEAVVWSHVTKTEitymRHVCIVNIATSLLIADVWFILASivhNTALNYPLCVAAT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  936 GLLHYFFLAAFSWLCLEGVH-LYLLLVEVFESEYSR-TKYYYLGGYCFPALVVGIAAAIDY--RSYGTEKACWLRVDNY- 1010
Cdd:cd15994     81 FFLHFFYLSLFFWMLTKALLiLYGILLVFFKITKSVfIATAFSIGYGCPLVIAVLTVAITEpkKGYLRPEACWLNWDETk 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1011 FIWSFIGPVSFVIVVNLVFLMVTLHKMIRSS--SVLKPDSSRLDNIKSwalgAIALLF-LLGLTWAFGL-LFINKESVVM 1086
Cdd:cd15994    161 ALLAFIIPALSIVVVNLIVVGVVVVKTQRSSigESCKQDVSNIIRISK----NVAILTpLLGLTWGFGLaTIIDSRSLPF 236
                          250       260
                   ....*....|....*....|....*.
gi 1034606781 1087 AYLFTTFNAFQGVFIFVFHCALQKKV 1112
Cdd:cd15994    237 HIIFALLNAFQGFFILLFGTILDRKI 262
Gal_Rha_Lectin_EVA1_EVA1C_rpt1 cd22828
first galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
40-130 2.72e-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: 84.64  E-value: 2.72e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   40 ACEGYPIELRCPGSDVIMVENANYGRTD--DKIC-----DADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFP 112
Cdd:cd22828      7 ACDGEELTLRCPPNTTISIQSAFYGRSVpsAQLCpsqsgPASSTSLEDTNCLAPTALQKVVEECQKKRSCRLLVSSRTFG 86
                           90
                   ....*....|....*....
gi 1034606781  113 -DPCPGTYKYLEVQYDCVP 130
Cdd:cd22828     87 lDPCPGTSKYLEVAYKCRP 105
7tmB1_CRF-R2 cd15446
corticotropin-releasing factor receptor 2, member of the class B family of seven-transmembrane ...
870-1118 2.78e-19

corticotropin-releasing factor receptor 2, member of the class B family of seven-transmembrane G protein-coupled receptors; The vertebrate corticotropin-releasing factor (CRF) receptors are predominantly expressed in central nervous system with high levels in cortex tissue, brain stem, and pituitary. They have two isoforms as a result of alternative splicing of the same receptor gene: CRF-R1 and CRF-R2, which differ in tissue distribution and ligand binding affinities. Recently, a third CRF receptor (CRF-R3) has been identified in catfish pituitary. The catfish CRF-R1 is highly homologous to CRF-R3. CRF is a 41-amino acid neuropeptide that plays a central role in coordinating neuroendocrine, behavioral, and autonomic responses to stress by acting as the primary neuroregulator of the hypothalamic-pituitary-adrenal axis, which controls the levels of cortisol and other stress related hormones. In addition, the CRF family of neuropeptides also includes structurally related peptides such as mammalian urocortin, fish urotensin I, and frog sauvagine. The actions of CRF and CRF-related peptides are mediated through specific binding to CRF-R1 and CRF-R2. CRF and urocortin 1 bind and activate mammalian CRF-R1 with similar high affinities. By contrast, urocortin 2 and urocortin 3 do not bind to CRF-R1 or stimulate CRF-R1-mediated cAMP formation. Urocortin 1 also shows high affinity for mammalian CRF-R2, whereas CRF has significantly lower affinity for this receptor. These evidence suggest that urocortin 1 is an endogenous ligand for CRF-R1 and CRF-R2. The CRF receptors are members of the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, and parathyroid hormone (PTH). These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on its cellular location and function, CRF receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320562 [Multi-domain]  Cd Length: 264  Bit Score: 89.63  E-value: 2.78e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  870 VITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLF--LVGIDKTQYE---IACPIFAGLLHYFFLA 944
Cdd:cd15446      6 IINYLGHCISVGALVVAFLLFLCLRSIRCLRNIIHWNLITTFILRNVMWflLQMIDHNIHEsneVWCRCITTIYNYFVVT 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  945 AFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVgIAAAIDYRSYGTEKaCWLRVD--NYFIWSFIGPVSFV 1022
Cdd:cd15446     86 NFFWMFVEGCYLHTAIVMTYSTDKLRKWVFLFIGWCIPCPII-VAWAIGKLYYENEQ-CWFGKEpgKYIDYIYQGPVILV 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1023 IVVNLVFL---MVTLHKMIRSSSvlkpdSSRLDNIKSWALGAIALLFLLGLTWAfgLLFINK-----ESVVMAYLFTTFN 1094
Cdd:cd15446    164 LLINFVFLfniVRILMTKLRAST-----TSETIQYRKAVKATLVLLPLLGITYM--LFFVNPgeddiSQIVFIYFNSFLQ 236
                          250       260
                   ....*....|....*....|....
gi 1034606781 1095 AFQGVFIFVFHCALQKKVHKEYSK 1118
Cdd:cd15446    237 SFQGFFVSVFYCFLNGEVRSAARK 260
7tmB1_CRF-R1 cd15445
corticotropin-releasing factor receptor 1, member of the class B family of seven-transmembrane ...
870-1122 4.37e-19

corticotropin-releasing factor receptor 1, member of the class B family of seven-transmembrane G protein-coupled receptors; The vertebrate corticotropin-releasing factor (CRF) receptors are predominantly expressed in central nervous system with high levels in cortex tissue, brain stem, and pituitary. They have two isoforms as a result of alternative splicing of the same receptor gene: CRF-R1 and CRF-R2, which differ in tissue distribution and ligand binding affinities. Recently, a third CRF receptor (CRF-R3) has been identified in catfish pituitary. The catfish CRF-R1 is highly homologous to CRF-R3. CRF is a 41-amino acid neuropeptide that plays a central role in coordinating neuroendocrine, behavioral, and autonomic responses to stress by acting as the primary neuroregulator of the hypothalamic-pituitary-adrenal axis, which controls the levels of cortisol and other stress related hormones. In addition, the CRF family of neuropeptides also includes structurally related peptides such as mammalian urocortin, fish urotensin I, and frog sauvagine. The actions of CRF and CRF-related peptides are mediated through specific binding to CRF-R1 and CRF-R2. CRF and urocortin 1 bind and activate mammalian CRF-R1 with similar high affinities. By contrast, urocortin 2 and urocortin 3 do not bind to CRF-R1 or stimulate CRF-R1-mediated cAMP formation. Urocortin 1 also shows high affinity for mammalian CRF-R2, whereas CRF has significantly lower affinity for this receptor. These evidence suggest that urocortin 1 is an endogenous ligand for CRF-R1 and CRF-R2. The CRF receptors are members of the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, and parathyroid hormone (PTH). These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on its cellular location and function, CRF receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320561 [Multi-domain]  Cd Length: 265  Bit Score: 88.84  E-value: 4.37e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  870 VITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIA------CPIFAGLLHYFFL 943
Cdd:cd15445      6 IINYLGHCISLVALLVAFVLFLRLRSIRCLRNIIHWNLITAFILRNATWFVVQLTMSPEVHqsnvvwCRLVTAAYNYFHV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  944 AAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVgIAAAIDYRSYGTEKaCWL--RVDNYFIWSFIGPVSF 1021
Cdd:cd15445     86 TNFFWMFGEGCYLHTAIVLTYSTDKLRKWMFICIGWCIPFPII-VAWAIGKLYYDNEK-CWFgkRAGVYTDYIYQGPMIL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1022 VIVVNLVFL---MVTLHKMIRSSSvlkpdSSRLDNIKSWALGAIALLFLLGLTWAfgLLFINK-ESVVMAYLFTTFNA-- 1095
Cdd:cd15445    164 VLLINFIFLfniVRILMTKLRAST-----TSETIQYRKAVKATLVLLPLLGITYM--LFFVNPgEDEISRIVFIYFNSfl 236
                          250       260
                   ....*....|....*....|....*....
gi 1034606781 1096 --FQGVFIFVFHCALQKKVHKEYSKCLRH 1122
Cdd:cd15445    237 esFQGFFVSVFYCFLNSEVRSAVRKRWHR 265
7tmB1_GlucagonR-like cd15929
glucagon receptor-like subfamily, member of the class B family of seven-transmembrane G ...
868-1122 4.51e-19

glucagon receptor-like subfamily, member of the class B family of seven-transmembrane G protein-coupled receptors; This group represents the glucagon receptor family of G protein-coupled receptors, which includes glucagon receptor (GCGR), glucagon-like peptide-1 receptor (GLP1R), GLP2R, and closely related receptors. These receptors are activated by the members of the glucagon (GCG) peptide family including GCG, glucagon-like peptide 1 (GLP1), and GLP2, which are derived from the large proglucagon precursor. GCGR regulates blood glucose levels by control of hepatic glycogenolysis and gluconeogenesis and by regulation of insulin secretion from the pancreatic beta-cells. Activation of GLP1R stimulates glucose-dependent insulin secretion from pancreatic beta cells, whereas activation of GLP2R stimulates intestinal epithelial proliferation and increases villus height in the small intestine. Receptors in this group belong to the B1 (or secretin-like) subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on their cellular location, GCGR and GLP receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 341353 [Multi-domain]  Cd Length: 279  Bit Score: 89.03  E-value: 4.51e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  868 LSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLV--GIDKTQYE----------------- 928
Cdd:cd15929      4 LQVMYTVGYSLSLAALVLALAILLGLRKLHCTRNYIHANLFASFILRALSVLVkdALLPRRYSqkgdqdlwstllsnqas 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  929 IACPIFAGLLHYFFLAAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEkaCWLRVD 1008
Cdd:cd15929     84 LGCRVAQVLMQYCVAANYYWLLVEGLYLHTLLVLAVFSERSIFRLYLLLGWGAPVLFVVPWGIVKYLYENTG--CWTRND 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1009 NYFIWSFI-GPVSFVIVVNLVFLMVTLHKMIrssSVLKPDSSRLDNIK-SWALGAIALLFLLGLTWAFgLLFINKESVV- 1085
Cdd:cd15929    162 NMAYWWIIrLPILLAILINFFIFVRILKILV---SKLRANQMCKTDYKfRLAKSTLTLIPLLGVHEVV-FAFVTDEQARg 237
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1034606781 1086 ---MAYLFT--TFNAFQGVFIFVFHCALQKKVHKEYSKCLRH 1122
Cdd:cd15929    238 tlrFIKLFFelFLSSFQGLLVAVLYCFANKEVQSELRKKWHR 279
7tmB1_PTH-R_related cd15272
invertebrate parathyroid hormone-related receptors, member of the class B family of ...
868-1118 1.04e-18

invertebrate parathyroid hormone-related receptors, member of the class B family of seven-transmembrane G protein-coupled receptors; This group includes parathyroid hormone (PTH)-related receptors found in invertebrates such as mollusks and annelid worms. The PTH family receptors are members of the B1 subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. The parathyroid hormone type 1 receptor (PTH1R) is found in all vertebrate species and is activated by two polypeptide ligands: parathyroid hormone (PTH), an endocrine hormone that regulates calcium homoeostasis and bone maintenance, and PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH1R couples predominantly to G(s)- protein that in turn activates adenylyl cyclase thereby producing cAMP, but it can also couple to several G protein subtypes, including G(q/11), G(i/o), and G(12/13), resulting in activation of multiple signaling pathways.


Pssm-ID: 320400 [Multi-domain]  Cd Length: 285  Bit Score: 88.21  E-value: 1.04e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  868 LSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINL-------FLAELLFLVGI------------------ 922
Cdd:cd15272      4 IRLMYNIGYGLSLVSLLIAVIIMLYFKKLHCPRNTIHINLFVSFilravlsFIKENLLVQGVgfpgdvyydsngviefkd 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  923 DKTQYEiaCPIFAGLLHYFFLAAFSWLCLEGVHLYLLL-VEVFeSEYSRTKYYYLGGYCFPALVVgiAAAIDYRSYGTEK 1001
Cdd:cd15272     84 EGSHWE--CKLFFTMFNYILGANYMWIFVEGLYLHMLIfVAVF-SENSRVKWYILLGWLSPLLFV--LPWVFVRATLEDT 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1002 ACW-LRVDNYFIWSFIGPVSFVIVVNLVFLM----VTLHKMiRSSSVLKPDSSRLdniKSWALGAIALLFLLGLTW-AFG 1075
Cdd:cd15272    159 LCWnTNTNKGYFWIIRGPIVISIAINFLFFInivrVLFTKL-KASNTQESRPFRY---RKLAKSTLVLIPLFGVHYmVFV 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1034606781 1076 LLFINKES----VVMAYLFTTFNAFQGVFIFVFHCALQKKVHKEYSK 1118
Cdd:cd15272    235 VLPDSMSSdeaeLVWLYFEMFFNSFQGFIVALLFCFLNGEVQSEIKK 281
HormR smart00008
Domain present in hormone receptors;
484-547 3.21e-18

Domain present in hormone receptors;


Pssm-ID: 214468  Cd Length: 70  Bit Score: 80.25  E-value: 3.21e-18
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034606781   484 PELFCEPREVRRVQWPATQQGMLVERPCPKGTRGI-----ASFQCLPALGlWNPRGPDLSNCTSPWVNQ 547
Cdd:smart00008    1 TDLGCPATWDGIICWPQTPAGQLVEVPCPKYFSGFsyktgASRNCTENGG-WSPPFPNYSNCTSNDYEE 68
7tmB2_GPR123 cd16000
G protein-coupled receptor 123, member of the class B2 family of seven-transmembrane G ...
867-1119 6.55e-18

G protein-coupled receptor 123, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR123 is an orphan receptor that has been classified as that belongs to the group III of adhesion GPCRs, and also includes orphan receptors GPR124 and GPR125. GPR123 is predominantly expressed in the CNS including thalamus, brain stem and regions containing large pyramidal cells, yet its biological function remains to be determined. 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. Furthermore, 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.


Pssm-ID: 320666 [Multi-domain]  Cd Length: 275  Bit Score: 85.77  E-value: 6.55e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  867 LLSVITWVGIVISLVCLAICISTFCFLRG-LQTDRNTIHK--NLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFL 943
Cdd:cd16000      3 FLHPVVYACTAVMLLCLFASIITYIVHHStIRISRKGWHMllNFCFHTALTFAVFAGGINRTKYPIICQAVGIVLHYSTL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  944 AAFSWLCLEGVHLYL-------LLVEVFESEYSRT---KYYYLGGyCFPALVVGIAAAIDYRSYGTEKA----CWLRVDN 1009
Cdd:cd16000     83 STMLWIGVTARNIYKqvtkkphLCQDTDQPPYPKQpllRFYLVSG-GVPFIICGITAATNINNYGTEDEdtpyCWMAWEP 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1010 YfIWSFIGPVSFVIVVNLVFLMVTLHKMIRSSS---VLKPDSSrldnIKSWALGAIALLFLLGLTWAFGLLFINKE---S 1083
Cdd:cd16000    162 S-LGAFYGPVAFIVLVTCIYFLCTYVQLRRHPErkyELKNEHS----FKAQLRAAAFTLFLFTATWAFGALAVSQGhflD 236
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1034606781 1084 VVMAYLFTTFNAFQGVFIFVFHCALQKKV-HKEYSKC 1119
Cdd:cd16000    237 MIFSCLYGAFCVTLGLFILIHHCAKRDDVwHCWWSCC 273
Gal_Rha_Lectin_LAT1 cd22839
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ...
38-128 1.37e-17

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: 1.37e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   38 ELACEGYPIELRCPGSDVIMVENANYGRTDDKICDaDPFQME-NVQCYLPDAFKIMSQRCNNRTQCVVVAGSD-AFPDPC 115
Cdd:cd22839      4 VIICEGDVANLSCPEGKYISIRLANYGRFSLGVCN-PSNNIDlSTTCQNDKTLPILQKSCDGKSECSFVVSNKfFFEDPC 82
                           90
                   ....*....|...
gi 1034606781  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 3.17e-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: 77.85  E-value: 3.17e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   41 CEGYPIELRCPGSdVIMVENANYGRTDDKICDADpfQMENVQCYLPDAFKIMSQrCNNRTQCVVVAGSDAFPDPCPGTYK 120
Cdd:cd22837      4 CENDSATITCSPE-TINVISAFYGRTDSTTCSHG--RPSTTNCSSDTLAYIRAL-CQGKQTCTLQASNSVFGDPCPGTYK 79

                   ....*...
gi 1034606781  121 YLEVQYDC 128
Cdd:cd22837     80 YLRITYSC 87
7tmB1_secretin cd15275
secretin receptor, member of the class B family of seven-transmembrane G protein-coupled ...
874-1115 3.18e-17

secretin receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; Secretin receptor is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include vasoactive intestinal peptide (VIP), growth-hormone-releasing hormone (GHRH), and pituitary adenylate cyclase activating polypeptide (PACAP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors, and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. Secretin, a polypeptide secreted by entero-endocrine S cells in the small intestine, is involved in maintaining body fluid balance. This polypeptide regulates the secretion of bile and bicarbonate into the duodenum from the pancreatic and biliary ducts, as well as regulates the duodenal pH by the control of gastric acid secretion. Studies with secretin receptor-null mice indicate that secretin plays a role in regulating renal water reabsorption. Secretin mediates its biological actions by elevating intracellular cAMP via G protein-coupled secretin receptor, which is expressed in the brain, pancreas, stomach, kidney, and liver.


Pssm-ID: 320403 [Multi-domain]  Cd Length: 271  Bit Score: 83.64  E-value: 3.18e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  874 VGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVG---IDKTQYEIACPIFAG-------LLHYFFL 943
Cdd:cd15275     10 VGYSVSLVSLAIALAILCSFRRLHCTRNYIHMQLFLSFILRAISIFIKdavLFSSEDDNHCDIYTVgckvamvFSNYCIM 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  944 AAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVgIAAAIdYRSYGTEKACWLRVDNYFIWSFI-GPVSFV 1022
Cdd:cd15275     90 ANYSWLLVEGLYLHSLLSISFFSERKHLWWYIALGWGSPLIFI-ISWAI-ARYLHENEGCWDTRRNAWIWWIIrGPVILS 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1023 IVVNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESV----VMAYLFTTFNAFQG 1098
Cdd:cd15275    168 IFVNFILFLNILRILMRKLRAPDMRGNEFSQYKRLAKSTLLLIPLFGLHYILFAFFPEDVSSgtmeIWLFFELALGSFQG 247
                          250
                   ....*....|....*..
gi 1034606781 1099 VFIFVFHCALQKKVHKE 1115
Cdd:cd15275    248 FVVAVLYCFLNGEVQLE 264
GPS pfam01825
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
810-852 5.71e-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: 5.71e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1034606781  810 CSFWNYSERSMlGYWSTQGCRLVESNKTHTTCACSHLTNFAVL 852
Cdd:pfam01825    3 CVFWDFTNSTT-GRWSTEGCTTVSLNDTHTVCSCNHLTSFAVL 44
7tmB1_PACAP-R1 cd15987
pituitary adenylate cyclase-activating polypeptide type 1 receptor, member of the class B ...
874-1121 1.36e-16

pituitary adenylate cyclase-activating polypeptide type 1 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; Pituitary adenylate cyclase-activating polypeptide type 1 receptor (PACAP-R1) is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, growth-hormone-releasing hormone (GHRH), and vasoactive intestinal peptide (VIP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. VIP and PACAP exert their effects through three G protein-coupled receptors, PACAP-R1, VIP-R1 (vasoactive intestinal receptor type 1, also known as VPAC1) and VIP-R2 (or VPAC2). PACAP-R1 binds only PACAP with high affinity, whereas VIP-R1 and -R2 specifically bind and respond to both VIP and PACAP. VIP and PACAP and their receptors are widely expressed in the brain and periphery. They are upregulated in neurons and immune cells in responses to CNS injury and/or inflammation and exert potent anti-inflammatory effects, as well as play important roles in the control of circadian rhythms and stress responses, among many others. PACAP-R1 is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level.


Pssm-ID: 320653 [Multi-domain]  Cd Length: 268  Bit Score: 81.55  E-value: 1.36e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  874 VGIVISLVCLAICISTFCFLRGLQTDRNTIHKNL-------CINLFLAELLFLVGIDKTQ---YEIACPIFAGLLHYFFL 943
Cdd:cd15987     10 VGYSTSLVSLTTAMVILCRFRKLHCTRNFIHMNLfvsfilrAISVFIKDGVLYAEQDSDHcfvSTVECKAVMVFFHYCVM 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  944 AAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIdyRSYGTEKACWLRVDNYFIWSFI-GPVSFV 1022
Cdd:cd15987     90 SNYFWLFIEGLYLFTLLVETFFPERRYFYWYTIIGWGTPTICVTVWAVL--RLHFDDTGCWDMNDNTALWWVIkGPVVGS 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1023 IVVNLVF---LMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLftTFNAFQGV 1099
Cdd:cd15987    168 IMINFVLfigIIIILVQKLQSPDIGGNESSIYLRLARSTLLLIPLFGIHYTVFAFSPENVSKRERLVFEL--GLGSFQGF 245
                          250       260
                   ....*....|....*....|..
gi 1034606781 1100 FIFVFHCALQKKVHKEYSKCLR 1121
Cdd:cd15987    246 VVAVLYCFLNGEVQSEIKRKWR 267
Gal_Rha_Lectin_nemgal cd22838
galactose/rhamnose binding lectin domain found in Hydra vulgaris nematogalectin and similar ...
39-130 2.98e-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: 75.77  E-value: 2.98e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   39 LACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQME-NVQCYL--PDAFKIMSQRCNNRTQCVVVAGSDAFPDP- 114
Cdd:cd22838      5 IACEGEKLWLQCPQYELIKIKSAFWGRDDKKTCPHPPPGLPsNKMCETdeENVKKKVNDQCQGEQACEVVASNIFFDDTi 84
                           90
                   ....*....|....*.
gi 1034606781  115 CPGTYKYLEVQYDCVP 130
Cdd:cd22838     85 CPDVYKYLKVKYECIP 100
7tmB1_calcitonin_R cd15274
calcitonin receptor, member of the class B family of seven-transmembrane G protein-coupled ...
866-1106 4.51e-16

calcitonin receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; This group includes G protein-coupled receptors for calcitonin (CT) and calcitonin gene-related peptides (CGRPs). Calcitonin, a 32-amino acid peptide hormone, is involved in calcium metabolism in many mammalian species and acts to reduce blood calcium levels and directly inhibits bone resorption by acting on osteoclast. Thus, CT acts as an antagonist to parathyroid hormone and is commonly used in the treatment of bone disorders. The CT receptor is predominantly found in osteoclasts, kidney, and brain, and is primarily coupled to stimulatory G(s) protein, which leads to activation of adenylate cyclase, thereby increasing cAMP production. CGRP, a member of the calcitonin family of peptides, is a potent vasodilator and may contribute to migraine. It is expressed in the peripheral and central nervous system and exists in two forms in humans (alpha-CGRP and beta-CGRP). CGRP meditates its physiological effects through calcitonin receptor-like receptor (CRLR) and receptor activity-modifying protein 1 (RAMP1), a single transmembrane domain protein. Thus, the CRLR/RAMP1 complex serves as a functional CGRP receptor. On the other hand, the CRLR/RAMP2 and CRLR/RAMP3 complexes function as adrenomedullin-specific receptors. The CT and CGRP receptors belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide.


Pssm-ID: 341343 [Multi-domain]  Cd Length: 274  Bit Score: 80.21  E-value: 4.51e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  866 LLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFL---AELLFLVGIDKTQYEIAC-PIFAGLLHYF 941
Cdd:cd15274      2 YNLYYLAIVGHSLSIATLLISLGIFFFFRSLSCQRVTLHKNLFLSYILnsiIIIIHLVAVVPNGELVARnPVSCKILHFI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  942 FLAAFS----WLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIdyRSYGTEKACWLRVDNYFIWSFIG 1017
Cdd:cd15274     82 HQYMMGcnyfWMLCEGIYLHTLIVVAVFAEKQRLMWYYLLGWGFPLIPTTIHAIT--RAVYYNDNCWLSSETHLLYIIHG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1018 PVSFVIVVNLVFLMVTLHKMIrssSVLKPDSSRLDNIKSWALGAIALLF-LLG-----LTWAfglLFINKESVVMAYLFT 1091
Cdd:cd15274    160 PIMAALVVNFFFLLNIVRVLV---TKLRETHEAESHMYLKAVKATLILVpLLGiqfvlFPWR---PSGKILGKIYDYVMH 233
                          250
                   ....*....|....*
gi 1034606781 1092 TFNAFQGVFIFVFHC 1106
Cdd:cd15274    234 SLIHFQGFFVATIFC 248
7tmB1_VIP-R2 cd15986
vasoactive intestinal polypeptide (VIP) receptor 2, member of the class B family of ...
866-1121 6.14e-15

vasoactive intestinal polypeptide (VIP) receptor 2, member of the class B family of seven-transmembrane G protein-coupled receptors; Vasoactive intestinal peptide (VIP) receptor 2 is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, growth-hormone-releasing hormone (GHRH), and pituitary adenylate cyclase activating polypeptide (PACAP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. VIP and PACAP exert their effects through three G protein-coupled receptors, PACAP-R1, VIP-R1 (vasoactive intestinal receptor type 1, also known as VPAC1) and VIP-R2 (or VPAC2). PACAP-R1 binds only PACAP with high affinity, whereas VIP-R1 and -R2 specifically bind and respond to both VIP and PACAP. VIP and PACAP and their receptors are widely expressed in the brain and periphery. They are upregulated in neurons and immune cells in responses to CNS injury and/or inflammation and exert potent anti-inflammatory effects, as well as play important roles in the control of circadian rhythms and stress responses, among many others. VIP-R1 is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level. However, depending on its cellular location, VIP-R1 is also capable of coupling to additional G proteins such as G(q) protein, thus leading to the activation of phospholipase C and intracellular calcium influx.


Pssm-ID: 320652 [Multi-domain]  Cd Length: 269  Bit Score: 76.77  E-value: 6.14e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  866 LLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGiDKTQYE-------------IACP 932
Cdd:cd15986      2 IVVKTIYTLGHSVSLIALTTGSTILCLFRKLHCTRNYIHLNLFFSFILRAISVLVK-DDILYSssntehctvppslIGCK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  933 IFAGLLHYFFLAAFSWLCLEGVHLYLLLVEVFeSEYSRTKYYYLGGYCFPALVVGiaAAIDYRSYGTEKACWLRVDNYFI 1012
Cdd:cd15986     81 VSLVILQYCIMANFYWLLVEGLYLHTLLVVIF-SENRHFIVYLLIGWGIPTVFII--AWIVARIYLEDTGCWDTNDHSVP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1013 WSFIG-PVSFVIVVNLVF---LMVTLHKMIRSSSVLKPDSSRLdniKSWALGAIALLFLLGLTWAFGLLFINKESVVMAY 1088
Cdd:cd15986    158 WWVIRiPIIISIILNFILfisIIRILLQKLRSPDVGGNDQSQY---KRLAKSTLLLIPLFGVHYIVFVYFPDSSSSNYQI 234
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1034606781 1089 LFT-TFNAFQGVFIFVFHCALQKKVHKEYSKCLR 1121
Cdd:cd15986    235 FFElCLGSFQGLVVAILYCFLNSEVQGELKRKWR 268
7tmB1_PTH2R cd15982
parathyroid hormone 2 receptor, member of the class B family of seven-transmembrane G ...
868-1118 1.46e-14

parathyroid hormone 2 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; The parathyroid hormone 2 receptor (PTH2R), one of the three subtypes of PTH receptor family, is found in mammals and fish, but not in chicken or frog. PTH2R is potently activated by tuberoinfundibular peptide-39 (TIP-39) but not by PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH, an endocrine hormone that regulates calcium homoeostasis and bone maintenance, strongly activates human PTH2R, but only weakly activates rat and zebrafish PTH2Rs. These results suggest that TIP-39 is a natural ligand for PTH2R. Conversely, PTH1R is activated by PTH and PTHrP, but not by TIP-39. The PTH family receptors are members of the B1 (or secretin-like) subfamily of class B GPCRs, which include receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways.


Pssm-ID: 320648 [Multi-domain]  Cd Length: 289  Bit Score: 76.13  E-value: 1.46e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  868 LSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFL-----------------------------AELLF 918
Cdd:cd15982      4 LYIMYTVGYSISFSSLAVAIFIIGYFRRLHCTRNYIHMHLFVSFMLraasifvkdkvvhthigvkeldavlmndfQNAVD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  919 LVGIDKTQYeIACPIFAGLLHYFFLAAFSWLCLEGVHLYLLLVEVFeseYSRTKY---YYLGGYCFPALVVGIAAAIdyR 995
Cdd:cd15982     84 APPVDKSQY-VGCKIAVVMFIYFLATNYYWILVEGLYLHSLIFVAF---FSDTKYlwgFTLIGWGFPAVFVAAWAVV--R 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  996 SYGTEKACWLRVDNYFIWSFIGPVSFVIVVNLVFLMVTLHkmIRSSSVLKPDSSRLDNIKSWALGAIALLFLLgltWAFG 1075
Cdd:cd15982    158 ATLADARCWELSAGDIKWIYQAPILAAIGLNFILFLNTVR--VLATKIWETNAVGYDTRKQYRKLAKSTLVLV---LVFG 232
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034606781 1076 LLFInkESVVMAYLFTT------------FNAFQGVFIFVFHCALQKKVHKEYSK 1118
Cdd:cd15982    233 VHYI--VFVCLPHTFTGlgweirmhcelfFNSFQGFFVSIIYCYCNGEVQTEIKK 285
7tmB1_GLP1R cd15268
glucagon-like peptide-1 receptor, member of the class B family of seven-transmembrane G ...
866-1118 1.47e-14

glucagon-like peptide-1 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; Glucagon-like peptide-1 receptor (GLP1R) is a member of the glucagon receptor family of G protein-coupled receptors, which also includes glucagon receptor and GLP2R. GLP1R is activated by glucagon-like peptide 1 (GLP1), which is derived from the large proglucagon precursor. Activation of GLP1R stimulates glucose-dependent insulin secretion from pancreatic beta cells, whereas activation of GLP2R stimulates intestinal epithelial proliferation and increases villus height in the small intestine. GCGR regulates blood glucose levels by control of hepatic glycogenolysis and gluconeogenesis and by regulation of insulin secretion from the pancreatic beta-cells. Receptors in this group belong to the B1 (or secretin-like) subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on their cellular location, GCGR and GLP receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 341342 [Multi-domain]  Cd Length: 279  Bit Score: 75.76  E-value: 1.47e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  866 LLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLV-------------------GIDKTQ 926
Cdd:cd15268      2 LFLYIIYTVGYALSFSALVIASAILLGFRHLHCTRNYIHLNLFASFILRALSVFIkdaalkwmystaaqqhqwdGLLSYQ 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  927 YEIACPIFAGLLHYFFLAAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSygTEKACWLR 1006
Cdd:cd15268     82 DSLSCRLVFLLMQYCVAANYYWLLVEGVYLYTLLAFSVFSEQRIFRLYLSIGWGVPLLFVIPWGIVKYLY--EDEGCWTR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1007 VDNYFIWSFIG-PVSFVIVVN-LVFLMV--TLHKMIRSSSVLKPD-SSRLdnikswALGAIALLFLLG---LTWAFGLLF 1078
Cdd:cd15268    160 NSNMNYWLIIRlPILFAIGVNfLIFIRVicIVVSKLKANLMCKTDiKCRL------AKSTLTLIPLLGtheVIFAFVMDE 233
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1034606781 1079 INKESVVMAYLFT--TFNAFQGVFIFVFHCALQKKVHKEYSK 1118
Cdd:cd15268    234 HARGTLRFVKLFTelSFTSFQGLMVAILYCFVNNEVQMEFRK 275
Gal_Rha_Lectin_LAT2 cd22840
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ...
39-128 3.14e-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: 69.75  E-value: 3.14e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   39 LACEGYPIELRCPGSDVIMVENANYGRTDD-KICDaDPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFP-DPCP 116
Cdd:cd22840      5 VACEGDPFEISCPSGQRIKVDYASYGAIGTrSTCG-DSVSPAGETCSAPNSLQTMRQRCQGRQSCEIRVLNSLFPnDPCP 83
                           90
                   ....*....|...
gi 1034606781  117 GTY-KYLEVQYDC 128
Cdd:cd22840     84 GTSkKYLEYRYRC 96
7tmB1_VIP-R1 cd15269
vasoactive intestinal polypeptide (VIP) receptor 1, member of the class B family of ...
874-1121 4.48e-14

vasoactive intestinal polypeptide (VIP) receptor 1, member of the class B family of seven-transmembrane G protein-coupled receptors; Vasoactive intestinal peptide (VIP) receptor 1 is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, growth-hormone-releasing hormone (GHRH), and pituitary adenylate cyclase activating polypeptide (PACAP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. VIP and PACAP exert their effects through three G protein-coupled receptors, PACAP-R1, VIP-R1 (vasoactive intestinal receptor type 1, also known as VPAC1) and VIP-R2 (or VPAC2). PACAP-R1 binds only PACAP with high affinity, whereas VIP-R1 and -R2 specifically bind and respond to both VIP and PACAP. VIP and PACAP and their receptors are widely expressed in the brain and periphery. They are upregulated in neurons and immune cells in responses to CNS injury and/or inflammation and exert potent anti-inflammatory effects, as well as play important roles in the control of circadian rhythms and stress responses, among many others. VIP-R1 is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level. However, depending on its cellular location, VIP-R1 is also capable of coupling to additional G proteins such as G(q) protein, thus leading to the activation of phospholipase C and intracellular calcium influx.


Pssm-ID: 320397 [Multi-domain]  Cd Length: 268  Bit Score: 74.12  E-value: 4.48e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  874 VGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGiDKTQYE-----------IACPIFAGLLHYFF 942
Cdd:cd15269     10 IGHSLSLISLTAAMIILCLFRKLHCTRNYIHMHLFMSFILRAIAVFIK-DAVLFEsgeedhcsvasVGCKAAMVFFQYCI 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  943 LAAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPAlvVGIAAAIDYRSYGTEKACWLRVDNYFIWSFI-GPVSF 1021
Cdd:cd15269     89 MANFFWLLVEGLYLHTLLAVSFFSERKYFWWYILIGWGAPS--VFITAWSVARIYFEDVGCWDTIIESLLWWIIkTPILV 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1022 VIVVNLVFLMV---TLHKMIRSSSVLKPDSSRLDNIkswALGAIALLFLLGLTWAFGLLFINKESVVMAYLFT-TFNAFQ 1097
Cdd:cd15269    167 SILVNFILFICiirILVQKLHSPDIGRNESSQYSRL---AKSTLLLIPLFGIHYIMFAFFPDNFKAEVKLVFElILGSFQ 243
                          250       260
                   ....*....|....*....|....
gi 1034606781 1098 GVFIFVFHCALQKKVHKEYSKCLR 1121
Cdd:cd15269    244 GFVVAVLYCFLNGEVQAELKRKWR 267
7tmB1_NPR_B3_insect-like cd15262
insect neuropeptide receptor subgroup B3 and related proteins belong to subfamily B1 of ...
878-1115 1.17e-13

insect neuropeptide receptor subgroup B3 and related proteins belong to subfamily B1 of hormone receptors; member of the class B secretin-like seven-transmembrane G protein-coupled receptors; This subgroup includes a neuropeptide receptor found in Bombyx mori (silk worm) and its closely related proteins from arthropods. They belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. The class B GPCRs have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi, or prokaryotes.


Pssm-ID: 320390 [Multi-domain]  Cd Length: 270  Bit Score: 72.86  E-value: 1.17e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  878 ISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVG-----IDK----------TQYEIACPIFAGLLHYFF 942
Cdd:cd15262     14 VSVVTSLPAVFIFYSYKRLRITRVILHRNLLISIIIRNILVIISkvfviLDAltssgddtvmNQNAVVCRLLSIFERAAR 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  943 LAAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGY--CFPALVVGIAAAIDYRSygtekACWLRVDNYFIWSFIGPVS 1020
Cdd:cd15262     94 NAVFACMFVEGFYLHRLIVAVFAEKSSIRFLYVIGAVlpLFPVIIWAIIRALHNDH-----SCWVVDIEGVQWVLDTPRL 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1021 FVIVVNLVFLMVTLHKMIRsssvlkpdSSRLDNIKSWALGAI-ALLFLLGLtwaFGLLF---INKESV-------VMAYL 1089
Cdd:cd15262    169 FILLVNTVLLVDIIRVLVT--------KLRNTEENSQTKSTTrATLFLVPL---FGLHFvitAYRPSTddcdwedIYYYA 237
                          250       260
                   ....*....|....*....|....*.
gi 1034606781 1090 FTTFNAFQGVFIFVFHCALQKKVHKE 1115
Cdd:cd15262    238 NYLIEGLQGFLVAILFCYINKEVHYL 263
7tmB1_GHRHR2 cd15271
growth-hormone-releasing hormone receptor type 2, member of the class B family of ...
874-1121 1.19e-13

growth-hormone-releasing hormone receptor type 2, member of the class B family of seven-transmembrane G protein-coupled receptors; Growth hormone-releasing hormone receptor type 2 (GHRHR2) is found in non-mammalian vertebrates such as chicken and frog. It is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, pituitary adenylate cyclase activating polypeptide (PACAP), vasoactive intestinal peptide, and mammalian growth hormone-releasing hormone. These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. Mammalian GHRHR is a specific receptor for the growth hormone-releasing hormone (GHRH) that controls the synthesis and release of growth hormone (GH) from the anterior pituitary somatotrophs. Mutations in the gene encoding GHRHR have been connected to isolated growth hormone deficiency (IGHD), a short-stature condition caused by deficient production of GH or lack of GH action. Mammalian GHRH is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level. GHRHR is found in mammals as well as zebrafish and chicken, whereas the GHRHR type 2, an ortholog of the GHRHR, has only been identified in ray-finned fish, chicken and Xenopus. Xenopus laevis GHRHR2 has been shown to interact with both endogenous GHRH and PACAP-related peptide (PRP).


Pssm-ID: 320399 [Multi-domain]  Cd Length: 267  Bit Score: 72.84  E-value: 1.19e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  874 VGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLV---------GIDK-TQYEIACPIFAGLLHYFFL 943
Cdd:cd15271     10 VGYGTSLTSLITAVLIFCTFRKLHCTRNYIHINLFVSFILRALAVFIkdavlfadeSVDHcTMSTVACKAAVTFFQFCVL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  944 AAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIdyRSYGTEKACWLRVDNYFIWSFIGPVSFVI 1023
Cdd:cd15271     90 ANFFWLLVEGMYLQTLLLLTFTSDRKYFWWYILIGWGAPSVTVTVWVLT--RLQYDNRGCWDDLESRIWWIIKTPILLSV 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1024 VVN-LVFLMVT---LHKmIRSSSVLKPDSSRLdniKSWALGAIALLFLLGLTWAFGLLFINKESV-VMAYLFTTFNAFQG 1098
Cdd:cd15271    168 FVNfLIFINVIrilVQK-LKSPDVGGNDTSHY---MRLAKSTLLLIPLFGVHYVVFAFFPEHVGVeARLYFELVLGSFQG 243
                          250       260
                   ....*....|....*....|...
gi 1034606781 1099 VFIFVFHCALQKKVHKEYSKCLR 1121
Cdd:cd15271    244 FIVALLYCFLNGEVQAEIKKRLG 266
7tmB1_PTHR cd15265
parathyroid hormone receptors, member of the class B family of seven-transmembrane G ...
868-1118 1.85e-13

parathyroid hormone receptors, member of the class B family of seven-transmembrane G protein-coupled receptors; The parathyroid hormone (PTH) receptor family has three subtypes: PTH1R, PTH2R and PTH3R. PTH1R is expressed in bone and kidney and is activated by two polypeptide ligands: PTH, an endocrine hormone that regulates calcium homoeostasis and bone maintenance, and PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH1R couples predominantly to a G(s)-protein that in turn activates adenylate cyclase thereby producing cAMP, but it can also couple to several G protein subtypes, including G(q/11), G(i/o), and G(12/13), resulting in activation of multiple intracellular signaling pathways. PTH2R is potently activated by tuberoinfundibular peptide-39 (TIP-39), but not by PTHrP. PTH also strongly activates human PTH2R, but only weakly activates rat and zebrafish PTH2Rs, suggesting that TIP-39 is a natural ligand for PTH2R. On the other hand, PTH3R binds and responds to both PTH and PTHrP, but not the TIP-39. Moreover, the PTH3R is more closely related to the PTH1R than PTH2R. PTH1R is found in all vertebrate species, whereas PTH2R is found in mammals and fish, but not in chicken or frog. The PTH3R is found in chicken and fish, but it is absent in mammals. The PTH receptors are members of the B1 (or secretin-like) subfamily of class B GPCRs, which include receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways.


Pssm-ID: 320393 [Multi-domain]  Cd Length: 289  Bit Score: 72.79  E-value: 1.85e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  868 LSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHknlcINLFLAELLFLVGI------------------------- 922
Cdd:cd15265      4 LYLIYTVGYSISLVSLTVAVFILGYFRRLHCTRNYIH----MHLFVSFMLRAVSIfvkdavlysgsgldelerpsmedlk 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  923 --------DKTQYeIACPIFAGLLHYFFLAAFSWLCLEGVHLYLLlveVFESEYSRTKYYY---LGGYCFPALVVGIAAA 991
Cdd:cd15265     80 siveappvDKSQY-VGCKVAVTLFLYFLATNYYWILVEGLYLHSL---IFMAFFSDKKYLWgftLIGWGFPAVFVIPWAS 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  992 IdyRSYGTEKACWLRVDNYFIWSFIGPVSFVIVVN-LVFLMV--TLHKMIRSSSVLKPDSSRLDniKSWALGAIALLFLL 1068
Cdd:cd15265    156 V--RATLADTRCWDLSAGNYKWIYQVPILAAIVVNfILFLNIvrVLATKLRETNAGRCDTRQQY--RKLAKSTLVLIPLF 231
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034606781 1069 GLTWafgLLFinkesVVMAYLFTT------------FNAFQGVFIFVFHCALQKKVHKEYSK 1118
Cdd:cd15265    232 GVHY---IVF-----MGMPYTEVGllwqirmhyelfFNSFQGFFVAIIYCFCNGEVQAEIKK 285
7tmB2_GPR124 cd15998
G protein-coupled receptor 124, member of the class B2 family of seven-transmembrane G ...
878-1119 3.55e-13

G protein-coupled receptor 124, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR124 is an orphan receptor that has been classified as that belongs to the group III of adhesion GPCRs, which also includes orphan GPR123 and GPR125. GPR124, also known as tumor endothelial marker 5 (TEM5), is highly expressed in tumor vessels and in the vasculature of the developing embryo. GPR124 is essentially required for proper angiogenic sprouting into neural tissue, CNS-specific vascularization, and formation of the blood-brain barrier. GPR124 interacts with the PDZ domain of DLG1 (discs large homolog 1) through its PDZ-binding motif. Recently, studies of double-knockout mice showed that GPR124 functions as a co-activator of Wnt7a/Wnt7b-dependent beta-catenin signaling in brain endothelium. Moreover, WNT7-stimulated beta-catenin signaling is regulated by GPR124's intracellular PDZ binding motif and leucine-rich repeats (LRR) in its N-terminal extracellular domain. 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. Furthermore, 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.


Pssm-ID: 320664 [Multi-domain]  Cd Length: 268  Bit Score: 71.53  E-value: 3.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  878 ISLVCLAICISTFCFLRG-LQTDRNTIHK--NLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLAAFSWLCLEGV 954
Cdd:cd15998     14 LLLLCLFSTIITYILNHSsIHVSRKGWHMllNLCFHIAMTSAVFAGGITLTNYQMVCQAVGITLHYSSLSTLLWMGVKAR 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  955 HLYLLLV---------EVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKA-CWLrvdnyfIW-----SFIGPV 1019
Cdd:cd15998     94 VLHKELTwrapppqegDPALPTPRPMLRFYLIAGGIPLIICGITAAVNIHNYRDHSPyCWL------VWrpslgAFYIPV 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1020 SFVIVVNLV-FLMVTLHKMIRSSSVlkpDSSRLDNIKSWALGAIALLFLlgLTWAFGLLFINKE---SVVMAYLFTTFNA 1095
Cdd:cd15998    168 ALILLVTWIyFLCAGLHLRGPSADG---DSVYSPGVQLGALVTTHFLYL--AMWACGALAVSQRwlpRVVCSCLYGVAAS 242
                          250       260
                   ....*....|....*....|....
gi 1034606781 1096 FQGVFIFVFHCALQKKVHKEYSKC 1119
Cdd:cd15998    243 ALGLFVFTHHCARRRDVRASWRAC 266
7tmB1_PTH1R cd15984
parathyroid hormone 1 receptor, member of the class B family of seven-transmembrane G ...
868-1118 3.58e-13

parathyroid hormone 1 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; The parathyroid hormone (PTH) receptor family has three subtypes: PTH1R, PTH2R and PTH3R. PTH1R is expressed in bone and kidney and is activated by two polypeptide ligands: PTH, an endocrine hormone that regulates calcium homoeostasis and bone maintenance, and PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH1R couples predominantly to G(s)-protein that in turn activates adenylate cyclase thereby producing cAMP, but it can also couple to several G protein subtypes, including G(q/11), G(i/o), and G(12/13), resulting in activation of multiple intracellular signaling pathways. PTH1R is found in all vertebrate species, whereas PTH2R is found in mammals and fish, but not in chicken or frog. PTH3R is found in chicken and fish, but it is absent in mammals. The PTH receptors are members of the B1 (or secretin-like) subfamily of class B GPCRs, which include receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways.


Pssm-ID: 320650 [Multi-domain]  Cd Length: 290  Bit Score: 71.90  E-value: 3.58e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  868 LSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNL-------CINLFLAELLFLVG------------------- 921
Cdd:cd15984      4 LYLIYTVGYSISLGSLTVAVLILGYFRRLHCTRNYIHMHLflsfmlrAVSIFVKDAVLYSGsaleemeriteedlksite 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  922 ---IDKTQYeIACPIFAGLLHYFFLAAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIdyRSYG 998
Cdd:cd15984     84 appADKAQF-VGCKVAVTFFLYFLATNYYWILVEGLYLHSLIFMAFFSEKKYLWGFTLFGWGLPAVFVTIWASV--RATL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  999 TEKACWLRVDNYFIWSFIGPVSFVIVVNLVFLMVTLHkmIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLtwaFGLLF 1078
Cdd:cd15984    161 ADTGCWDLSAGNLKWIIQVPILAAIVVNFILFINIVR--VLATKLRETNAGRCDTRQQYRKLLKSTLVLMPL---FGVHY 235
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034606781 1079 InkesVVMAYLFTT---------------FNAFQGVFIFVFHCALQKKVHKEYSK 1118
Cdd:cd15984    236 I----VFMAMPYTEvsgilwqvqmhyemlFNSFQGFFVAIIYCFCNGEVQAEIKK 286
7tmB2_GPR125 cd15999
G protein-coupled receptor 125, member of the class B2 family of seven-transmembrane G ...
865-1126 5.25e-13

G protein-coupled receptor 125, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR125 is an orphan receptor that has been classified as that belongs to the group III of adhesion GPCRs, which also includes orphan receptors GPR123 and GPR124. GPR125 directly interacts with dishevelled (Dvl) via its intracellular C-terminus, and together, GPR125 and Dvl recruit a subset of planar cell polarity (PCP) components into membrane subdomains, a prerequisite for activation of Wnt/PCP signaling. Thus, GPR125 influences the noncanonical WNT/PCP pathway, which does not involve beta-catenin, through interacting with and modulating the distribution of Dvl. 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. Furthermore, 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.


Pssm-ID: 320665  Cd Length: 312  Bit Score: 71.82  E-value: 5.25e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  865 ELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHK--NLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFF 942
Cdd:cd15999      2 DLLHPVVYATAVVLLLCLLTIIVSYIYHHSLVRISRKSWHMlvNLCFHIFLTCAVFVGGINQTRNASVCQAVGIILHYST 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  943 LAAFSWLCLEGVHLYLLLV----------EVFESEYSRTKYYYLGGyCFPALVVGIAAAIDYRSYGTEKA---CWLRVDN 1009
Cdd:cd15999     82 LATVLWVGVTARNIYKQVTrkakrcqdpdEPPPPPRPMLRFYLIGG-GIPIIVCGITAAANIKNYGSRPNapyCWMAWEP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1010 YfIWSFIGPVSFVIVVNL-----VFLMVTLH-----------------------------KMIRSSSVLKPDSSRLDNIK 1055
Cdd:cd15999    161 S-LGAFYGPAGFIIFVNCmyflsIFIQLKRHperkyelkepteeqqrlaasehgelnhqdSGSSSASCSLVSTSALENEH 239
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034606781 1056 SWA---LGAIALLFLLGLTWAFGLLFINKE---SVVMAYLFTTFNAFQGVFIFVFHCALQKKVHKEYSkclrhSYCC 1126
Cdd:cd15999    240 SFQaqlLGASLALFLYVALWIFGALAVSLYypmDLVFSCLFGATCLSLGAFLVVHHCVNREDVRRAWI-----ATCC 311
7tmB1_GHRHR cd15270
growth-hormone-releasing hormone receptor, member of the class B family of seven-transmembrane ...
868-1118 1.09e-12

growth-hormone-releasing hormone receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; Growth hormone-releasing hormone receptor (GHRHR) is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, pituitary adenylate cyclase activating polypeptide (PACAP), and vasoactive intestinal peptide. These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. GHRHR is a specific receptor for the growth hormone-releasing hormone (GHRH) that controls the synthesis and release of growth hormone (GH) from the anterior pituitary somatotrophs. Mutations in the gene encoding GHRHR have been connected to isolated growth hormone deficiency (IGHD), a short-stature condition caused by deficient production of GH or lack of GH action. GHRH is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level. GHRHR is found in mammals as well as zebrafish and chicken, whereas the GHRHR type 2, an ortholog of the GHRHR, has only been identified in ray-finned fish, chicken and Xenopus. Xenopus laevis GHRHR2 has been shown to interact with both endogenous GHRH and PACAP-related peptide (PRP).


Pssm-ID: 320398 [Multi-domain]  Cd Length: 268  Bit Score: 70.21  E-value: 1.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  868 LSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHknlcINLFLAELLFLVGI---DKTQYE-----------IACPI 933
Cdd:cd15270      4 VKIIYTVGYSISIVSLCVAVAILVAFRRLHCPRNYIH----IQLFFTFILKAIAVfikDAALFQeddtdhcsmstVLCKV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  934 FAGLLHYFFLAAFSWLCLEGVHLYLLLVEVFeseySRTKYYY----LGGYCFPALVVGIaaAIDYRSYGTEKACW-LRVD 1008
Cdd:cd15270     80 SVVFCHYCVMTNFFWLLVEAVYLNCLLASSF----PRGKRYFwwlvLLGWGLPTLCTGT--WILCKLYFEDTECWdINND 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1009 NYFIWSFIGPVSFVIVVNLVFLMVTLHKMIRSssvLKPDSSRLDN-IKSWALGAIALLF--LLGLTW-AFGLLFINKESV 1084
Cdd:cd15270    154 SPYWWIIKGPIVISVGVNFLLFLNIIRILLKK---LDPRQINFNNsAQYRRLSKSTLLLipLFGTHYiIFNFLPDYAGLG 230
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1034606781 1085 VMAYLFTTFNAFQGVFIFVFHCALQKKVHKEYSK 1118
Cdd:cd15270    231 IRLYLELCLGSFQGFIVAVLYCFLNQEVQTEISR 264
7tmB1_GlucagonR-like_1 cd15985
uncharacterized group of glucagon receptor-like proteins, member of the class B family of ...
874-1121 8.04e-12

uncharacterized group of glucagon receptor-like proteins, member of the class B family of seven-transmembrane G protein-coupled receptors; This group consists of uncharacterized proteins with similarity to members of the glucagon receptor family of G protein-coupled receptors, which include glucagon receptor (GCGR), and glucagon-like peptide-1 receptor (GLP1R), and GLP2R. The glucagon receptors are activated by the members of the glucagon (GCG) peptide family including GCG, glucagon-like peptide 1 (GLP1), and GLP2, which are derived from the large proglucagon precursor. GCGR regulates blood glucose levels by control of hepatic glycogenolysis and gluconeogenesis and by regulation of insulin secretion from the pancreatic beta-cells. Activation of GLP1R stimulates glucose-dependent insulin secretion from pancreatic beta cells, whereas activation of GLP2R stimulates intestinal epithelial proliferation and increases villus height in the small intestine. Receptors in this group belong to the B1 (or secretin-like) subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on their cellular location, GCGR and GLP receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320651 [Multi-domain]  Cd Length: 280  Bit Score: 67.65  E-value: 8.04e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  874 VGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLV---------GIDKTQYE-----------IACPI 933
Cdd:cd15985     10 VGYTLSLLTLVSALLILTSIRKLHCTRNYIHANLFASFILRAVSVIVkdtllerrwGREIMRVAdwgellshkaaIGCRM 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  934 FAGLLHYFFLAAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEkaCWLRVDNYFIW 1013
Cdd:cd15985     90 AQVVMQYCILANHYWFFVEAVYLYKLLIGAVFSEKNYYLLYLYLGWGTPVLFVVPWMLAKYLKENKE--CWALNENMAYW 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1014 SFIG-PVSFVIVVNLVFLM----VTLHKMiRSSSVLKPDSS-RLdnikswalgAIALLFLLGLTWAFGLLFI----NKES 1083
Cdd:cd15985    168 WIIRiPILLASLINLLIFMrilkVILSKL-RANQKGYADYKlRL---------AKATLTLIPLFGIHEVVFIfatdEQTT 237
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1034606781 1084 VVMAYL---FTTF-NAFQGVFIFVFHCALQKKVHKEYSKCLR 1121
Cdd:cd15985    238 GILRYIkvfFTLFlNSFQGFLVAVLYCFANKEVKSELLKKWR 279
7tmB1_GCGR cd15267
glucagon receptor, member of the class B family of seven-transmembrane G protein-coupled ...
874-1118 3.02e-11

glucagon receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; Glucagon receptor (GCGR) is a member of the glucagon receptor family of G protein-coupled receptors, which also includes glucagon-like peptide-1 receptor (GLP1R) and GLP2R. GCGR is activated by glucagon, which is derived from the large proglucagon precursor. GCGR regulates blood glucose levels by control of hepatic glycogenolysis and gluconeogenesis and by regulation of insulin secretion from the pancreatic beta-cells. Activation of GLP1R stimulates glucose-dependent insulin secretion from pancreatic beta cells, whereas activation of GLP2R stimulates intestinal epithelial proliferation and increases villus height in the small intestine. GCGR belongs to the B1 (or secretin-like) subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on their cellular location, GCGR and GLP receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320395 [Multi-domain]  Cd Length: 281  Bit Score: 66.00  E-value: 3.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  874 VGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLV--GIDKTQYE-----------------IACPIF 934
Cdd:cd15267     12 VGYSLSLGALLLALAILGGFSKLHCMRNAIHMNLFASFILKASSVLVidGLLRTRYSqkieddlsstwlsdeavAGCRVA 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  935 AGLLHYFFLAAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEkaCWLRVDNYFIWS 1014
Cdd:cd15267     92 AVFMQYGIVANYCWLLVEGIYLHNLLVLAVFPERSYFSLYLCIGWGAPALFVVPWVVVKCLYENVQ--CWTSNDNMGFWW 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1015 FI-GPVSFVIVVNLVFLMVTLHKMIrssSVLKPDSSRLDNIK-SWALGAIALLFLLGLTwAFGLLFINKESVV----MAY 1088
Cdd:cd15267    170 ILrFPVFLAILINFFIFVRIIQILV---SKLRARQMHYTDYKfRLAKSTLTLIPLLGIH-EVVFAFVTDEHAQgtlrSAK 245
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1034606781 1089 LFTT--FNAFQGVFIFVFHCALQKKVHKEYSK 1118
Cdd:cd15267    246 LFFDlfLSSFQGLLVAVLYCFLNKEVQSELRR 277
Gal_Rha_Lectin_PKD1L2 cd22831
galactose binding lectin domain found in polycystic kidney disease protein 1-like 2 ...
37-128 5.48e-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: 5.48e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   37 RELACEGYPIELRCPGSDVIMVENANYGRTDDKIC--DADPFQMENVQ-CYLPDAFKIMSQRCNNRTQCVVVAGSDAFPD 113
Cdd:cd22831      2 RSLACEDYNATLQCGSGQVIEIDDSFYGRNTPHYCrsENPSPPTDSQErCSWVDVRDLVAAQCHGLQVCQIPADPSSFGE 81
                           90
                   ....*....|....*
gi 1034606781  114 PCPGTYKYLEVQYDC 128
Cdd:cd22831     82 PCPELGSYLSVEYHC 96
HRM pfam02793
Hormone receptor domain; This extracellular domain contains four conserved cysteines that ...
485-543 6.94e-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: 56.22  E-value: 6.94e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034606781  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 3.62e-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: 54.98  E-value: 3.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   40 ACEGYP---IELRCPGSDVI-MVENANYGrTDDKICDAdpFQMENvqCYLPDAFKIMSQRCNNRTQCVVVAGSDA-FPDP 114
Cdd:cd22842      3 VNEGGPgstLTLSCPAGQVIsSIDFASYG-TPTGTCGS--FSKGS--CHAPNSLSVVEKACLGKNSCSIPASNSVfFGDP 77
                           90
                   ....*....|....
gi 1034606781  115 CPGTYKYLEVQYDC 128
Cdd:cd22842     78 CPGTTKRLAVQATC 91
7tmB1_PTH3R cd15983
parathyroid hormone 3 receptor, member of the class B family of seven-transmembrane G ...
868-1118 8.43e-09

parathyroid hormone 3 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; The parathyroid hormone 3 receptor (PTH3R), one of the three subtypes of PTH receptor family, is found in chicken and fish, but it is absent in mammals. On the other hand, the PTH1R is found in all vertebrate species, whereas PTH2R is found in mammals and fish, but not in chicken or frog. PTH1R is activated by two polypeptide ligands: PTH, an endocrine hormone that regulates calcium homoeostasis and bone maintenance, and PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH2R is potently activated by tuberoinfundibular peptide-39 (TIP-39), but not by PTHrP. PTH also strongly activates human PTH2R, but only weakly activates rat and zebrafish PTH2Rs, suggesting that TIP-39 is a natural ligand for PTH2R. Conversely, PTH3R binds and responds to both PTH and PTHrP, but not the TIP-39. The PTH family receptors are members of the B1 (or secretin-like) subfamily of class B GPCRs, which include receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways.


Pssm-ID: 320649 [Multi-domain]  Cd Length: 285  Bit Score: 58.40  E-value: 8.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  868 LSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNL-------CINLFLAELLFLVGIDKTQYE------------ 928
Cdd:cd15983      4 LHLMYTIGYSISLAALLVAVCILCYFKRLHCTRNYIHIHLfasficrAGSIFVKDAVLYSGTNEGEALdekiefglspgt 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  929 ----IACPIFAGLLHYFFLAAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIdyRSYGTEKACW 1004
Cdd:cd15983     84 rlqwVGCKVTVTLFLYFLATNHYWILVEGLYLHSLIFMAFLSDKNYLWALTIIGWGLPAVFVSVWASV--RVSLADTQCW 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1005 LRVDNYFIWSFIGPVSFVIVVNLvFLMVTLHKMIrSSSVLKPDSSRLDNIKSWALGAIALLFLLGLtwaFGLLFInkesV 1084
Cdd:cd15983    162 DLSAGNLKWIYQVPILAAILVNF-FLFLNIVRVL-ASKLWETNTGKLDPRQQYRKLLKSTLVLMPL---FGVHYV----L 232
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1034606781 1085 VMAYLFTT---------------FNAFQGVFIFVFHCALQKKVHKEYSK 1118
Cdd:cd15983    233 FMAMPYTDvtgllwqiqmhyemlFNSSQGFFVAFIYCFCNGEVQAEIKK 281
Gal_Rha_Lectin-like_P113 cd22843
galactose/rhamnose binding lectin-like domain found in Plasmodium falciparum P113 and similar ...
39-128 3.24e-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: 3.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781   39 LACEGYPIELRCPGSDVIMVENANYGR--TDDKICdadpFQMENVQCYLPDAFkimSQRCNNRTQCVVVAGSDAFPDPCP 116
Cdd:cd22843      5 FVCFGQEVTIHCPGDGNISIKSATYGYnnSNVCIY----CNSFNCDKDITSPV---NKKCCGKNTCVLTVSDILEGNPCG 77
                           90
                   ....*....|..
gi 1034606781  117 GTYKYLEVQYDC 128
Cdd:cd22843     78 IGNSYIRVVYTC 89
PHA03247 PHA03247
large tegument protein UL36; Provisional
399-503 2.10e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 2.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  399 PPDPSAGED-DSLPGPATSPPLSTTTTARPTPLTSTASPAATTPLRRAPLTTHPVGAINQLGPDLPPATAPVPS---TRR 474
Cdd:PHA03247  2786 PAVASLSESrESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGgdvRRR 2865
                           90       100
                   ....*....|....*....|....*....
gi 1034606781  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 ...
427-581 2.48e-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: 2.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  427 PTP--LTSTASPAATTPLRR-------APLTTHPVGAINQLGPDlppATAPVPSTrRPPAPNLhVSPEL-FCEPREVRRV 496
Cdd:pfam05109  476 PTPagTTSGASPVTPSPSPRdngteskAPDMTSPTSAVTTPTPN---ATSPTPAV-TTPTPNA-TSPTLgKTSPTSAVTT 550
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  497 QWP-ATQQGMLVERPCPKGTrgiasfqcLPALGLWNPRgpdlSNCTSPWVNQVAQKIKSGENAANIASelarHTRGSIYA 575
Cdd:pfam05109  551 PTPnATSPTPAVTTPTPNAT--------IPTLGKTSPT----SAVTTPTPNATSPTVGETSPQANTTN----HTLGGTSS 614

                   ....*.
gi 1034606781  576 GDVSSS 581
Cdd:pfam05109  615 TPVVTS 620
PHA03247 PHA03247
large tegument protein UL36; Provisional
399-501 2.64e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 2.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  399 PPDPSAGEDDSLPGPATSpplsttttARPTPLTSTASPAATTPLRRAPLTTHPVGAinqlGPDLPPATAPVPSTRRPPAP 478
Cdd:PHA03247  2722 PPGPAAARQASPALPAAP--------APPAVPAGPATPGGPARPARPPTTAGPPAP----APPAAPAAGPPRRLTRPAVA 2789
                           90       100
                   ....*....|....*....|...
gi 1034606781  479 NLHVSPELFCEPREVRRVQWPAT 501
Cdd:PHA03247  2790 SLSESRESLPSPWDPADPPAAVL 2812
7tm_GPCRs cd14964
seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary ...
868-1107 3.83e-03

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.


Pssm-ID: 410628 [Multi-domain]  Cd Length: 267  Bit Score: 40.87  E-value: 3.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  868 LSVITWVGIVISLVCLAICISTFCFLRglqtDRNTIHKNLCINLFLAELLFLVGID-----KTQYEIA------CPIFAG 936
Cdd:cd14964      1 TTIILSLLTCLGLLGNLLVLLSLVRLR----KRPRSTRLLLASLAACDLLASLVVLvlfflLGLTEASsrpqalCYLIYL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  937 LLHYFFLAAFSWLCLEGVHLYLLLVEVFESEYSR----TKYYYLGGYCFPALVVGIAAA----IDYRSYGTEKACWLRVD 1008
Cdd:cd14964     77 LWYGANLASIWTTLVLTYHRYFALCGPLKYTRLSspgkTRVIILGCWGVSLLLSIPPLVgkgaIPRYNTLTGSCYLICTT 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781 1009 NYFIWSF-IGPVSFVIVVNLVFLMVTLHKMIRSSSVLKPDSSRLD--NIKSWALGAIALLFLLGLTWAFGLLFINKESV- 1084
Cdd:cd14964    157 IYLTWGFlLVSFLLPLVAFLVIFSRIVLRLRRRVRAIRSAASLNTdkNLKATKSLLILVITFLLCWLPFSIVFILHALVa 236
                          250       260
                   ....*....|....*....|....*....
gi 1034606781 1085 ------VMAYLFTTFNAFQGVFIFVFHCA 1107
Cdd:cd14964    237 agqglnLLSILANLLAVLASTLNPFIYCL 265
7tmE_cAMP_R_Slime_mold cd14940
slime mold cyclic AMP receptor, member of the class E family of seven-transmembrane G ...
877-1081 9.13e-03

slime mold cyclic AMP receptor, member of the class E family of seven-transmembrane G protein-coupled receptors; This family represents the class E of seven-transmembrane G-protein coupled receptors found in soil-living amoebas, commonly referred to as slime molds. The class E family includes cAMP receptors (cAR1-4) and cAMP receptors-like proteins (CrlA-C) from Dictyostelium discoideum, and their highly homologous cAMP receptors (TasA and TasB) from Polysphondylium pallidum. So far, four subtypes of cAMP receptors (cAR1-4) have been identified that play an essential role in the detection and transmit of the periodic extracellular cAMP waves that regulate chemotactic cell movement during Dictyostelium development, from the unicellular amoeba aggregate into many multicellular slugs and then differentiate into a sporocarp, a fruiting body with cells specialized for different functions. These four subtypes differ in their expression levels and patterns during development. cAR1 is high-affinity receptor that is the first one to be expressed highly during early aggregation and continues to be expressed at low levels during later developmental stages. cAR1 detects extracellular cAMP and is coupled to G-alpha2 protein. Cells lacking cAR1 fail to aggregate, demonstrating that cAR1 is responsible for aggregation. During later aggregation the high-affinity cAR3 receptor is expressed at low levels. Nonetheless, cells lacking cAR3 do not show an obviously altered pattern of development and are still able to aggregate into fruiting bodies. In contrast, cAR2 and cAR4 are low affinity receptors expressed predominantly after aggregation in pre-stalk cells. cAR2 is essential for normal tip formation and deletion of the receptor arrests development at the mound stage. On the other hand, CAR4 regulates axial patterning and cellular differentiation, and deletion of the receptor results in defects during culmination. Furthermore, three cAMP receptor-like proteins (CrlA-C) were identified in Dictyostelium that show limited sequence similarity to the cAMP receptors. Of these CrlA is thought to be required for normal cell growth and tip formation in developing aggregates.


Pssm-ID: 320094 [Multi-domain]  Cd Length: 256  Bit Score: 39.64  E-value: 9.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  877 VISLV-CLAICIStFCFLRGLqtdRNTIHK---NLCINLFLAELLFLVG-IDKTQYE--IACPIFAGLLHYFFLAAFSWL 949
Cdd:cd14940     11 FSSIIgCLFVLVG-FWLLKLL---RNHITRvisCFCLTSLLKDIIYTMLtLTQSARPdgFLCYLYAIVITYGSLSCWLWT 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034606781  950 CLEGVHLYLLLV-EVFESEYSRtKYYYLGGYCFPALVVGIAAAIDyrSYGTEKA-CWLRVDN--YFIWSFIGPVSFVIVV 1025
Cdd:cd14940     87 LCLAISIYLLIVkREPEPEKFE-KYYHFVCWGLPLISTIIMLIKH--HYGPVGNwCWIGNQYtgYRFGLFYGPFFIIFGI 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034606781 1026 NLV---FLMVTLHKMIRSSSVLKPDSSRLDNIKswalgAIALLFLLGLTWAFGLlfINK 1081
Cdd:cd14940    164 SAVlvgLTSHYTYQVIHNWVSDNKDLHKTYQFK-----LVNYIIVFLLCWIFAV--INR 215
 
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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