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Conserved domains on  [gi|1880350455|ref|XP_035509159|]
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adhesion G protein-coupled receptor L2 isoform X2 [Morone saxatilis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Latrophilin pfam02354
Latrophilin Cytoplasmic C-terminal region; This family consists of the cytoplasmic C-terminal ...
 1102-1499 0e+00

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: 634.60  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1102 RHTYCCGGLPTESSHGSAKTSTTRTSARYSSGTQSRIRRMWNDTVRKQSESSFISGDINSTSTLNQGMTGNYLLTNPLLR 1181
Cdd:pfam02354    1 RHSHCCSGLSSEGSHGSAKTSASRTTARYSTGTQSRIRRMWNDTVRKQSESSFIAGDINSTPTLNRGTMGNHLLTNPLLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1182 PQGTNNPYNTLLAETVVCNTPTAPVFNSPvtyreTRHSLNNAvRDTSAMDTLPLNGNFNNSYSLRNGDF--GDSVQVVDC 1259
Cdd:pfam02354   81 PHGTTNPYNTLLAESVVFNPPSPPVFNSP-----GKHSLSNS-RDSSGMDTLPLNGNFNNSYSLRSGDYenPDGTATYGC 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1260 GLSLDDAAFEKMIISELVHNNLRACNKSHqqqqqqhpslhhpphhqqppQYHQHHHAERAPPKVTVV----GGSSSSEDD 1335
Cdd:pfam02354  155 RRNLDDAAFEKMIISELVHNNLRGRGNPK--------------------GRDHTRTSDRALPPHTNSggagGGGSGEEDD 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1336 AIVADASSLVHM---GDTVGLELhHQQELEAPLIPQRTHSLLYAPQKKVRTDGGVDTFVSQLTPTNPDDSlQSPNRDSLY 1412
Cdd:pfam02354  215 AMVADAPFPSRGpgrGGNLGLEL-HYEALEAPLLPQRAQSLLYQSQKARLDQEESESFTADLTETLDDSH-HSPNRDSLY 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1413 TSMPNLRDSPYPESSPEVVEDLSPSKRSENEDVYYKSMPNLGSGHQLQAYYQIGRGSSDGYIIPINTEGCIPEGDvREGQ 1492
Cdd:pfam02354  293 TSMPNLRDSPYPDSSPEEEEELSPSAQSESEDVYYKSMPALGSRNQLQSYYQIRRGSSDGYIAPPSKEDPSPEGE-PDGQ 371


                   ....*..
gi 1880350455 1493 MQLVTSL 1499
Cdd:pfam02354  372 MQLVTSL 378
7tm_GPCRs super family cl28897
seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary ...
 849-1103 1.01e-166

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.


The actual alignment was detected with superfamily member cd16006:

Pssm-ID: 475119 [Multi-domain]  Cd Length: 258  Bit Score: 500.98  E-value: 1.01e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLASFS 928
Cdd:cd16006      4 LTVITWVGIVISLVCLAICIFTFCFFRGLQSDRNTIHKNLCINLFIAEFIFLIGIDKTEYKIACPIFAGLLHFFFLAAFA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  929 WMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKNACWLRVDNHFIWSFIGPVTFIIMLNL 1008
Cdd:cd16006     84 WMCLEGVQLYLMLVEVFESEYSRKKYYYVAGYLFPATVVGVSAAIDYKSYGTEKACWLRVDNYFIWSFIGPVTFIILLNL 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1009 IFLVITMYKMVKHSTTLKPDSSRLENIKSWVMGAFALLCLLGLTWSFGLFFINEASIVMAYLFTIFNAFQGMFIFIFHCL 1088
Cdd:cd16006    164 IFLVITLCKMVKHSNTLKPDSSRLENIKSWVLGAFALLCLLGLTWSFGLLFINEETIVMAYLFTIFNAFQGMFIFIFHCA 243

                          250
                   ....*....|....*
gi 1880350455 1089 LQKKVRKEYSKCFRH 1103
Cdd:cd16006    244 LQKKVRKEYSKCFRH 258
OLF super family cl02549
Olfactomedin-like domain;
144-400 2.99e-124

Olfactomedin-like domain;


The actual alignment was detected with superfamily member smart00284:

Pssm-ID: 470611  Cd Length: 255  Bit Score: 387.27  E-value: 2.99e-124
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   144 GTLKAVGDPSFLFEAEQ-QAGAWCKDPLQA---GDKIYFMPWTPYRTDTLIEYSSLDDFQNARQTITYKLPHRVDGTGFV 219
Cdd:smart00284    1 GGLAGISKPVTLQTSWKgKSGAWMKDPLWNttkKSLYWYMPLNTRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGTGVV 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   220 VYDGAVFFNKERTRNIVKFDLRTRIKSGEAIINNANYHDTSPYKWGGKTDIDLAVDENGLWVIYATEQNNGMMVISQLNP 299
Cdd:smart00284   81 VYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNP 160

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   300 YTLRFEATWDTAYDKRSASNAFMVCGVLYVVRSTYEDNESevskslIDYIYNTKQNRGEYVDIHFPNQYQYIAAVDYNPR 379
Cdd:smart00284  161 ATLTIENTWITTYNKRSASNAFMICGILYVTRSLGSKGEK------VFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPN 234

                           250       260
                    ....*....|....*....|.
gi 1880350455   380 DNQLYVWNNFYILRYNLEFGP 400
Cdd:smart00284  235 DRKLYAWNNGHLVHYDIALKP 255
Gal_Rha_Lectin_LPHN2 cd22845
galactose/rhamnose binding lectin domain found in latrophilin-2 and similar proteins; ...
 37-133 3.11e-64

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: 212.56  E-value: 3.11e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   37 VRRELSCEGYPIDLRCPGSDVIMIESANYGRTDDKICDADPFQMENINCYLPDAYKIMSQRCNNRTQCIVITGSDVFPDP 116
Cdd:cd22845      1 VRRELSCEGYPIDLRCPGSDVIMIESANYGRTDDKICDADPFQMENTDCYLPDAYKIMTQRCNNRTQCIVVTGSDVFPDP 80

                           90
                   ....*....|....*..
gi 1880350455  117 CPGTYKYLEVQYECVPY 133
Cdd:cd22845     81 CPGTYKYLEVQYECVPY 97
GAIN pfam16489
GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and ...
 543-764 2.97e-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: 197.10  E-value: 2.97e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  543 NAANLANELAKHTK-GPIFAGDVSSSVRLMEQLVDILDAQLQELrpsekdsagrsfnklqkrertCRAYMKAIVDTVDNL 621
Cdd:pfam16489    1 GAKELARELRNATRhGPLYGGDVLTAVELLSQLFDLLATQDATL---------------------SNAFLENFVQTVSNL 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  622 LRQEALNSWKDMNSTEQTHAATMLLDTLEEGAFVLADNLMEPAIVKVPADNIILDVYVLSTDGQVQDF--KFPQSS---K 696
Cdd:pfam16489   60 LDPENRESWEDLQQTERGTAATKLLRTLEEYALLLAQNMKYLTPFTIVTPNIVLSVDRLDTHNFKGARfpRFPMKGerpK 139

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1880350455  697 DGVSIQLSANTVKLNSRNGVAKLVFVLYKNLGQFLSAENStikmaNEAYGRNVSV---AVNSDIIAASINK 764
Cdd:pfam16489  140 DEDSVKLPPKAFKPPDSNGTVVVVFILYRNLGSLLPPSSR-----YDPDRRSLRLprrVVNSPVVSASVHS 205
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
 788-840 1.22e-21

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: 89.37  E-value: 1.22e-21
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1880350455   788 FNPNCSFWNYSErsmmGYWSTQGCKLLDTNKTHTTCSCSHLTNFAILMAHREI 840
Cdd:smart00303    1 FNPICVFWDESS----GEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPPI 49
HormR smart00008
Domain present in hormone receptors;
472-533 3.68e-19

Domain present in hormone receptors;


:

Pssm-ID: 214468  Cd Length: 70  Bit Score: 82.95  E-value: 3.68e-19
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1880350455   472 PERFCEATEKRDITWPQTQRGMLVERPCPKGTRG-----TASYLC-STGAWHPKGPDLSNCTSHWVNQ 533
Cdd:smart00008    1 TDLGCPATWDGIICWPQTPAGQLVEVPCPKYFSGfsyktGASRNCtENGGWSPPFPNYSNCTSNDYEE 68
 
Name Accession Description Interval E-value
Latrophilin pfam02354
Latrophilin Cytoplasmic C-terminal region; This family consists of the cytoplasmic C-terminal ...
 1102-1499 0e+00

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: 634.60  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1102 RHTYCCGGLPTESSHGSAKTSTTRTSARYSSGTQSRIRRMWNDTVRKQSESSFISGDINSTSTLNQGMTGNYLLTNPLLR 1181
Cdd:pfam02354    1 RHSHCCSGLSSEGSHGSAKTSASRTTARYSTGTQSRIRRMWNDTVRKQSESSFIAGDINSTPTLNRGTMGNHLLTNPLLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1182 PQGTNNPYNTLLAETVVCNTPTAPVFNSPvtyreTRHSLNNAvRDTSAMDTLPLNGNFNNSYSLRNGDF--GDSVQVVDC 1259
Cdd:pfam02354   81 PHGTTNPYNTLLAESVVFNPPSPPVFNSP-----GKHSLSNS-RDSSGMDTLPLNGNFNNSYSLRSGDYenPDGTATYGC 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1260 GLSLDDAAFEKMIISELVHNNLRACNKSHqqqqqqhpslhhpphhqqppQYHQHHHAERAPPKVTVV----GGSSSSEDD 1335
Cdd:pfam02354  155 RRNLDDAAFEKMIISELVHNNLRGRGNPK--------------------GRDHTRTSDRALPPHTNSggagGGGSGEEDD 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1336 AIVADASSLVHM---GDTVGLELhHQQELEAPLIPQRTHSLLYAPQKKVRTDGGVDTFVSQLTPTNPDDSlQSPNRDSLY 1412
Cdd:pfam02354  215 AMVADAPFPSRGpgrGGNLGLEL-HYEALEAPLLPQRAQSLLYQSQKARLDQEESESFTADLTETLDDSH-HSPNRDSLY 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1413 TSMPNLRDSPYPESSPEVVEDLSPSKRSENEDVYYKSMPNLGSGHQLQAYYQIGRGSSDGYIIPINTEGCIPEGDvREGQ 1492
Cdd:pfam02354  293 TSMPNLRDSPYPDSSPEEEEELSPSAQSESEDVYYKSMPALGSRNQLQSYYQIRRGSSDGYIAPPSKEDPSPEGE-PDGQ 371


                   ....*..
gi 1880350455 1493 MQLVTSL 1499
Cdd:pfam02354  372 MQLVTSL 378
7tmB2_Latrophilin-2 cd16006
Latrophilin-2, member of the class B2 family of seven-transmembrane G protein-coupled ...
 849-1103 1.01e-166

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: 500.98  E-value: 1.01e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLASFS 928
Cdd:cd16006      4 LTVITWVGIVISLVCLAICIFTFCFFRGLQSDRNTIHKNLCINLFIAEFIFLIGIDKTEYKIACPIFAGLLHFFFLAAFA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  929 WMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKNACWLRVDNHFIWSFIGPVTFIIMLNL 1008
Cdd:cd16006     84 WMCLEGVQLYLMLVEVFESEYSRKKYYYVAGYLFPATVVGVSAAIDYKSYGTEKACWLRVDNYFIWSFIGPVTFIILLNL 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1009 IFLVITMYKMVKHSTTLKPDSSRLENIKSWVMGAFALLCLLGLTWSFGLFFINEASIVMAYLFTIFNAFQGMFIFIFHCL 1088
Cdd:cd16006    164 IFLVITLCKMVKHSNTLKPDSSRLENIKSWVLGAFALLCLLGLTWSFGLLFINEETIVMAYLFTIFNAFQGMFIFIFHCA 243

                          250
                   ....*....|....*
gi 1880350455 1089 LQKKVRKEYSKCFRH 1103
Cdd:cd16006    244 LQKKVRKEYSKCFRH 258
OLF smart00284
Olfactomedin-like domains;
144-400 2.99e-124

Olfactomedin-like domains;


Pssm-ID: 128580  Cd Length: 255  Bit Score: 387.27  E-value: 2.99e-124
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   144 GTLKAVGDPSFLFEAEQ-QAGAWCKDPLQA---GDKIYFMPWTPYRTDTLIEYSSLDDFQNARQTITYKLPHRVDGTGFV 219
Cdd:smart00284    1 GGLAGISKPVTLQTSWKgKSGAWMKDPLWNttkKSLYWYMPLNTRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGTGVV 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   220 VYDGAVFFNKERTRNIVKFDLRTRIKSGEAIINNANYHDTSPYKWGGKTDIDLAVDENGLWVIYATEQNNGMMVISQLNP 299
Cdd:smart00284   81 VYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNP 160

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   300 YTLRFEATWDTAYDKRSASNAFMVCGVLYVVRSTYEDNESevskslIDYIYNTKQNRGEYVDIHFPNQYQYIAAVDYNPR 379
Cdd:smart00284  161 ATLTIENTWITTYNKRSASNAFMICGILYVTRSLGSKGEK------VFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPN 234

                           250       260
                    ....*....|....*....|.
gi 1880350455   380 DNQLYVWNNFYILRYNLEFGP 400
Cdd:smart00284  235 DRKLYAWNNGHLVHYDIALKP 255
OLF pfam02191
Olfactomedin-like domain;
146-398 7.98e-117

Olfactomedin-like domain;


Pssm-ID: 460482  Cd Length: 246  Bit Score: 366.86  E-value: 7.98e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  146 LKAVGDPSFLFEAEQQAGAWCKDPLQAGDKIYFMPwTPYRTDTLIEYSSLDDFQNARQTITYKLPHRVDGTGFVVYDGAV 225
Cdd:pfam02191    1 LVSVSKPVTVKLSGGKYGAWMKDPLPPSDKIYVTD-RGTSGNTLREYASLDDFKNGSPSKKYKLPYPWQGTGHVVYNGSL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  226 FFNKERTRNIVKFDLRTRIKSGEAIINNANYHDTSPYKWGGKTDIDLAVDENGLWVIYATEQNNGMMVISQLNPYTLRFE 305
Cdd:pfam02191   80 YYNKYNSRNIVKYDLTTRTVAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLDPETLEVE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  306 ATWDTAYDKRSASNAFMVCGVLYVVRSTYEDNESevskslIDYIYNTKQNRGEYVDIHFPNQYQYIAAVDYNPRDNQLYV 385
Cdd:pfam02191  160 QTWNTSYPKRSAGNAFMVCGVLYAVRSVNTRREE------IFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLYA 233

                          250
                   ....*....|...
gi 1880350455  386 WNNFYILRYNLEF 398
Cdd:pfam02191  234 WDDGYQVTYPVTF 246
7tm_2 pfam00002
7 transmembrane receptor (Secretin family); This family is known as Family B, the ...
 849-1082 5.92e-96

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: 309.21  E-value: 5.92e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEP--------RIGCAIIAGILH 920
Cdd:pfam00002    4 LKVIYTVGYSLSLVALLLAIAIFLLFRKLHCTRNYIHLNLFASFILRALLFLVGDAVLFNkqdldhcsWVGCKVVAVFLH 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  921 FFFLASFSWMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKNACWLRVDNHFIWSFIGPV 1000
Cdd:pfam00002   84 YFFLANFFWMLVEGLYLYTLLVEVFFSERKYFWWYLLIGWGVPALVVGIWAGVDPKGYGEDDGCWLSNENGLWWIIRGPI 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1001 TFIIMLNLIFLVITMYKMVKHSTTLKPDSSRLENIKSWVMGAFALLCLLGLTWSFGLFFINE---ASIVMAYLFTIFNAF 1077
Cdd:pfam00002  164 LLIILVNFIIFINIVRILVQKLRETNMGKSDLKQYRRLAKSTLLLLPLLGITWVFGLFAFNPentLRVVFLYLFLILNSF 243


                   ....*
gi 1880350455 1078 QGMFI 1082
Cdd:pfam00002  244 QGFFV 248
Gal_Rha_Lectin_LPHN2 cd22845
galactose/rhamnose binding lectin domain found in latrophilin-2 and similar proteins; ...
 37-133 3.11e-64

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: 212.56  E-value: 3.11e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   37 VRRELSCEGYPIDLRCPGSDVIMIESANYGRTDDKICDADPFQMENINCYLPDAYKIMSQRCNNRTQCIVITGSDVFPDP 116
Cdd:cd22845      1 VRRELSCEGYPIDLRCPGSDVIMIESANYGRTDDKICDADPFQMENTDCYLPDAYKIMTQRCNNRTQCIVVTGSDVFPDP 80

                           90
                   ....*....|....*..
gi 1880350455  117 CPGTYKYLEVQYECVPY 133
Cdd:cd22845     81 CPGTYKYLEVQYECVPY 97
GAIN pfam16489
GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and ...
 543-764 2.97e-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: 197.10  E-value: 2.97e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  543 NAANLANELAKHTK-GPIFAGDVSSSVRLMEQLVDILDAQLQELrpsekdsagrsfnklqkrertCRAYMKAIVDTVDNL 621
Cdd:pfam16489    1 GAKELARELRNATRhGPLYGGDVLTAVELLSQLFDLLATQDATL---------------------SNAFLENFVQTVSNL 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  622 LRQEALNSWKDMNSTEQTHAATMLLDTLEEGAFVLADNLMEPAIVKVPADNIILDVYVLSTDGQVQDF--KFPQSS---K 696
Cdd:pfam16489   60 LDPENRESWEDLQQTERGTAATKLLRTLEEYALLLAQNMKYLTPFTIVTPNIVLSVDRLDTHNFKGARfpRFPMKGerpK 139

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1880350455  697 DGVSIQLSANTVKLNSRNGVAKLVFVLYKNLGQFLSAENStikmaNEAYGRNVSV---AVNSDIIAASINK 764
Cdd:pfam16489  140 DEDSVKLPPKAFKPPDSNGTVVVVFILYRNLGSLLPPSSR-----YDPDRRSLRLprrVVNSPVVSASVHS 205
Gal_Lectin pfam02140
Galactose binding lectin domain;
50-130 8.90e-33

Galactose binding lectin domain;


Pssm-ID: 460460 [Multi-domain]  Cd Length: 79  Bit Score: 122.01  E-value: 8.90e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   50 LRCPGSDVIMIESANYGRTDDKICdadPFQMENINCYLPDAYKIMSQRCNNRTQCIVITGSDVF-PDPCPGTYKYLEVQY 128
Cdd:pfam02140    1 LSCPPGKVISILFASYGRPDGTTC---PSFIQGTNCHSPNSLAIVSKACQGKNSCSVPASNSVFgGDPCPGTYKYLEVEY 77


                   ..
gi 1880350455  129 EC 130
Cdd:pfam02140   78 KC 79
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
 788-840 1.22e-21

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: 89.37  E-value: 1.22e-21
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1880350455   788 FNPNCSFWNYSErsmmGYWSTQGCKLLDTNKTHTTCSCSHLTNFAILMAHREI 840
Cdd:smart00303    1 FNPICVFWDESS----GEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPPI 49
HormR smart00008
Domain present in hormone receptors;
472-533 3.68e-19

Domain present in hormone receptors;


Pssm-ID: 214468  Cd Length: 70  Bit Score: 82.95  E-value: 3.68e-19
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1880350455   472 PERFCEATEKRDITWPQTQRGMLVERPCPKGTRG-----TASYLC-STGAWHPKGPDLSNCTSHWVNQ 533
Cdd:smart00008    1 TDLGCPATWDGIICWPQTPAGQLVEVPCPKYFSGfsyktGASRNCtENGGWSPPFPNYSNCTSNDYEE 68
GPS pfam01825
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
 790-834 7.77e-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: 75.42  E-value: 7.77e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1880350455  790 PNCSFWNYSErSMMGYWSTQGCKLLDTNKTHTTCSCSHLTNFAIL 834
Cdd:pfam01825    1 PQCVFWDFTN-STTGRWSTEGCTTVSLNDTHTVCSCNHLTSFAVL 44
HRM pfam02793
Hormone receptor domain; This extracellular domain contains four conserved cysteines that ...
 473-529 1.07e-09

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


Pssm-ID: 397086  Cd Length: 64  Bit Score: 55.84  E-value: 1.07e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1880350455  473 ERFCEATEKRDITWPQTQRGMLVERPCPKGT-----RGTASYLC-STGAWHPKGP-DLSNCTSH 529
Cdd:pfam02793    1 GLGCPRTWDGILCWPRTPAGETVEVPCPDYFsgfdpRGNASRNCtEDGTWSEHPPsNYSNCTSN 64
 
Name Accession Description Interval E-value
Latrophilin pfam02354
Latrophilin Cytoplasmic C-terminal region; This family consists of the cytoplasmic C-terminal ...
 1102-1499 0e+00

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: 634.60  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1102 RHTYCCGGLPTESSHGSAKTSTTRTSARYSSGTQSRIRRMWNDTVRKQSESSFISGDINSTSTLNQGMTGNYLLTNPLLR 1181
Cdd:pfam02354    1 RHSHCCSGLSSEGSHGSAKTSASRTTARYSTGTQSRIRRMWNDTVRKQSESSFIAGDINSTPTLNRGTMGNHLLTNPLLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1182 PQGTNNPYNTLLAETVVCNTPTAPVFNSPvtyreTRHSLNNAvRDTSAMDTLPLNGNFNNSYSLRNGDF--GDSVQVVDC 1259
Cdd:pfam02354   81 PHGTTNPYNTLLAESVVFNPPSPPVFNSP-----GKHSLSNS-RDSSGMDTLPLNGNFNNSYSLRSGDYenPDGTATYGC 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1260 GLSLDDAAFEKMIISELVHNNLRACNKSHqqqqqqhpslhhpphhqqppQYHQHHHAERAPPKVTVV----GGSSSSEDD 1335
Cdd:pfam02354  155 RRNLDDAAFEKMIISELVHNNLRGRGNPK--------------------GRDHTRTSDRALPPHTNSggagGGGSGEEDD 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1336 AIVADASSLVHM---GDTVGLELhHQQELEAPLIPQRTHSLLYAPQKKVRTDGGVDTFVSQLTPTNPDDSlQSPNRDSLY 1412
Cdd:pfam02354  215 AMVADAPFPSRGpgrGGNLGLEL-HYEALEAPLLPQRAQSLLYQSQKARLDQEESESFTADLTETLDDSH-HSPNRDSLY 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1413 TSMPNLRDSPYPESSPEVVEDLSPSKRSENEDVYYKSMPNLGSGHQLQAYYQIGRGSSDGYIIPINTEGCIPEGDvREGQ 1492
Cdd:pfam02354  293 TSMPNLRDSPYPDSSPEEEEELSPSAQSESEDVYYKSMPALGSRNQLQSYYQIRRGSSDGYIAPPSKEDPSPEGE-PDGQ 371


                   ....*..
gi 1880350455 1493 MQLVTSL 1499
Cdd:pfam02354  372 MQLVTSL 378
7tmB2_Latrophilin-2 cd16006
Latrophilin-2, member of the class B2 family of seven-transmembrane G protein-coupled ...
 849-1103 1.01e-166

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: 500.98  E-value: 1.01e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLASFS 928
Cdd:cd16006      4 LTVITWVGIVISLVCLAICIFTFCFFRGLQSDRNTIHKNLCINLFIAEFIFLIGIDKTEYKIACPIFAGLLHFFFLAAFA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  929 WMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKNACWLRVDNHFIWSFIGPVTFIIMLNL 1008
Cdd:cd16006     84 WMCLEGVQLYLMLVEVFESEYSRKKYYYVAGYLFPATVVGVSAAIDYKSYGTEKACWLRVDNYFIWSFIGPVTFIILLNL 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1009 IFLVITMYKMVKHSTTLKPDSSRLENIKSWVMGAFALLCLLGLTWSFGLFFINEASIVMAYLFTIFNAFQGMFIFIFHCL 1088
Cdd:cd16006    164 IFLVITLCKMVKHSNTLKPDSSRLENIKSWVLGAFALLCLLGLTWSFGLLFINEETIVMAYLFTIFNAFQGMFIFIFHCA 243

                          250
                   ....*....|....*
gi 1880350455 1089 LQKKVRKEYSKCFRH 1103
Cdd:cd16006    244 LQKKVRKEYSKCFRH 258
7tmB2_Latrophilin-1 cd16007
Latrophilin-1, member of the class B2 family of seven-transmembrane G protein-coupled ...
 849-1103 2.10e-153

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: 465.55  E-value: 2.10e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLASFS 928
Cdd:cd16007      4 LSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLIGIDKTQYQIACPIFAGLLHFFFLAAFS 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  929 WMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKNACWLRVDNHFIWSFIGPVTFIIMLNL 1008
Cdd:cd16007     84 WLCLEGVQLYLMLVEVFESEYSRKKYYYLCGYCFPALVVGISAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIVVNL 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1009 IFLVITMYKMVKHSTTLKPDSSRLENIKSWVMGAFALLCLLGLTWSFGLFFINEASIVMAYLFTIFNAFQGMFIFIFHCL 1088
Cdd:cd16007    164 VFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAITLLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGMFIFIFHCA 243

                          250
                   ....*....|....*
gi 1880350455 1089 LQKKVRKEYSKCFRH 1103
Cdd:cd16007    244 LQKKVHKEYSKCLRH 258
7tmB2_Latrophilin cd15436
Latrophilins, member of the class B2 family of seven-transmembrane G protein-coupled receptors; ...
 849-1103 3.18e-152

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: 462.73  E-value: 3.18e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLASFS 928
Cdd:cd15436      4 LFVITWVGIVISLVCLLICIFTFCFFRGLQTDRNTIHKNLCINLFIAELLFLIGINRTQYTIACPIFAGLLHFFFLAAFC 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  929 WMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKNACWLRVDNHFIWSFIGPVTFIIMLNL 1008
Cdd:cd15436     84 WLCLEGVQLYLLLVEVFESEYSRRKYFYLCGYSFPALVVAVSAAIDYRSYGTEKACWLRVDNYFIWSFIGPVTFVITLNL 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1009 IFLVITMYKMVKHSTTLKPDSSRLENIKSWVMGAFALLCLLGLTWSFGLFFINEASIVMAYLFTIFNAFQGMFIFIFHCL 1088
Cdd:cd15436    164 VFLVITLHKMVSHSDLLKPDSSRLDNIKSWALGAIALLFLLGLTWSFGLMFINEESVVMAYLFTIFNAFQGVFIFIFHCA 243

                          250
                   ....*....|....*
gi 1880350455 1089 LQKKVRKEYSKCFRH 1103
Cdd:cd15436    244 LQKKVRKEYSKCLRH 258
7tmB2_Latrophilin_Adhesion_I cd15252
Latrophilins and similar receptors, group I adhesion GPCRs, member of class B2 family of ...
 849-1102 1.01e-139

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: 429.23  E-value: 1.01e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLASFS 928
Cdd:cd15252      4 LTRITQVGIIISLVCLAICIFTFWFFRGLQSDRTTIHKNLCISLFLAELVFLIGINTTTNKIFCSVIAGLLHYFFLAAFA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  929 WMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKNACWLRVDNHFIWSFIGPVTFIIMLNL 1008
Cdd:cd15252     84 WMFIEGIQLYLMLVEVFENEGSRHKNFYIFGYGSPAVIVGVSAALGYRYYGTTKVCWLSTENYFIWSFIGPATLIILLNL 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1009 IFLVITMYKMVKHSTTLKPDSSRLENIKSWVMGAFALLCLLGLTWSFGLFFINEASIVMAYLFTIFNAFQGMFIFIFHCL 1088
Cdd:cd15252    164 IFLGVAIYKMFRHTAGLKPEVSCLENIRSWARGAIALLFLLGLTWIFGVLHINHASVVMAYLFTVSNSLQGMFIFLFHCV 243

                          250
                   ....*....|....
gi 1880350455 1089 LQKKVRKEYSKCFR 1102
Cdd:cd15252    244 LSRKVRKEYYKLFR 257
7tmB2_latrophilin-like_invertebrate cd15440
invertebrate latrophilin-like receptors, member of the class B2 family of seven-transmembrane ...
 849-1102 1.09e-135

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: 418.59  E-value: 1.09e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLASFS 928
Cdd:cd15440      4 LTFITYIGCIISIVCLLLAFITFTCFRNLQCDRNTIHKNLCLCLLIAEIVFLLGIDQTENRTLCGVIAGLLHYFFLAAFS 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  929 WMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKNACWLRVDNHFIWSFIGPVTFIIMLNL 1008
Cdd:cd15440     84 WMLLEGFQLYVMLVEVFEPEKSRIKWYYLFGYGLPALIVAVSAGVDPTGYGTEDHCWLSTENGFIWSFVGPVIVVLLANL 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1009 IFLVITMYKMVKHSTTL--KPDSSRLENIKSWVMGAFALLCLLGLTWSFGLFFINEASIVMAYLFTIFNAFQGMFIFIFH 1086
Cdd:cd15440    164 VFLGMAIYVMCRHSSRSasKKDASKLKNIRGWLKGSIVLVVLLGLTWTFGLLFINQESIVMAYIFTILNSLQGLFIFIFH 243

                          250
                   ....*....|....*.
gi 1880350455 1087 CLLQKKVRKEYSKCFR 1102
Cdd:cd15440    244 CVLNEKVRKELRRWLR 259
7tmB2_Latrophilin-3 cd16005
Latrophilin-3, member of the class B2 family of seven-transmembrane G protein-coupled ...
 846-1102 2.39e-127

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: 395.85  E-value: 2.39e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  846 DPQLDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLA 925
Cdd:cd16005      1 DLLLDVITWVGILLSLVCLLICIFTFCFFRGLQSDRNTIHKNLCISLFVAELLFLIGINRTDQPIACAVFAALLHFFFLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  926 SFSWMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKNACWLRVDNHFIWSFIGPVTFIIM 1005
Cdd:cd16005     81 AFTWMFLEGVQLYIMLVEVFESEHSRRKYFYLVGYGMPALIVAVSAAVDYRSYGTDKVCWLRLDTYFIWSFIGPATLIIM 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1006 LNLIFLVITMYKMVKHSTTLKPDSSRLENIKSWVMGAFALLCLLGLTWSFGLFFINEASIVMAYLFTIFNAFQGMFIFIF 1085
Cdd:cd16005    161 LNVIFLGIALYKMFHHTAILKPESGCLDNIKSWVIGAIALLCLLGLTWAFGLMYINESTVIMAYLFTIFNSLQGMFIFIF 240

                          250
                   ....*....|....*..
gi 1880350455 1086 HCLLQKKVRKEYSKCFR 1102
Cdd:cd16005    241 HCVLQKKVRKEYGKCLR 257
OLF smart00284
Olfactomedin-like domains;
144-400 2.99e-124

Olfactomedin-like domains;


Pssm-ID: 128580  Cd Length: 255  Bit Score: 387.27  E-value: 2.99e-124
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   144 GTLKAVGDPSFLFEAEQ-QAGAWCKDPLQA---GDKIYFMPWTPYRTDTLIEYSSLDDFQNARQTITYKLPHRVDGTGFV 219
Cdd:smart00284    1 GGLAGISKPVTLQTSWKgKSGAWMKDPLWNttkKSLYWYMPLNTRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGTGVV 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   220 VYDGAVFFNKERTRNIVKFDLRTRIKSGEAIINNANYHDTSPYKWGGKTDIDLAVDENGLWVIYATEQNNGMMVISQLNP 299
Cdd:smart00284   81 VYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNP 160

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   300 YTLRFEATWDTAYDKRSASNAFMVCGVLYVVRSTYEDNESevskslIDYIYNTKQNRGEYVDIHFPNQYQYIAAVDYNPR 379
Cdd:smart00284  161 ATLTIENTWITTYNKRSASNAFMICGILYVTRSLGSKGEK------VFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPN 234

                           250       260
                    ....*....|....*....|.
gi 1880350455   380 DNQLYVWNNFYILRYNLEFGP 400
Cdd:smart00284  235 DRKLYAWNNGHLVHYDIALKP 255
OLF pfam02191
Olfactomedin-like domain;
146-398 7.98e-117

Olfactomedin-like domain;


Pssm-ID: 460482  Cd Length: 246  Bit Score: 366.86  E-value: 7.98e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  146 LKAVGDPSFLFEAEQQAGAWCKDPLQAGDKIYFMPwTPYRTDTLIEYSSLDDFQNARQTITYKLPHRVDGTGFVVYDGAV 225
Cdd:pfam02191    1 LVSVSKPVTVKLSGGKYGAWMKDPLPPSDKIYVTD-RGTSGNTLREYASLDDFKNGSPSKKYKLPYPWQGTGHVVYNGSL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  226 FFNKERTRNIVKFDLRTRIKSGEAIINNANYHDTSPYKWGGKTDIDLAVDENGLWVIYATEQNNGMMVISQLNPYTLRFE 305
Cdd:pfam02191   80 YYNKYNSRNIVKYDLTTRTVAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLDPETLEVE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  306 ATWDTAYDKRSASNAFMVCGVLYVVRSTYEDNESevskslIDYIYNTKQNRGEYVDIHFPNQYQYIAAVDYNPRDNQLYV 385
Cdd:pfam02191  160 QTWNTSYPKRSAGNAFMVCGVLYAVRSVNTRREE------IFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLYA 233

                          250
                   ....*....|...
gi 1880350455  386 WNNFYILRYNLEF 398
Cdd:pfam02191  234 WDDGYQVTYPVTF 246
7tmB2_CD97 cd15438
CD97 antigen, member of the class B2 family of seven-transmembrane G protein-coupled receptors; ...
 846-1101 4.44e-107

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: 340.59  E-value: 4.44e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  846 DPQLDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLA 925
Cdd:cd15438      1 DWPLTLITKVGLSVSLFCLFLCILTFLFCRSIRGTRNTIHLHLCLSLFLAHLIFLLGINNTNNQVACAVVAGLLHYFFLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  926 SFSWMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKNACWLRVDNHFIWSFIGPVTFIIM 1005
Cdd:cd15438     81 AFCWMSLEGVELYLMVVQVFNTQSLKKRYLLLIGYGVPLVIVAISAAVNSKGYGTQRHCWLSLERGFLWSFLGPVCLIIL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1006 LNLIFLVITMYKMVKHSTTLKPDSSRLENIKSWVMGAFALLCLLGLTWSFGLFFINEASIVMAYLFTIFNAFQGMFIFIF 1085
Cdd:cd15438    161 VNAIIFVITVWKLAEKFSSINPDMEKLRKIRALTITAIAQLCILGCTWIFGFFQFSDSTLVMSYLFTILNSLQGLFIFLL 240

                          250
                   ....*....|....*.
gi 1880350455 1086 HCLLQKKVRKEYSKCF 1101
Cdd:cd15438    241 HCLLSKQVREEYSRWL 256
7tmB2_ETL cd15437
Epidermal Growth Factor, latrophilin and seven transmembrane domain-containing protein 1; ...
 852-1103 6.60e-101

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: 323.37  E-value: 6.60e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  852 ITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLASFSWMC 931
Cdd:cd15437      7 ITQLGIIISLICLSMCIFTFWFFSEIQSTRTTIHKNLCCSLFLAELIFLIGINMNANKLFCSIIAGLLHYFFLAAFAWMC 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  932 LEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKNACWLRVDNHFIWSFIGPVTFIIMLNLIFL 1011
Cdd:cd15437     87 IEGIHLYLIVVGVIYNKGFLHKNFYIFGYGSPAVVVGISAALGYKYYGTTKVCWLSTENNFIWSFIGPACLIILVNLLAF 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1012 VITMYKMVKHSTTLKPDSSRLENIKSWVMGAFALLCLLGLTWSFGLFFINEASIVMAYLFTIFNAFQGMFIFIFHCLLQK 1091
Cdd:cd15437    167 GVIIYKVFRHTAMLKPEVSCYENIRSCARGALALLFLLGATWIFGVLHVVYGSVVTAYLFTISNAFQGMFIFIFLCVLSR 246

                          250
                   ....*....|..
gi 1880350455 1092 KVRKEYSKCFRH 1103
Cdd:cd15437    247 KIQEEYYRLFKN 258
7tmB2_EMR cd15439
epidermal growth factor-like module-containing mucin-like hormone receptors, member of the ...
 846-1102 7.23e-101

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: 323.52  E-value: 7.23e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  846 DPQLDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLA 925
Cdd:cd15439      1 DLALTVITYVGLIISLLCLFLAILTFLLCRSIRNTSTSLHLQLSLCLFLADLLFLVGIDRTDNKVLCSIIAGFLHYLFLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  926 SFSWMCLEGVQLYLML-----VEVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKNACWLRVDNHFIWSFIGPV 1000
Cdd:cd15439     81 CFAWMFLEAVHLFLTVrnlkvVNYFSSHRFKKRFMYPVGYGLPAVIVAISAAVNPQGYGTPKHCWLSMEKGFIWSFLGPV 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1001 TFIIMLNLIFLVITMYKMVKHSTTLKPDSSRLENIKSWVMGAFALLCLLGLTWSFGLFFINEASIVMAYLFTIFNAFQGM 1080
Cdd:cd15439    161 CVIIVINLVLFCLTLWILREKLSSLNAEVSTLKNTRLLTFKAIAQLFILGCTWILGLFQVGPVATVMAYLFTITNSLQGV 240

                          250       260
                   ....*....|....*....|..
gi 1880350455 1081 FIFIFHCLLQKKVRKEYSKCFR 1102
Cdd:cd15439    241 FIFLVHCLLNRQVREEYRRWIT 262
7tmB2_Adhesion cd15040
adhesion receptors, subfamily B2 of the class B family of seven-transmembrane G ...
 849-1097 5.66e-99

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: 317.59  E-value: 5.66e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSD-RNTIHKNLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLASF 927
Cdd:cd15040      4 LSIITYIGCGLSLLGLLLTIITYILFRKLRKRkPTKILLNLCLALLLANLLFLFGINSTDNPVLCTAVAALLHYFLLASF 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  928 SWMCLEGVQLYLMLVEVFESEYSRK-KYFYVSGYLFPAIVVGVSAAIDYSSYG-TKNACWLRVDNHFIWSFIGPVTFIIM 1005
Cdd:cd15040     84 MWMLVEALLLYLRLVKVFGTYPRHFiLKYALIGWGLPLIIVIITLAVDPDSYGnSSGYCWLSNGNGLYYAFLGPVLLIIL 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1006 LNLIFLVITMYKMVKHSTTLkpDSSRLENIKSWVMGAFALLCLLGLTWSFGLFFINEASIVMAYLFTIFNAFQGMFIFIF 1085
Cdd:cd15040    164 VNLVIFVLVLRKLLRLSAKR--NKKKRKKTKAQLRAAVSLFFLLGLTWIFGILAIFGARVVFQYLFAIFNSLQGFFIFIF 241

                          250
                   ....*....|..
gi 1880350455 1086 HCLLQKKVRKEY 1097
Cdd:cd15040    242 HCLRNKEVRKAW 253
7tm_2 pfam00002
7 transmembrane receptor (Secretin family); This family is known as Family B, the ...
 849-1082 5.92e-96

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: 309.21  E-value: 5.92e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEP--------RIGCAIIAGILH 920
Cdd:pfam00002    4 LKVIYTVGYSLSLVALLLAIAIFLLFRKLHCTRNYIHLNLFASFILRALLFLVGDAVLFNkqdldhcsWVGCKVVAVFLH 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  921 FFFLASFSWMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKNACWLRVDNHFIWSFIGPV 1000
Cdd:pfam00002   84 YFFLANFFWMLVEGLYLYTLLVEVFFSERKYFWWYLLIGWGVPALVVGIWAGVDPKGYGEDDGCWLSNENGLWWIIRGPI 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1001 TFIIMLNLIFLVITMYKMVKHSTTLKPDSSRLENIKSWVMGAFALLCLLGLTWSFGLFFINE---ASIVMAYLFTIFNAF 1077
Cdd:pfam00002  164 LLIILVNFIIFINIVRILVQKLRETNMGKSDLKQYRRLAKSTLLLLPLLGITWVFGLFAFNPentLRVVFLYLFLILNSF 243


                   ....*
gi 1880350455 1078 QGMFI 1082
Cdd:pfam00002  244 QGFFV 248
7tmB2_GPR133-like_Adhesion_V cd15933
orphan GPR133 and related proteins, group V adhesion GPCRs, member of class B2 family of ...
 849-1097 8.81e-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: 283.45  E-value: 8.81e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLASFS 928
Cdd:cd15933      4 LSIISYIGCGISIACLALTLIIFLVLRVLSSDRFQIHKNLCVALLLAQILLLAGEWAEGNKVACKVVAILLHFFFMAAFS 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  929 WMCLEGVQLYLMLVEVFeSEYSRKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKNACWLRVDNHFIWSFIGPVTFIIMLNL 1008
Cdd:cd15933     84 WMLVEGLHLYLMIVKVF-NYKSKMRYYYFIGWGLPAIIVAISLAILFDDYGSPNVCWLSLDDGLIWAFVGPVIFIITVNT 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1009 IFLVITMYKMVKHSTT-LKPDSSRLENIKSWVMGAFALLCLLGLTWSFGLFFINEASIVMAYLFTIFNAFQGMFIFIFHC 1087
Cdd:cd15933    163 VILILVVKITVSLSTNdAKKSQGTLAQIKSTAKASVVLLPILGLTWLFGVLVVNSQTIVFQYIFVILNSLQGLMIFLFHC 242

                          250
                   ....*....|
gi 1880350455 1088 LLQKKVRKEY 1097
Cdd:cd15933    243 VLNSEVRSAF 252
7tm_classB cd13952
class B family of seven-transmembrane G protein-coupled receptors; The class B of ...
 849-1097 5.45e-85

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: 278.71  E-value: 5.45e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEPR--IGCAIIAGILHFFFLAS 926
Cdd:cd13952      4 LSIITYIGCSLSLVGLLLTIITYLLFPKLRNLRGKILINLCLSLLLAQLLFLIGQLLTSSDrpVLCKALAILLHYFLLAS 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  927 FSWMCLEGVQLYLMLVEVFESEYSRK-KYFYVSGYLFPAIVVGVSAAIDYSSYGTK-----NACWLRVDNHFIWSFIGPV 1000
Cdd:cd13952     84 FFWMLVEAFDLYRTFVKVFGSSERRRfLKYSLYGWGLPLLIVIITAIVDFSLYGPSpgyggEYCWLSNGNALLWAFYGPV 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1001 TFIIMLNLIFLVITMYKMVKHSTTLkPDSSRLENIKSWVMGAFALLCLLGLTWSFGLF-FINEASIVMAYLFTIFNAFQG 1079
Cdd:cd13952    164 LLILLVNLVFFILTVRILLRKLRET-PKQSERKSDRKQLRAYLKLFPLMGLTWIFGILaPFVGGSLVFWYLFDILNSLQG 242

                          250
                   ....*....|....*...
gi 1880350455 1080 MFIFIFHCLLQKKVRKEY 1097
Cdd:cd13952    243 FFIFLIFCLKNKEVRRLL 260
7tmB2_CELSR_Adhesion_IV cd15441
cadherin EGF LAG seven-pass G-type receptors, group IV adhesion GPCRs, member of the class B2 ...
 848-1102 3.67e-84

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: 276.05  E-value: 3.67e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  848 QLDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLASF 927
Cdd:cd15441      3 LLKIVTYIGIGISLVLLVIAFLVLSCLRGLQSNSNSIHKNLVACLLLAELLFLLGINQTENLFPCKLIAILLHYFYLSAF 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  928 SWMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKNACWLRVDNHFIWSFIGPVTFIIMLN 1007
Cdd:cd15441     83 SWLLVESLHLYRMLTEPRDINHGHMRFYYLLGYGIPAIIVGLSVGLRPDGYGNPDFCWLSVNETLIWSFAGPIAFVIVIT 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1008 LIFLVITMykmvKHSTTLKPDSSRLENIKSWVMGAFALLCLLGLTWSFGLFFINEASIVMAYLFTIFNAFQGMFIFIFHC 1087
Cdd:cd15441    163 LIIFILAL----RASCTLKRHVLEKASVRTDLRSSFLLLPLLGATWVFGLLAVNEDSELLHYLFAGLNFLQGLFIFLFYC 238

                          250
                   ....*....|....*
gi 1880350455 1088 LLQKKVRKEYSKCFR 1102
Cdd:cd15441    239 IFNKKVRRELKNALL 253
7tmB2_EMR_Adhesion_II cd15931
EGF-like module receptors, group II adhesion GPCRs, member of class B2 family of ...
 846-1099 2.64e-80

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: 265.53  E-value: 2.64e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  846 DPQLDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLA 925
Cdd:cd15931      1 DPFLEWINRVGVIVSLFCLGLAIFTFLLCRWIPKINTTAHLHLCLCLSMSHTLFLAGIEYVENELACTVMAGLLHYLFLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  926 SFSWMCLEGVQLYLMLVEVFESEYSRKK-----YFYVSGYLFPAIVVGVSAAIDYSSYGTKNACWLRVDNHFIWSFIGPV 1000
Cdd:cd15931     81 SFVWMLLEALQLHLLVRRLTKVQVIQRDglprpLLCLIGYGVPFLIVGVSALVYSDGYGEAKMCWLSQERGFNWSFLGPV 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1001 TFIIMLNLIFLVITMYKMVKHSTTLKPDSSRLENIKSWVMGAFALLCLLGLTWSFGLFFINEASIVMAYLFTIFNAFQGM 1080
Cdd:cd15931    161 IAIIGINWILFCATLWCLRQTLSNMNSDISQLKDTRLLTFKAVAQLFILGCTWVLGLFQTNPVALVFQYLFTILNSLQGA 240

                          250
                   ....*....|....*....
gi 1880350455 1081 FIFIFHCLLQKKVRKEYSK 1099
Cdd:cd15931    241 FLFLVHCLLNKEVREEYIK 259
Gal_Rha_Lectin_LPHN2 cd22845
galactose/rhamnose binding lectin domain found in latrophilin-2 and similar proteins; ...
 37-133 3.11e-64

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: 212.56  E-value: 3.11e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   37 VRRELSCEGYPIDLRCPGSDVIMIESANYGRTDDKICDADPFQMENINCYLPDAYKIMSQRCNNRTQCIVITGSDVFPDP 116
Cdd:cd22845      1 VRRELSCEGYPIDLRCPGSDVIMIESANYGRTDDKICDADPFQMENTDCYLPDAYKIMTQRCNNRTQCIVVTGSDVFPDP 80

                           90
                   ....*....|....*..
gi 1880350455  117 CPGTYKYLEVQYECVPY 133
Cdd:cd22845     81 CPGTYKYLEVQYECVPY 97
Gal_Rha_Lectin_LPHN1 cd22844
galactose/rhamnose binding lectin domain found in latrophilin-1 and similar proteins; ...
 37-133 1.42e-63

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: 210.68  E-value: 1.42e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   37 VRRELSCEGYPIDLRCPGSDVIMIESANYGRTDDKICDADPFQMENINCYLPDAYKIMSQRCNNRTQCIVITGSDVFPDP 116
Cdd:cd22844      1 MRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDP 80

                           90
                   ....*....|....*..
gi 1880350455  117 CPGTYKYLEVQYECVPY 133
Cdd:cd22844     81 CPGTYKYLEVQYDCVPY 97
Gal_Rha_Lectin_LPHN3 cd22846
galactose/rhamnose binding lectin domain found in latrophilin-3 and similar proteins; ...
 36-134 1.33e-62

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: 208.03  E-value: 1.33e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   36 LVRRELSCEGYPIDLRCPGSDVIMIESANYGRTDDKICDADPFQMENINCYLPDAYKIMSQRCNNRTQCIVITGSDVFPD 115
Cdd:cd22846      1 VVRRELSCESYPIELRCPGTDVIMIESANYGRTDDKICDSDPAQMENIRCYLPDAYKIMSQRCNNRTQCAVVAGPDVFPD 80

                           90
                   ....*....|....*....
gi 1880350455  116 PCPGTYKYLEVQYECVPYK 134
Cdd:cd22846     81 PCPGTYKYLEVQYECVPYK 99
7tmB2_CELSR1 cd15991
Cadherin EGF LAG seven-pass G-type receptor 1, member of the class B2 family of ...
 849-1101 1.13e-59

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: 205.85  E-value: 1.13e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLASFS 928
Cdd:cd15991      4 LKIITYTTVSLSLVALLITFILLVLIRTLRSNLHSIHKNLVAALFFSELIFLIGINQTENPFVCTVVAILLHYFYMSTFA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  929 WMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKNACWLRVDNHFIWSFIGPVTFIIMLNL 1008
Cdd:cd15991     84 WMFVEGLHIYRMLTEVRNINTGHMRFYYVVGWGIPAIITGLAVGLDPQGYGNPDFCWLSVQDTLIWSFAGPIGIVVIINT 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1009 IFLVITMykmvKHSTTLKPDSSRLENIKSWVMGAFALLCLLGLTWSFGLFFINEASIVMAYLFTIFNAFQGMFIFIFHCL 1088
Cdd:cd15991    164 VIFVLAA----KASCGRRQRYFEKSGVISMLRTAFLLLLLISATWLLGLMAVNSDTLSFHYLFAIFSCLQGIFIFFFHCI 239

                          250
                   ....*....|...
gi 1880350455 1089 LQKKVRKEYSKCF 1101
Cdd:cd15991    240 FNKEVRKHLKNVL 252
7tmB2_GPR133 cd15256
orphan adhesion receptor GPR133, member of the class B2 family of seven-transmembrane G ...
 849-1103 2.65e-57

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: 199.38  E-value: 2.65e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNT---IHKNLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLA 925
Cdd:cd15256      4 LSSITYVGCSLSIFCLAITLVTFAVLSSVSTIRNQryhIHANLSFAVLVAQILLLISFRFEPGTLPCKIMAILLHFFFLS 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  926 SFSWMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKNACWLRVDNHFIWSFIGPVTFIIM 1005
Cdd:cd15256     84 AFAWMLVEGLHLYSMVIKVFGSEESKHFYYYGIGWGSPLLICIISLTSALDSYGESDNCWLSLENGAIWAFVAPALFVIV 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1006 LNlIFLVITMYKMVKHSTTLKPDSSRLENIKSWVMGAFA-LLCLLGLTWSFGLFFINEASIVMAYLFTIFNAFQGMFIFI 1084
Cdd:cd15256    164 VN-IGILIAVTRVISRISADNYKVHGDANAFKLTAKAVAvLLPILGSSWVFGVLAVNTHALVFQYMFAIFNSLQGFFIFL 242

                          250
                   ....*....|....*....
gi 1880350455 1085 FHCLLQKKVRkeysKCFRH 1103
Cdd:cd15256    243 FHCLLNSEVR----AAFKH 257
GAIN pfam16489
GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and ...
 543-764 2.97e-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: 197.10  E-value: 2.97e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  543 NAANLANELAKHTK-GPIFAGDVSSSVRLMEQLVDILDAQLQELrpsekdsagrsfnklqkrertCRAYMKAIVDTVDNL 621
Cdd:pfam16489    1 GAKELARELRNATRhGPLYGGDVLTAVELLSQLFDLLATQDATL---------------------SNAFLENFVQTVSNL 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  622 LRQEALNSWKDMNSTEQTHAATMLLDTLEEGAFVLADNLMEPAIVKVPADNIILDVYVLSTDGQVQDF--KFPQSS---K 696
Cdd:pfam16489   60 LDPENRESWEDLQQTERGTAATKLLRTLEEYALLLAQNMKYLTPFTIVTPNIVLSVDRLDTHNFKGARfpRFPMKGerpK 139

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1880350455  697 DGVSIQLSANTVKLNSRNGVAKLVFVLYKNLGQFLSAENStikmaNEAYGRNVSV---AVNSDIIAASINK 764
Cdd:pfam16489  140 DEDSVKLPPKAFKPPDSNGTVVVVFILYRNLGSLLPPSSR-----YDPDRRSLRLprrVVNSPVVSASVHS 205
Gal_Rha_Lectin_LPHNs cd22826
galactose/rhamnose binding lectin domain found in latrophilins; Latrophilins, also called ...
 38-130 3.43e-55

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: 186.37  E-value: 3.43e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   38 RRELSCEGYPIDLRCPGSDVIMIESANYGRTDDKICDADPfQMENINCYLPDAYKIMSQRCNNRTQCIVITGSDVFPDPC 117
Cdd:cd22826      1 KREIACEGYKIRLRCPGSDVIMIESANYGRTDSSTCPSDP-NMTDTNCYLPDALAIVSQRCNNRTRCNVRADSSFFPDPC 79

                           90
                   ....*....|...
gi 1880350455  118 PGTYKYLEVQYEC 130
Cdd:cd22826     80 PGTFKYLEVIYEC 92
7tmB2_CELSR2 cd15992
Cadherin EGF LAG seven-pass G-type receptor 2, member of the class B2 family of ...
 849-1109 8.76e-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: 171.54  E-value: 8.76e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLASFS 928
Cdd:cd15992      4 LKTLTWSSVGVTLGFLLLTFLFLLCLRALRSNKTSIRKNGATALFLSELVFILGINQADNPFACTVIAILLHFFYLCTFS 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  929 WMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKNACWLRVDNHFIWSFIGPVTFIIMLNL 1008
Cdd:cd15992     84 WLFLEGLHIYRMLSEVRDINYGPMRFYYLIGWGVPAFITGLAVGLDPEGYGNPDFCWLSIYDTLIWSFAGPVAFAVSMNV 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1009 iFLVITMYKmvkhsTTLKPDSSRLENIKSWVMG---AFALLCLLGLTWSFGLFFINEASIVMAYLFTIFNAFQGMFIFIF 1085
Cdd:cd15992    164 -FLYILSSR-----ASCSAQQQSFEKKKGPVSGlrtAFTVLLLVSVTCLLALLSVNSDVILFHYLFAGFNCLQGPFIFLS 237

                          250       260
                   ....*....|....*....|....
gi 1880350455 1086 HCLLQKKVRKEYSkcfrhtYCCGG 1109
Cdd:cd15992    238 HVVLLKEVRKALK------TLCGP 255
7tmB2_CELSR3 cd15993
Cadherin EGF LAG seven-pass G-type receptor 3, member of the class B2 family of ...
 849-1097 2.03e-47

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: 170.79  E-value: 2.03e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLASFS 928
Cdd:cd15993      4 LAIVTYSSVSASLAALVLTFSVLTCLRGLKSNTRGIHSNIAAALFLSELLFLLGINRTENQFLCTVVAILLHYFFLSTFA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  929 WMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKNACWLRVDNHFIWSFIGPVTFIIMLNL 1008
Cdd:cd15993     84 WLFVQGLHIYRMQTEARNVNFGAMRFYYAIGWGVPAIITGLAVGLDPEGYGNPDFCWISIHDKLVWSFAGPIVVVIVMNG 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1009 IFLVITMYKMVKHSTTLKPDSSRLENIKSwvmgAFALLCLLGLTWSFGLFFINEASIVMAYLFTIFNAFQGMFIFIFHCL 1088
Cdd:cd15993    164 VMFLLVARMSCSPGQKETKKTSVLMTLRS----SFLLLLLISATWLFGLLAVNNSVLAFHYLHAILCCLQGLAVLLLFCV 239


                   ....*....
gi 1880350455 1089 LQKKVRKEY 1097
Cdd:cd15993    240 LNEEVQEAW 248
7tmB2_GPR126-like_Adhesion_VIII cd15258
orphan GPR126 and related proteins, group VIII adhesion GPCRs, member of the class B2 family ...
 849-1098 2.82e-47

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: 170.67  E-value: 2.82e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNT-IHKNLCINLFIAELIFLI--GINMTEPRIGCAIIAGILHFFFLA 925
Cdd:cd15258      4 LTFISYVGCGISAIFLAITILTYIAFRKLRRDYPSkIHMNLCAALLLLNLAFLLssWIASFGSDGLCIAVAVALHYFLLA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  926 SFSWMCLEGVQLYLMLVEVFESeYSRKKYFYVS--GYLFPAIVVGVSAAIDYSSYGT-----------KNACWLRVDNHF 992
Cdd:cd15258     84 CLTWMGLEAFHLYLLLVKVFNT-YIRRYILKLClvGWGLPALLVTLVLSVRSDNYGPitipngegfqnDSFCWIRDPVVF 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  993 IWSFIGPVTFIIMLNLIFLVITMYKMvkhsTTLKPDSSRLENIKSW--VMGAFALLCLLGLTWSFGLFFINEASIVMAYL 1070
Cdd:cd15258    163 YITVVGYFGLTFLFNMVMLATVLVQI----CRLREKAQATPRKRALhdLLTLLGLTFLLGLTWGLAFFAWGPFNLPFLYL 238

                          250       260
                   ....*....|....*....|....*...
gi 1880350455 1071 FTIFNAFQGMFIFIFHCLLQKKVRKEYS 1098
Cdd:cd15258    239 FAIFNSLQGFFIFIWYCSMKENVRKQWR 266
7tmB3_Methuselah-like cd15039
Methuselah-like subfamily B3, member of the class B family of seven-transmembrane G ...
 849-1102 4.34e-47

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: 170.10  E-value: 4.34e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLqsdRNTIHKN---LCINLFIAELIFLIGINMTEPR-IGCAIIAGILHFFFL 924
Cdd:cd15039      4 LGILTLIGLIISLVFLLLTLAVYALLPEL---RNLHGKClmcLVLSLFVAYLLLLIGQLLSSGDsTLCVALGILLHFFFL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  925 ASFSWMCLEGVQLYLML---VEVFESEYSRKKYFYVS--GYLFPAIVVGVSAAIDYS--------SYGTKNaCWLRVDNH 991
Cdd:cd15039     81 AAFFWLNVMSFDIWRTFrgkRSSSSRSKERKRFLRYSlyAWGVPLLLVAVTIIVDFSpntdslrpGYGEGS-CWISNPWA 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  992 FIWSFIGPVTFIIMLNLIFLVITMYKMVKHSTTLKPDSSRLENIKSWVMGAFALLCLLGLTWSFGLF-FINEASIVMAYL 1070
Cdd:cd15039    160 LLLYFYGPVALLLLFNIILFILTAIRIRKVKKETAKVQSRLRSDKQRFRLYLKLFVIMGVTWILEIIsWFVGGSSVLWYI 239

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1880350455 1071 FTIFNAFQGMFIFIFhCLLQKKVRKEYSKCFR 1102
Cdd:cd15039    240 FDILNGLQGVFIFLI-FVCKRRVLRLLKKKIR 270
7tmB2_GPR112 cd15997
Probable G protein-coupled receptor 112, member of the class B2 family of seven-transmembrane ...
 849-1097 2.50e-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: 165.22  E-value: 2.50e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDR-NTIHKNLCINLFIAELIFLIG--INMTEPRIGCAIIAGILHFFFLA 925
Cdd:cd15997      4 LTLITYLGCGISSIFLGITLVTYLAFEKLRRDYpSKILINLCTALLMLNLVFLLNswLSSFNNYGLCITVAAFLHYFLLA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  926 SFSWMCLEGVQLYLMLVEVFES---EYSRKkyFYVSGYLFPAIVVGVSAAIDYSSYGTKNA----------CWLRVDNHF 992
Cdd:cd15997     84 SFTWMGLEAVHMYFALVKVFNIyipNYILK--FCIAGWGIPAVVVALVLAINKDFYGNELSsdslhpstpfCWIQDDVVF 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  993 IWSFIGPVTFIIMLNL-IFLV----ITMYKMVKHSTTLKPDSsrLENIKSwvmgAFALLCLLGLTWSFGLFFINEASIVM 1067
Cdd:cd15997    162 YISVVAYFCLIFLCNIsMFITvliqIRSMKAKKPSRNWKQGF--LHDLKS----VASLTFLLGLTWGFAFFAWGPVRIFF 235

                          250       260       270
                   ....*....|....*....|....*....|
gi 1880350455 1068 AYLFTIFNAFQGMFIFIFHCLLQKKVRKEY 1097
Cdd:cd15997    236 LYLFSICNTLQGFFIFVFHCLMKENVRKQW 265
7tmB2_GPR144 cd15255
orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G ...
 849-1094 1.29e-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: 154.24  E-value: 1.29e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLaisIFTFCFFRGL---QSDRNTIHKNLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLA 925
Cdd:cd15255      4 LRTLSFIGCGVSLCAL---IVTFILFLAVgvpKSERTTVHKNLIFALAAAEFLLMFSEWAKGNQVACWAVTALLHLFFLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  926 SFSWMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKNACWLRVDNHFIWSFIGPVTFIIM 1005
Cdd:cd15255     81 AFSWMLVEGLLLWSKVVAVNMSEDRRMKFYYVTGWGLPVVIVAVTLATSFNKYVADQHCWLNVQTDIIWAFVGPVLFVLT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1006 LNLIFL----VITMYKMVKHSTTLKPDSSRLENIKSWVMGA----FALLCLLGLTWSFGLFFinEASIVMAYLFTIFNAF 1077
Cdd:cd15255    161 VNTFVLfrvvMVTVSSARRRAKMLTPSSDLEKQIGIQIWATakpvLVLLPVLGLTWLCGVLV--HLSDVWAYVFITLNSF 238

                          250
                   ....*....|....*..
gi 1880350455 1078 QGMFIFIFHCLLQKKVR 1094
Cdd:cd15255    239 QGLYIFLVYAIYNSEVR 255
7tmB2_GPR116-like_Adhesion_VI cd15932
orphan GPR116 and related proteins, group IV adhesion GPCRs, member of the class B2 family of ...
 846-1094 3.95e-41

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: 152.85  E-value: 3.95e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  846 DPQLDIITQVGISVSLVCLAISIFTF-CFFRGLQSDRNTIHKNLCI-----NLFIAELIFLIGINMTEPRI---GCAIIA 916
Cdd:cd15932      1 SPALDYITYVGLGISILSLVLCLIIEaLVWKSVTKNKTSYMRHVCLvnialSLLIADIWFIIGAAISTPPNpspACTAAT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  917 GILHFFFLASFSWMCLEGVQLYLMLVEVFeSEYSRKKYFYVS---GYLFPAIVVGVSAAIDYSS--YGTKNACWLRVD-N 990
Cdd:cd15932     81 FFIHFFYLALFFWMLTLGLLLFYRLVLVF-HDMSKSTMMAIAfslGYGCPLIIAIITVAATAPQggYTRKGVCWLNWDkT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  991 HFIWSFIGPVTFIIMLNLIFLVITMYKMVKHSTTLKPdSSRLENIKSWVMGAFALLC-LLGLTWSFGLF-FINEASIVMA 1068
Cdd:cd15932    160 KALLAFVIPALAIVVVNFIILIVVIFKLLRPSVGERP-SKDEKNALVQIGKSVAILTpLLGLTWGFGLGtMIDPKSLAFH 238

                          250       260
                   ....*....|....*....|....*.
gi 1880350455 1069 YLFTIFNAFQGMFIFIFHCLLQKKVR 1094
Cdd:cd15932    239 IIFAILNSFQGFFILVFGTLLDSKVR 264
7tmB1_hormone_R cd15041
The subfamily B1 of hormone receptors (secretin-like), member of the class B family ...
 851-1103 4.01e-39

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: 147.37  E-value: 4.01e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  851 IITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINlFIAELIFLI----------------GINMTEPRIGCAI 914
Cdd:cd15041      6 YIYLVGYSLSLVALLPAIVIFLYFRSLRCTRIRLHINLFLS-FILRAVFWIiwdllvvydrltssgvETVLMQNPVGCKL 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  915 IAGILHFFFLASFSWMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKnaCWL-RVDNHFI 993
Cdd:cd15041     85 LSVLKRYFKSANYFWMLCEGLYLHRLIVVAFFSEPSSLKLYYAIGWGLPLVIVVIWAIVRALLSNES--CWIsYNNGHYE 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  994 WSFIGPVTFIIMLNLIFLV----ITMYKMvKHSTTLKPDssrleNIKSWVMGAFALLCLLGLTwsFGLFFIN-----EAS 1064
Cdd:cd15041    163 WILYGPNLLALLVNLFFLInilrILLTKL-RSHPNAEPS-----NYRKAVKATLILIPLFGIQ--YLLTIYRppdgsEGE 234

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1880350455 1065 IVMAYLFTIFNAFQGMFIFIFHCLLQKKVRKEYSKCFRH 1103
Cdd:cd15041    235 LVYEYFNAILNSSQGFFVAVIYCFLNGEVQSELKRKWSR 273
7tmB2_GPR128 cd15257
orphan adhesion receptor GPR128, member of the class B2 family of seven-transmembrane G ...
 849-1099 3.09e-38

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: 145.79  E-value: 3.09e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNT-IHKNLCINLFIAELIFLIGINMTEPRIG---------------- 911
Cdd:cd15257      4 LDIISTIGCVLSIAGLVITIIFHLHTRKLRKSSVTwVLLNLCSSLLLFNIIFTSGVENTNNDYEistvpdretntvllse 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  912 ---------CAIIAGILHFFFLASFSWMCLEGVQLYLMLVEVFEseySRKKYFYVS----GYLFPAIVVGVSAAIDYS-- 976
Cdd:cd15257     84 eyvepdtdvCTAVAALLHYFLLVTFMWNAVYSAQLYLLLIRMMK---PLPEMFILQasaiGWGIPAVVVAITLGATYRfp 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  977 --------SYGTKNACWLRV-DNHF------IWSFIGPVTFIIMLNLIFLVITMYKMVKHST---TLKPDSSRLEniksw 1038
Cdd:cd15257    161 tslpvftrTYRQEEFCWLAAlDKNFdikkplLWGFLLPVGLILITNVILFIMTSQKVLKKNNkklTTKKRSYMKK----- 235

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1880350455 1039 VMGAFALLCLLGLTWSFGLFFI---NEASIVMAYLFTIFNAFQGMFIFIFHCLLQKKVRKEYSK 1099
Cdd:cd15257    236 IYITVSVAVVFGITWILGYLMLvnnDLSKLVFSYIFCITNTTQGVQIFILYTWRTPEFRKLVSK 299
7tmB2_GPR126 cd15996
orphan adhesion receptor GPR126, member of the class B2 family of seven-transmembrane G ...
 849-1099 2.14e-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: 142.33  E-value: 2.14e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDR-NTIHKNLCINLFIAELIFLIGINMTEPRIG--CAIIAGILHFFFLA 925
Cdd:cd15996      4 LTFITYIGCGISAIFSAATLLTYIAFEKLRRDYpSKILMNLSTALLFLNLVFLLDGWIASFEIDelCITVAVLLHFFLLA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  926 SFSWMCLEGVQLYLMLVEVFESeYSRKKY--FYVSGYLFPAIVVGVSAAIDYSSY------------GTKNACWLRVDNH 991
Cdd:cd15996     84 TFTWMGLEAIHMYIALVKVFNT-YIRRYIlkFCIIGWGLPALIVSIVLASTNDNYgygyygkdkdgqGGDEFCWIKNPVV 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  992 FIWSFIGPVTFIIMLNLIFLVITMYKMV-----KHSTTLKPDSsrLENIKSWVmgafALLCLLGLTWSFGLFFINEASIV 1066
Cdd:cd15996    163 FYVTCAAYFGIMFLMNVAMFIVVMVQICgrngkRSNRTLREEI--LRNLRSVV----SLTFLLGMTWGFAFFAWGPVNLA 236

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1880350455 1067 MAYLFTIFNAFQGMFIFIFHCLLQKKVRKEYSK 1099
Cdd:cd15996    237 FMYLFTIFNSLQGLFIFVFHCALKENVQKQWRR 269
7tmB2_GPR64 cd15444
orphan adhesion receptor GPR64 and related proteins, member of subfamily B2 of the class B ...
 849-1099 1.39e-36

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: 139.96  E-value: 1.39e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDR-NTIHKNLCINLFIAELIFLIG--INMTEPRIG-CAIIAGILHFFFL 924
Cdd:cd15444      4 LTFITYIGCGLSAIFLSVTLVTYIAFEKIRRDYpSKILIQLCVALLLLNLVFLLDswIALYKDIVGlCISVAVFLHYFLL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  925 ASFSWMCLEGVQLYLMLVEVFESeYSRKKY--FYVSGYLFPAIVVGVSAAIDYSSYG-----------TKNACWLRVDNH 991
Cdd:cd15444     84 VSFTWMGLEAFHMYLALVKVFNT-YIRKYIlkFCIVGWGVPAVVVAIVLAVSKDNYGlgsygkspngsTDDFCWINNNIV 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  992 FIWSFIGPVTFIIMLNLIFLVITMYKMVKHSTTlKPDSSRLENIKSWVMGAFALLCLLGLTWSFGLFFINEASIVMAYLF 1071
Cdd:cd15444    163 FYITVVGYFCVIFLLNISMFIVVLVQLCRIKKQ-KQLGAQRKTSLQDLRSVAGITFLLGITWGFAFFAWGPVNLAFMYLF 241

                          250       260
                   ....*....|....*....|....*...
gi 1880350455 1072 TIFNAFQGMFIFIFHCLLQKKVRKEYSK 1099
Cdd:cd15444    242 AIFNTLQGFFIFIFYCVAKENVRKQWRR 269
7tmB2_BAI_Adhesion_VII cd15251
brain-specific angiogenesis inhibitors, group VII adhesion GPCRs, member of the class B2 ...
 847-1100 2.34e-35

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: 135.84  E-value: 2.34e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  847 PQLDIITQVGISvSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLAS 926
Cdd:cd15251      4 PSVTLIVGCGVS-CLALLTLLAIYAAFWRYIRSERSIILINFCLSIISSNILILVGQTQTLNKGVCTMTAAFLHFFFLSS 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  927 FSWMCLEGVQLYLMLVEVFESEYSRKKyFYVSGYLFPAIVVGVSAAIDYSS-YGTKNACWLRVDNHFIWSFIGPVTFIIM 1005
Cdd:cd15251     83 FCWVLTEAWQSYMAVTGRMRTRLIRKR-FLCLGWGLPALVVAVSVGFTRTKgYGTSSYCWLSLEGGLLYAFVGPAAAVVL 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1006 LNLIFLVITMYKMVKHSTTlkpdssrLENIKSWVMGAFALLCLLGLTW-SFGLFFINEASIVMAYLFTIFNAFQGMFIFI 1084
Cdd:cd15251    162 VNMVIGILVFNKLVSRDGI-------SDNAMASLWSSCVVLPLLALTWmSAVLAMTDRRSVLFQILFAVFDSLQGFVIVM 234

                          250
                   ....*....|....*.
gi 1880350455 1085 FHCLLQKKVRKEYsKC 1100
Cdd:cd15251    235 VHCILRREVQDAV-KC 249
7tmB2_GPR113 cd15253
orphan adhesion receptor GPR113, member of the class B2 family of seven-transmembrane G ...
 847-1094 3.01e-35

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: 136.04  E-value: 3.01e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  847 PQLDIITQVGISVSLVCLAISIFTFC------------FFRglqsdrNTIHKNLCINLFIAELIFLIGINMTEPRIG--C 912
Cdd:cd15253      2 FWLDFLSQVGLGASILALLLCLGIYRlvwrsvvrnkisYFR------HMTLVNIAFSLLLADTCFLGATFLSAGHESplC 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  913 AIIAGILHFFFLASFSWMCLEGVQLYLMLVEVFE--SEYSRKKYFYVSGYLFPAIVVGVSAAIDY--SSYGTKNACWLRV 988
Cdd:cd15253     76 LAAAFLCHFFYLATFFWMLVQALMLFHQLLFVFHqlAKRSVLPLMVTLGYLCPLLIAAATVAYYYpkRQYLHEGACWLNG 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  989 DNHFIWSFIGPVTFIIMLNLIFLVITMYKMVKHSTTLKPDSSRLENIKSWVMGAFALLCLLGLTWSFGLF-FINEASIVM 1067
Cdd:cd15253    156 ESGAIYAFSIPVLAIVLVNLLVLFVVLMKLMRPSVSEGPPPEERKALLSIFKALLVLTPVFGLTWGLGVAtLTGESSQVS 235

                          250       260
                   ....*....|....*....|....*..
gi 1880350455 1068 AYLFTIFNAFQGMFIFIFHCLLQKKVR 1094
Cdd:cd15253    236 HYGFAILNAFQGVFILLFGCLMDKKVR 262
7tmB2_GPR97 cd15442
orphan adhesion receptor GPR97, member of the class B2 family of seven-transmembrane G ...
 852-1089 2.45e-34

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: 133.77  E-value: 2.45e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  852 ITQVGISVSLVCLAISI----FTFCFFRGLQSDRNT-IHKNLCINLFIAELIFLI--GINMTEPRIGCAIIAGILHFFFL 924
Cdd:cd15442      7 ISSAGCGVSMVFLIFTIilyfFLRFTYQKFKSEDAPkIHVNLSSSLLLLNLAFLLnsGVSSRAHPGLCKALGGVTHYFLL 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  925 ASFSWMCLEGVQLYLMLVEVFESEYSrkkYFYVS----GYLFPAIVVGVSAAIDysSYG-----------TKNACWLRVD 989
Cdd:cd15442     87 CCFTWMAIEAFHLYLLAIKVFNTYIH---HYFAKlclvGWGFPALVVTITGSIN--SYGaytimdmanrtTLHLCWINSK 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  990 N---HFIwSFIGPVTFIIMLNLIFLVITMYKMVkhstTLKPDSSRLENIKSW--VMGAFALLCLLGLTWSFGLFFINEAS 1064
Cdd:cd15442    162 HltvHYI-TVCGYFGLTFLFNTVVLGLVAWKIF----HLQSATAGKEKCQAWkgGLTVLGLSCLLGVTWGLAFFTYGSMS 236

                          250       260
                   ....*....|....*....|....*
gi 1880350455 1065 IVMAYLFTIFNAFQGMFIFIFHCLL 1089
Cdd:cd15442    237 VPTVYIFALLNSLQGLFIFIWFVIL 261
7tmB1_CRF-R cd15264
corticotropin-releasing factor receptors, member of the class B family of seven-transmembrane ...
 851-1103 1.59e-33

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: 131.00  E-value: 1.59e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  851 IITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEPRIG------CAIIAGILHFFFL 924
Cdd:cd15264      6 IIYYLGFSISLVALAVALIIFLYFRSLRCLRNNIHCNLIVTFILRNVTWFIMQNTLTEIHHqsnqwvCRLIVTVYNYFQV 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  925 ASFSWMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYssYGTKNACWL--RVDNHFIWSFIGPVTF 1002
Cdd:cd15264     86 TNFFWMFVEGLYLHTMIVWAYSADKIRFWYYIVIGWCIPCPFVLAWAIVKL--LYENEHCWLpkSENSYYDYIYQGPILL 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1003 IIMLNLIFL----VITMYKMvKHSTTLKPDSSRleniKSwVMGAFALLCLLGLTWSfgLFFINEASIVMAYL-FTIFNA- 1076
Cdd:cd15264    164 VLLINFIFLfnivWVLITKL-RASNTLETIQYR----KA-VKATLVLLPLLGITYM--LFFINPGDDKTSRLvFIYFNTf 235

                          250       260       270
                   ....*....|....*....|....*....|
gi 1880350455 1077 ---FQGMFIFIFHCLLQKKVRKEYSKCFRH 1103
Cdd:cd15264    236 lqsFQGLFVAVFYCFLNGEVRSAIRKKFSR 265
Gal_Lectin pfam02140
Galactose binding lectin domain;
50-130 8.90e-33

Galactose binding lectin domain;


Pssm-ID: 460460 [Multi-domain]  Cd Length: 79  Bit Score: 122.01  E-value: 8.90e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   50 LRCPGSDVIMIESANYGRTDDKICdadPFQMENINCYLPDAYKIMSQRCNNRTQCIVITGSDVF-PDPCPGTYKYLEVQY 128
Cdd:pfam02140    1 LSCPPGKVISILFASYGRPDGTTC---PSFIQGTNCHSPNSLAIVSKACQGKNSCSVPASNSVFgGDPCPGTYKYLEVEY 77


                   ..
gi 1880350455  129 EC 130
Cdd:pfam02140   78 KC 79
Gal_Rha_Lectin_CSL1_rpt2 cd22834
second galactose/rhamnose binding lectin domain found in Oncorhynchus keta CSL1 and similar ...
 38-130 2.17e-32

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


Pssm-ID: 438691 [Multi-domain]  Cd Length: 95  Bit Score: 121.41  E-value: 2.17e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   38 RRELSCEGYPIDLRCpGSDVIMIESANYGRTDDKICDAD--PFQMENINCYLPDAYKIMSQRCNNRTQCIVITgSDVFPD 115
Cdd:cd22834      3 KTSITCEGSPVSLDC-GPDVIKIYDANYGRRDSTTCSHGrpESQLTNTNCYLPETTKVMSERCNGKSLCDLLA-SNVVTD 80

                           90
                   ....*....|....*
gi 1880350455  116 PCPGTYKYLEVQYEC 130
Cdd:cd22834     81 PCYGTYKYLEVSYSC 95
7tmB2_BAI2 cd15988
brain-specific angiogenesis inhibitor 2, a group VII adhesion GPCR, member of the class B2 ...
 855-1100 3.22e-32

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: 127.76  E-value: 3.22e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  855 VGISVSLVCLAISIFTFC-FFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLASFSWMCLE 933
Cdd:cd15988     10 IGCAVSCMALLILLAIYAaFWRFIRSERSIILLNFCLSILASNILILVGQSQTLSKGVCTMTAAFLHFFFLSSFCWVLTE 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  934 GVQLYLMLVEVFESEYSRKKyFYVSGYLFPAIVVGVSAAIDYS-SYGTKNACWLRVDNHFIWSFIGPVTFIIMLNLIFLV 1012
Cdd:cd15988     90 AWQSYLAVIGRMRTRLVRKR-FLCLGWGLPALVVAVSVGFTRTkGYGTASYCWLSLEGGLLYAFVGPAAVIVLVNMLIGI 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1013 ITMYKMVKHSTTLKPDSSRLENIKSWVMGAFALLC-------------------------------LLGLTW-SFGLFFI 1060
Cdd:cd15988    169 IVFNKLMSRDGISDKSKKQRAGSEAEPCSSLLLKCskcgvvssaamssatassamaslwsscvvlpLLALTWmSAVLAMT 248

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1880350455 1061 NEASIVMAYLFTIFNAFQGMFIFIFHCLLQKKVrKEYSKC 1100
Cdd:cd15988    249 DRRSILFQVLFAVFNSVQGFVIITVHCFLRREV-QDVVKC 287
7tmB2_BAI1 cd15990
brain-specific angiogenesis inhibitor 1, a group VII adhesion GPCR, member of the class B2 ...
 847-1100 9.28e-32

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: 125.87  E-value: 9.28e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  847 PQLDIITQVGISvSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLAS 926
Cdd:cd15990      7 PSVTLIVGCGVS-SLTLLLLIIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSS 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  927 FSWMCLEGVQLYLMLVEVFESEYSRKKyFYVSGYLFPAIVVGVSAAIDYSS-YGTKNACWLRVDNHFIWSFIGPVTFIIM 1005
Cdd:cd15990     86 FCWVLTEAWQSYMAVTGRLRNRIIRKR-FLCLGWGLPALVVAISVGFTKAKgYGTVNYCWLSLEGGLLYAFVGPAAAVVL 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1006 LNLIFLVITMYKMVKHSTTlkPDSSRLENIKSWVMGAFALLCLLGLTW-SFGLFFINEASIVMAYLFTIFNAFQGMFIFI 1084
Cdd:cd15990    165 VNMVIGILVFNKLVSKDGI--TDKKLKERAGASLWSSCVVLPLLALTWmSAVLAITDRRSALFQILFAVFDSLEGFVIVM 242

                          250
                   ....*....|....*.
gi 1880350455 1085 FHCLLQKKVrKEYSKC 1100
Cdd:cd15990    243 VHCILRREV-QDAVKC 257
Gal_Rha_Lectin cd22823
Galactose/rhamnose-binding lectin domain; Galactose/rhamnose-binding lectin domain is formed ...
 43-130 5.21e-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: 117.22  E-value: 5.21e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   43 CEGYPIDLRCPGSDVIMIESANYGRTDDKICDADPFQMENINCYLPDAYKIMSQRCNNRTQCIVITGSDVFPDPCPGTYK 122
Cdd:cd22823      4 CEGETLTLSCPSGQVIKILSAFYGRTDGTTCCCGPNNTSDTNCCSPDVLDIVKELCDGKQSCSVPASNSVFGDPCPGTSK 83


                   ....*...
gi 1880350455  123 YLEVQYEC 130
Cdd:cd22823     84 YLEVTYTC 91
7tmB2_GPR116_Ig-Hepta cd15254
The immunoglobulin-repeat-containing receptor Ig-hepta/GPR116, member of the class B2 family ...
 849-1095 5.66e-31

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: 123.76  E-value: 5.66e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCF-FRGLQSDRNTIHKNLCI-----NLFIAELIFLIGINMTEPRIG-----CAIIAG 917
Cdd:cd15254      4 LDYITYIGLSISILSLAICIVIESLvWKSVTKNRTSYMRHVCIlniavSLLIADIWFIVVAAIQDQNYAvngnvCVAATF 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  918 ILHFFFLASFSWMCLEGVQLYLMLVEVFE--SEYSRKKYFYVSGYLFPAI--VVGVSAAIDYSSYGTKNACWLR-VDNHF 992
Cdd:cd15254     84 FIHFFYLCVFFWMLALGLMLFYRLVFILHdtSKTIQKAVAFCLGYGCPLIisVITIAVTLPRDSYTRKKVCWLNwEDSKA 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  993 IWSFIGPVTFIIMLNLIFLVITMYKMVKHSTTLKP----DSSRLENIKSWVMgafaLLCLLGLTWSFGL-FFINEASIVM 1067
Cdd:cd15254    164 LLAFVIPALIIVAVNSIITVVVIVKILRPSIGEKPskqeRSSLFQIIKSIGV----LTPLLGLTWGFGLaTVIKGSSIVF 239

                          250       260
                   ....*....|....*....|....*...
gi 1880350455 1068 AYLFTIFNAFQGMFIFIFHCLLQKKVRK 1095
Cdd:cd15254    240 HILFTLLNAFQGLFILVFGTLWDKKVQE 267
7tmB1_NPR_B4_insect-like cd15260
insect neuropeptide receptor subgroup B4 and related proteins, member of the class B family of ...
 852-1012 3.64e-30

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: 121.23  E-value: 3.64e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  852 ITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLI--------GINMTEPRIGCAIIAGILHFFF 923
Cdd:cd15260      7 VYIGGYSVSLIALIISLAIFFSFRSLRCTRITIHMNLFISFALNNLLWIVwyklvvdnPEVLLENPIWCQALHVLLQYFM 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  924 LASFSWMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKNACWLRvDNHFIWSFIGPVTFI 1003
Cdd:cd15260     87 VCNYFWMFCEGLYLHTVLVVAFISEKSLMRWFIAIGWGVPLVITAIYAGVRASLPDDTERCWME-ESSYQWILIVPVVLS 165


                   ....*....
gi 1880350455 1004 IMLNLIFLV 1012
Cdd:cd15260    166 LLINLIFLI 174
7tmB2_GPR114 cd15443
orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G ...
 849-1096 2.52e-29

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: 118.70  E-value: 2.52e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNT-IHKNLCINLFIAELIFLIG--INMTEPRIGCAIIAGILHFFFLA 925
Cdd:cd15443      4 LTYISIVGCSISAAASLLTILLHFFSRKQPKDSTTrIHMNLLGSLFLLNGSFLLSppLATSQSTWLCRAAAALLHYSLLC 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  926 SFSWMCLEGVQLYLMLVEVFESeYSRKKYFY--VSGYLFPAIVVGVSAAIDYSSYG-----------TKNACWLRVDN-- 990
Cdd:cd15443     84 CLTWMAIEGFHLYLLLVKVYNI-YIRRYVLKlcVLGWGLPALIVLLVLIFKREAYGphtiptgtgyqNASMCWITSSKvh 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  991 HFIWSFIGPVTfiIMLNLIFLVITMYKMVKHSTTLKPDSSRLENIKSWVMGafaLLCLLGLTWSFGLFFINEASIVMAYL 1070
Cdd:cd15443    163 YVLVLGYAGLT--SLFNLVVLAWVVRMLRRLRSRKQELGERARRDWVTVLG---LTCLLGTTWALAFFSFGVFLIPQLFL 237

                          250       260
                   ....*....|....*....|....*.
gi 1880350455 1071 FTIFNAFQGMFIFIFHCLLQKKVRKE 1096
Cdd:cd15443    238 FTIINSLYGFFICLWYCTQRRRSDAS 263
Gal_Rha_Lectin_SUL-I-like cd22827
galactose/rhamnose binding lectin domain found in Toxopneustes pileolus rhamnose-binding ...
 40-130 6.79e-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: 6.79e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   40 ELSCEGYPIDLRCPGSDVIMIESANYGRTDDKICdadP-FQMENINCYLPDAYKIMSQRCNNRTQCIVITGSDVFPDPCP 118
Cdd:cd22827      1 KRVCEGQTLTISCPAGKVIDIVSANYGRTDSSTC---PsGGIKNTNCRASNSLSIVRNRCNGKRSCSVKASNSVFGDPCV 77

                           90
                   ....*....|..
gi 1880350455  119 GTYKYLEVQYEC 130
Cdd:cd22827     78 GTYKYLEVRYRC 89
7tmB2_GPR124-like_Adhesion_III cd15259
orphan GPR124 and related proteins, group III adhesion GPCRs, member of class B2 family of ...
 849-1101 2.04e-28

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: 115.94  E-value: 2.04e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFC-FFRGLQSDRNTIHK--NLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLA 925
Cdd:cd15259      4 LHPVVYAGAALCLLCLLATIITYIvFHRLIRISRKGRHMlvNLCLHLLLTCVVFVGGINRTANQLVCQAVGILLHYSTLC 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  926 SFSWMCLEGVQLYLMLVEVFES-------EYSRKKY--FYVSGYLFPAIVVGVSAAIDYSSYGTKNACWLrVDNHFIWSF 996
Cdd:cd15259     84 TLLWVGVTARNMYKQVTKTAKPpqdedqpPRPPKPMlrFYLIGWGIPLIICGITAAVNLDNYSTYDYCWL-AWDPSLGAF 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  997 IGPVTFIIMLNLIFLVITMYKMvkhsttlkpdSSRLENIKSWVMGAFALLCLLGLTWSFGLFFINEA---SIVMAYLFTI 1073
Cdd:cd15259    163 YGPAALIVLVNCIYFLRIYCQL----------KGAPVSFQSQLRGAVITLFLYVAMWACGALAVSQRyflDLVFSCLYGA 232

                          250       260
                   ....*....|....*....|....*...
gi 1880350455 1074 FNAFQGMFIFIFHCLLQKKVRKEYSKCF 1101
Cdd:cd15259    233 TCSSLGLFVLIHHCLSREDVRQSWRQCC 260
Gal_Rha_Lectin_RBL_rpt2 cd22836
second galactose/rhamnose binding lectin domain found in Silurus asotus rhamnose-binding ...
 43-130 5.57e-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: 108.91  E-value: 5.57e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   43 CEGYPIDLRCpGSDVIMIESANYGRTDDKICDADP--FQMENINCYLPDAYKIMSQRCNNRTQCIVITGSDVFPDPCPGT 120
Cdd:cd22836      7 CEGGYAVLKC-GSGVIQIISANYGRTDSTTCSAGRpaSQVQNTNCYASNSLAIVSQSCNGKKSCTVSASNSVFSDPCVGT 85

                           90
                   ....*....|
gi 1880350455  121 YKYLEVQYEC 130
Cdd:cd22836     86 YKYLYVTYSC 95
7tmB1_DH_R cd15263
insect diuretic hormone receptors, member of the class B family of seven-transmembrane G ...
 851-1101 6.69e-28

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: 114.77  E-value: 6.69e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  851 IITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIG----INMTEPRIGCAIIAGILHFFFLAS 926
Cdd:cd15263      6 TIYFIGYSLSLVALSLALWIFLYFKDLRCLRNTIHTNLMFTYILADLTWILTltlqVSIGEDQKSCIILVVLLHYFHLTN 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  927 FSWMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVGV-----SAAIDYSSYGT------KNACWLRvDNHFIWS 995
Cdd:cd15263     86 FFWMFVEGLYLYMLVVETFSGENIKLRVYAFIGWGIPAVVIVIwaivkALAPTAPNTALdpngllKHCPWMA-EHIVDWI 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  996 FIGPVTFIIMLNLIFLVITMYKMVkhsTTLKpdSSRLENIKSWVMGAFALLC---LLGLTWSFGLFFINEAsiVMAYLFT 1072
Cdd:cd15263    165 FQGPAILVLAVNLVFLVRIMWVLI---TKLR--SANTVETQQYRKAAKALLVlipLLGITYILVIAGPTEG--IAANIFE 237

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1880350455 1073 IFNAF----QGMFIFIFHCLLQKKVRKEYSKCF 1101
Cdd:cd15263    238 YVRAVllstQGFTVALFYCFLNTEVRNTLRHHF 270
7tmB2_BAI3 cd15989
brain-specific angiogenesis inhibitor 3, a group VII adhesion GPCR, member of the class B2 ...
 847-1097 1.21e-27

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: 114.78  E-value: 1.21e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  847 PQLDIITQVGISVsLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLAS 926
Cdd:cd15989      6 PSVTLIVGCGLSC-LALITLAVVYAALWRYIRSERSIILINFCLSIISSNILILVGQTQTHNKGICTMTTAFLHFFFLAS 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  927 FSWMCLEGVQLYLMLVEVFESEYSRKKYFYVsGYLFPAIVVGVSAAIDYSS-YGTKNACWLRVDNHFIWSFIGPVTFIIM 1005
Cdd:cd15989     85 FCWVLTEAWQSYMAVTGKIRTRLIRKRFLCL-GWGLPALVVAISMGFTKAKgYGTPHYCWLSLEGGLLYAFVGPAAAVVL 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1006 LNLIFLVITMYKMV----------KHS---------------------TTLKPDSSRLENIKSWVMGAFALLCLLGLTW- 1053
Cdd:cd15989    164 VNMVIGILVFNKLVsrdgildkklKHRagqmsephsgltlkcakcgvvSTTALSATTASNAMASLWSSCVVLPLLALTWm 243

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1880350455 1054 SFGLFFINEASIVMAYLFTIFNAFQGMFIFIFHCLLQKKVRKEY 1097
Cdd:cd15989    244 SAVLAMTDKRSILFQILFAVFDSLQGFVIVMVHCILRREVQDAF 287
Gal_Rha_Lectin_dCirl cd22830
galactose/rhamnose binding lectin domain found in Drosophila melanogaster Latrophilin Cirl and ...
 43-130 5.81e-27

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: 105.78  E-value: 5.81e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   43 CEGYPIDLRCPGSDVIMIESANYGRTDDKICDADPFQMENINCYLPDAYKIMSQRCNNRTQCIVITGSDVFPDPCPGTYK 122
Cdd:cd22830      5 CEGSQLTLECEDGTVIRIIRANYGRFSIAICNDHGNTDWSVNCMSPRSLRVVQERCDGKRSCSIPASSSVFGDPCPGTPK 84


                   ....*...
gi 1880350455  123 YLEVQYEC 130
Cdd:cd22830     85 YLEVHYQC 92
7tmB2_GPR56 cd15995
orphan adhesion receptor GPR56, member of the class B2 family of seven-transmembrane G ...
 849-1098 1.42e-26

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: 110.69  E-value: 1.42e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNT-IHKNLCINLFIAELIFLIGINM--TEPRIGCAIIAGILHFFFLA 925
Cdd:cd15995      4 LTILTYVGCIISALASVFTIAFYLCSRRKPRDYTIyVHMNLLLAIFLLDTSFLISEPLalTGSEAACRAGGMFLHFSLLA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  926 SFSWMCLEGVQLYLMLVEVFESeysrkkyfYVSGYL---------FPAIVVGVSAAIDYSSYG--------------TKN 982
Cdd:cd15995     84 CLTWMGIEGYNLYRLVVEVFNT--------YVPHFLlklcavgwgLPIFLVTLIFLVDQDNYGpiilavhrspekvtYAT 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  983 ACWLRVDNHFIWSFIGPVTFIIMLNLIFLVITMYKMVKhsttLKPDSSRLEniksWVMGAFALLCLLGLTWSFGLFFINE 1062
Cdd:cd15995    156 ICWITDSLISNITNLGLFSLVFLFNMAMLATMVVEILR----LRPRTHKWS----HVLTLLGLSLVLGIPWALAFFSFAS 227

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1880350455 1063 AS--IVMAYLFTIFNAFQGMFIFIFHCLLQKKVRKEYS 1098
Cdd:cd15995    228 GTfqLVIVYLFTIINSLQGFLIFLWYWSMVLQARGGPS 265
7tmB1_NPR_B7_insect-like cd15273
insect neuropeptide receptor subgroup B7 and related proteins, member of the class B family of ...
 847-1099 4.40e-25

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: 107.07  E-value: 4.40e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  847 PQLDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCI-------------NLFI------AELIFLIG----- 902
Cdd:cd15273      2 PIIKGISQIGYIVSLITLIIAFAIFLSFKKLHCARNKLHMHLFAsfilrafmtllkdSLFIdglgllADIVERNGggnev 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  903 INMTEPRIGCAIIAGILHFFFLASFSWMCLEGVQLY-LMLVEVFESEySRKKYFYVSGYLFPAIVVG---VSAAIDYSSY 978
Cdd:cd15273     82 IANIGSNWVCKAITSLWQYFIIANYSWILMEGLYLHnLIFLALFSDE-NNIILYILLGWGLPLIFVVpwiVARILFENSL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  979 gtknaCWLRVDNHFIWSFI-GPVTFIIMLNLI-FLVITMYKMVKHSTTLKPDSSRLeniKSWVMGAFALLCLLGL--TWS 1054
Cdd:cd15273    161 -----CWTTNSNLLNFLIIrIPIMISVLINFIlFLNIVRVLLVKLRSSVNEDSRRY---KKWAKSTLVLVPLFGVhyTIF 232

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1880350455 1055 FGLFFIN--EASIVMAYLFT--IFNAFQGMFIFIFHCLLQKKVRKEYSK 1099
Cdd:cd15273    233 LILSYLDdtNEAVELIWLFCdqLFASFQGFFVALLYCFLNGEVRAEIQR 281
Gal_Rha_Lectin_REJ3 cd22841
galactose/rhamnose binding lectin domain found in Strongylocentrotus purpuratus receptor for ...
 43-130 1.87e-24

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: 98.70  E-value: 1.87e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   43 CEGYPIDLRCpGSDVIMIESANYGRTDDKICDADPFqMENINCYLPDAYKIMSQRCNNRTQCIVITGSDVFPDPCPGTYK 122
Cdd:cd22841      7 CEGDTDVIDC-GNGVINIHSAVYGRTDSTTCSHDQS-VSNTNCHSDDSVNILSACCNGQSQCTVTATNSIFGDPCPGTYK 84


                   ....*...
gi 1880350455  123 YLEVQYEC 130
Cdd:cd22841     85 YLNVTYTC 92
Gal_Rha_Lectin_EVA1_EVA1C_rpt2 cd22829
second galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
 37-132 4.22e-24

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: 98.10  E-value: 4.22e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   37 VRRELSCEGYPIDLRCPGSDVIMIESANYGRT--DDKICDADPFQMENINCYLPDAYKIMSQRCNNRTQCIVITGSDVFP 114
Cdd:cd22829      1 FKSKVVCEGEKLRLSCKPSSRLAIYSASYGRTleGSVECPSTPKGDPDEECLSDVALETVMKRCHGKRRCSLTADSETFG 80

                           90
                   ....*....|....*....
gi 1880350455  115 DPC-PGTYKYLEVQYECVP 132
Cdd:cd22829     81 DPCpPGVRKYLKVVYTCVP 99
Gal_Rha_Lectin_SML_rpt2 cd22835
second galactose/rhamnose binding lectin domain found in Scomberomorus niphonius ...
 39-130 5.02e-24

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: 97.37  E-value: 5.02e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   39 RELSCEGYPIDLRCPGSDVIMIESANYGRTDDKICDA--DPFQMENINCYLPdaYKIMSQRCNNRTQCIVITGSDVFPDP 116
Cdd:cd22835      1 HLVACEGSLAHLKCDEGQVISVYGADYGRRDKTTCSFgrPPSQIQNVECSNP--TDKVAERCNGKNSCSIKASNSVFGDP 78

                           90
                   ....*....|....
gi 1880350455  117 CPGTYKYLEVQYEC 130
Cdd:cd22835     79 CVGTYKYLEVAYTC 92
Gal_Rha_Lectin_CSL3_rpt1_rpt2-like cd22832
first and second galactose/rhamnose binding lectin domain found in Oncorhynchus keta ...
 39-130 3.11e-23

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


Pssm-ID: 438689 [Multi-domain]  Cd Length: 94  Bit Score: 95.25  E-value: 3.11e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   39 RELSCEGYPIDLRCpGSDVIMIESANYGRTDDKICDAD-PF-QMENINCYLPDAYKIMSQRCNNRTQCIVITGSDVFPDP 116
Cdd:cd22832      2 SSITCEGSDAQLDC-DGGKIRIQRANYGRRDHDVCSIGrPAnQLTNTNCLSQSTTSKMAERCDGKSQCIVPASNSVFGDP 80

                           90
                   ....*....|....
gi 1880350455  117 CPGTYKYLEVQYEC 130
Cdd:cd22832     81 CVGTYKYLDVAYTC 94
7tmB1_PDFR cd15261
The pigment dispersing factor receptor, member of the class B seven-transmembrane G ...
 855-1102 5.86e-23

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: 100.52  E-value: 5.86e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  855 VGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLI-----------------------GINMTEprIG 911
Cdd:cd15261     10 VGLCLSLVSLIISLFIFSYFRTLRNHRTRIHKNLFLAILLQVIIRLVlyidqaitrsrgshtnaattegrTINSTP--IL 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  912 CAIIAGILHFFFLASFSWMCLEGVQLYLML-VEVFESEYSRKKYfYVSGYLFPaIVVGVSAAIDYSSYGTKNACWL--RV 988
Cdd:cd15261     88 CEGFYVLLEYAKTVMFMWMFIEGLYLHNIIvVSVFSGKPNYLFY-YILGWGIP-IVHTSAWAIVTLIKMKVNRCWFgyYL 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  989 DNHFiWSFIGPVTFIIMLNLIFLVITMYKMVkhSTTLKPDSSRLENIKSWVMGAFALLCLLGLTWSFGLF-FINEASI-- 1065
Cdd:cd15261    166 TPYY-WILEGPRLAVILINLFFLLNIIRVLV--SKLRESHSREIEQVRKAVKAAIVLLPLLGITNILQMIpPPLTSVIvg 242

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1880350455 1066 --VMAYLFTIFNAFQGMFIFIFHCLLQKKVRKEYSKCFR 1102
Cdd:cd15261    243 faVWSYSTHFLTSFQGFFVALIYCFLNGEVKNVLKKFWR 281
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
 788-840 1.22e-21

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: 89.37  E-value: 1.22e-21
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1880350455   788 FNPNCSFWNYSErsmmGYWSTQGCKLLDTNKTHTTCSCSHLTNFAILMAHREI 840
Cdd:smart00303    1 FNPICVFWDESS----GEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPPI 49
7tmB1_CRF-R1 cd15445
corticotropin-releasing factor receptor 1, member of the class B family of seven-transmembrane ...
 851-1103 2.71e-21

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: 95.39  E-value: 2.71e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  851 IITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLcINLFIAELI--FLIGINMT----EPRIG-CAIIAGILHFFF 923
Cdd:cd15445      6 IINYLGHCISLVALLVAFVLFLRLRSIRCLRNIIHWNL-ITAFILRNAtwFVVQLTMSpevhQSNVVwCRLVTAAYNYFH 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  924 LASFSWMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVgVSAAIDYSSYGTKNaCWL--RVDNHFIWSFIGPVT 1001
Cdd:cd15445     85 VTNFFWMFGEGCYLHTAIVLTYSTDKLRKWMFICIGWCIPFPII-VAWAIGKLYYDNEK-CWFgkRAGVYTDYIYQGPMI 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1002 FIIMLNLIFLV----ITMYKMvKHSTTlkpdsSRLENIKSWVMGAFALLCLLGLTWSfgLFFINE-----ASIVMAYLFT 1072
Cdd:cd15445    163 LVLLINFIFLFnivrILMTKL-RASTT-----SETIQYRKAVKATLVLLPLLGITYM--LFFVNPgedeiSRIVFIYFNS 234

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1880350455 1073 IFNAFQGMFIFIFHCLLQKKVRKEYSKCFRH 1103
Cdd:cd15445    235 FLESFQGFFVSVFYCFLNSEVRSAVRKRWHR 265
Gal_Rha_Lectin_CSL1-2_RBL_SML_rpt1 cd22833
first galactose/rhamnose binding lectin domain found in Oncorhynchus keta CSL1-2, Silurus ...
 42-132 4.27e-21

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: 89.24  E-value: 4.27e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   42 SCEGYPID-LRCpGSDVIMIESANYGRTDDKICDA--DPFQMENINCYLPDAYKIMSQRCNNRTQCIVITGSDVFPDPCP 118
Cdd:cd22833      5 TCDGNNVHrLSC-DTGVINVQSALYGRTDSETCSEgrPPEQLTNTQCSQSGTLDLLKNRCDGKKVCELNTNDFRTSDPCP 83

                           90
                   ....*....|....
gi 1880350455  119 GTYKYLEVQYECVP 132
Cdd:cd22833     84 GTYKYLQTNYTCLP 97
7tmB1_CRF-R2 cd15446
corticotropin-releasing factor receptor 2, member of the class B family of seven-transmembrane ...
 851-1099 7.12e-21

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: 94.26  E-value: 7.12e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  851 IITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLcINLFIAE-----LIFLIGINMTEP-RIGCAIIAGILHFFFL 924
Cdd:cd15446      6 IINYLGHCISVGALVVAFLLFLCLRSIRCLRNIIHWNL-ITTFILRnvmwfLLQMIDHNIHESnEVWCRCITTIYNYFVV 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  925 ASFSWMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVgVSAAIDYSSYGTKNaCWLRVD--NHFIWSFIGPVTF 1002
Cdd:cd15446     85 TNFFWMFVEGCYLHTAIVMTYSTDKLRKWVFLFIGWCIPCPII-VAWAIGKLYYENEQ-CWFGKEpgKYIDYIYQGPVIL 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1003 IIMLNLIFLV----ITMYKMvKHSTTlkpdsSRLENIKSWVMGAFALLCLLGLTWSfgLFFINE-----ASIVMAYLFTI 1073
Cdd:cd15446    163 VLLINFVFLFnivrILMTKL-RASTT-----SETIQYRKAVKATLVLLPLLGITYM--LFFVNPgeddiSQIVFIYFNSF 234

                          250       260
                   ....*....|....*....|....*.
gi 1880350455 1074 FNAFQGMFIFIFHCLLQKKVRKEYSK 1099
Cdd:cd15446    235 LQSFQGFFVSVFYCFLNGEVRSAARK 260
7tmB2_GPR111_115 cd15994
orphan adhesion receptors GPR111 and GPR115, member of the class B2 family of ...
 849-1094 1.13e-20

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: 93.75  E-value: 1.13e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAI--SIFTFCFFRGLQSD----RNTIHKNLCINLFIAELIFLIGINMTEPRI---GCAIIAGIL 919
Cdd:cd15994      4 LDYITRIGLGLSIFSLALclTIEAVVWSHVTKTEitymRHVCIVNIATSLLIADVWFILASIVHNTALnypLCVAATFFL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  920 HFFFLASFSWMCLEGVQ-LYLMLVEVFESEYSRKKYFYVS-GYLFPAIVVGVSAAIDY--SSYGTKNACWLRVDN-HFIW 994
Cdd:cd15994     84 HFFYLSLFFWMLTKALLiLYGILLVFFKITKSVFIATAFSiGYGCPLVIAVLTVAITEpkKGYLRPEACWLNWDEtKALL 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  995 SFIGPVTFIIMLNLIFLVITMYKMVKHS--TTLKPDSSRLENIKSWVmgafALLC-LLGLTWSFGL-FFINEASIVMAYL 1070
Cdd:cd15994    164 AFIIPALSIVVVNLIVVGVVVVKTQRSSigESCKQDVSNIIRISKNV----AILTpLLGLTWGFGLaTIIDSRSLPFHII 239

                          250       260
                   ....*....|....*....|....
gi 1880350455 1071 FTIFNAFQGMFIFIFHCLLQKKVR 1094
Cdd:cd15994    240 FALLNAFQGFFILLFGTILDRKIR 263
7tmB1_Secretin_R-like cd15930
secretin receptor-like group of hormone receptors, member of the class B family of ...
 849-1102 4.80e-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: 4.80e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNL-------CINLFIAELIFLIGINMTE---PRIGCAIIAGI 918
Cdd:cd15930      4 VKIIYTVGYSLSLTSLTTAMIILCLFRKLHCTRNYIHMNLfvsfilrAIAVFIKDAVLFSSEDVDHcfvSTVGCKASMVF 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  919 LHFFFLASFSWMCLEGVQLYLMLVEVFESEysrKKYFY---VSGYLFPAIVVGVSAAIDYssYGTKNACWLRVDNHFIWS 995
Cdd:cd15930     84 FQYCVMANFFWLLVEGLYLHTLLVISFFSE---RRYFWwyvLIGWGAPTVFVTVWIVARL--YFEDTGCWDINDESPYWW 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  996 FI-GPVTFIIMLNLIFLVITMYKMVKHSTTLKPDSSRLENIKSWVMGAFALLCLLGLTWS-FGLFFINEASIVMAYLFTI 1073
Cdd:cd15930    159 IIkGPILISILVNFVLFINIIRILLQKLRSPDIGGNESSQYKRLARSTLLLIPLFGIHYIvFAFFPENISLGIRLYFELC 238

                          250       260
                   ....*....|....*....|....*....
gi 1880350455 1074 FNAFQGMFIFIFHCLLQKKVRKEYSKCFR 1102
Cdd:cd15930    239 LGSFQGFVVAVLYCFLNGEVQAEIKRKWR 267
Gal_Rha_Lectin_EVA1_EVA1C_rpt1 cd22828
first galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
 43-132 6.88e-20

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: 86.18  E-value: 6.88e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   43 CEGYPIDLRCPGSDVIMIESANYGRTD--DKIC-----DADPFQMENINCYLPDAYKIMSQRCNNRTQCIVITGSDVFP- 114
Cdd:cd22828      8 CDGEELTLRCPPNTTISIQSAFYGRSVpsAQLCpsqsgPASSTSLEDTNCLAPTALQKVVEECQKKRSCRLLVSSRTFGl 87

                           90
                   ....*....|....*...
gi 1880350455  115 DPCPGTYKYLEVQYECVP 132
Cdd:cd22828     88 DPCPGTSKYLEVAYKCRP 105
7tmB1_PTH-R_related cd15272
invertebrate parathyroid hormone-related receptors, member of the class B family of ...
 847-1099 2.78e-19

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: 89.76  E-value: 2.78e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  847 PQLDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINL-------FIAELIFLIGINMTEPRI--------- 910
Cdd:cd15272      2 PSIRLMYNIGYGLSLVSLLIAVIIMLYFKKLHCPRNTIHINLFVSFilravlsFIKENLLVQGVGFPGDVYydsngvief 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  911 -------GCAIIAGILHFFFLASFSWMCLEGVQLY-LMLVEVFeSEYSRKKYFYVSGYLFPAIV----VGVSAAIDyssy 978
Cdd:cd15272     82 kdegshwECKLFFTMFNYILGANYMWIFVEGLYLHmLIFVAVF-SENSRVKWYILLGWLSPLLFvlpwVFVRATLE---- 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  979 gtKNACW-LRVDNHFIWSFIGPVTFIIMLNLIF---LVITMYKMVKHSTTLKPDSSRLENIkswvmgAFALLCLLGLtws 1054
Cdd:cd15272    157 --DTLCWnTNTNKGYFWIIRGPIVISIAINFLFfinIVRVLFTKLKASNTQESRPFRYRKL------AKSTLVLIPL--- 225

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1880350455 1055 FGLFFI-----------NEASIVMAYLFTIFNAFQGMFIFIFHCLLQKKVRKEYSK 1099
Cdd:cd15272    226 FGVHYMvfvvlpdsmssDEAELVWLYFEMFFNSFQGFIVALLFCFLNGEVQSEIKK 281
7tmB1_GLP2R cd15266
glucagon-like peptide-2 receptor, member of the class B family of seven-transmembrane G ...
 849-1103 3.19e-19

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: 89.80  E-value: 3.19e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNL-------CINLFIAELIF-------------LIGINMTEP 908
Cdd:cd15266      4 LQLIYTIGYSLSLISLSLALLILLLLRKLHCTRNYIHMNLfasfilrALAVLIKDIVLystyskrpddetgWISYLSEES 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  909 RIGCAIIAGILHFFFLASFSWMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVgVSAAIDYSSYgTKNACWLRV 988
Cdd:cd15266     84 STSCRVAQVFMHYFVGANYFWLLVEGLYLHTLLVTAVLSERRLLKKYMLIGWGTPVLFV-VPWGVAKILL-ENTGCWGRN 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  989 DNHFIWSFI-GPVTFIIMLN-LIFLVITMYKMVKhsttLKPDSSRLENIK-SWVMGAFALLCLLGLTWSFGLFFINE--- 1062
Cdd:cd15266    162 ENMGIWWIIrGPILLCITVNfYIFLKILKLLLSK----LKAQQMRFTDYKyRLARSTLVLIPLLGIHEVVFSFITDEqve 237

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1880350455 1063 --ASIVMAYLFTIFNAFQGMFIFIFHCLLQKKVRKEYSKCFRH 1103
Cdd:cd15266    238 gfSRHIRLFIQLTLSSFQGFLVAVLYCFANGEVKAELKKRWQL 280
HormR smart00008
Domain present in hormone receptors;
472-533 3.68e-19

Domain present in hormone receptors;


Pssm-ID: 214468  Cd Length: 70  Bit Score: 82.95  E-value: 3.68e-19
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1880350455   472 PERFCEATEKRDITWPQTQRGMLVERPCPKGTRG-----TASYLC-STGAWHPKGPDLSNCTSHWVNQ 533
Cdd:smart00008    1 TDLGCPATWDGIICWPQTPAGQLVEVPCPKYFSGfsyktGASRNCtENGGWSPPFPNYSNCTSNDYEE 68
7tmB1_PACAP-R1 cd15987
pituitary adenylate cyclase-activating polypeptide type 1 receptor, member of the class B ...
 855-1102 1.49e-18

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: 87.33  E-value: 1.49e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  855 VGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLI--GINMTEP--------RIGCAIIAGILHFFFL 924
Cdd:cd15987     10 VGYSTSLVSLTTAMVILCRFRKLHCTRNFIHMNLFVSFILRAISVFIkdGVLYAEQdsdhcfvsTVECKAVMVFFHYCVM 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  925 ASFSWMCLEGVQLYLMLVEVFeseYSRKKYFY---VSGYLFPAIVVGVSAAIDYssYGTKNACWLRVDNHFIWSFI-GPV 1000
Cdd:cd15987     90 SNYFWLFIEGLYLFTLLVETF---FPERRYFYwytIIGWGTPTICVTVWAVLRL--HFDDTGCWDMNDNTALWWVIkGPV 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1001 TFIIMLNLIFLVITMYKMVKHSTTlkPDSSRLENIKSWVMGAFALLC--LLGLTWSFGLFFINEASIVMAYLFTI-FNAF 1077
Cdd:cd15987    165 VGSIMINFVLFIGIIIILVQKLQS--PDIGGNESSIYLRLARSTLLLipLFGIHYTVFAFSPENVSKRERLVFELgLGSF 242

                          250       260
                   ....*....|....*....|....*
gi 1880350455 1078 QGMFIFIFHCLLQKKVRKEYSKCFR 1102
Cdd:cd15987    243 QGFVVAVLYCFLNGEVQSEIKRKWR 267
7tmB1_secretin cd15275
secretin receptor, member of the class B family of seven-transmembrane G protein-coupled ...
 849-1102 1.95e-18

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: 87.10  E-value: 1.95e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINlFI--AELIFL--------IGINMTEP-RIGCAIIAG 917
Cdd:cd15275      4 LKTMYTVGYSVSLVSLAIALAILCSFRRLHCTRNYIHMQLFLS-FIlrAISIFIkdavlfssEDDNHCDIyTVGCKVAMV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  918 ILHFFFLASFSWMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVgvsAAIDYSSYGTKNA-CWLRVDNHFIWSF 996
Cdd:cd15275     83 FSNYCIMANYSWLLVEGLYLHSLLSISFFSERKHLWWYIALGWGSPLIFI---ISWAIARYLHENEgCWDTRRNAWIWWI 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  997 I-GPVTFIIMLNLIFLVITMYKMVKHSTTLKPDSSRLENIKSWVMGAFALLCLLGLTWSFGLFFINEASIVMAYLFTIFN 1075
Cdd:cd15275    160 IrGPVILSIFVNFILFLNILRILMRKLRAPDMRGNEFSQYKRLAKSTLLLIPLFGLHYILFAFFPEDVSSGTMEIWLFFE 239

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1880350455 1076 ----AFQGMFIFIFHCLLQKKVRKEYSKCFR 1102
Cdd:cd15275    240 lalgSFQGFVVAVLYCFLNGEVQLEIQRKWR 270
7tmB1_calcitonin_R cd15274
calcitonin receptor, member of the class B family of seven-transmembrane G protein-coupled ...
 855-1093 2.17e-18

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: 87.14  E-value: 2.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  855 VGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGI----NMTEPRIGCAIIAGILHFFFLASFS-- 928
Cdd:cd15274     10 VGHSLSIATLLISLGIFFFFRSLSCQRVTLHKNLFLSYILNSIIIIIHLvavvPNGELVARNPVSCKILHFIHQYMMGcn 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  929 --WMCLEGVQLY-LMLVEVFeSEYSRKKYFYVSGYLFPAIVVGVSaAIDYSSYGTKNaCWLRVDNHFIWSFIGPVTFIIM 1005
Cdd:cd15274     90 yfWMLCEGIYLHtLIVVAVF-AEKQRLMWYYLLGWGFPLIPTTIH-AITRAVYYNDN-CWLSSETHLLYIIHGPIMAALV 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1006 LNLIFLV-ITMYKMVKHSTTLKPDSSRLenIKSwVMGAFALLCLLGLtwSFGLF----FINEASIVMAYLFTIFNAFQGM 1080
Cdd:cd15274    167 VNFFFLLnIVRVLVTKLRETHEAESHMY--LKA-VKATLILVPLLGI--QFVLFpwrpSGKILGKIYDYVMHSLIHFQGF 241

                          250
                   ....*....|...
gi 1880350455 1081 FIFIFHCLLQKKV 1093
Cdd:cd15274    242 FVATIFCFCNGEV 254
7tmB2_GPR123 cd16000
G protein-coupled receptor 123, member of the class B2 family of seven-transmembrane G ...
 858-1087 1.45e-17

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: 84.62  E-value: 1.45e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  858 SVSLVCLAISIFTFCFFRG-LQSDRNTIHK--NLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLASFSWMCLEG 934
Cdd:cd16000     13 AVMLLCLFASIITYIVHHStIRISRKGWHMllNFCFHTALTFAVFAGGINRTKYPIICQAVGIVLHYSTLSTMLWIGVTA 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  935 VQLYLMLV-------EVFESEYSRK---KYFYVSGYLfPAIVVGVSAAIDYSSYGTKNA----CWLRVDNHfIWSFIGPV 1000
Cdd:cd16000     93 RNIYKQVTkkphlcqDTDQPPYPKQpllRFYLVSGGV-PFIICGITAATNINNYGTEDEdtpyCWMAWEPS-LGAFYGPV 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1001 TFIIMLNLIFLVITMYKMVKHST---TLKPDSSRLENIKSwvmGAFALLcLLGLTWSFGLFFINEA---SIVMAYLFTIF 1074
Cdd:cd16000    171 AFIVLVTCIYFLCTYVQLRRHPErkyELKNEHSFKAQLRA---AAFTLF-LFTATWAFGALAVSQGhflDMIFSCLYGAF 246

                          250
                   ....*....|...
gi 1880350455 1075 NAFQGMFIFIFHC 1087
Cdd:cd16000    247 CVTLGLFILIHHC 259
Gal_Rha_Lectin_RBL_rpt3 cd22837
third galactose/rhamnose binding lectin domain found in Silurus asotus rhamnose-binding lectin ...
 43-130 5.14e-17

third galactose/rhamnose binding lectin domain found in Silurus asotus rhamnose-binding lectin (RBL) and similar proteins; RBL, also known as Silurus asotus (catfish) roe lectin (SAL), is a lectin that binds L-rhamnose. It also binds monosaccharides possessing steric similarity to the hydroxyl group orientation at C2 and C4 of the pyranose ring structure of L-rhamnose, such as L-mannose and L-lyxose. RBL does not require a Ca2+ ion or free thiol group for its agglutination activity. RBL contains three galactose/rhamnose-binding lectin domains. This model corresponds to the third one.


Pssm-ID: 438694 [Multi-domain]  Cd Length: 87  Bit Score: 77.47  E-value: 5.14e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   43 CEGYPIDLRCPGSdVIMIESANYGRTDDKICDADpfQMENINCYLPDAYKIMSQrCNNRTQCIVITGSDVFPDPCPGTYK 122
Cdd:cd22837      4 CENDSATITCSPE-TINVISAFYGRTDSTTCSHG--RPSTTNCSSDTLAYIRAL-CQGKQTCTLQASNSVFGDPCPGTYK 79


                   ....*...
gi 1880350455  123 YLEVQYEC 130
Cdd:cd22837     80 YLRITYSC 87
7tmB1_PTHR cd15265
parathyroid hormone receptors, member of the class B family of seven-transmembrane G ...
 849-1099 6.20e-17

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: 83.19  E-value: 6.20e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNL---------CINLFIAELIFLIGINMTE------------ 907
Cdd:cd15265      4 LYLIYTVGYSISLVSLTVAVFILGYFRRLHCTRNYIHMHLfvsfmlravSIFVKDAVLYSGSGLDELErpsmedlksive 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  908 -------PRIGCAIIAGILHFFFLASFSWMCLEGvqLYLMLVeVFESEYSRKKYFY---VSGYLFPAIVVGVSAAIDYSS 977
Cdd:cd15265     84 appvdksQYVGCKVAVTLFLYFLATNYYWILVEG--LYLHSL-IFMAFFSDKKYLWgftLIGWGFPAVFVIPWASVRATL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  978 YGTKnaCWLRVDNHFIWSFIGPVTFIIMLNLI-FLVITMYKMVKHSTTlkpDSSRLENIKSWVMGAFALLCLLGLtwsFG 1056
Cdd:cd15265    161 ADTR--CWDLSAGNYKWIYQVPILAAIVVNFIlFLNIVRVLATKLRET---NAGRCDTRQQYRKLAKSTLVLIPL---FG 232

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1880350455 1057 LFFI-------NEASI---VMAYLFTIFNAFQGMFIFIFHCLLQKKVRKEYSK 1099
Cdd:cd15265    233 VHYIvfmgmpyTEVGLlwqIRMHYELFFNSFQGFFVAIIYCFCNGEVQAEIKK 285
Gal_Rha_Lectin_LAT1 cd22839
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ...
 43-130 7.00e-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: 77.08  E-value: 7.00e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   43 CEGYPIDLRCPGSDVIMIESANYGRTDDKICDaDPFQME-NINCYLPDAYKIMSQRCNNRTQCIVITGSDVF-PDPCPGT 120
Cdd:cd22839      7 CEGDVANLSCPEGKYISIRLANYGRFSLGVCN-PSNNIDlSTTCQNDKTLPILQKSCDGKSECSFVVSNKFFfEDPCPGT 85

                           90
                   ....*....|
gi 1880350455  121 YKYLEVQYEC 130
Cdd:cd22839     86 PKYLEATYSC 95
GPS pfam01825
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
 790-834 7.77e-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: 75.42  E-value: 7.77e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1880350455  790 PNCSFWNYSErSMMGYWSTQGCKLLDTNKTHTTCSCSHLTNFAIL 834
Cdd:pfam01825    1 PQCVFWDFTN-STTGRWSTEGCTTVSLNDTHTVCSCNHLTSFAVL 44
7tmB1_NPR_B3_insect-like cd15262
insect neuropeptide receptor subgroup B3 and related proteins belong to subfamily B1 of ...
 857-1102 1.34e-16

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: 81.72  E-value: 1.34e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  857 ISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGIN---------------MTEPRIGCAIIAGILHF 921
Cdd:cd15262     12 LSVSVVTSLPAVFIFYSYKRLRITRVILHRNLLISIIIRNILVIISKVfvildaltssgddtvMNQNAVVCRLLSIFERA 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  922 FFLASFSWMCLEGVQLYLMLVEVFESEYSrKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKnaCWLRVDNHFIWSFIGPVT 1001
Cdd:cd15262     92 ARNAVFACMFVEGFYLHRLIVAVFAEKSS-IRFLYVIGAVLPLFPVIIWAIIRALHNDHS--CWVVDIEGVQWVLDTPRL 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1002 FIIMLNLIFLVITMYKMVkhsTTLKPDSSRlENIKSWVMGAFALLCLLGLTWSFGLFFI----NEASIVMAYLFTIFNAF 1077
Cdd:cd15262    169 FILLVNTVLLVDIIRVLV---TKLRNTEEN-SQTKSTTRATLFLVPLFGLHFVITAYRPstddCDWEDIYYYANYLIEGL 244

                          250       260
                   ....*....|....*....|....*
gi 1880350455 1078 QGMFIFIFHCLLQKKVRKEYSKCFR 1102
Cdd:cd15262    245 QGFLVAILFCYINKEVHYLIKNTYR 269
7tmB1_GlucagonR-like cd15929
glucagon receptor-like subfamily, member of the class B family of seven-transmembrane G ...
 849-1099 4.90e-16

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: 80.17  E-value: 4.90e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLI-------------------GINMTEPR 909
Cdd:cd15929      4 LQVMYTVGYSLSLAALVLALAILLGLRKLHCTRNYIHANLFASFILRALSVLVkdallprrysqkgdqdlwsTLLSNQAS 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  910 IGCAIIAGILHFFFLASFSWMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKnaCWLRVD 989
Cdd:cd15929     84 LGCRVAQVLMQYCVAANYYWLLVEGLYLHTLLVLAVFSERSIFRLYLLLGWGAPVLFVVPWGIVKYLYENTG--CWTRND 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  990 NHFIWSFI-GPVTFIIMLN-LIFLVITMYKMVKhsttLKPDSSRLENIKSWVMGA-FALLCLLGLTWSFGLFFINE---A 1063
Cdd:cd15929    162 NMAYWWIIrLPILLAILINfFIFVRILKILVSK----LRANQMCKTDYKFRLAKStLTLIPLLGVHEVVFAFVTDEqarG 237

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1880350455 1064 SIVMAYLFT--IFNAFQGMFIFIFHCLLQKKVRKEYSK 1099
Cdd:cd15929    238 TLRFIKLFFelFLSSFQGLLVAVLYCFANKEVQSELRK 275
7tmB1_VIP-R1 cd15269
vasoactive intestinal polypeptide (VIP) receptor 1, member of the class B family of ...
 855-1102 9.28e-16

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: 79.13  E-value: 9.28e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  855 VGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNL-------CINLFIAELIFLIGI---NMTEPRIGCAIIAGILHFFFL 924
Cdd:cd15269     10 IGHSLSLISLTAAMIILCLFRKLHCTRNYIHMHLfmsfilrAIAVFIKDAVLFESGeedHCSVASVGCKAAMVFFQYCIM 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  925 ASFSWMCLEGVQLYLMLVEVFeseYSRKKYFY---VSGYLFPAIVVGVSAAIdySSYGTKNACWLRVDNHFIWSFI-GPV 1000
Cdd:cd15269     90 ANFFWLLVEGLYLHTLLAVSF---FSERKYFWwyiLIGWGAPSVFITAWSVA--RIYFEDVGCWDTIIESLLWWIIkTPI 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1001 TFIIMLNLIFLVITMYKMVKHSTTlkPDSSRLENIKSWVMGAFALLC--LLGLTWSFGLFFINEASIVMAYLFT-IFNAF 1077
Cdd:cd15269    165 LVSILVNFILFICIIRILVQKLHS--PDIGRNESSQYSRLAKSTLLLipLFGIHYIMFAFFPDNFKAEVKLVFElILGSF 242

                          250       260
                   ....*....|....*....|....*
gi 1880350455 1078 QGMFIFIFHCLLQKKVRKEYSKCFR 1102
Cdd:cd15269    243 QGFVVAVLYCFLNGEVQAELKRKWR 267
Gal_Rha_Lectin_LAT2 cd22840
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ...
 41-130 1.23e-15

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: 73.60  E-value: 1.23e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   41 LSCEGYPIDLRCPGSDVIMIESANYGRTDD-KICDaDPFQMENINCYLPDAYKIMSQRCNNRTQCIV-ITGSDVFPDPCP 118
Cdd:cd22840      5 VACEGDPFEISCPSGQRIKVDYASYGAIGTrSTCG-DSVSPAGETCSAPNSLQTMRQRCQGRQSCEIrVLNSLFPNDPCP 83

                           90
                   ....*....|...
gi 1880350455  119 GTY-KYLEVQYEC 130
Cdd:cd22840     84 GTSkKYLEYRYRC 96
Gal_Rha_Lectin_nemgal cd22838
galactose/rhamnose binding lectin domain found in Hydra vulgaris nematogalectin and similar ...
 43-132 1.88e-15

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: 73.46  E-value: 1.88e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   43 CEGYPIDLRCPGSDVIMIESANYGRTDDKICDADPFQME-NINCYL--PDAYKIMSQRCNNRTQCIVITGSDVFPDP-CP 118
Cdd:cd22838      7 CEGEKLWLQCPQYELIKIKSAFWGRDDKKTCPHPPPGLPsNKMCETdeENVKKKVNDQCQGEQACEVVASNIFFDDTiCP 86

                           90
                   ....*....|....
gi 1880350455  119 GTYKYLEVQYECVP 132
Cdd:cd22838     87 DVYKYLKVKYECIP 100
7tmB1_PTH1R cd15984
parathyroid hormone 1 receptor, member of the class B family of seven-transmembrane G ...
 848-1099 2.96e-15

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: 78.07  E-value: 2.96e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  848 QLDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNL-------CINLFIAELIFLIGINMTEPR----------- 909
Cdd:cd15984      3 RLYLIYTVGYSISLGSLTVAVLILGYFRRLHCTRNYIHMHLflsfmlrAVSIFVKDAVLYSGSALEEMEriteedlksit 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  910 ----------IGCAIIAGILHFFFLASFSWMCLEGVQLYLMlveVFESEYSRKKY---FYVSGYLFPAIVVGVSAAIDYS 976
Cdd:cd15984     83 eappadkaqfVGCKVAVTFFLYFLATNYYWILVEGLYLHSL---IFMAFFSEKKYlwgFTLFGWGLPAVFVTIWASVRAT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  977 SYGTKnaCWLRVDNHFIWSFIGPVTFIIMLNLIfLVITMYKMVkhSTTLK-PDSSRLENIKSWVMGAFALLCLLGLtwsF 1055
Cdd:cd15984    160 LADTG--CWDLSAGNLKWIIQVPILAAIVVNFI-LFINIVRVL--ATKLReTNAGRCDTRQQYRKLLKSTLVLMPL---F 231

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1880350455 1056 GLFFIneasIVMAYLFT---------------IFNAFQGMFIFIFHCLLQKKVRKEYSK 1099
Cdd:cd15984    232 GVHYI----VFMAMPYTevsgilwqvqmhyemLFNSFQGFFVAIIYCFCNGEVQAEIKK 286
7tmB1_VIP-R2 cd15986
vasoactive intestinal polypeptide (VIP) receptor 2, member of the class B family of ...
 852-1102 3.30e-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: 77.54  E-value: 3.30e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  852 ITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLI----------GINMTEPR--IGCAIIAGIL 919
Cdd:cd15986      7 IYTLGHSVSLIALTTGSTILCLFRKLHCTRNYIHLNLFFSFILRAISVLVkddilysssnTEHCTVPPslIGCKVSLVIL 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  920 HFFFLASFSWMCLEGVQLYLMLVEVFESEYSRKKYFYVsGYLFPAIVVGvsAAIDYSSYGTKNACWLRVDNHFIWSFIG- 998
Cdd:cd15986     87 QYCIMANFYWLLVEGLYLHTLLVVIFSENRHFIVYLLI-GWGIPTVFII--AWIVARIYLEDTGCWDTNDHSVPWWVIRi 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  999 PVTFIIMLNLIFLVITMYKMVKHSTTLKPDSSRLENIKSWVMGAFALLCLLGLTWSFGLFFINEASIVMAYLFTI-FNAF 1077
Cdd:cd15986    164 PIIISIILNFILFISIIRILLQKLRSPDVGGNDQSQYKRLAKSTLLLIPLFGVHYIVFVYFPDSSSSNYQIFFELcLGSF 243

                          250       260
                   ....*....|....*....|....*
gi 1880350455 1078 QGMFIFIFHCLLQKKVRKEYSKCFR 1102
Cdd:cd15986    244 QGLVVAILYCFLNSEVQGELKRKWR 268
7tmB1_PTH2R cd15982
parathyroid hormone 2 receptor, member of the class B family of seven-transmembrane G ...
 848-1099 4.51e-15

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: 77.67  E-value: 4.51e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  848 QLDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFI-AELIFL--------IGIN------MTEPR--- 909
Cdd:cd15982      3 RLYIMYTVGYSISFSSLAVAIFIIGYFRRLHCTRNYIHMHLFVSFMLrAASIFVkdkvvhthIGVKeldavlMNDFQnav 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  910 ----------IGCAIIAGILHFFFLASFSWMCLEGVQLYLMLVEVFeseYSRKKY---FYVSGYLFPAIVVGVSAAIDYS 976
Cdd:cd15982     83 dappvdksqyVGCKIAVVMFIYFLATNYYWILVEGLYLHSLIFVAF---FSDTKYlwgFTLIGWGFPAVFVAAWAVVRAT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  977 SYGTKnaCWLRVDNHFIWSFIGPVTFIIMLNLIFLVITMykMVKHSTTLKPDSSRLENIKSWVMGAFALLCLLgltWSFG 1056
Cdd:cd15982    160 LADAR--CWELSAGDIKWIYQAPILAAIGLNFILFLNTV--RVLATKIWETNAVGYDTRKQYRKLAKSTLVLV---LVFG 232

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1880350455 1057 LFFIneASIVMAYLFT------------IFNAFQGMFIFIFHCLLQKKVRKEYSK 1099
Cdd:cd15982    233 VHYI--VFVCLPHTFTglgweirmhcelFFNSFQGFFVSIIYCYCNGEVQTEIKK 285
7tmB2_GPR124 cd15998
G protein-coupled receptor 124, member of the class B2 family of seven-transmembrane G ...
 861-1100 1.06e-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: 73.07  E-value: 1.06e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  861 LVCLAISIFTFCF-FRGLQSDRNTIHK--NLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLASFSWMCLEGVQL 937
Cdd:cd15998     16 LLCLFSTIITYILnHSSIHVSRKGWHMllNLCFHIAMTSAVFAGGITLTNYQMVCQAVGITLHYSSLSTLLWMGVKARVL 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  938 YLMLV---------EVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKNA-CWLrvdnhfIW-----SFIGPVTF 1002
Cdd:cd15998     96 HKELTwrapppqegDPALPTPRPMLRFYLIAGGIPLIICGITAAVNIHNYRDHSPyCWL------VWrpslgAFYIPVAL 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1003 IIMLNLIFLVITMYKMVKHSTtlkpDSSRLENIKSWvMGAFALLCLLGLT-WSFGLFFINE---ASIVMAYLFTIFNAFQ 1078
Cdd:cd15998    170 ILLVTWIYFLCAGLHLRGPSA----DGDSVYSPGVQ-LGALVTTHFLYLAmWACGALAVSQrwlPRVVCSCLYGVAASAL 244

                          250       260
                   ....*....|....*....|..
gi 1880350455 1079 GMFIFIFHCLLQKKVRKEYSKC 1100
Cdd:cd15998    245 GLFVFTHHCARRRDVRASWRAC 266
7tmB1_GHRHR2 cd15271
growth-hormone-releasing hormone receptor type 2, member of the class B family of ...
 855-1102 1.06e-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: 1.06e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  855 VGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNL-------CINLFIAELIFLIGINM---TEPRIGCAIIAGILHFFFL 924
Cdd:cd15271     10 VGYGTSLTSLITAVLIFCTFRKLHCTRNYIHINLfvsfilrALAVFIKDAVLFADESVdhcTMSTVACKAAVTFFQFCVL 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  925 ASFSWMCLEGVQLYLMLVEVFESEysrKKYFY---VSGYLFPAIVVGV--SAAIDYSSYGtknaCWLRVDNHFIWSFIGP 999
Cdd:cd15271     90 ANFFWLLVEGMYLQTLLLLTFTSD---RKYFWwyiLIGWGAPSVTVTVwvLTRLQYDNRG----CWDDLESRIWWIIKTP 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1000 VTFIIMLN-LIFLVITMYKMVKHSTtlkPDSSRleNIKSWVM----GAFALLCLLGLTWS-FGLFFINEASIVMAYLFTI 1073
Cdd:cd15271    163 ILLSVFVNfLIFINVIRILVQKLKS---PDVGG--NDTSHYMrlakSTLLLIPLFGVHYVvFAFFPEHVGVEARLYFELV 237

                          250       260
                   ....*....|....*....|....*....
gi 1880350455 1074 FNAFQGMFIFIFHCLLQKKVRKEYSKCFR 1102
Cdd:cd15271    238 LGSFQGFIVALLYCFLNGEVQAEIKKRLG 266
7tmB1_PTH3R cd15983
parathyroid hormone 3 receptor, member of the class B family of seven-transmembrane G ...
 848-1099 1.15e-13

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: 73.42  E-value: 1.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  848 QLDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNL-------CINLFIAELIFLIGINMTE------------- 907
Cdd:cd15983      3 RLHLMYTIGYSISLAALLVAVCILCYFKRLHCTRNYIHIHLfasficrAGSIFVKDAVLYSGTNEGEaldekiefglspg 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  908 ---PRIGCAIIAGILHFFFLASFSWMCLEGVQLYLMLVEVFESEysrKKYFY---VSGYLFPAIVVGVSAAIDYSSYGTK 981
Cdd:cd15983     83 trlQWVGCKVTVTLFLYFLATNHYWILVEGLYLHSLIFMAFLSD---KNYLWaltIIGWGLPAVFVSVWASVRVSLADTQ 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  982 naCWLRVDNHFIWSFIGPVTFIIMLNLI-FLVITMYKMVK--HSTTLKPDSSrlENIKSWVMGAFALLCLLGLtwSFGLF 1058
Cdd:cd15983    160 --CWDLSAGNLKWIYQVPILAAILVNFFlFLNIVRVLASKlwETNTGKLDPR--QQYRKLLKSTLVLMPLFGV--HYVLF 233

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1880350455 1059 FINEASIVMAYLFTI-------FNAFQGMFIFIFHCLLQKKVRKEYSK 1099
Cdd:cd15983    234 MAMPYTDVTGLLWQIqmhyemlFNSSQGFFVAFIYCFCNGEVQAEIKK 281
7tmB1_GHRHR cd15270
growth-hormone-releasing hormone receptor, member of the class B family of seven-transmembrane ...
 851-1099 1.91e-13

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: 72.14  E-value: 1.91e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  851 IITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNL-------CINLFIAELIFLIGINM---TEPRIGCAIIAGILH 920
Cdd:cd15270      6 IIYTVGYSISIVSLCVAVAILVAFRRLHCPRNYIHIQLfftfilkAIAVFIKDAALFQEDDTdhcSMSTVLCKVSVVFCH 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  921 FFFLASFSWMCLEGVQLYLMLVEVFEseySRKKYFY---VSGYLFPAIVVGvsAAIDYSSYGTKNACW-LRVDNHFIWSF 996
Cdd:cd15270     86 YCVMTNFFWLLVEAVYLNCLLASSFP---RGKRYFWwlvLLGWGLPTLCTG--TWILCKLYFEDTECWdINNDSPYWWII 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  997 IGPVTFIIMLN-LIFLVITMYKMVKhsttLKPDSSRLEN-IKSWVMGAFALLC--LLGLTWSFGLFFINEASI-VMAYLF 1071
Cdd:cd15270    161 KGPIVISVGVNfLLFLNIIRILLKK----LDPRQINFNNsAQYRRLSKSTLLLipLFGTHYIIFNFLPDYAGLgIRLYLE 236

                          250       260
                   ....*....|....*....|....*...
gi 1880350455 1072 TIFNAFQGMFIFIFHCLLQKKVRKEYSK 1099
Cdd:cd15270    237 LCLGSFQGFIVAVLYCFLNQEVQTEISR 264
7tmB1_GlucagonR-like_1 cd15985
uncharacterized group of glucagon receptor-like proteins, member of the class B family of ...
 855-1102 4.04e-13

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: 71.50  E-value: 4.04e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  855 VGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEPR--------------------IGCAI 914
Cdd:cd15985     10 VGYTLSLLTLVSALLILTSIRKLHCTRNYIHANLFASFILRAVSVIVKDTLLERRwgreimrvadwgellshkaaIGCRM 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  915 IAGILHFFFLASFSWMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKnaCWLRVDNHFIW 994
Cdd:cd15985     90 AQVVMQYCILANHYWFFVEAVYLYKLLIGAVFSEKNYYLLYLYLGWGTPVLFVVPWMLAKYLKENKE--CWALNENMAYW 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  995 SFIG-PVTFIIMLNL-IFLVITMYKMVKhsttLKPDSSRLENIKSWVMGA-FALLCLLGLTWSFGLFFINEASI-VMAYL 1070
Cdd:cd15985    168 WIIRiPILLASLINLlIFMRILKVILSK----LRANQKGYADYKLRLAKAtLTLIPLFGIHEVVFIFATDEQTTgILRYI 243

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1880350455 1071 ---FTIF-NAFQGMFIFIFHCLLQKKVRKEYSKCFR 1102
Cdd:cd15985    244 kvfFTLFlNSFQGFLVAVLYCFANKEVKSELLKKWR 279
7tmB1_GLP1R cd15268
glucagon-like peptide-1 receptor, member of the class B family of seven-transmembrane G ...
 849-1099 6.12e-12

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: 68.05  E-value: 6.12e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLI-------------------GINMTEPR 909
Cdd:cd15268      4 LYIIYTVGYALSFSALVIASAILLGFRHLHCTRNYIHLNLFASFILRALSVFIkdaalkwmystaaqqhqwdGLLSYQDS 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  910 IGCAIIAGILHFFFLASFSWMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYssYGTKNACWLRVD 989
Cdd:cd15268     84 LSCRLVFLLMQYCVAANYYWLLVEGVYLYTLLAFSVFSEQRIFRLYLSIGWGVPLLFVIPWGIVKY--LYEDEGCWTRNS 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  990 NHFIWSFIG-PVTFIIMLN-LIFLVITMYKMVKHSTTLKPDSSRLENIKSWVMGAFALLCLLGLTWSFGLFFINEASIVM 1067
Cdd:cd15268    162 NMNYWLIIRlPILFAIGVNfLIFIRVICIVVSKLKANLMCKTDIKCRLAKSTLTLIPLLGTHEVIFAFVMDEHARGTLRF 241

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1880350455 1068 AYLFT--IFNAFQGMFIFIFHCLLQKKVRKEYSK 1099
Cdd:cd15268    242 VKLFTelSFTSFQGLMVAILYCFVNNEVQMEFRK 275
7tmB2_GPR125 cd15999
G protein-coupled receptor 125, member of the class B2 family of seven-transmembrane G ...
 859-1107 7.23e-11

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: 65.27  E-value: 7.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  859 VSLVCLAISIFTFCFFRGL-QSDRNTIHK--NLCINLFIAELIFLIGINMTEPRIGCAIIAGILHFFFLASFSWMCLEGV 935
Cdd:cd15999     14 VLLLCLLTIIVSYIYHHSLvRISRKSWHMlvNLCFHIFLTCAVFVGGINQTRNASVCQAVGIILHYSTLATVLWVGVTAR 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  936 QLYLMLVEvfeseySRKKY---------------FYVSGYLFPAIVVGVSAAIDYSSYGTK-NA--CWLRVDNHfIWSFI 997
Cdd:cd15999     94 NIYKQVTR------KAKRCqdpdeppppprpmlrFYLIGGGIPIIVCGITAAANIKNYGSRpNApyCWMAWEPS-LGAFY 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  998 GPVTFIIMLNLIFLVITMYKMVKH-------------------------------STTLKPD---SSRLENIKSW---VM 1040
Cdd:cd15999    167 GPAGFIIFVNCMYFLSIFIQLKRHperkyelkepteeqqrlaasehgelnhqdsgSSSASCSlvsTSALENEHSFqaqLL 246

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1041 GAFALLCLLGLTWSFGLFFINEA---SIVMAYLFTIFNAFQGMFIFIFHCLLQKKVRKEYSkcfrhTYCC 1107
Cdd:cd15999    247 GASLALFLYVALWIFGALAVSLYypmDLVFSCLFGATCLSLGAFLVVHHCVNREDVRRAWI-----ATCC 311
7tmB1_GCGR cd15267
glucagon receptor, member of the class B family of seven-transmembrane G protein-coupled ...
 851-1099 8.96e-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: 64.46  E-value: 8.96e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  851 IITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNLCINLFIAELIFLIGINMTEPR-------------------IG 911
Cdd:cd15267      8 VMYTVGYSLSLGALLLALAILGGFSKLHCMRNAIHMNLFASFILKASSVLVIDGLLRTRysqkieddlsstwlsdeavAG 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  912 CAIIAGILHFFFLASFSWMCLEGVQLYLMLVEVFESEYSRKKYFYVSGYLFPAIVVGVSAAIDYSSYGTKnaCWLRVDNH 991
Cdd:cd15267     88 CRVAAVFMQYGIVANYCWLLVEGIYLHNLLVLAVFPERSYFSLYLCIGWGAPALFVVPWVVVKCLYENVQ--CWTSNDNM 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  992 FIWSFI-GPVTFIIMLNLIFLV----ITMYKMVKHSTTLKPDSSRLEniKSwvmgAFALLCLLGLTWSFGLFFINE---A 1063
Cdd:cd15267    166 GFWWILrFPVFLAILINFFIFVriiqILVSKLRARQMHYTDYKFRLA--KS----TLTLIPLLGIHEVVFAFVTDEhaqG 239

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1880350455 1064 SIVMAYLF--TIFNAFQGMFIFIFHCLLQKKVRKEYSK 1099
Cdd:cd15267    240 TLRSAKLFfdLFLSSFQGLLVAVLYCFLNKEVQSELRR 277
Gal_Rha_Lectin_BGal cd22842
galactose/rhamnose binding lectin domain found in plant beta-galactosidases and similar ...
 43-130 8.19e-10

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: 56.91  E-value: 8.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   43 CEGYP---IDLRCPGSDVI-MIESANYGrTDDKICDAdpFQMENinCYLPDAYKIMSQRCNNRTQC-IVITGSDVFPDPC 117
Cdd:cd22842      4 NEGGPgstLTLSCPAGQVIsSIDFASYG-TPTGTCGS--FSKGS--CHAPNSLSVVEKACLGKNSCsIPASNSVFFGDPC 78

                           90
                   ....*....|...
gi 1880350455  118 PGTYKYLEVQYEC 130
Cdd:cd22842     79 PGTTKRLAVQATC 91
HRM pfam02793
Hormone receptor domain; This extracellular domain contains four conserved cysteines that ...
 473-529 1.07e-09

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


Pssm-ID: 397086  Cd Length: 64  Bit Score: 55.84  E-value: 1.07e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1880350455  473 ERFCEATEKRDITWPQTQRGMLVERPCPKGT-----RGTASYLC-STGAWHPKGP-DLSNCTSH 529
Cdd:pfam02793    1 GLGCPRTWDGILCWPRTPAGETVEVPCPDYFsgfdpRGNASRNCtEDGTWSEHPPsNYSNCTSN 64
Gal_Rha_Lectin_PKD1L2 cd22831
galactose binding lectin domain found in polycystic kidney disease protein 1-like 2 ...
 39-130 1.41e-08

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: 53.89  E-value: 1.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   39 RELSCEGYPIDLRCPGSDVIMIESANYGRTDDKICDAD---PFQMENINCYLPDAYKIMSQRCNNRTQCIVITGSDVFPD 115
Cdd:cd22831      2 RSLACEDYNATLQCGSGQVIEIDDSFYGRNTPHYCRSEnpsPPTDSQERCSWVDVRDLVAAQCHGLQVCQIPADPSSFGE 81

                           90
                   ....*....|....*
gi 1880350455  116 PCPGTYKYLEVQYEC 130
Cdd:cd22831     82 PCPELGSYLSVEYHC 96
Gal_Rha_Lectin-like_P113 cd22843
galactose/rhamnose binding lectin-like domain found in Plasmodium falciparum P113 and similar ...
 41-130 2.40e-08

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: 52.83  E-value: 2.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455   41 LSCEGYPIDLRCPGSDVIMIESANYGRTDDKICdadpFQMENINCYLpDAYKIMSQRCNNRTQCiVITGSDV-FPDPCPG 119
Cdd:cd22843      5 FVCFGQEVTIHCPGDGNISIKSATYGYNNSNVC----IYCNSFNCDK-DITSPVNKKCCGKNTC-VLTVSDIlEGNPCGI 78

                           90
                   ....*....|.
gi 1880350455  120 TYKYLEVQYEC 130
Cdd:cd22843     79 GNSYIRVVYTC 89
7tmE_cAMP_R_Slime_mold cd14940
slime mold cyclic AMP receptor, member of the class E family of seven-transmembrane G ...
 849-1090 5.02e-05

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: 46.58  E-value: 5.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  849 LDIITQVGISVSLVCLAISIFTFCFFRGLqsdRNTIHK---NLCINLFIAELIFLIGINMTEPR---IGCAIIAGILHFF 922
Cdd:cd14940      2 LYAILLFADFSSIIGCLFVLVGFWLLKLL---RNHITRvisCFCLTSLLKDIIYTMLTLTQSARpdgFLCYLYAIVITYG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  923 FLASFSWMCLEGVQLYLMLV-EVFESEYSRKKYFYVSgYLFPAIVVGVSAAIDYSSYgTKNACWLRVDN--HFIWSFIGP 999
Cdd:cd14940     79 SLSCWLWTLCLAISIYLLIVkREPEPEKFEKYYHFVC-WGLPLISTIIMLIKHHYGP-VGNWCWIGNQYtgYRFGLFYGP 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455 1000 VTFIIMLNLIFLVITMYKMVKHSTTLKPDSSRL--ENIKSWVMGAFALLcllgLTWSFGLffINEasivmaylftIFNAF 1077
Cdd:cd14940    157 FFIIFGISAVLVGLTSHYTYQVIHNWVSDNKDLhkTYQFKLVNYIIVFL----LCWIFAV--INR----------IQNAL 220

                          250
                   ....*....|....*.
gi 1880350455 1078 qGMFIF---IFHCLLQ 1090
Cdd:cd14940    221 -NPFPFalnLLHTYLS 235
7tm_GPCRs cd14964
seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary ...
 851-1089 2.77e-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: 41.26  E-value: 2.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  851 IITQVGISVSLVCLAISIFTFCFFRGLQSDRNTIHKNL-CINLFIAELIFLI------GINMTEPRIGCAIIAGILHFFF 923
Cdd:cd14964      3 IILSLLTCLGLLGNLLVLLSLVRLRKRPRSTRLLLASLaACDLLASLVVLVLffllglTEASSRPQALCYLIYLLWYGAN 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  924 LASFSWMCLEGVQLYLMLVEVF---ESEYSRKKYFYVSGY--------LFPAIVVGVSAAIDYSSYGTKNACWLRVDN-- 990
Cdd:cd14964     83 LASIWTTLVLTYHRYFALCGPLkytRLSSPGKTRVIILGCwgvslllsIPPLVGKGAIPRYNTLTGSCYLICTTIYLTwg 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880350455  991 HFIWSFIGPVTFIIMLNL-IFLVITMYKMVKHSTTLKPDSSRLENIKSWV--MGAFALLCLLgltwsFGLFFINEAS--- 1064
Cdd:cd14964    163 FLLVSFLLPLVAFLVIFSrIVLRLRRRVRAIRSAASLNTDKNLKATKSLLilVITFLLCWLP-----FSIVFILHALvaa 237

                          250       260
                   ....*....|....*....|....*
gi 1880350455 1065 IVMAYLFTIFnafqGMFIFIFHCLL 1089
Cdd:cd14964    238 GQGLNLLSIL----ANLLAVLASTL 258
 
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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