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Conserved domains on  [gi|530376257|ref|XP_005248194|]
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adhesion G protein-coupled receptor A3 isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
7tm_GPCRs super family cl28897
seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary ...
756-827 1.06e-32

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 cd15999:

Pssm-ID: 475119  Cd Length: 312  Bit Score: 128.83  E-value: 1.06e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530376257 756 ASLLHPVVYTTAIILLLCLLAVIVSYIYHHSLIRISLKSWHMLVNLCFHIFLTCVVFVGGITQTRNASICQA 827
Cdd:cd15999    1 ADLLHPVVYATAVVLLLCLLTIIVSYIYHHSLVRISRKSWHMLVNLCFHIFLTCAVFVGGINQTRNASVCQA 72
LRR_8 pfam13855
Leucine rich repeat;
85-141 7.00e-18

Leucine rich repeat;


:

Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 78.34  E-value: 7.00e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530376257   85 TLILSNNKISELKNGSFSGLSLLERLDLRNNLISSIDPGAFWGLSSLKRLDLTNNRI 141
Cdd:pfam13855   5 SLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
76-190 1.85e-13

Leucine-rich repeat (LRR) protein [Transcription];


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 73.43  E-value: 1.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257  76 PDTLPNRT--VTLILSNNKISELkNGSFSGLSLLERLDLRNNLISSIDpgAFWGLSSLKRLDLTNNRIGCLNADIfrGLT 153
Cdd:COG4886  198 PEPLGNLTnlEELDLSGNQLTDL-PEPLANLTNLETLDLSNNQLTDLP--ELGNLTNLEELDLSNNQLTDLPPLA--NLT 272
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 530376257 154 NLVRLNLSGNLFSSLSQGTFDYLASLRSLEFQTEYLL 190
Cdd:COG4886  273 NLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLN 309
GPS pfam01825
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
704-743 3.81e-06

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: 44.22  E-value: 3.81e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 530376257  704 WDFDLlNGQGGWKSDGCHILYSDENITTIQCYSLSNYAVL 743
Cdd:pfam01825   6 WDFTN-STTGRWSTEGCTTVSLNDTHTVCSCNHLTSFAVL 44
HRM pfam02793
Hormone receptor domain; This extracellular domain contains four conserved cysteines that ...
363-416 5.58e-05

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: 41.59  E-value: 5.58e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530376257  363 WPRTLAGITAYLQCTRNTHGSgiypgnpQDERKAWRRCDRGGFWAD---DDYSRCQY 416
Cdd:pfam02793  14 WPRTPAGETVEVPCPDYFSGF-------DPRGNASRNCTEDGTWSEhppSNYSNCTS 63
LRRCT smart00082
Leucine rich repeat C-terminal domain;
189-223 6.55e-05

Leucine rich repeat C-terminal domain;


:

Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 41.26  E-value: 6.55e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 530376257   189 LLCDCNILWMHRWVKEKNITVR--DTRCVYPKSLQAQ 223
Cdd:smart00082   3 FICDCELRWLLRWLQANEHLQDpvDLRCASPSSLRGP 39
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
249-341 2.41e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


:

Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 37.87  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257   249 SHRQVVFEGDSLPFQCMASYiDQDMQVLWYQDGriVETDESQGIFVEKNMIHNCSLiasalTISNIQAGSTGNWGCHVQT 328
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASG-SPPPEVTWYKQG--GKLLAESGRFSVSRSGSTSTL-----TISNVTPEDSGTYTCAATN 72
                           90
                   ....*....|...
gi 530376257   329 KRGNNTRTVDIVV 341
Cdd:smart00410  73 SSGSASSGTTLTV 85
 
Name Accession Description Interval E-value
7tmB2_GPR125 cd15999
G protein-coupled receptor 125, member of the class B2 family of seven-transmembrane G ...
756-827 1.06e-32

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: 128.83  E-value: 1.06e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530376257 756 ASLLHPVVYTTAIILLLCLLAVIVSYIYHHSLIRISLKSWHMLVNLCFHIFLTCVVFVGGITQTRNASICQA 827
Cdd:cd15999    1 ADLLHPVVYATAVVLLLCLLTIIVSYIYHHSLVRISRKSWHMLVNLCFHIFLTCAVFVGGINQTRNASVCQA 72
LRR_8 pfam13855
Leucine rich repeat;
85-141 7.00e-18

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 78.34  E-value: 7.00e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530376257   85 TLILSNNKISELKNGSFSGLSLLERLDLRNNLISSIDPGAFWGLSSLKRLDLTNNRI 141
Cdd:pfam13855   5 SLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
85-183 8.84e-17

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 83.44  E-value: 8.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257  85 TLILSNNKISELKNgSFSGLSLLERLDLRNNLISSIdPGAFWGLSSLKRLDLTNNRIGCLNADIFrGLTNLVRLNLSGNL 164
Cdd:COG4886  140 ELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDL-PEELGNLTNLKELDLSNNQITDLPEPLG-NLTNLEELDLSGNQ 216
                         90
                 ....*....|....*....
gi 530376257 165 FSSLSQGtfdyLASLRSLE 183
Cdd:COG4886  217 LTDLPEP----LANLTNLE 231
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
76-190 1.85e-13

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 73.43  E-value: 1.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257  76 PDTLPNRT--VTLILSNNKISELkNGSFSGLSLLERLDLRNNLISSIDpgAFWGLSSLKRLDLTNNRIGCLNADIfrGLT 153
Cdd:COG4886  198 PEPLGNLTnlEELDLSGNQLTDL-PEPLANLTNLETLDLSNNQLTDLP--ELGNLTNLEELDLSNNQLTDLPPLA--NLT 272
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 530376257 154 NLVRLNLSGNLFSSLSQGTFDYLASLRSLEFQTEYLL 190
Cdd:COG4886  273 NLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLN 309
LRR_8 pfam13855
Leucine rich repeat;
129-182 3.94e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 61.77  E-value: 3.94e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530376257  129 SSLKRLDLTNNRIGCLNADIFRGLTNLVRLNLSGNLFSSLSQGTFDYLASLRSL 182
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYL 54
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
77-183 6.78e-12

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 65.96  E-value: 6.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257  77 DTLPNRTvTLILSNNKISELKNgsFSGLSLLERLDLRNNLISSI---------------------------DPGAFWGLS 129
Cdd:cd21340   43 EFLTNLT-HLYLQNNQIEKIEN--LENLVNLKKLYLGGNRISVVeglenltnleelhienqrlppgekltfDPRSLAALS 119
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530376257 130 -SLKRLDLTNNRIGCLNAdiFRGLTNLVRLNLSGNLFSSLSQgTFDYLASLRSLE 183
Cdd:cd21340  120 nSLRVLNISGNNIDSLEP--LAPLRNLEQLDASNNQISDLEE-LLDLLSSWPSLR 171
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
135-236 3.61e-09

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 60.87  E-value: 3.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257   135 DLTNNRIGCLNADIFRGLTNLVRLNLSGNLFSslsqgtfdylaslrslefqteyllCDCNILWMHRWVKEKNITVRD--- 211
Cdd:TIGR00864    1 DISNNKISTIEEGICANLCNLSEIDLSGNPFE------------------------CDCGLARLPRWAEEKGVKVRQpea 56
                           90       100
                   ....*....|....*....|....*
gi 530376257   212 TRCVYPKSLQAQPVTGVKQELLTCD 236
Cdd:TIGR00864   57 ALCAGPGALAGQPLLGIPLLDSGCD 81
GPS pfam01825
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
704-743 3.81e-06

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: 44.22  E-value: 3.81e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 530376257  704 WDFDLlNGQGGWKSDGCHILYSDENITTIQCYSLSNYAVL 743
Cdd:pfam01825   6 WDFTN-STTGRWSTEGCTTVSLNDTHTVCSCNHLTSFAVL 44
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
703-746 1.79e-05

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: 42.76  E-value: 1.79e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 530376257   703 RWDFDllngQGGWKSDGCHILYSDENITTIQCYSLSNYAVLMDL 746
Cdd:smart00303   7 FWDES----SGEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDV 46
HRM pfam02793
Hormone receptor domain; This extracellular domain contains four conserved cysteines that ...
363-416 5.58e-05

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: 41.59  E-value: 5.58e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530376257  363 WPRTLAGITAYLQCTRNTHGSgiypgnpQDERKAWRRCDRGGFWAD---DDYSRCQY 416
Cdd:pfam02793  14 WPRTPAGETVEVPCPDYFSGF-------DPRGNASRNCTEDGTWSEhppSNYSNCTS 63
LRRCT smart00082
Leucine rich repeat C-terminal domain;
189-223 6.55e-05

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 41.26  E-value: 6.55e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 530376257   189 LLCDCNILWMHRWVKEKNITVR--DTRCVYPKSLQAQ 223
Cdd:smart00082   3 FICDCELRWLLRWLQANEHLQDpvDLRCASPSSLRGP 39
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
81-186 1.45e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 45.61  E-value: 1.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257  81 NRTVTLILSNNKISELKNGSFSGLSLLERLDLRNNLISSIDPGA-FWGLSSLKRLDLTNNRigcLNADIFRG-LTNLVRL 158
Cdd:PLN00113  69 SRVVSIDLSGKNISGKISSAIFRLPYIQTINLSNNQLSGPIPDDiFTTSSSLRYLNLSNNN---FTGSIPRGsIPNLETL 145
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 530376257 159 NLSGNLFSS---LSQGTFD------------------YLASLRSLEFQT 186
Cdd:PLN00113 146 DLSNNMLSGeipNDIGSFSslkvldlggnvlvgkipnSLTNLTSLEFLT 194
HormR smart00008
Domain present in hormone receptors;
363-416 3.84e-04

Domain present in hormone receptors;


Pssm-ID: 214468  Cd Length: 70  Bit Score: 39.42  E-value: 3.84e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 530376257   363 WPRTLAGITAYLQCTRNThgSGIYPGNpqderKAWRRCDRGGFWA--DDDYSRCQY 416
Cdd:smart00008  15 WPQTPAGQLVEVPCPKYF--SGFSYKT-----GASRNCTENGGWSppFPNYSNCTS 63
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
249-341 2.41e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 37.87  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257   249 SHRQVVFEGDSLPFQCMASYiDQDMQVLWYQDGriVETDESQGIFVEKNMIHNCSLiasalTISNIQAGSTGNWGCHVQT 328
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASG-SPPPEVTWYKQG--GKLLAESGRFSVSRSGSTSTL-----TISNVTPEDSGTYTCAATN 72
                           90
                   ....*....|...
gi 530376257   329 KRGNNTRTVDIVV 341
Cdd:smart00410  73 SSGSASSGTTLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
242-326 2.42e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 37.55  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257  242 PSFYMTPSHrQVVFEGDSLPFQCMASYIDQDmQVLWYQDGRIVETDESQGIFVEKNMihncsliaSALTISNIQAGSTGN 321
Cdd:pfam13927   2 PVITVSPSS-VTVREGETVTLTCEATGSPPP-TITWYKNGEPISSGSTRSRSLSGSN--------STLTISNVTRSDAGT 71

                  ....*
gi 530376257  322 WGCHV 326
Cdd:pfam13927  72 YTCVA 76
LRR smart00370
Leucine-rich repeats, outliers;
104-127 2.56e-03

Leucine-rich repeats, outliers;


Pssm-ID: 197688 [Multi-domain]  Cd Length: 24  Bit Score: 35.79  E-value: 2.56e-03
                           10        20
                   ....*....|....*....|....
gi 530376257   104 LSLLERLDLRNNLISSIDPGAFWG 127
Cdd:smart00370   1 LPNLRELDLSNNQLSSLPPGAFQG 24
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
62-183 5.90e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 40.22  E-value: 5.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257  62 KVVCSSLELAQVLPPDTLPNRTVTLI-LSNNKIS-ELKNGsFSGLSLLERLDLR-NNLISSIDPGAfWGLSSLKRLDLTN 138
Cdd:PLN00113 384 KLILFSNSLEGEIPKSLGACRSLRRVrLQDNSFSgELPSE-FTKLPLVYFLDISnNNLQGRINSRK-WDMPSLQMLSLAR 461
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 530376257 139 NRIGCLNADIFRGlTNLVRLNLSGNLFSSLSQGTFDYLASLRSLE 183
Cdd:PLN00113 462 NKFFGGLPDSFGS-KRLENLDLSRNQFSGAVPRKLGSLSELMQLK 505
LRR smart00370
Leucine-rich repeats, outliers;
152-174 8.08e-03

Leucine-rich repeats, outliers;


Pssm-ID: 197688 [Multi-domain]  Cd Length: 24  Bit Score: 34.63  E-value: 8.08e-03
                           10        20
                   ....*....|....*....|...
gi 530376257   152 LTNLVRLNLSGNLFSSLSQGTFD 174
Cdd:smart00370   1 LPNLRELDLSNNQLSSLPPGAFQ 23
 
Name Accession Description Interval E-value
7tmB2_GPR125 cd15999
G protein-coupled receptor 125, member of the class B2 family of seven-transmembrane G ...
756-827 1.06e-32

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: 128.83  E-value: 1.06e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530376257 756 ASLLHPVVYTTAIILLLCLLAVIVSYIYHHSLIRISLKSWHMLVNLCFHIFLTCVVFVGGITQTRNASICQA 827
Cdd:cd15999    1 ADLLHPVVYATAVVLLLCLLTIIVSYIYHHSLVRISRKSWHMLVNLCFHIFLTCAVFVGGINQTRNASVCQA 72
7tmB2_GPR124-like_Adhesion_III cd15259
orphan GPR124 and related proteins, group III adhesion GPCRs, member of class B2 family of ...
756-827 1.38e-21

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: 95.13  E-value: 1.38e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530376257 756 ASLLHPVVYTTAIILLLCLLAVIVSYIYHHSLIRISLKSWHMLVNLCFHIFLTCVVFVGGITQTRNASICQA 827
Cdd:cd15259    1 FELLHPVVYAGAALCLLCLLATIITYIVFHRLIRISRKGRHMLVNLCLHLLLTCVVFVGGINRTANQLVCQA 72
LRR_8 pfam13855
Leucine rich repeat;
85-141 7.00e-18

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 78.34  E-value: 7.00e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530376257   85 TLILSNNKISELKNGSFSGLSLLERLDLRNNLISSIDPGAFWGLSSLKRLDLTNNRI 141
Cdd:pfam13855   5 SLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
7tmB2_GPR124 cd15998
G protein-coupled receptor 124, member of the class B2 family of seven-transmembrane G ...
759-832 1.82e-17

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: 83.47  E-value: 1.82e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530376257 759 LHPVVYTTAIILLLCLLAVIVSYIYHHSLIRISLKSWHMLVNLCFHIFLTCVVFVGGITQTRNASICQA-AVTTH 832
Cdd:cd15998    4 LHPVVYPCTALLLLCLFSTIITYILNHSSIHVSRKGWHMLLNLCFHIAMTSAVFAGGITLTNYQMVCQAvGITLH 78
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
85-183 8.84e-17

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 83.44  E-value: 8.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257  85 TLILSNNKISELKNgSFSGLSLLERLDLRNNLISSIdPGAFWGLSSLKRLDLTNNRIGCLNADIFrGLTNLVRLNLSGNL 164
Cdd:COG4886  140 ELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDL-PEELGNLTNLKELDLSNNQITDLPEPLG-NLTNLEELDLSGNQ 216
                         90
                 ....*....|....*....
gi 530376257 165 FSSLSQGtfdyLASLRSLE 183
Cdd:COG4886  217 LTDLPEP----LANLTNLE 231
LRR_8 pfam13855
Leucine rich repeat;
107-165 1.94e-16

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 74.10  E-value: 1.94e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530376257  107 LERLDLRNNLISSIDPGAFWGLSSLKRLDLTNNRIGCLNADIFRGLTNLVRLNLSGNLF 165
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
7tmB2_GPR123 cd16000
G protein-coupled receptor 123, member of the class B2 family of seven-transmembrane G ...
758-827 3.55e-16

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: 79.61  E-value: 3.55e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257 758 LLHPVVYTTAIILLLCLLAVIVSYIYHHSLIRISLKSWHMLVNLCFHIFLTCVVFVGGITQTRNASICQA 827
Cdd:cd16000    3 FLHPVVYACTAVMLLCLFASIITYIVHHSTIRISRKGWHMLLNFCFHTALTFAVFAGGINRTKYPIICQA 72
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
76-190 1.85e-13

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 73.43  E-value: 1.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257  76 PDTLPNRT--VTLILSNNKISELkNGSFSGLSLLERLDLRNNLISSIDpgAFWGLSSLKRLDLTNNRIGCLNADIfrGLT 153
Cdd:COG4886  198 PEPLGNLTnlEELDLSGNQLTDL-PEPLANLTNLETLDLSNNQLTDLP--ELGNLTNLEELDLSNNQLTDLPPLA--NLT 272
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 530376257 154 NLVRLNLSGNLFSSLSQGTFDYLASLRSLEFQTEYLL 190
Cdd:COG4886  273 NLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLN 309
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
85-182 8.92e-13

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 71.12  E-value: 8.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257  85 TLILSNNKiselkngSFSGLSLLERLDLRNNLISSIdPGAFWGLSSLKRLDLTNNRIGCLNADIFrGLTNLVRLNLSGNL 164
Cdd:COG4886  100 ELDLSGNE-------ELSNLTNLESLDLSGNQLTDL-PEELANLTNLKELDLSNNQLTDLPEPLG-NLTNLKSLDLSNNQ 170
                         90
                 ....*....|....*...
gi 530376257 165 FSSLSQGtFDYLASLRSL 182
Cdd:COG4886  171 LTDLPEE-LGNLTNLKEL 187
LRR_8 pfam13855
Leucine rich repeat;
129-182 3.94e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 61.77  E-value: 3.94e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530376257  129 SSLKRLDLTNNRIGCLNADIFRGLTNLVRLNLSGNLFSSLSQGTFDYLASLRSL 182
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYL 54
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
77-183 6.78e-12

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 65.96  E-value: 6.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257  77 DTLPNRTvTLILSNNKISELKNgsFSGLSLLERLDLRNNLISSI---------------------------DPGAFWGLS 129
Cdd:cd21340   43 EFLTNLT-HLYLQNNQIEKIEN--LENLVNLKKLYLGGNRISVVeglenltnleelhienqrlppgekltfDPRSLAALS 119
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530376257 130 -SLKRLDLTNNRIGCLNAdiFRGLTNLVRLNLSGNLFSSLSQgTFDYLASLRSLE 183
Cdd:cd21340  120 nSLRVLNISGNNIDSLEP--LAPLRNLEQLDASNNQISDLEE-LLDLLSSWPSLR 171
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
85-170 1.44e-09

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 61.10  E-value: 1.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257  85 TLILSNNKISELKngSFSGLSLLERLDLRNNLISSIDPGAfwGLSSLKRLDLTNNRIGCLNADIFRGLTNLVRLNLSGNL 164
Cdd:COG4886  232 TLDLSNNQLTDLP--ELGNLTNLEELDLSNNQLTDLPPLA--NLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLL 307

                 ....*.
gi 530376257 165 FSSLSQ 170
Cdd:COG4886  308 LNLLEL 313
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
135-236 3.61e-09

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 60.87  E-value: 3.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257   135 DLTNNRIGCLNADIFRGLTNLVRLNLSGNLFSslsqgtfdylaslrslefqteyllCDCNILWMHRWVKEKNITVRD--- 211
Cdd:TIGR00864    1 DISNNKISTIEEGICANLCNLSEIDLSGNPFE------------------------CDCGLARLPRWAEEKGVKVRQpea 56
                           90       100
                   ....*....|....*....|....*
gi 530376257   212 TRCVYPKSLQAQPVTGVKQELLTCD 236
Cdd:TIGR00864   57 ALCAGPGALAGQPLLGIPLLDSGCD 81
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
65-141 4.87e-07

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 51.33  E-value: 4.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257  65 CSSL-EL---AQVLPPD-----------TLPNRTVTLILSNNKISELKngSFSGLSLLERLDLRNNLISSIDP--GAFWG 127
Cdd:cd21340   89 LTNLeELhieNQRLPPGekltfdprslaALSNSLRVLNISGNNIDSLE--PLAPLRNLEQLDASNNQISDLEEllDLLSS 166
                         90
                 ....*....|....
gi 530376257 128 LSSLKRLDLTNNRI 141
Cdd:cd21340  167 WPSLRELDLTGNPV 180
GPS pfam01825
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
704-743 3.81e-06

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: 44.22  E-value: 3.81e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 530376257  704 WDFDLlNGQGGWKSDGCHILYSDENITTIQCYSLSNYAVL 743
Cdd:pfam01825   6 WDFTN-STTGRWSTEGCTTVSLNDTHTVCSCNHLTSFAVL 44
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
703-746 1.79e-05

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: 42.76  E-value: 1.79e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 530376257   703 RWDFDllngQGGWKSDGCHILYSDENITTIQCYSLSNYAVLMDL 746
Cdd:smart00303   7 FWDES----SGEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDV 46
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
107-146 3.84e-05

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 41.46  E-value: 3.84e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 530376257  107 LERLDLRNNLISSIDPgaFWGLSSLKRLDLT-NNRIGCLNA 146
Cdd:pfam12799   3 LEVLDLSNNQITDIPP--LAKLPNLETLDLSgNNKITDLSD 41
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
84-166 4.51e-05

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 46.19  E-value: 4.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257  84 VTLILSNNKISELKNGSFSG----LSLLERLDLRNNLISS-----IDPGAFWGLSSLKRLDLTNNRIGCLNA-DIFRGLT 153
Cdd:cd00116  196 EVLDLNNNGLTDEGASALAEtlasLKSLEVLNLGDNNLTDagaaaLASALLSPNISLLTLSLSCNDITDDGAkDLAEVLA 275
                         90
                 ....*....|....*.
gi 530376257 154 N---LVRLNLSGNLFS 166
Cdd:cd00116  276 EkesLLELDLRGNKFG 291
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
70-182 4.92e-05

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 46.19  E-value: 4.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257  70 LAQVLPPdtLPNRTVTLILSNNKISelkNGS-------FSGLSLLERLDLRNNLISsiDPG------AFWGLSSLKRLDL 136
Cdd:cd00116  128 LAKGLKD--LPPALEKLVLGRNRLE---GAScealakaLRANRDLKELNLANNGIG--DAGiralaeGLKANCNLEVLDL 200
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530376257 137 TNNRIGCLN----ADIFRGLTNLVRLNLSGNLFSS-----LSQGTFDYLASLRSL 182
Cdd:cd00116  201 NNNGLTDEGasalAETLASLKSLEVLNLGDNNLTDagaaaLASALLSPNISLLTL 255
HRM pfam02793
Hormone receptor domain; This extracellular domain contains four conserved cysteines that ...
363-416 5.58e-05

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: 41.59  E-value: 5.58e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530376257  363 WPRTLAGITAYLQCTRNTHGSgiypgnpQDERKAWRRCDRGGFWAD---DDYSRCQY 416
Cdd:pfam02793  14 WPRTPAGETVEVPCPDYFSGF-------DPRGNASRNCTEDGTWSEhppSNYSNCTS 63
LRRCT smart00082
Leucine rich repeat C-terminal domain;
189-223 6.55e-05

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 41.26  E-value: 6.55e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 530376257   189 LLCDCNILWMHRWVKEKNITVR--DTRCVYPKSLQAQ 223
Cdd:smart00082   3 FICDCELRWLLRWLQANEHLQDpvDLRCASPSSLRGP 39
LRR_5 pfam13306
BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich ...
82-180 9.52e-05

BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich repeats. This family contains a large number of BSPA-like surface antigens from Trichomonas vaginalis.


Pssm-ID: 463839 [Multi-domain]  Cd Length: 127  Bit Score: 42.92  E-value: 9.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257   82 RTVTLilsNNKISELKNGSFSGlSLLERLDLRNNlISSIDPGAFWGLSSLKRLDLTNNrIGCLNADIFRGlTNLVRLNLS 161
Cdd:pfam13306  37 KSITL---PSSLTSIGSYAFYN-CSLTSITIPSS-LTSIGEYAFSNCSNLKSITLPSN-LTSIGSYAFSN-CSLKSITIP 109
                          90
                  ....*....|....*....
gi 530376257  162 GNLfSSLSQGTFDYLASLR 180
Cdd:pfam13306 110 SSV-TTIGSYAFSNCSNLK 127
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
86-183 1.28e-04

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 44.01  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257  86 LILSNNKISELKNgsFSGLSLLERLDLRNNLISSIDpgafwGLSSLKRL---DLTNNRIGCLnaDIFRGLTNLVRLNLSG 162
Cdd:cd21340    7 LYLNDKNITKIDN--LSLCKNLKVLYLYDNKITKIE-----NLEFLTNLthlYLQNNQIEKI--ENLENLVNLKKLYLGG 77
                         90       100
                 ....*....|....*....|.
gi 530376257 163 NLFSSLSQgtfdyLASLRSLE 183
Cdd:cd21340   78 NRISVVEG-----LENLTNLE 93
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
81-186 1.45e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 45.61  E-value: 1.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257  81 NRTVTLILSNNKISELKNGSFSGLSLLERLDLRNNLISSIDPGA-FWGLSSLKRLDLTNNRigcLNADIFRG-LTNLVRL 158
Cdd:PLN00113  69 SRVVSIDLSGKNISGKISSAIFRLPYIQTINLSNNQLSGPIPDDiFTTSSSLRYLNLSNNN---FTGSIPRGsIPNLETL 145
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 530376257 159 NLSGNLFSS---LSQGTFD------------------YLASLRSLEFQT 186
Cdd:PLN00113 146 DLSNNMLSGeipNDIGSFSslkvldlggnvlvgkipnSLTNLTSLEFLT 194
LRR_5 pfam13306
BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich ...
85-184 2.24e-04

BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich repeats. This family contains a large number of BSPA-like surface antigens from Trichomonas vaginalis.


Pssm-ID: 463839 [Multi-domain]  Cd Length: 127  Bit Score: 41.76  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257   85 TLILSNNkISELKNGSFSGLSLLERLDLRNNLIsSIDPGAFWGlSSLKRLDLTNN--RIGcLNAdiFRGLTNLVRLNLSG 162
Cdd:pfam13306  15 SITIPSS-LTSIGEYAFSNCTSLKSITLPSSLT-SIGSYAFYN-CSLTSITIPSSltSIG-EYA--FSNCSNLKSITLPS 88
                          90       100
                  ....*....|....*....|..
gi 530376257  163 NLfSSLSQGTFdYLASLRSLEF 184
Cdd:pfam13306  89 NL-TSIGSYAF-SNCSLKSITI 108
7tmB2_Adhesion cd15040
adhesion receptors, subfamily B2 of the class B family of seven-transmembrane G ...
791-832 3.64e-04

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: 42.95  E-value: 3.64e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 530376257 791 SLKSWHMLVNLCFHIFLTCVVFVGGITQTRNASICQA-AVTTH 832
Cdd:cd15040   34 KRKPTKILLNLCLALLLANLLFLFGINSTDNPVLCTAvAALLH 76
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
130-163 3.73e-04

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 38.77  E-value: 3.73e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 530376257  130 SLKRLDLTNNRIGCLnaDIFRGLTNLVRLNLSGN 163
Cdd:pfam12799   2 NLEVLDLSNNQITDI--PPLAKLPNLETLDLSGN 33
HormR smart00008
Domain present in hormone receptors;
363-416 3.84e-04

Domain present in hormone receptors;


Pssm-ID: 214468  Cd Length: 70  Bit Score: 39.42  E-value: 3.84e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 530376257   363 WPRTLAGITAYLQCTRNThgSGIYPGNpqderKAWRRCDRGGFWA--DDDYSRCQY 416
Cdd:smart00008  15 WPQTPAGQLVEVPCPKYF--SGFSYKT-----GASRNCTENGGWSppFPNYSNCTS 63
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
85-122 4.41e-04

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 38.38  E-value: 4.41e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 530376257   85 TLILSNNKISELknGSFSGLSLLERLDL-RNNLISSIDP 122
Cdd:pfam12799   5 VLDLSNNQITDI--PPLAKLPNLETLDLsGNNKITDLSD 41
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
66-158 1.33e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 42.53  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257  66 SSLELAQVLPPD--TLPNRTVTLILSNNKIS-ELKNGSfsgLSLLERLDLRNNLISSIDPGAFWGLSSLKRLDLTNNrig 142
Cdd:PLN00113 101 SNNQLSGPIPDDifTTSSSLRYLNLSNNNFTgSIPRGS---IPNLETLDLSNNMLSGEIPNDIGSFSSLKVLDLGGN--- 174
                         90
                 ....*....|....*.
gi 530376257 143 CLNADIFRGLTNLVRL 158
Cdd:PLN00113 175 VLVGKIPNSLTNLTSL 190
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
249-341 2.41e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 37.87  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257   249 SHRQVVFEGDSLPFQCMASYiDQDMQVLWYQDGriVETDESQGIFVEKNMIHNCSLiasalTISNIQAGSTGNWGCHVQT 328
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASG-SPPPEVTWYKQG--GKLLAESGRFSVSRSGSTSTL-----TISNVTPEDSGTYTCAATN 72
                           90
                   ....*....|...
gi 530376257   329 KRGNNTRTVDIVV 341
Cdd:smart00410  73 SSGSASSGTTLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
242-326 2.42e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 37.55  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257  242 PSFYMTPSHrQVVFEGDSLPFQCMASYIDQDmQVLWYQDGRIVETDESQGIFVEKNMihncsliaSALTISNIQAGSTGN 321
Cdd:pfam13927   2 PVITVSPSS-VTVREGETVTLTCEATGSPPP-TITWYKNGEPISSGSTRSRSLSGSN--------STLTISNVTRSDAGT 71

                  ....*
gi 530376257  322 WGCHV 326
Cdd:pfam13927  72 YTCVA 76
LRR smart00370
Leucine-rich repeats, outliers;
104-127 2.56e-03

Leucine-rich repeats, outliers;


Pssm-ID: 197688 [Multi-domain]  Cd Length: 24  Bit Score: 35.79  E-value: 2.56e-03
                           10        20
                   ....*....|....*....|....
gi 530376257   104 LSLLERLDLRNNLISSIDPGAFWG 127
Cdd:smart00370   1 LPNLRELDLSNNQLSSLPPGAFQG 24
LRR_TYP smart00369
Leucine-rich repeats, typical (most populated) subfamily;
104-127 2.56e-03

Leucine-rich repeats, typical (most populated) subfamily;


Pssm-ID: 197687 [Multi-domain]  Cd Length: 24  Bit Score: 35.79  E-value: 2.56e-03
                           10        20
                   ....*....|....*....|....
gi 530376257   104 LSLLERLDLRNNLISSIDPGAFWG 127
Cdd:smart00369   1 LPNLRELDLSNNQLSSLPPGAFQG 24
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
90-183 3.02e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 41.37  E-value: 3.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257  90 NNKISELKNgSFSGLSLLERLDL-RNNLISSIdPGAFWGLSSLKRLDLTNNRI-GCLNADIFrGLTNLVRLNLSGNlfsS 167
Cdd:PLN00113 222 NNLSGEIPY-EIGGLTSLNHLDLvYNNLTGPI-PSSLGNLKNLQYLFLYQNKLsGPIPPSIF-SLQKLISLDLSDN---S 295
                         90
                 ....*....|....*.
gi 530376257 168 LSQGTFDYLASLRSLE 183
Cdd:PLN00113 296 LSGEIPELVIQLQNLE 311
LRR_5 pfam13306
BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich ...
94-195 3.51e-03

BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich repeats. This family contains a large number of BSPA-like surface antigens from Trichomonas vaginalis.


Pssm-ID: 463839 [Multi-domain]  Cd Length: 127  Bit Score: 38.29  E-value: 3.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257   94 SELKNGSFSGLSLLErLDLRNNLISsIDPGAFWGLSSLKRLDLTNNrIGCLNADIFRGlTNLVRLNLSGNLfSSLSQGTF 173
Cdd:pfam13306   1 TSIGSYAFYNCSLTS-ITIPSSLTS-IGEYAFSNCTSLKSITLPSS-LTSIGSYAFYN-CSLTSITIPSSL-TSIGEYAF 75
                          90       100
                  ....*....|....*....|....*...
gi 530376257  174 DYLASLRSLEFQT------EYLLCDCNI 195
Cdd:pfam13306  76 SNCSNLKSITLPSnltsigSYAFSNCSL 103
PLN03150 PLN03150
hypothetical protein; Provisional
102-166 4.35e-03

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 40.57  E-value: 4.35e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530376257 102 SGLSLLERLDLRNNLISSIDPGAFWGLSSLKRLDLTNNRIGCLNADIFRGLTNLVRLNLSGNLFS 166
Cdd:PLN03150 439 SKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSLS 503
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
62-183 5.90e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 40.22  E-value: 5.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257  62 KVVCSSLELAQVLPPDTLPNRTVTLI-LSNNKIS-ELKNGsFSGLSLLERLDLR-NNLISSIDPGAfWGLSSLKRLDLTN 138
Cdd:PLN00113 384 KLILFSNSLEGEIPKSLGACRSLRRVrLQDNSFSgELPSE-FTKLPLVYFLDISnNNLQGRINSRK-WDMPSLQMLSLAR 461
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 530376257 139 NRIGCLNADIFRGlTNLVRLNLSGNLFSSLSQGTFDYLASLRSLE 183
Cdd:PLN00113 462 NKFFGGLPDSFGS-KRLENLDLSRNQFSGAVPRKLGSLSELMQLK 505
I-set pfam07679
Immunoglobulin I-set domain;
242-324 6.88e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 36.47  E-value: 6.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257  242 PSFyMTPSHRQVVFEGDSLPFQCMASYiDQDMQVLWYQDGRIVETDesqGIFVEKNMIHNCSliasaLTISNIQAGSTGN 321
Cdd:pfam07679   1 PKF-TQKPKDVEVQEGESARFTCTVTG-TPDPEVSWFKDGQPLRSS---DRFKVTYEGGTYT-----LTISNVQPDDSGK 70

                  ...
gi 530376257  322 WGC 324
Cdd:pfam07679  71 YTC 73
LRR smart00370
Leucine-rich repeats, outliers;
152-174 8.08e-03

Leucine-rich repeats, outliers;


Pssm-ID: 197688 [Multi-domain]  Cd Length: 24  Bit Score: 34.63  E-value: 8.08e-03
                           10        20
                   ....*....|....*....|...
gi 530376257   152 LTNLVRLNLSGNLFSSLSQGTFD 174
Cdd:smart00370   1 LPNLRELDLSNNQLSSLPPGAFQ 23
LRR_TYP smart00369
Leucine-rich repeats, typical (most populated) subfamily;
152-174 8.08e-03

Leucine-rich repeats, typical (most populated) subfamily;


Pssm-ID: 197687 [Multi-domain]  Cd Length: 24  Bit Score: 34.63  E-value: 8.08e-03
                           10        20
                   ....*....|....*....|...
gi 530376257   152 LTNLVRLNLSGNLFSSLSQGTFD 174
Cdd:smart00369   1 LPNLRELDLSNNQLSSLPPGAFQ 23
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
253-337 8.77e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 36.02  E-value: 8.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257  253 VVFEGDSLPFQCMASYIDQDMQVLWYQDGrivetdeSQGIFVEKNMIHNCSLIASALTISNIQAGSTGNWGCHVQTKRGN 332
Cdd:pfam00047   7 TVLEGDSATLTCSASTGSPGPDVTWSKEG-------GTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGS 79

                  ....*
gi 530376257  333 NTRTV 337
Cdd:pfam00047  80 ATLST 84
LRR_9 pfam14580
Leucine-rich repeat;
85-185 9.70e-03

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 37.82  E-value: 9.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530376257   85 TLILSNNKISELKNgsFSGLSLLERLDLRNNLISSIDPGAFWGLSSLKRLDLTNNRIGCL-NADIFRGLTNLVRLNLSGN 163
Cdd:pfam14580  46 TIDFSDNEIRKLDG--FPLLRRLKTLLLNNNRICRIGEGLGEALPNLTELILTNNNLQELgDLDPLASLKKLTFLSLLRN 123
                          90       100
                  ....*....|....*....|....*....
gi 530376257  164 LFSSLSqgtfDY-------LASLRSLEFQ 185
Cdd:pfam14580 124 PVTNKP----HYrlyviykVPQLRLLDFR 148
 
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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