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Conserved domains on  [gi|1370468395|ref|XP_024306025|]
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polycystin-1-like protein 3 isoform X4 [Homo sapiens]

Protein Classification

C-type lectin domain-containing protein( domain architecture ID 12868071)

C-type lectin (CTL)/C-type lectin-like (CTLD) domain-containing protein may bind carbohydrate in a calcium-dependent manner

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 681-797 4.12e-57

PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


:

Pssm-ID: 238850  Cd Length: 120  Bit Score: 193.26  E-value: 4.12e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395  681 FHYLIQVYTGYRRSAATTAKVVITLYGSEGRSEPHHLCDPQKTVFERGGLDVFLLTTWTSLGNLHSLRLWHDNSGVSPSW 760
Cdd:cd01752      1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1370468395  761 YVSQVIVCDMAVKRKWHFLCNCWLAVDLGDCELDRVF 797
Cdd:cd01752     81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTF 117
PKD_channel super family cl37568
Polycystin cation channel; This family contains the cation channel region from group II of ...
 1405-1616 1.97e-29

Polycystin cation channel; This family contains the cation channel region from group II of Transient receptor potential (TRP) channels, the TRPP subfamily, including PKD1, PKD2, PKD2L and mucolipin proteins.


The actual alignment was detected with superfamily member pfam08016:

Pssm-ID: 462341 [Multi-domain]  Cd Length: 225  Bit Score: 117.76  E-value: 1.97e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395 1405 IISQVIYYLLVCYYAFIQGCQLKQQKWRFFTGKRNILDTSIILISFILLGLDMKSISLHKKNMARYRDDQDRFISFYEAV 1484
Cdd:pfam08016   11 LLCEIVFVVFFLYFVVEEILKIRKHRPSYLRSVWNLLDLAIVILSVVLIVLNIYRDFLADRLIKSVEASPVTFIDFDRVA 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395 1485 KVNSAATHLVGFPVLLATVQLWNLLRHSPRLRVISRTLSRAWDEVVGFLLIILILLTGYAIAFNLLFGCSISDYRTFFSS 1564
Cdd:pfam08016   91 QLDNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFGYLLFGTQAPNFSNFVKS 170

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1370468395 1565 AVTVVGLLMGISHQEEVFALDPVLGTFLILTSVILMVLVVINLFVSAILMAF 1616
Cdd:pfam08016  171 ILTLFRTILGDFGYNEIFSGNRVLGPLLFLTFVFLVIFILLNLFLAIINDSY 222
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 33-138 4.79e-09

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.


:

Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 55.70  E-value: 4.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395   33 NCYQLNRFQCSFEEAQHYCHVQRGFLAHIWNKEVQDLIRDYLEEGK--KWWIGQNVMPLKKH---QDNKYPADVAANGPP 107
Cdd:cd00037      1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSssDVWIGLNDLSSEGTwkwSDGSPLVDYTNWAPG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1370468395  108 KPLS-----CTYLSRNfirisSKG----DKCLLKYYFICQ 138
Cdd:cd00037     81 EPNPggsedCVVLSSS-----SDGkwndVSCSSKLPFICE 115
GPS super family cl02559
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
 571-610 1.20e-07

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.


The actual alignment was detected with superfamily member smart00303:

Pssm-ID: 470616  Cd Length: 49  Bit Score: 49.69  E-value: 1.20e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1370468395   571 TQCYYWEIHNQTWSSAGCQVGP-QSTilRTQCLCNHLTFFA 610
Cdd:smart00303    3 PICVFWDESSGEWSTRGCELLEtNGT--HTTCSCNHLTTFA 41
 
Name Accession Description Interval E-value
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 681-797 4.12e-57

PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238850  Cd Length: 120  Bit Score: 193.26  E-value: 4.12e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395  681 FHYLIQVYTGYRRSAATTAKVVITLYGSEGRSEPHHLCDPQKTVFERGGLDVFLLTTWTSLGNLHSLRLWHDNSGVSPSW 760
Cdd:cd01752      1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1370468395  761 YVSQVIVCDMAVKRKWHFLCNCWLAVDLGDCELDRVF 797
Cdd:cd01752     81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTF 117
PKD_channel pfam08016
Polycystin cation channel; This family contains the cation channel region from group II of ...
 1405-1616 1.97e-29

Polycystin cation channel; This family contains the cation channel region from group II of Transient receptor potential (TRP) channels, the TRPP subfamily, including PKD1, PKD2, PKD2L and mucolipin proteins.


Pssm-ID: 462341 [Multi-domain]  Cd Length: 225  Bit Score: 117.76  E-value: 1.97e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395 1405 IISQVIYYLLVCYYAFIQGCQLKQQKWRFFTGKRNILDTSIILISFILLGLDMKSISLHKKNMARYRDDQDRFISFYEAV 1484
Cdd:pfam08016   11 LLCEIVFVVFFLYFVVEEILKIRKHRPSYLRSVWNLLDLAIVILSVVLIVLNIYRDFLADRLIKSVEASPVTFIDFDRVA 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395 1485 KVNSAATHLVGFPVLLATVQLWNLLRHSPRLRVISRTLSRAWDEVVGFLLIILILLTGYAIAFNLLFGCSISDYRTFFSS 1564
Cdd:pfam08016   91 QLDNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFGYLLFGTQAPNFSNFVKS 170

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1370468395 1565 AVTVVGLLMGISHQEEVFALDPVLGTFLILTSVILMVLVVINLFVSAILMAF 1616
Cdd:pfam08016  171 ILTLFRTILGDFGYNEIFSGNRVLGPLLFLTFVFLVIFILLNLFLAIINDSY 222
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 683-797 2.04e-21

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 90.95  E-value: 2.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395  683 YLIQVYTGYRRSAATTAKVVITLYGSEGRS--EPHHLCDPQktvFERGGLDVFLLTTWTSLGNLHSLRLWHDNSGVSPSW 760
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESaqLEITLDNPD---FERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEW 77

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1370468395  761 YVSQVIVC-DMAVKRKWHFLCNCWLAVDLgDCELDRVF 797
Cdd:pfam01477   78 FLKSITVEvPGETGGKYTFPCNSWVYGSK-KYKETRVF 114
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
681-787 1.26e-13

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 68.44  E-value: 1.26e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395   681 FHYLIQVYTGYRRSAATTAKVVITLYGSEGRSEPHHLCDPQKTVFERGGLDVFLLTTWTSLGNLHSLRLWHDNSgvSPSW 760
Cdd:smart00308    1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR--HPEW 78

                            90       100
                    ....*....|....*....|....*..
gi 1370468395   761 YVSQVIVCDMAVKRKWHFLCNCWLAVD 787
Cdd:smart00308   79 FLKSITVKDLPTGGKYHFPCNSWVYPD 105
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 33-138 4.79e-09

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 55.70  E-value: 4.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395   33 NCYQLNRFQCSFEEAQHYCHVQRGFLAHIWNKEVQDLIRDYLEEGK--KWWIGQNVMPLKKH---QDNKYPADVAANGPP 107
Cdd:cd00037      1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSssDVWIGLNDLSSEGTwkwSDGSPLVDYTNWAPG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1370468395  108 KPLS-----CTYLSRNfirisSKG----DKCLLKYYFICQ 138
Cdd:cd00037     81 EPNPggsedCVVLSSS-----SDGkwndVSCSSKLPFICE 115
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
 571-610 1.20e-07

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: 49.69  E-value: 1.20e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1370468395   571 TQCYYWEIHNQTWSSAGCQVGP-QSTilRTQCLCNHLTFFA 610
Cdd:smart00303    3 PICVFWDESSGEWSTRGCELLEtNGT--HTTCSCNHLTTFA 41
GPS pfam01825
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
 572-610 1.56e-07

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: 49.23  E-value: 1.56e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1370468395  572 QCYYWEIHNQT---WSSAGCQVGpQSTILRTQCLCNHLTFFA 610
Cdd:pfam01825    2 QCVFWDFTNSTtgrWSTEGCTTV-SLNDTHTVCSCNHLTSFA 42
PLN03223 PLN03223
Polycystin cation channel protein; Provisional
 1493-1645 4.42e-06

Polycystin cation channel protein; Provisional


Pssm-ID: 215637 [Multi-domain]  Cd Length: 1634  Bit Score: 51.87  E-value: 4.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395 1493 LVGFPVLLATVQLWNLLRHSPRLRVISRTLSRAWDEVVGFLLIILILLTGYAIAFNLLFGCSISDYRTFFSSAVTVVGLL 1572
Cdd:PLN03223  1294 LSGINIILLLGRILKLMDFQPRLGVITRTLWLAGADLMHFFVIFGMVFVGYAFIGHVIFGNASVHFSDMTDSINSLFENL 1373

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370468395 1573 MG-ISHQEEVF----ALDPVLGTFLILTSVILMVLVVINLFVSAILMAFGkERKSLKKEAALIDTllqKLSNLLGISW 1645
Cdd:PLN03223  1374 LGdITYFNEDLknltGLQFVVGMIYFYSYNIFVFMILFNFLLAIICDAFG-EVKANAAETVSVHT---ELFPMLRDKW 1447
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 31-138 3.44e-05

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 44.90  E-value: 3.44e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395    31 QNNCYQLNRFQCSFEEAQHYCHVQRGFLAHIWNKEVQDLIRDYLEEGKK---WWIGQNVMPLKKH---QDNKYPAD---V 101
Cdd:smart00034    9 GGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSsdyYWIGLSDPDSNGSwqwSDGSGPVSysnW 88

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 1370468395   102 AANGPPKPL-SCTYLSRNFIRISSKGdkCLLKYYFICQ 138
Cdd:smart00034   89 APGEPNNSSgDCVVLSTSGGKWNDVS--CTSKLPFVCE 124
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 11-137 2.54e-04

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 43.32  E-value: 2.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395   11 LYIRTSIILGSELNSPAPHGQ--NNCYQLNRFQCSFEEAQHYCHVQRGFLAHIWNKEVQDLIRDYLeEGKKWWIGqnvMP 88
Cdd:PHA03097    32 LSCKLSPGDRSGLNCRSGWVGynNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFVSRYK-GGQDLWIG---IE 107

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1370468395   89 LKKHQDNKYPADVAANGPPKPLSCTYLSRNFIrISSkgdKCLLKYYFIC 137
Cdd:PHA03097   108 KKKGDDDDREVLDKVVKPPKSGKCAYLKDKTI-ISS---NCNATKGWIC 152
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 43-139 1.84e-03

Lectin C-type domain; This family includes both long and short form C-type


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 39.38  E-value: 1.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395   43 SFEEAQHYCHVQRGFLAHIWNKEVQDLIRDYLEE-GKKWWIGQNVMPLKKhqDNKYP----------ADVAANGPPKPlS 111
Cdd:pfam00059    3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLKKsNKYFWIGLTDRKNEG--TWKWVdgspvnytnwAPEPNNNGENE-D 79

                           90       100
                   ....*....|....*....|....*...
gi 1370468395  112 CTYLSRNFIRISSKGdkCLLKYYFICQT 139
Cdd:pfam00059   80 CVELSSSSGKWNDEN--CNSKNPFVCEK 105
 
Name Accession Description Interval E-value
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 681-797 4.12e-57

PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238850  Cd Length: 120  Bit Score: 193.26  E-value: 4.12e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395  681 FHYLIQVYTGYRRSAATTAKVVITLYGSEGRSEPHHLCDPQKTVFERGGLDVFLLTTWTSLGNLHSLRLWHDNSGVSPSW 760
Cdd:cd01752      1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1370468395  761 YVSQVIVCDMAVKRKWHFLCNCWLAVDLGDCELDRVF 797
Cdd:cd01752     81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTF 117
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 683-800 2.42e-31

PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238854  Cd Length: 120  Bit Score: 119.58  E-value: 2.42e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395  683 YLIQVYTGYRRSAATTAKVVITLYGSEGRSEPHHLCDPQKTV-FERGGLDVFLLTTwTSLGNLHSLRLWHDNSGVSPSWY 761
Cdd:cd01756      3 YEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNkFERGQTDKFTVEA-VDLGKLKKIRIGHDNSGLGAGWF 81

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1370468395  762 VSQVIVCDMAVKRKWHFLCNCWLAVDLGDCELDRVFIPV 800
Cdd:cd01756     82 LDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PKD_channel pfam08016
Polycystin cation channel; This family contains the cation channel region from group II of ...
 1405-1616 1.97e-29

Polycystin cation channel; This family contains the cation channel region from group II of Transient receptor potential (TRP) channels, the TRPP subfamily, including PKD1, PKD2, PKD2L and mucolipin proteins.


Pssm-ID: 462341 [Multi-domain]  Cd Length: 225  Bit Score: 117.76  E-value: 1.97e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395 1405 IISQVIYYLLVCYYAFIQGCQLKQQKWRFFTGKRNILDTSIILISFILLGLDMKSISLHKKNMARYRDDQDRFISFYEAV 1484
Cdd:pfam08016   11 LLCEIVFVVFFLYFVVEEILKIRKHRPSYLRSVWNLLDLAIVILSVVLIVLNIYRDFLADRLIKSVEASPVTFIDFDRVA 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395 1485 KVNSAATHLVGFPVLLATVQLWNLLRHSPRLRVISRTLSRAWDEVVGFLLIILILLTGYAIAFNLLFGCSISDYRTFFSS 1564
Cdd:pfam08016   91 QLDNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFGYLLFGTQAPNFSNFVKS 170

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1370468395 1565 AVTVVGLLMGISHQEEVFALDPVLGTFLILTSVILMVLVVINLFVSAILMAF 1616
Cdd:pfam08016  171 ILTLFRTILGDFGYNEIFSGNRVLGPLLFLTFVFLVIFILLNLFLAIINDSY 222
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 683-797 2.04e-21

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 90.95  E-value: 2.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395  683 YLIQVYTGYRRSAATTAKVVITLYGSEGRS--EPHHLCDPQktvFERGGLDVFLLTTWTSLGNLHSLRLWHDNSGVSPSW 760
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESaqLEITLDNPD---FERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEW 77

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1370468395  761 YVSQVIVC-DMAVKRKWHFLCNCWLAVDLgDCELDRVF 797
Cdd:pfam01477   78 FLKSITVEvPGETGGKYTFPCNSWVYGSK-KYKETRVF 114
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 682-784 1.87e-16

PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates.


Pssm-ID: 238061  Cd Length: 116  Bit Score: 76.99  E-value: 1.87e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395  682 HYLIQVYTGYRRSAATTAKVVITLYGSEGRSEPHhLCDPQKTVFERGGLDVFLLTTWTSLGNLHSLRLWHDNSGVSPSWY 761
Cdd:cd00113      2 RYTVTIKTGDKKGAGTDSNISLALYGENGNSSDI-PILDGPGSFERGSTDTFQIDLKLDIGDITKVYLRRDGSGLSDGWY 80

                           90       100
                   ....*....|....*....|...
gi 1370468395  762 VSQVIVCDMAVKRKWHFLCNCWL 784
Cdd:cd00113     81 CESITVQALGTKKVYTFPVNRWV 103
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
681-787 1.26e-13

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 68.44  E-value: 1.26e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395   681 FHYLIQVYTGYRRSAATTAKVVITLYGSEGRSEPHHLCDPQKTVFERGGLDVFLLTTWTSLGNLHSLRLWHDNSgvSPSW 760
Cdd:smart00308    1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR--HPEW 78

                            90       100
                    ....*....|....*....|....*..
gi 1370468395   761 YVSQVIVCDMAVKRKWHFLCNCWLAVD 787
Cdd:smart00308   79 FLKSITVKDLPTGGKYHFPCNSWVYPD 105
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 33-138 4.79e-09

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 55.70  E-value: 4.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395   33 NCYQLNRFQCSFEEAQHYCHVQRGFLAHIWNKEVQDLIRDYLEEGK--KWWIGQNVMPLKKH---QDNKYPADVAANGPP 107
Cdd:cd00037      1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSssDVWIGLNDLSSEGTwkwSDGSPLVDYTNWAPG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1370468395  108 KPLS-----CTYLSRNfirisSKG----DKCLLKYYFICQ 138
Cdd:cd00037     81 EPNPggsedCVVLSSS-----SDGkwndVSCSSKLPFICE 115
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
 571-610 1.20e-07

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: 49.69  E-value: 1.20e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1370468395   571 TQCYYWEIHNQTWSSAGCQVGP-QSTilRTQCLCNHLTFFA 610
Cdd:smart00303    3 PICVFWDESSGEWSTRGCELLEtNGT--HTTCSCNHLTTFA 41
GPS pfam01825
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
 572-610 1.56e-07

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: 49.23  E-value: 1.56e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1370468395  572 QCYYWEIHNQT---WSSAGCQVGpQSTILRTQCLCNHLTFFA 610
Cdd:pfam01825    2 QCVFWDFTNSTtgrWSTEGCTTV-SLNDTHTVCSCNHLTSFA 42
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
 683-787 1.76e-07

PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of its members are stress induced. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238852  Cd Length: 129  Bit Score: 51.77  E-value: 1.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395  683 YLIQVYTGYRRSAATTAKVVITLYGSEGR-------SEPHHLCDPQKTVFERGGLDVFLLTTWTSLGNLHSLRLWHDNSG 755
Cdd:cd01754      3 YTIYVQTGSIWKAGTDSRISLQIYDADGPglrianlEAWGGLMGAGHDYFERGNLDRFSGRGPCLPSPPCWMNLTSDGTG 82

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1370468395  756 VSPSWYVSQVIVCDMAVKR---KWHFLCNCWLAVD 787
Cdd:cd01754     83 NHPGWYVNYVEVTQAGQHApcmQHLFAVEQWLATD 117
PLN03223 PLN03223
Polycystin cation channel protein; Provisional
 1493-1645 4.42e-06

Polycystin cation channel protein; Provisional


Pssm-ID: 215637 [Multi-domain]  Cd Length: 1634  Bit Score: 51.87  E-value: 4.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395 1493 LVGFPVLLATVQLWNLLRHSPRLRVISRTLSRAWDEVVGFLLIILILLTGYAIAFNLLFGCSISDYRTFFSSAVTVVGLL 1572
Cdd:PLN03223  1294 LSGINIILLLGRILKLMDFQPRLGVITRTLWLAGADLMHFFVIFGMVFVGYAFIGHVIFGNASVHFSDMTDSINSLFENL 1373

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370468395 1573 MG-ISHQEEVF----ALDPVLGTFLILTSVILMVLVVINLFVSAILMAFGkERKSLKKEAALIDTllqKLSNLLGISW 1645
Cdd:PLN03223  1374 LGdITYFNEDLknltGLQFVVGMIYFYSYNIFVFMILFNFLLAIICDAFG-EVKANAAETVSVHT---ELFPMLRDKW 1447
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 31-138 7.51e-06

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.


Pssm-ID: 153063  Cd Length: 116  Bit Score: 46.56  E-value: 7.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395   31 QNNCYQLNRFQCSFEEAQHYCHVQRGFLAHIWNKEVQDLIRDYLEEgKKWWIGqnvmpLKKHQDNK---------YPADV 101
Cdd:cd03593      9 GNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGS-SSYWIG-----LSREKSEKpwkwidgspLNNLF 82

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1370468395  102 AANGPPKPLSCTYLSRNfiRISSkgDKCLLKYYFICQ 138
Cdd:cd03593     83 NIRGSTKSGNCAYLSST--GIYS--EDCSTKKRWICE 115
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 31-138 3.44e-05

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 44.90  E-value: 3.44e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395    31 QNNCYQLNRFQCSFEEAQHYCHVQRGFLAHIWNKEVQDLIRDYLEEGKK---WWIGQNVMPLKKH---QDNKYPAD---V 101
Cdd:smart00034    9 GGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSsdyYWIGLSDPDSNGSwqwSDGSGPVSysnW 88

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 1370468395   102 AANGPPKPL-SCTYLSRNFIRISSKGdkCLLKYYFICQ 138
Cdd:smart00034   89 APGEPNNSSgDCVVLSTSGGKWNDVS--CTSKLPFVCE 124
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 683-793 1.25e-04

PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they catalyze enzymatic lipid peroxidation in complex biological structures via direct dioxygenation of phospholipids and cholesterol esters of biomembranes and plasma lipoproteins. Both types of enzymes are cytosolic but need this domain to access their sequestered membrane or micelle bound substrates.


Pssm-ID: 238851  Cd Length: 113  Bit Score: 43.07  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395  683 YLIQVYTGYRRSAATTAKVVITLYGSEGRSEPhHLCDPQKTVFERGGLDVFLLTTWTSLGNLHSLRLWHDNSGVSPSWYV 762
Cdd:cd01753      3 YKVTVATGSSLFAGTDDYIYLTLVGTAGESEK-QLLDRPGYDFERGAVDEYKVKVPEDLGELLLVRLRKRKYLLFDAWFC 81

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1370468395  763 SQVIVCDMAvKRKWHFLCNCWLAvdlGDCEL 793
Cdd:cd01753     82 NYITVTGPG-GDEYHFPCYRWIE---GYGTL 108
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 11-137 2.54e-04

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 43.32  E-value: 2.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395   11 LYIRTSIILGSELNSPAPHGQ--NNCYQLNRFQCSFEEAQHYCHVQRGFLAHIWNKEVQDLIRDYLeEGKKWWIGqnvMP 88
Cdd:PHA03097    32 LSCKLSPGDRSGLNCRSGWVGynNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFVSRYK-GGQDLWIG---IE 107

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1370468395   89 LKKHQDNKYPADVAANGPPKPLSCTYLSRNFIrISSkgdKCLLKYYFIC 137
Cdd:PHA03097   108 KKKGDDDDREVLDKVVKPPKSGKCAYLKDKTI-ISS---NCNATKGWIC 152
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 1430-1624 1.34e-03

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 42.25  E-value: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395 1430 KWRFFTGKRNILDTSIILISFILLGLDMKSISLhkknmaryrddqdrfisfyeAVKVNSAathlvgFPVLLatvqLWNLL 1509
Cdd:pfam00520   60 KKRYFRSPWNILDFVVVLPSLISLVLSSVGSLS--------------------GLRVLRL------LRLLR----LLRLI 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395 1510 RHSPRLRVISRTLSRAWDEVVGFLLIILILLTGYAIAFNLLFGCS----------ISDYRTFFSSAVTVVGLLMGIS--- 1576
Cdd:pfam00520  110 RRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKlktwenpdngRTNFDNFPNAFLWLFQTMTTEGwgd 189

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1370468395 1577 -HQEEVFALDPVLGTFLILTSVILMVLVVINLFVSAILMAFGKERKSLK 1624
Cdd:pfam00520  190 iMYDTIDGKGEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 43-139 1.84e-03

Lectin C-type domain; This family includes both long and short form C-type


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 39.38  E-value: 1.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468395   43 SFEEAQHYCHVQRGFLAHIWNKEVQDLIRDYLEE-GKKWWIGQNVMPLKKhqDNKYP----------ADVAANGPPKPlS 111
Cdd:pfam00059    3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLKKsNKYFWIGLTDRKNEG--TWKWVdgspvnytnwAPEPNNNGENE-D 79

                           90       100
                   ....*....|....*....|....*...
gi 1370468395  112 CTYLSRNFIRISSKGdkCLLKYYFICQT 139
Cdd:pfam00059   80 CVELSSSSGKWNDEN--CNSKNPFVCEK 105
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 741-798 6.51e-03

PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains consists of an eight stranded beta-barrel. In RabIP1 this domain may participate in lipid-mediated modulation of Rab6IP1's function via it's generally proposed function of mediating interaction with lipids or membrane bound proteins.


Pssm-ID: 238855  Cd Length: 114  Bit Score: 38.29  E-value: 6.51e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370468395  741 LGNLHSLRLWHDNSGVSPSWYVSQVIVCDMAVKRKWHFLCNCWL--AVDLGDCE---LDRVFI 798
Cdd:cd01757     52 LGKLTTVQIGHDNSGLLAKWLVEYVMVRNEITGHTYKFPCGRWLgeGVDDGNGEdgsLERVLV 114
 
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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