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Conserved domains on  [gi|568926885|ref|XP_006538078|]
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FRAS1-related extracellular matrix protein 1 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cadherin_3 pfam16184
Cadherin-like;
1489-1596 4.99e-38

Cadherin-like;


:

Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 138.50  E-value: 4.99e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  1489 QTQRGVFEITLQTVDSALPVLTKNKRLRLAEGAMGLLSADHLQLTDPDTPPENLTFFLAQLPRHGYLFLRGK--ALQHNF 1566
Cdd:pfam16184    1 RSVPFTFNITIIPVNDEAPVLTTNTGLRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLALKGApgLPVTNF 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 568926885  1567 TQRDVDSGGVAYQHSGGGAREDYFTFLATD 1596
Cdd:pfam16184   81 TQADIDSGLVVYVHDGSESTSDGFTFQVTD 110
Cadherin_3 pfam16184
Cadherin-like;
402-508 2.25e-34

Cadherin-like;


:

Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 128.10  E-value: 2.25e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885   402 RSAPITVHISIRTADTNAPRVSWNTGLNLLEGQSRAITWEQFQIVDNDDI-GAVQLVTIGGLQHGRLTVREGKGFL---F 477
Cdd:pfam16184    1 RSVPFTFNITIIPVNDEAPVLTTNTGLRLWEGSSRPITPDLLQAEDPDTPpEDLTYTVVQGPSHGHLALKGAPGLPvtnF 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 568926885   478 TVTDLQAGVVRYHHDDSDTTKDFVAFRIFDG 508
Cdd:pfam16184   81 TQADIDSGLVVYVHDGSESTSDGFTFQVTDG 111
Cadherin_3 pfam16184
Cadherin-like;
1258-1373 1.18e-29

Cadherin-like;


:

Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 114.62  E-value: 1.18e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  1258 HKILKTISVNITPVNDETPTLSKKAEISMAVGDTRVLSSAVLSATDKDSPREKIHYVFERLPQNGQLQLKiGRDWVPLSt 1337
Cdd:pfam16184    1 RSVPFTFNITIIPVNDEAPVLTTNTGLRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLALK-GAPGLPVT- 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 568926885  1338 gmQCTQEDVDLNLLRYTHAGkTDSQDgDSFTFYLWD 1373
Cdd:pfam16184   79 --NFTQADIDSGLVVYVHDG-SESTS-DGFTFQVTD 110
Frem_N super family cl44740
Frem protein N-terminal domain; This entry represents a presumed domain found at the ...
 35-267 2.57e-29

Frem protein N-terminal domain; This entry represents a presumed domain found at the N-terminus of Frem related proteins.


The actual alignment was detected with superfamily member pfam19309:

Pssm-ID: 466034  Cd Length: 202  Bit Score: 117.05  E-value: 2.57e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885    35 NRGLRVMKGSSAFLsgDHLRVAVPKEK--DACRLEVVMNEPVTQRVGKLSPQVFDCHFLPNEVKYVHNGCPILDEDSVKL 112
Cdd:pfam19309    5 NRGLRVPFGRSVWL--DPLRDLVIQVQpgDRCEVTVLDNDPLPQRPGALSPRRFPCDFGPREVQYTHFGSRSPSRDRVRL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885   113 RLYRFTETDTFMETFLLRVYLVEPDCNIIrmSSNV-LEVTEFYGLSQAIDKNLLQFDYDRTASLdCTIRLDPLRTQLPAH 191
Cdd:pfam19309   83 QLRYDAPTDTLVLPFTLEVEVVFSQLEIV--TRNLpLTVEKLLGTSNPIDRRVLEFAYDPGTER-CKVTVLPGAGGLPRY 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568926885   192 GKLVvvnrksegprgDQPHsffsetelgaglkcpdgscalelkqvASLKVSCEEFLLTGFHYQHMQPP-SPNIDYIP 267
Cdd:pfam19309  160 GRLV-----------NATG--------------------------APLMVDCEAFLRAGVRYQHTATTsSPNRDYVP 199
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 2046-2168 1.53e-25

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: 103.45  E-value: 1.53e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885   2046 CPGGWLLHSGYCHILVTRQKgTWTTATRACREQHqGDLVTVLSRRHMQWLW----AMSGRKPFWIGLKNQPRTGHWEWI- 2120
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKK-TWEDAQAFCQSLG-GHLASIHSEAENDFVAsllkNSGSSDYYWIGLSDPDSNGSWQWSd 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 568926885   2121 GGEPVAFTNWRRGAPlhPKPGKNCALV-QKRGQWQTKNCSkgKAHNFVC 2168
Cdd:smart00034   79 GSGPVSYSNWAPGEP--NNSSGDCVVLsTSGGKWNDVSCT--SKLPFVC 123
Cadherin_3 pfam16184
Cadherin-like;
510-622 9.04e-25

Cadherin-like;


:

Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 100.75  E-value: 9.04e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885   510 HSSHHKFPINILPKDDSPPFLITNVVIELEEGKTILIQGSMLRASDMDSSDDYIFFNITKFPQAGEIMKKPGPrliGYPV 589
Cdd:pfam16184    1 RSVPFTFNITIIPVNDEAPVLTTNTGLRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLALKGAP---GLPV 77

                           90       100       110
                   ....*....|....*....|....*....|...
gi 568926885   590 PGFLQRDLFSGIIYYRHFGGEIFEDSFEFVLWD 622
Cdd:pfam16184   78 TNFTQADIDSGLVVYVHDGSESTSDGFTFQVTD 110
Cadherin_3 pfam16184
Cadherin-like;
772-875 9.29e-24

Cadherin-like;


:

Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 98.06  E-value: 9.29e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885   772 FNITVLPVDNQVPEVFTNT-LRVVEGGQCTISTEHILVSDVDTPLDSISLSLKERPLHGGVELDGFPLNPRGTFSWRDLN 850
Cdd:pfam16184    7 FNITIIPVNDEAPVLTTNTgLRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLALKGAPGLPVTNFTQADID 86

                           90       100
                   ....*....|....*....|....*
gi 568926885   851 TLKVWYQHDGSEVLQDEIFLEVTDG 875
Cdd:pfam16184   87 SGLVVYVHDGSESTSDGFTFQVTDG 111
Cadherin_3 pfam16184
Cadherin-like;
1137-1256 2.52e-21

Cadherin-like;


:

Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 91.12  E-value: 2.52e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  1137 RSLETTFHVIINPTNDEAPDLaVQN--ITVYEGHMVELDSSIISATDRDIPKDPLLFSIALKPQHGLLVdaaiskdshQI 1214
Cdd:pfam16184    1 RSVPFTFNITIIPVNDEAPVL-TTNtgLRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLA---------LK 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 568926885  1215 KQLQHEIHSFSVDLLKNGmKLVYAHDDSESSADNFVIQLSDG 1256
Cdd:pfam16184   71 GAPGLPVTNFTQADIDSG-LVVYVHDGSESTSDGFTFQVTDG 111
Cadherin_3 pfam16184
Cadherin-like;
1019-1134 1.32e-20

Cadherin-like;


:

Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 88.81  E-value: 1.32e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  1019 LNITVHPVDNQPPSIIIGRMLTVDEGFSAALTTHHLTVVDWDTAPDDLKFMLASQPQFGYLENalpsagfeKSNIGIRIA 1098
Cdd:pfam16184    7 FNITIIPVNDEAPVLTTNTGLRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLAL--------KGAPGLPVT 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 568926885  1099 SFQWTDMKASHINYVqsrHLRVEPTADQFTVYATDG 1134
Cdd:pfam16184   79 NFTQADIDSGLVVYV---HDGSESTSDGFTFQVTDG 111
Cadherin_3 pfam16184
Cadherin-like;
877-990 1.55e-20

Cadherin-like;


:

Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 88.81  E-value: 1.55e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885   877 NSAAFVLHIEVFPVNDEPPILKADLIpmMHCSEGGEVTITPEYISATDADSDDLELLFLIAREPQHG---VVRKAGLHVD 953
Cdd:pfam16184    1 RSVPFTFNITIIPVNDEAPVLTTNTG--LRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGPSHGhlaLKGAPGLPVT 78

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 568926885   954 RFSQGDVISGAVTYKHTGGeiglEPCSDTVVLVVSDG 990
Cdd:pfam16184   79 NFTQADIDSGLVVYVHDGS----ESTSDGFTFQVTDG 111
Cadherin_3 super family cl28802
Cadherin-like;
1395-1487 1.48e-18

Cadherin-like;


The actual alignment was detected with superfamily member pfam16184:

Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 83.04  E-value: 1.48e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  1395 IVIHaKPLVVVKGDRGLLTTATLLAVDGADKPEELLYLITSPPRHGQVEYVHSPGVPIASFSQMDIAGQTVCYIHKSrTA 1474
Cdd:pfam16184   21 LTTN-TGLRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLALKGAPGLPVTNFTQADIDSGLVVYVHDG-SE 98

                           90
                   ....*....|...
gi 568926885  1475 VPTDSFRFTISNG 1487
Cdd:pfam16184   99 STSDGFTFQVTDG 111
Cadherin_3 super family cl28802
Cadherin-like;
1609-1724 2.58e-12

Cadherin-like;


The actual alignment was detected with superfamily member pfam16184:

Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 65.32  E-value: 2.58e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  1609 QKEPVRFTIQVDQLDKAAPRIThlhspTQVGL-LKNGCYGIyITSRVLKASDPDTEDDQIIFKILRGPLYGRLENTTTGE 1687
Cdd:pfam16184    1 RSVPFTFNITIIPVNDEAPVLT-----TNTGLrLWEGSSRP-ITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLALKGAPG 74

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 568926885  1688 FIHERFSQKDLSHKTILYIINPSlQVTSDILEFQAMD 1724
Cdd:pfam16184   75 LPVTNFTQADIDSGLVVYVHDGS-ESTSDGFTFQVTD 110
Cadherin_3 super family cl28802
Cadherin-like;
630-761 8.87e-12

Cadherin-like;


The actual alignment was detected with superfamily member pfam16184:

Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 63.78  E-value: 8.87e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885   630 SVPQVVTIHITPVDDqlpkEAPGISRH--LVVKETEVAYITKKHLHFLDMESRDGELIYTVTRPPcfsfSHRHLdagklf 707
Cdd:pfam16184    2 SVPFTFNITIIPVND----EAPVLTTNtgLRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGP----SHGHL------ 67

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568926885   708 mvdsipKLTKNPTAPgLSSFTQHAVNHMKVAYmppmQDIGPSPRHVQFTVSVSN 761
Cdd:pfam16184   68 ------ALKGAPGLP-VTNFTQADIDSGLVVY----VHDGSESTSDGFTFQVTD 110
Cadherin_3 super family cl28802
Cadherin-like;
319-377 9.15e-07

Cadherin-like;


The actual alignment was detected with superfamily member pfam16184:

Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 49.52  E-value: 9.15e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 568926885   319 TPLTTSVLDCEEDETPKPLLVFNITKAPLQGYVTHLLDHTRPISSFTWKDLSDMQVAYQ 377
Cdd:pfam16184   35 RPITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLALKGAPGLPVTNFTQADIDSGLVVYV 93
Calx-beta super family cl02522
Calx-beta domain;
1746-1828 1.20e-05

Calx-beta domain;


The actual alignment was detected with superfamily member pfam03160:

Pssm-ID: 413355 [Multi-domain]  Cd Length: 91  Bit Score: 45.70  E-value: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  1746 QTAYEVCENVGLLPLEVTRRGYPMDSaFVGVEVNQV--SATVGKDFTVTPsKLLQFDPGMSTKMWNIAITYDGLEEDDEV 1823
Cdd:pfam03160    8 PPTYQVSENDGVAEVCVVRMSGTLRR-TVVVPYRTEdgTATAGDDYEPVE-GELVFGPGETEKCINVTIIDDDVYEGDEN 85


                   ....*
gi 568926885  1824 FEVIL 1828
Cdd:pfam03160   86 FFVLL 90
 
Name Accession Description Interval E-value
Cadherin_3 pfam16184
Cadherin-like;
1489-1596 4.99e-38

Cadherin-like;


Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 138.50  E-value: 4.99e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  1489 QTQRGVFEITLQTVDSALPVLTKNKRLRLAEGAMGLLSADHLQLTDPDTPPENLTFFLAQLPRHGYLFLRGK--ALQHNF 1566
Cdd:pfam16184    1 RSVPFTFNITIIPVNDEAPVLTTNTGLRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLALKGApgLPVTNF 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 568926885  1567 TQRDVDSGGVAYQHSGGGAREDYFTFLATD 1596
Cdd:pfam16184   81 TQADIDSGLVVYVHDGSESTSDGFTFQVTD 110
Cadherin_3 pfam16184
Cadherin-like;
402-508 2.25e-34

Cadherin-like;


Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 128.10  E-value: 2.25e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885   402 RSAPITVHISIRTADTNAPRVSWNTGLNLLEGQSRAITWEQFQIVDNDDI-GAVQLVTIGGLQHGRLTVREGKGFL---F 477
Cdd:pfam16184    1 RSVPFTFNITIIPVNDEAPVLTTNTGLRLWEGSSRPITPDLLQAEDPDTPpEDLTYTVVQGPSHGHLALKGAPGLPvtnF 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 568926885   478 TVTDLQAGVVRYHHDDSDTTKDFVAFRIFDG 508
Cdd:pfam16184   81 TQADIDSGLVVYVHDGSESTSDGFTFQVTDG 111
Cadherin_3 pfam16184
Cadherin-like;
1258-1373 1.18e-29

Cadherin-like;


Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 114.62  E-value: 1.18e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  1258 HKILKTISVNITPVNDETPTLSKKAEISMAVGDTRVLSSAVLSATDKDSPREKIHYVFERLPQNGQLQLKiGRDWVPLSt 1337
Cdd:pfam16184    1 RSVPFTFNITIIPVNDEAPVLTTNTGLRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLALK-GAPGLPVT- 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 568926885  1338 gmQCTQEDVDLNLLRYTHAGkTDSQDgDSFTFYLWD 1373
Cdd:pfam16184   79 --NFTQADIDSGLVVYVHDG-SESTS-DGFTFQVTD 110
Frem_N pfam19309
Frem protein N-terminal domain; This entry represents a presumed domain found at the ...
 35-267 2.57e-29

Frem protein N-terminal domain; This entry represents a presumed domain found at the N-terminus of Frem related proteins.


Pssm-ID: 466034  Cd Length: 202  Bit Score: 117.05  E-value: 2.57e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885    35 NRGLRVMKGSSAFLsgDHLRVAVPKEK--DACRLEVVMNEPVTQRVGKLSPQVFDCHFLPNEVKYVHNGCPILDEDSVKL 112
Cdd:pfam19309    5 NRGLRVPFGRSVWL--DPLRDLVIQVQpgDRCEVTVLDNDPLPQRPGALSPRRFPCDFGPREVQYTHFGSRSPSRDRVRL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885   113 RLYRFTETDTFMETFLLRVYLVEPDCNIIrmSSNV-LEVTEFYGLSQAIDKNLLQFDYDRTASLdCTIRLDPLRTQLPAH 191
Cdd:pfam19309   83 QLRYDAPTDTLVLPFTLEVEVVFSQLEIV--TRNLpLTVEKLLGTSNPIDRRVLEFAYDPGTER-CKVTVLPGAGGLPRY 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568926885   192 GKLVvvnrksegprgDQPHsffsetelgaglkcpdgscalelkqvASLKVSCEEFLLTGFHYQHMQPP-SPNIDYIP 267
Cdd:pfam19309  160 GRLV-----------NATG--------------------------APLMVDCEAFLRAGVRYQHTATTsSPNRDYVP 199
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 2046-2168 1.53e-25

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: 103.45  E-value: 1.53e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885   2046 CPGGWLLHSGYCHILVTRQKgTWTTATRACREQHqGDLVTVLSRRHMQWLW----AMSGRKPFWIGLKNQPRTGHWEWI- 2120
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKK-TWEDAQAFCQSLG-GHLASIHSEAENDFVAsllkNSGSSDYYWIGLSDPDSNGSWQWSd 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 568926885   2121 GGEPVAFTNWRRGAPlhPKPGKNCALV-QKRGQWQTKNCSkgKAHNFVC 2168
Cdd:smart00034   79 GSGPVSYSNWAPGEP--NNSSGDCVVLsTSGGKWNDVSCT--SKLPFVC 123
Cadherin_3 pfam16184
Cadherin-like;
510-622 9.04e-25

Cadherin-like;


Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 100.75  E-value: 9.04e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885   510 HSSHHKFPINILPKDDSPPFLITNVVIELEEGKTILIQGSMLRASDMDSSDDYIFFNITKFPQAGEIMKKPGPrliGYPV 589
Cdd:pfam16184    1 RSVPFTFNITIIPVNDEAPVLTTNTGLRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLALKGAP---GLPV 77

                           90       100       110
                   ....*....|....*....|....*....|...
gi 568926885   590 PGFLQRDLFSGIIYYRHFGGEIFEDSFEFVLWD 622
Cdd:pfam16184   78 TNFTQADIDSGLVVYVHDGSESTSDGFTFQVTD 110
Cadherin_3 pfam16184
Cadherin-like;
772-875 9.29e-24

Cadherin-like;


Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 98.06  E-value: 9.29e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885   772 FNITVLPVDNQVPEVFTNT-LRVVEGGQCTISTEHILVSDVDTPLDSISLSLKERPLHGGVELDGFPLNPRGTFSWRDLN 850
Cdd:pfam16184    7 FNITIIPVNDEAPVLTTNTgLRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLALKGAPGLPVTNFTQADID 86

                           90       100
                   ....*....|....*....|....*
gi 568926885   851 TLKVWYQHDGSEVLQDEIFLEVTDG 875
Cdd:pfam16184   87 SGLVVYVHDGSESTSDGFTFQVTDG 111
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 2056-2170 6.20e-22

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: 93.07  E-value: 6.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885 2056 YCHILVTrQKGTWTTATRACREQHqGDLVTVLSRRHMQWLWAM---SGRKPFWIGLKNQPRTGHWEWIGGEP-VAFTNWR 2131
Cdd:cd00037     1 SCYKFST-EKLTWEEAQEYCRSLG-GHLASIHSEEENDFLASLlkkSSSSDVWIGLNDLSSEGTWKWSDGSPlVDYTNWA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 568926885 2132 RGAPlHPKPGKNCALVQKR--GQWQTKNCSkgKAHNFVCSR 2170
Cdd:cd00037    79 PGEP-NPGGSEDCVVLSSSsdGKWNDVSCS--SKLPFICEK 116
Cadherin_3 pfam16184
Cadherin-like;
1137-1256 2.52e-21

Cadherin-like;


Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 91.12  E-value: 2.52e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  1137 RSLETTFHVIINPTNDEAPDLaVQN--ITVYEGHMVELDSSIISATDRDIPKDPLLFSIALKPQHGLLVdaaiskdshQI 1214
Cdd:pfam16184    1 RSVPFTFNITIIPVNDEAPVL-TTNtgLRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLA---------LK 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 568926885  1215 KQLQHEIHSFSVDLLKNGmKLVYAHDDSESSADNFVIQLSDG 1256
Cdd:pfam16184   71 GAPGLPVTNFTQADIDSG-LVVYVHDGSESTSDGFTFQVTDG 111
Cadherin_3 pfam16184
Cadherin-like;
1019-1134 1.32e-20

Cadherin-like;


Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 88.81  E-value: 1.32e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  1019 LNITVHPVDNQPPSIIIGRMLTVDEGFSAALTTHHLTVVDWDTAPDDLKFMLASQPQFGYLENalpsagfeKSNIGIRIA 1098
Cdd:pfam16184    7 FNITIIPVNDEAPVLTTNTGLRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLAL--------KGAPGLPVT 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 568926885  1099 SFQWTDMKASHINYVqsrHLRVEPTADQFTVYATDG 1134
Cdd:pfam16184   79 NFTQADIDSGLVVYV---HDGSESTSDGFTFQVTDG 111
Cadherin_3 pfam16184
Cadherin-like;
877-990 1.55e-20

Cadherin-like;


Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 88.81  E-value: 1.55e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885   877 NSAAFVLHIEVFPVNDEPPILKADLIpmMHCSEGGEVTITPEYISATDADSDDLELLFLIAREPQHG---VVRKAGLHVD 953
Cdd:pfam16184    1 RSVPFTFNITIIPVNDEAPVLTTNTG--LRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGPSHGhlaLKGAPGLPVT 78

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 568926885   954 RFSQGDVISGAVTYKHTGGeiglEPCSDTVVLVVSDG 990
Cdd:pfam16184   79 NFTQADIDSGLVVYVHDGS----ESTSDGFTFQVTDG 111
Cadherin_3 pfam16184
Cadherin-like;
1395-1487 1.48e-18

Cadherin-like;


Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 83.04  E-value: 1.48e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  1395 IVIHaKPLVVVKGDRGLLTTATLLAVDGADKPEELLYLITSPPRHGQVEYVHSPGVPIASFSQMDIAGQTVCYIHKSrTA 1474
Cdd:pfam16184   21 LTTN-TGLRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLALKGAPGLPVTNFTQADIDSGLVVYVHDG-SE 98

                           90
                   ....*....|...
gi 568926885  1475 VPTDSFRFTISNG 1487
Cdd:pfam16184   99 STSDGFTFQVTDG 111
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 2067-2170 1.83e-15

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 74.05  E-value: 1.83e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  2067 TWTTATRACREqHQGDLVTVLSRRHMQWLWAMSGR--KPFWIGLKNQPRTGHWEWIGGEPVAFTNWRRGAplHPKPGK-N 2143
Cdd:pfam00059    3 TWDEAREACRK-LGGHLVSINSAEELDFLSSTLKKsnKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEP--NNNGENeD 79

                           90       100
                   ....*....|....*....|....*...
gi 568926885  2144 CA-LVQKRGQWQTKNCSkgKAHNFVCSR 2170
Cdd:pfam00059   80 CVeLSSSSGKWNDENCN--SKNPFVCEK 105
Cadherin_3 pfam16184
Cadherin-like;
1609-1724 2.58e-12

Cadherin-like;


Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 65.32  E-value: 2.58e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  1609 QKEPVRFTIQVDQLDKAAPRIThlhspTQVGL-LKNGCYGIyITSRVLKASDPDTEDDQIIFKILRGPLYGRLENTTTGE 1687
Cdd:pfam16184    1 RSVPFTFNITIIPVNDEAPVLT-----TNTGLrLWEGSSRP-ITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLALKGAPG 74

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 568926885  1688 FIHERFSQKDLSHKTILYIINPSlQVTSDILEFQAMD 1724
Cdd:pfam16184   75 LPVTNFTQADIDSGLVVYVHDGS-ESTSDGFTFQVTD 110
Cadherin_3 pfam16184
Cadherin-like;
630-761 8.87e-12

Cadherin-like;


Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 63.78  E-value: 8.87e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885   630 SVPQVVTIHITPVDDqlpkEAPGISRH--LVVKETEVAYITKKHLHFLDMESRDGELIYTVTRPPcfsfSHRHLdagklf 707
Cdd:pfam16184    2 SVPFTFNITIIPVND----EAPVLTTNtgLRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGP----SHGHL------ 67

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568926885   708 mvdsipKLTKNPTAPgLSSFTQHAVNHMKVAYmppmQDIGPSPRHVQFTVSVSN 761
Cdd:pfam16184   68 ------ALKGAPGLP-VTNFTQADIDSGLVVY----VHDGSESTSDGFTFQVTD 110
Cadherin_3 pfam16184
Cadherin-like;
319-377 9.15e-07

Cadherin-like;


Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 49.52  E-value: 9.15e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 568926885   319 TPLTTSVLDCEEDETPKPLLVFNITKAPLQGYVTHLLDHTRPISSFTWKDLSDMQVAYQ 377
Cdd:pfam16184   35 RPITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLALKGAPGLPVTNFTQADIDSGLVVYV 93
Calx-beta pfam03160
Calx-beta domain;
1746-1828 1.20e-05

Calx-beta domain;


Pssm-ID: 397326 [Multi-domain]  Cd Length: 91  Bit Score: 45.70  E-value: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  1746 QTAYEVCENVGLLPLEVTRRGYPMDSaFVGVEVNQV--SATVGKDFTVTPsKLLQFDPGMSTKMWNIAITYDGLEEDDEV 1823
Cdd:pfam03160    8 PPTYQVSENDGVAEVCVVRMSGTLRR-TVVVPYRTEdgTATAGDDYEPVE-GELVFGPGETEKCINVTIIDDDVYEGDEN 85


                   ....*
gi 568926885  1824 FEVIL 1828
Cdd:pfam03160   86 FFVLL 90
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 2046-2168 5.55e-05

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: 48.93  E-value: 5.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  2046 CPGGWLLH--SGYCHILVTrQKGTWTTATRACREQHQGDLVTVLS---RRHMQWLWAMSGRKPFWIGLK--NQPRTGHWE 2118
Cdd:TIGR00864  318 CPKDGEIFeeNGHCFQIVP-EEAAWLDAQEQCLARAGAALAIVDNdalQNFLARKVTHSLDRGVWIGFSdvNGAEKGPAH 396

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568926885  2119 WIGG-EPVAFTNWRRGAPlHPKPGKNCALVQKRGQWQTKNCSkgKAHNFVC 2168
Cdd:TIGR00864  397 QGEAfEAEECEEGLAGEP-HPARAEHCVRLDPRGQCNSDLCN--APHAYVC 444
Calx_beta smart00237
Domains in Na-Ca exchangers and integrin-beta4; Domain in Na-Ca exchangers and integrin ...
 1745-1828 1.08e-04

Domains in Na-Ca exchangers and integrin-beta4; Domain in Na-Ca exchangers and integrin subunit beta4 (and some cyanobacterial proteins)


Pssm-ID: 197594 [Multi-domain]  Cd Length: 90  Bit Score: 43.01  E-value: 1.08e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885   1745 AQTAYEVCENVGLLPLEVTRRGYPMDSAFVGVEVNQVSATVGKDFTVTPsKLLQFDPGMSTKMWNIAITYDGLEEDDEVF 1824
Cdd:smart00237    7 EQPVYTVSESDGEVEVCVVRTGGARGPVVVPYSTEDGTATAGSDYEPVP-GELTFPPGETEKEIRIKIIDDDIYEKDETF 85


                    ....
gi 568926885   1825 EVIL 1828
Cdd:smart00237   86 YVRL 89
caca TIGR00845
sodium/calcium exchanger 1; The Ca2+:Cation Antiporter (CaCA) Family (TC 2.A.19)Proteins of ...
 1746-1848 1.44e-04

sodium/calcium exchanger 1; The Ca2+:Cation Antiporter (CaCA) Family (TC 2.A.19)Proteins of the CaCA family are found ubiquitously, having been identified in animals, plants, yeast, archaea and widely divergent bacteria.All of the characterized animal proteins catalyze Ca2+:Na+ exchange although some also transport K+. The NCX1 plasma membrane protein exchanges 3 Na+ for 1 Ca2+. The E. coli ChaA protein catalyzes Ca2+:H+ antiport but may also catalyze Na+:H+ antiport. All remaining well-characterized members of the family catalyze Ca2+:H+ exchange.This model is specific for the eukaryotic sodium ion/calcium ion exchangers of the Caca family [Transport and binding proteins, Other]


Pssm-ID: 273296 [Multi-domain]  Cd Length: 928  Bit Score: 47.09  E-value: 1.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  1746 QTAYEVCENVGLLPLEVTRRGYPMDS-AFVGVEVNQVSATVGKDFTVTPSkLLQFDPGMSTKMWNIAITYDGLEEDDEVF 1824
Cdd:TIGR00845  406 PGHYTCLENCGTVALTVVRRGGDLTNtVYVDYRTEDGTANAGSDYEFTEG-TLVFKPGETQKEFRIGIIDDDIFEEDEHF 484

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 568926885  1825 EV------------ILNSPVN---AVLGTQTKAAVKILD 1848
Cdd:TIGR00845  485 YVrlsnlrvgsedgILEANHVsavAQLASPNTATVTILD 523
 
Name Accession Description Interval E-value
Cadherin_3 pfam16184
Cadherin-like;
1489-1596 4.99e-38

Cadherin-like;


Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 138.50  E-value: 4.99e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  1489 QTQRGVFEITLQTVDSALPVLTKNKRLRLAEGAMGLLSADHLQLTDPDTPPENLTFFLAQLPRHGYLFLRGK--ALQHNF 1566
Cdd:pfam16184    1 RSVPFTFNITIIPVNDEAPVLTTNTGLRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLALKGApgLPVTNF 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 568926885  1567 TQRDVDSGGVAYQHSGGGAREDYFTFLATD 1596
Cdd:pfam16184   81 TQADIDSGLVVYVHDGSESTSDGFTFQVTD 110
Cadherin_3 pfam16184
Cadherin-like;
402-508 2.25e-34

Cadherin-like;


Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 128.10  E-value: 2.25e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885   402 RSAPITVHISIRTADTNAPRVSWNTGLNLLEGQSRAITWEQFQIVDNDDI-GAVQLVTIGGLQHGRLTVREGKGFL---F 477
Cdd:pfam16184    1 RSVPFTFNITIIPVNDEAPVLTTNTGLRLWEGSSRPITPDLLQAEDPDTPpEDLTYTVVQGPSHGHLALKGAPGLPvtnF 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 568926885   478 TVTDLQAGVVRYHHDDSDTTKDFVAFRIFDG 508
Cdd:pfam16184   81 TQADIDSGLVVYVHDGSESTSDGFTFQVTDG 111
Cadherin_3 pfam16184
Cadherin-like;
1258-1373 1.18e-29

Cadherin-like;


Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 114.62  E-value: 1.18e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  1258 HKILKTISVNITPVNDETPTLSKKAEISMAVGDTRVLSSAVLSATDKDSPREKIHYVFERLPQNGQLQLKiGRDWVPLSt 1337
Cdd:pfam16184    1 RSVPFTFNITIIPVNDEAPVLTTNTGLRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLALK-GAPGLPVT- 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 568926885  1338 gmQCTQEDVDLNLLRYTHAGkTDSQDgDSFTFYLWD 1373
Cdd:pfam16184   79 --NFTQADIDSGLVVYVHDG-SESTS-DGFTFQVTD 110
Frem_N pfam19309
Frem protein N-terminal domain; This entry represents a presumed domain found at the ...
 35-267 2.57e-29

Frem protein N-terminal domain; This entry represents a presumed domain found at the N-terminus of Frem related proteins.


Pssm-ID: 466034  Cd Length: 202  Bit Score: 117.05  E-value: 2.57e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885    35 NRGLRVMKGSSAFLsgDHLRVAVPKEK--DACRLEVVMNEPVTQRVGKLSPQVFDCHFLPNEVKYVHNGCPILDEDSVKL 112
Cdd:pfam19309    5 NRGLRVPFGRSVWL--DPLRDLVIQVQpgDRCEVTVLDNDPLPQRPGALSPRRFPCDFGPREVQYTHFGSRSPSRDRVRL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885   113 RLYRFTETDTFMETFLLRVYLVEPDCNIIrmSSNV-LEVTEFYGLSQAIDKNLLQFDYDRTASLdCTIRLDPLRTQLPAH 191
Cdd:pfam19309   83 QLRYDAPTDTLVLPFTLEVEVVFSQLEIV--TRNLpLTVEKLLGTSNPIDRRVLEFAYDPGTER-CKVTVLPGAGGLPRY 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568926885   192 GKLVvvnrksegprgDQPHsffsetelgaglkcpdgscalelkqvASLKVSCEEFLLTGFHYQHMQPP-SPNIDYIP 267
Cdd:pfam19309  160 GRLV-----------NATG--------------------------APLMVDCEAFLRAGVRYQHTATTsSPNRDYVP 199
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 2046-2168 1.53e-25

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: 103.45  E-value: 1.53e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885   2046 CPGGWLLHSGYCHILVTRQKgTWTTATRACREQHqGDLVTVLSRRHMQWLW----AMSGRKPFWIGLKNQPRTGHWEWI- 2120
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKK-TWEDAQAFCQSLG-GHLASIHSEAENDFVAsllkNSGSSDYYWIGLSDPDSNGSWQWSd 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 568926885   2121 GGEPVAFTNWRRGAPlhPKPGKNCALV-QKRGQWQTKNCSkgKAHNFVC 2168
Cdd:smart00034   79 GSGPVSYSNWAPGEP--NNSSGDCVVLsTSGGKWNDVSCT--SKLPFVC 123
Cadherin_3 pfam16184
Cadherin-like;
510-622 9.04e-25

Cadherin-like;


Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 100.75  E-value: 9.04e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885   510 HSSHHKFPINILPKDDSPPFLITNVVIELEEGKTILIQGSMLRASDMDSSDDYIFFNITKFPQAGEIMKKPGPrliGYPV 589
Cdd:pfam16184    1 RSVPFTFNITIIPVNDEAPVLTTNTGLRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLALKGAP---GLPV 77

                           90       100       110
                   ....*....|....*....|....*....|...
gi 568926885   590 PGFLQRDLFSGIIYYRHFGGEIFEDSFEFVLWD 622
Cdd:pfam16184   78 TNFTQADIDSGLVVYVHDGSESTSDGFTFQVTD 110
Cadherin_3 pfam16184
Cadherin-like;
772-875 9.29e-24

Cadherin-like;


Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 98.06  E-value: 9.29e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885   772 FNITVLPVDNQVPEVFTNT-LRVVEGGQCTISTEHILVSDVDTPLDSISLSLKERPLHGGVELDGFPLNPRGTFSWRDLN 850
Cdd:pfam16184    7 FNITIIPVNDEAPVLTTNTgLRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLALKGAPGLPVTNFTQADID 86

                           90       100
                   ....*....|....*....|....*
gi 568926885   851 TLKVWYQHDGSEVLQDEIFLEVTDG 875
Cdd:pfam16184   87 SGLVVYVHDGSESTSDGFTFQVTDG 111
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 2056-2170 6.20e-22

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: 93.07  E-value: 6.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885 2056 YCHILVTrQKGTWTTATRACREQHqGDLVTVLSRRHMQWLWAM---SGRKPFWIGLKNQPRTGHWEWIGGEP-VAFTNWR 2131
Cdd:cd00037     1 SCYKFST-EKLTWEEAQEYCRSLG-GHLASIHSEEENDFLASLlkkSSSSDVWIGLNDLSSEGTWKWSDGSPlVDYTNWA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 568926885 2132 RGAPlHPKPGKNCALVQKR--GQWQTKNCSkgKAHNFVCSR 2170
Cdd:cd00037    79 PGEP-NPGGSEDCVVLSSSsdGKWNDVSCS--SKLPFICEK 116
Cadherin_3 pfam16184
Cadherin-like;
1137-1256 2.52e-21

Cadherin-like;


Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 91.12  E-value: 2.52e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  1137 RSLETTFHVIINPTNDEAPDLaVQN--ITVYEGHMVELDSSIISATDRDIPKDPLLFSIALKPQHGLLVdaaiskdshQI 1214
Cdd:pfam16184    1 RSVPFTFNITIIPVNDEAPVL-TTNtgLRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLA---------LK 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 568926885  1215 KQLQHEIHSFSVDLLKNGmKLVYAHDDSESSADNFVIQLSDG 1256
Cdd:pfam16184   71 GAPGLPVTNFTQADIDSG-LVVYVHDGSESTSDGFTFQVTDG 111
Cadherin_3 pfam16184
Cadherin-like;
1019-1134 1.32e-20

Cadherin-like;


Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 88.81  E-value: 1.32e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  1019 LNITVHPVDNQPPSIIIGRMLTVDEGFSAALTTHHLTVVDWDTAPDDLKFMLASQPQFGYLENalpsagfeKSNIGIRIA 1098
Cdd:pfam16184    7 FNITIIPVNDEAPVLTTNTGLRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLAL--------KGAPGLPVT 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 568926885  1099 SFQWTDMKASHINYVqsrHLRVEPTADQFTVYATDG 1134
Cdd:pfam16184   79 NFTQADIDSGLVVYV---HDGSESTSDGFTFQVTDG 111
Cadherin_3 pfam16184
Cadherin-like;
877-990 1.55e-20

Cadherin-like;


Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 88.81  E-value: 1.55e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885   877 NSAAFVLHIEVFPVNDEPPILKADLIpmMHCSEGGEVTITPEYISATDADSDDLELLFLIAREPQHG---VVRKAGLHVD 953
Cdd:pfam16184    1 RSVPFTFNITIIPVNDEAPVLTTNTG--LRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGPSHGhlaLKGAPGLPVT 78

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 568926885   954 RFSQGDVISGAVTYKHTGGeiglEPCSDTVVLVVSDG 990
Cdd:pfam16184   79 NFTQADIDSGLVVYVHDGS----ESTSDGFTFQVTDG 111
Cadherin_3 pfam16184
Cadherin-like;
1395-1487 1.48e-18

Cadherin-like;


Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 83.04  E-value: 1.48e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  1395 IVIHaKPLVVVKGDRGLLTTATLLAVDGADKPEELLYLITSPPRHGQVEYVHSPGVPIASFSQMDIAGQTVCYIHKSrTA 1474
Cdd:pfam16184   21 LTTN-TGLRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLALKGAPGLPVTNFTQADIDSGLVVYVHDG-SE 98

                           90
                   ....*....|...
gi 568926885  1475 VPTDSFRFTISNG 1487
Cdd:pfam16184   99 STSDGFTFQVTDG 111
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 2046-2168 1.68e-16

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.


Pssm-ID: 153060 [Multi-domain]  Cd Length: 126  Bit Score: 77.73  E-value: 1.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885 2046 CPGGWLLHSGYCHiLVTRQKGTWTTATRACREQHqGDLVTVLSRRHMQWLWA-MSGRKPFWIGLKNQPRTGHWEWIGGEP 2124
Cdd:cd03590     1 CPTNWKSFQSSCY-FFSTEKKSWEESRQFCEDMG-AHLVIINSQEEQEFISKiLSGNRSYWIGLSDEETEGEWKWVDGTP 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 568926885 2125 VA--FTNWRRGAPLHPK-PGKNCA-LVQKRGQWQTKNCSkgKAHNFVC 2168
Cdd:cd03590    79 LNssKTFWHPGEPNNWGgGGEDCAeLVYDSGGWNDVPCN--LEYRWIC 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 2067-2170 1.83e-15

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 74.05  E-value: 1.83e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  2067 TWTTATRACREqHQGDLVTVLSRRHMQWLWAMSGR--KPFWIGLKNQPRTGHWEWIGGEPVAFTNWRRGAplHPKPGK-N 2143
Cdd:pfam00059    3 TWDEAREACRK-LGGHLVSINSAEELDFLSSTLKKsnKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEP--NNNGENeD 79

                           90       100
                   ....*....|....*....|....*...
gi 568926885  2144 CA-LVQKRGQWQTKNCSkgKAHNFVCSR 2170
Cdd:pfam00059   80 CVeLSSSSGKWNDENCN--SKNPFVCEK 105
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 2058-2170 6.44e-14

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. 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. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.


Pssm-ID: 153072  Cd Length: 108  Bit Score: 69.71  E-value: 6.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885 2058 HILVTRQKgTWTTATRACREQHqGDLVTVLSRRHMQWL---WAMSGRKpFWIGLKNQprTGHWEWIGGEPVAFTNWrrgA 2134
Cdd:cd03602     3 FYLVNESK-TWSEAQQYCRENY-TDLATVQNQEDNALLsnlSRVSNSA-AWIGLYRD--VDSWRWSDGSESSFRNW---N 74

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568926885 2135 PLHPKPGKNCALVQKRGQWQTKNCSKGKAhnFVCSR 2170
Cdd:cd03602    75 TFQPFGQGDCATMYSSGRWYAALCSALKP--FICYD 108
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 2046-2168 2.14e-13

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.


Pssm-ID: 153059  Cd Length: 137  Bit Score: 69.31  E-value: 2.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885 2046 CPGGWLLHSGYCHilvtRQKG---TWTTATRACRE----QHQGDLVTVLSRRHMQWLWAM--SGRKP-----FWIGLKNQ 2111
Cdd:cd03589     1 CPTFWTAFGGYCY----RFFGdrlTWEEAELRCRSfsipGLIAHLVSIHSQEENDFVYDLfeSSRGPdtpygLWIGLHDR 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568926885 2112 PRTGHWEWIGGEPVAFTNWRRGAPLHPKPGKNCALVQKR----GQWQTKNCSkgKAHNFVC 2168
Cdd:cd03589    77 TSEGPFEWTDGSPVDFTKWAGGQPDNYGGNEDCVQMWRRgdagQSWNDMPCD--AVFPYIC 135
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 2046-2170 2.50e-12

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: 65.43  E-value: 2.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885 2046 CPGGWLLHSGYCHiLVTRQKGTWTTATRACREQHqGDLVTVLSRRHMQWLWAMSGRKPFWIGLKNQPRTGHWEWIGGEPv 2125
Cdd:cd03593     1 CPKDWICYGNKCY-YFSMEKKTWNESKEACSSKN-SSLLKIDDEEELEFLQSQIGSSSYWIGLSREKSEKPWKWIDGSP- 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 568926885 2126 aFTNWRRGAPLHPKpgKNCALVQKRGqWQTKNCSkgKAHNFVCSR 2170
Cdd:cd03593    78 -LNNLFNIRGSTKS--GNCAYLSSTG-IYSEDCS--TKKRWICEK 116
Cadherin_3 pfam16184
Cadherin-like;
1609-1724 2.58e-12

Cadherin-like;


Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 65.32  E-value: 2.58e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  1609 QKEPVRFTIQVDQLDKAAPRIThlhspTQVGL-LKNGCYGIyITSRVLKASDPDTEDDQIIFKILRGPLYGRLENTTTGE 1687
Cdd:pfam16184    1 RSVPFTFNITIIPVNDEAPVLT-----TNTGLrLWEGSSRP-ITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLALKGAPG 74

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 568926885  1688 FIHERFSQKDLSHKTILYIINPSlQVTSDILEFQAMD 1724
Cdd:pfam16184   75 LPVTNFTQADIDSGLVVYVHDGS-ESTSDGFTFQVTD 110
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 2060-2141 3.19e-12

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.


Pssm-ID: 153073 [Multi-domain]  Cd Length: 118  Bit Score: 65.14  E-value: 3.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885 2060 LVTRQKGTWTTATRACREqHQGDLVTVLSRRHMQWLWA-MSGRKPFWIGLKNQPRTGHWEWIGGEPVAFTNWRRGAPLHP 2138
Cdd:cd03603     4 KFVDGGMTWEAAQTLAES-LGGHLVTINSAEENDWLLSnFGGYGASWIGASDAATEGTWKWSDGEESTYTNWGSGEPHNN 82


                  ...
gi 568926885 2139 KPG 2141
Cdd:cd03603    83 GGG 85
Cadherin_3 pfam16184
Cadherin-like;
630-761 8.87e-12

Cadherin-like;


Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 63.78  E-value: 8.87e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885   630 SVPQVVTIHITPVDDqlpkEAPGISRH--LVVKETEVAYITKKHLHFLDMESRDGELIYTVTRPPcfsfSHRHLdagklf 707
Cdd:pfam16184    2 SVPFTFNITIIPVND----EAPVLTTNtgLRLWEGSSRPITPDLLQAEDPDTPPEDLTYTVVQGP----SHGHL------ 67

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568926885   708 mvdsipKLTKNPTAPgLSSFTQHAVNHMKVAYmppmQDIGPSPRHVQFTVSVSN 761
Cdd:pfam16184   68 ------ALKGAPGLP-VTNFTQADIDSGLVVY----VHDGSESTSDGFTFQVTD 110
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 2046-2168 1.87e-11

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 63.54  E-value: 1.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885 2046 CPGGWLLHSGYCHILVtRQKGTWTTATRACREQHQG-DLVTVLSRRHMQWLWAM-----SGRKPFWIGL--KNQPRTghW 2117
Cdd:cd03594     1 CPKGWLPYKGNCYGYF-RQPLSWSDAELFCQKYGPGaHLASIHSPAEAAAIASLissyqKAYQPVWIGLhdPQQSRG--W 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568926885 2118 EWIGGEPVAFTNWRRGAPLhpKPGKNCA-LVQKRG--QWQTKNCSKGKAhnFVC 2168
Cdd:cd03594    78 EWSDGSKLDYRSWDRNPPY--ARGGYCAeLSRSTGflKWNDANCEERNP--FIC 127
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 2046-2159 1.29e-10

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.


Pssm-ID: 153058  Cd Length: 124  Bit Score: 61.05  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885 2046 CPGGWLLHSGYCHILVTRQKgTWTTATRACREQhQGDLVTVLSRRHMQWLwAMSGRKPFWIGLKNQPRTGHWEWIGGEPV 2125
Cdd:cd03588     1 CEEGWDKFQGHCYRHFPDRE-TWEDAERRCREQ-QGHLSSIVTPEEQEFV-NNNAQDYQWIGLNDRTIEGDFRWSDGHPL 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 568926885 2126 AFTNWRRGAP-LHPKPGKNCALV--QKRGQWQTKNCS 2159
Cdd:cd03588    78 QFENWRPNQPdNFFATGEDCVVMiwHEEGEWNDVPCN 114
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 2060-2168 1.19e-08

C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF); CLECT_tetranectin_like: C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TN binds to plasminogen and stimulates activation of plasminogen, playing a key role in the regulation of proteolytic processes. The TN CTLD binds two calcium ions. Its calcium free form binds to various kringle-like protein ligands. Two residues involved in the coordination of calcium are critical for the binding of TN to the fourth kringle (K4) domain of plasminogen (Plg K4). TN binds the kringle 1-4 form of angiostatin (AST K1-4). AST K1-4 is a fragment of Plg, commonly found in cancer tissues. TN inhibits the binding of Plg and AST K1-4 to the extracellular matrix (EMC) of endothelial cells and counteracts the antiproliferative effects of AST K1-4 on these cells. TN also binds the tenth kringle domain of apolipoprotein (a). In addition, TN binds fibrin and complex polysaccharides in a Ca2+ dependent manner. The binding site for complex sulfated polysaccharides is N-terminal to the CTLD. TN is homotrimeric; N-terminal to the CTLD is an alpha helical domain responsible for trimerization of monomeric units. TN may modulate angiogenesis through interactions with angiostatin and coagulation through interaction with fibrin. TN may play a role in myogenesis and in bone development. Mice having a deletion in the TN gene exhibit a kyphotic spine abnormality. TN is a useful prognostic marker of certain cancer types. CLECSF1 is expressed in cartilage tissue, which is primarily intracellular matrix (ECM), and is a candidate for organizing ECM. SCGF is strongly expressed in bone marrow and is a cytokine for primitive hematopoietic progenitor cells.


Pssm-ID: 153066  Cd Length: 129  Bit Score: 55.47  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885 2060 LVTRQKGTWTTATRACREQhQGDLVTVLSRRHMQWLW-----AMSGRKPFWIGLKNQPRTGHWEWIGGEPVAFTNWRRGA 2134
Cdd:cd03596    13 LVSEETKHYHEASEDCIAR-GGTLATPRDSDENDALRdyvkaSVPGNWEVWLGINDMVAEGKWVDVNGSPISYFNWEREI 91

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568926885 2135 PLHPKPGK--NCALVQ--KRGQWQTKNCSKGKahNFVC 2168
Cdd:cd03596    92 TAQPDGGKreNCVALSssAQGKWFDEDCRREK--PYVC 127
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 2060-2168 3.43e-07

C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1); CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis.


Pssm-ID: 153061 [Multi-domain]  Cd Length: 114  Bit Score: 50.76  E-value: 3.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885 2060 LVTRQKGTWTTATRACREQhQGDLVTVLS---RRHMQWLWAMSGRKPFwIGLKNQPRTGHWEWIGGEPVAFTNWRRGAPL 2136
Cdd:cd03591     5 VTNGEEKNFDDAQKLCSEA-GGTLAMPRNaaeNAAIASYVKKGNTYAF-IGITDLETEGQFVYLDGGPLTYTNWKPGEPN 82

                          90       100       110
                  ....*....|....*....|....*....|..
gi 568926885 2137 HPKPGKNCALVQKRGQWQTKNCSkgKAHNFVC 2168
Cdd:cd03591    83 NAGGGEDCVEMYTSGKWNDVACN--LTRLFVC 112
Cadherin_3 pfam16184
Cadherin-like;
319-377 9.15e-07

Cadherin-like;


Pssm-ID: 465048 [Multi-domain]  Cd Length: 111  Bit Score: 49.52  E-value: 9.15e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 568926885   319 TPLTTSVLDCEEDETPKPLLVFNITKAPLQGYVTHLLDHTRPISSFTWKDLSDMQVAYQ 377
Cdd:pfam16184   35 RPITPDLLQAEDPDTPPEDLTYTVVQGPSHGHLALKGAPGLPVTNFTQADIDSGLVVYV 93
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 2055-2169 2.71e-06

C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH); CLECT_EMBP_like: C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Eosinophils and basophils carry out various functions in allergic, parasitic, and inflammatory diseases. EMBP is stored in eosinophil crystalloid granules and is released upon degranulation. EMBP is also expressed in basophils. The proform of EMBP is expressed in placental X cells and breast tissue and increases significantly during human pregnancy. EMBP has cytotoxic properties and damages bacteria and mammalian cells, in vitro, as well as, helminth parasites. EMBP deposition has been observed in the inflamed tissue of allergy patients in a variety of diseases including asthma, atopic dermatitis, and rhinitis. In addition to its cytotoxic functions, EMBP activates cells and stimulates cytokine production. EMBP has been shown to bind the proteoglycan heparin. The binding site is similar to the carbohydrate binding site of other classical CTLD, such as mannose-binding protein (MBP1), however, heparin binding to EMBP is calcium ion independent. MBPH has reduced potency in cytotoxic and cytostimulatory assays compared with EMBP.


Pssm-ID: 153068  Cd Length: 117  Bit Score: 48.22  E-value: 2.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885 2055 GYCHILVtRQKGTWTTATRACREQHQGDLVTVLSRR-HMQWLWAMSGRKP--FWIGLKNQPRTGHWE--WIGGEPVAFTN 2129
Cdd:cd03598     1 GRCYRFV-KSPRTFRDAQVICRRCYRGNLASIHSFAfNYRVQRLVSTLNQaqVWIGGIITGKGRCRRfsWVDGSVWNYAY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568926885 2130 WRRGaplHPKPGK-NC-ALVQKRGQWQTKNCSKGKAhnFVCS 2169
Cdd:cd03598    80 WAPG---QPGNRRgHCvELCTRGGHWRRAHCKLRRP--FICS 116
Calx-beta pfam03160
Calx-beta domain;
1746-1828 1.20e-05

Calx-beta domain;


Pssm-ID: 397326 [Multi-domain]  Cd Length: 91  Bit Score: 45.70  E-value: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  1746 QTAYEVCENVGLLPLEVTRRGYPMDSaFVGVEVNQV--SATVGKDFTVTPsKLLQFDPGMSTKMWNIAITYDGLEEDDEV 1823
Cdd:pfam03160    8 PPTYQVSENDGVAEVCVVRMSGTLRR-TVVVPYRTEdgTATAGDDYEPVE-GELVFGPGETEKCINVTIIDDDVYEGDEN 85


                   ....*
gi 568926885  1824 FEVIL 1828
Cdd:pfam03160   86 FFVLL 90
CLECT_thrombomodulin_like cd03600
C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, ...
 2053-2168 1.30e-05

C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR; CLECT_thrombomodulin_like: C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In these thrombomodulin-like proteins the residues involved in coordinating Ca2+ in the classical MBP-A CTLD are not conserved. TM exerts anti-fibrinolytic and anti-inflammatory activity. TM also regulates blood coagulation in the anticoagulant protein C pathway. In this pathway, the procoagulant properties of thrombin (T) are lost when it binds TM. TM also plays a key role in tumor biology. It is expressed on endothelial cells and on several type of tumor cell including squamous cell carcinoma. Loss of TM expression correlates with advanced stage and poor prognosis. Loss of function of TM function may be associated with arterial or venous thrombosis and with late fetal loss. Soluble molecules of TM retaining the CTLD are detected in human plasma and urine where higher levels indicate injury and/or enhanced turnover of the endothelium. C1qR is expressed on endothelial cells and stem cells. It is also expressed on monocots and neutrophils, where it is subject to ectodomain shedding. Soluble forms of C1qR retaining the CTLD is detected in human plasma. C1qR modulates the phagocytosis of apoptotic cells in vivo. C1qR-deficient mice are defective in clearance of apoptotic cells in vivo. The cytoplasmic tail of C1qR, C-terminal to the CTLD of CD93, contains a PDZ binding domain which interacts with the PDZ domain-containing adaptor protein, GIPC. The juxtamembrane region of this tail interacts with the ezrin/radixin/moesin family. Endosialin functions in the growth and progression of abdominal tumors and is expressed in the stroma of several tumors.


Pssm-ID: 153070  Cd Length: 141  Bit Score: 47.04  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885 2053 HSGYCHILvTRQKGTWTTATRACREQHqGDLVTVLSR---RHMQWLWAMSGRKP------FWIGLKNQPRT--------- 2114
Cdd:cd03600     2 VSDACYTL-HPQKLTFLEAQRSCIELG-GNLATVRSGeeaDVVSLLLAAGPGRHgrgslrLWIGLQREPRQcsdpslplr 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568926885 2115 GhWEWI-GGEPVAFTNWRRgAPLHPKPGKNCALVQKRGQ------WQTKNCSkGKAHNFVC 2168
Cdd:cd03600    80 G-FSWVtGDQDTDFSNWLQ-EPAGTCTSPRCVALSAAGStpdnlkWKDGPCS-ARADGYLC 137
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 2046-2168 5.55e-05

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: 48.93  E-value: 5.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  2046 CPGGWLLH--SGYCHILVTrQKGTWTTATRACREQHQGDLVTVLS---RRHMQWLWAMSGRKPFWIGLK--NQPRTGHWE 2118
Cdd:TIGR00864  318 CPKDGEIFeeNGHCFQIVP-EEAAWLDAQEQCLARAGAALAIVDNdalQNFLARKVTHSLDRGVWIGFSdvNGAEKGPAH 396

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568926885  2119 WIGG-EPVAFTNWRRGAPlHPKPGKNCALVQKRGQWQTKNCSkgKAHNFVC 2168
Cdd:TIGR00864  397 QGEAfEAEECEEGLAGEP-HPARAEHCVRLDPRGQCNSDLCN--APHAYVC 444
Calx_beta smart00237
Domains in Na-Ca exchangers and integrin-beta4; Domain in Na-Ca exchangers and integrin ...
 1745-1828 1.08e-04

Domains in Na-Ca exchangers and integrin-beta4; Domain in Na-Ca exchangers and integrin subunit beta4 (and some cyanobacterial proteins)


Pssm-ID: 197594 [Multi-domain]  Cd Length: 90  Bit Score: 43.01  E-value: 1.08e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885   1745 AQTAYEVCENVGLLPLEVTRRGYPMDSAFVGVEVNQVSATVGKDFTVTPsKLLQFDPGMSTKMWNIAITYDGLEEDDEVF 1824
Cdd:smart00237    7 EQPVYTVSESDGEVEVCVVRTGGARGPVVVPYSTEDGTATAGSDYEPVP-GELTFPPGETEKEIRIKIIDDDIYEKDETF 85


                    ....
gi 568926885   1825 EVIL 1828
Cdd:smart00237   86 YVRL 89
caca TIGR00845
sodium/calcium exchanger 1; The Ca2+:Cation Antiporter (CaCA) Family (TC 2.A.19)Proteins of ...
 1746-1848 1.44e-04

sodium/calcium exchanger 1; The Ca2+:Cation Antiporter (CaCA) Family (TC 2.A.19)Proteins of the CaCA family are found ubiquitously, having been identified in animals, plants, yeast, archaea and widely divergent bacteria.All of the characterized animal proteins catalyze Ca2+:Na+ exchange although some also transport K+. The NCX1 plasma membrane protein exchanges 3 Na+ for 1 Ca2+. The E. coli ChaA protein catalyzes Ca2+:H+ antiport but may also catalyze Na+:H+ antiport. All remaining well-characterized members of the family catalyze Ca2+:H+ exchange.This model is specific for the eukaryotic sodium ion/calcium ion exchangers of the Caca family [Transport and binding proteins, Other]


Pssm-ID: 273296 [Multi-domain]  Cd Length: 928  Bit Score: 47.09  E-value: 1.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926885  1746 QTAYEVCENVGLLPLEVTRRGYPMDS-AFVGVEVNQVSATVGKDFTVTPSkLLQFDPGMSTKMWNIAITYDGLEEDDEVF 1824
Cdd:TIGR00845  406 PGHYTCLENCGTVALTVVRRGGDLTNtVYVDYRTEDGTANAGSDYEFTEG-TLVFKPGETQKEFRIGIIDDDIFEEDEHF 484

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 568926885  1825 EV------------ILNSPVN---AVLGTQTKAAVKILD 1848
Cdd:TIGR00845  485 YVrlsnlrvgsedgILEANHVsavAQLASPNTATVTILD 523
 
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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