|
Name |
Accession |
Description |
Interval |
E-value |
| PCC |
TIGR00864 |
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ... |
97-2768 |
0e+00 |
|
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: 4844.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 97 DISNNKISTLEEGIFANLFNLSEINLSGNPFECDCGLAWLPRWAEEQQVRVVQPEAATCAGPGSLAGQPLLGIPLLDSGC 176
Cdd:TIGR00864 1 DISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPEAALCAGPGALAGQPLLGIPLLDSGC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 177 GEEYVACLPDNSSGTVAAVS----FSAAHEGLLQPEACSAFCFSTGQGLAALSEQGWCLCGAAQPSSASFACLSLCSGPP 252
Cdd:TIGR00864 81 DEEYVACLKDNSSGGGAARSelviFSAAHEGLFQPEACNAFCFSAGHGLAALGEQGECLCGAAQPSEANFACESLCSGPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 253 PPPAPTCRGPTLLQHVFPASPGATLVGPHGPLASGQLAAFHIAAPLPVTATRWDFGDGSAEVDAAGP----AASHRYVLP 328
Cdd:TIGR00864 161 PPPAAACRGPQLLEHIFPALPGAPIQGPHGPIASGQLAAFHAAAPLAPTAMRWDFGDGSAEVDAAGAggttAASHKYGHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 329 GRYHVTAVLALGAGSALLGTDVQVEAAPAALELVCPSSVQSDESLDLSIQNRGGSGLEAAYSIVALGEEPARAVHPLCPS 408
Cdd:TIGR00864 241 GRYHVSAMGALGAGKALAGGDVQVEAAPAALELHCPSLVQADESLDLSIQNRGGSDLDAAWKITAHGEEPAKASHPHCPK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 409 DTEIFPGNGHCYRLVVEKAAWLQAQEQCQAWAGAALAMVDSPAVQRFLVSRVTRSLD--VWIGFSTVQGVEVGPAPQGEA 486
Cdd:TIGR00864 321 DGEIFEENGHCFQIVPEEAAWLDAQEQCLARAGAALAIVDNDALQNFLARKVTHSLDrgVWIGFSDVNGAEKGPAHQGEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 487 FSLESCQNWLPGEPHPATAEHCVRLGPTGWCNTDLCSAPHSYVCELQPGGPVQDAENLLVGAPSGDLQGPLTPLAQQDGL 566
Cdd:TIGR00864 401 FEAEECEEGLAGEPHPARAEHCVRLDPRGQCNSDLCNAPHAYVCELNPGGPVPDAENFAMGAASFDLHGLLQALAAMDGL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 567 SAP-HEPVEVMVFPGLRLSREAFLTTAEFGTQELRRPAQLRLQVYRL---LSTAGTPENGSEPESRSPDNRTQLAPACMP 642
Cdd:TIGR00864 481 PAPpHEGVEVLLFPALRFSRAAFLSSAEFGTQELRRPAHILFQIYRLrcrLPGAGGPACGPEAECRPPDNRSADAPACMK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 643 GGRWCPGANICLPLDASCHPQACANGCTSGPGLPGAP----YALWREFLFSVPAGPPAQYSVTLHGQDVLMLPGDLVGLQ 718
Cdd:TIGR00864 561 GEQWCPFAHICLPLDAPCHPQACANGCSQGHGLPGAArmplYALQREFLFSLPAGPAAHVLLQDHGEDLLMLPGDLIALQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 719 HDAGPGALLHCSPAPGHPGPRAPYLSANASSWLPH------------------------LPAQLEGTWA----CPACALR 770
Cdd:TIGR00864 641 HDAGPAALIHCQPAPGHPGPRAPVFAANASEWFGHnntpvppdnlagdgadplpdpeldLKALLEGTRAswleCAACAIR 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 771 LLAATEQLTVLLGLRPNPGLRLPGRYEVRAEVGNGVSRHNLSCSFDVVSPVAGLRVIYPAPRDGRLYVPTNGSALVLQVD 850
Cdd:TIGR00864 721 LLAAGEQETRLLGAELNAGLPLPGLYELLAESAKGSDLHNASCSFDVLPPLAGLRVIHPAPQDGRLFLESNGSALLLQVD 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 851 SGANATATARWPGGSVSARFENVCPALVA-------TFVPGCPWETNDTLFSVVALPWLSEGEHV----VDVVVENSASR 919
Cdd:TIGR00864 801 SGANAEAKAFWPGGNSSARFENVCPAEFAsrlchpsTFEGGCAEEAEDSLFAVLALNWLKEGEHTgpvqVDLMAENNASE 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 920 ANLSLRVTAEEPICGLRATPSPEARVLQGVLVRYSPVVEAGSDMVFRWTINDKQSLTFQNVVFNVIYQSAAVFKLSVggr 999
Cdd:TIGR00864 881 ANLSLLVQAEEPICGLRAQPHPAARVLMESLVRYSASVEAGSDMTFKWTIDDKPFFTFQNTVFNVIYQHAAVFKLSL--- 957
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1000 gwggegmgrgragagstftsafcsasccprtlpwlwlTASNHVSNVTVNYNVTVERMNRMQGLQVSTVPAVLSPNATLAL 1079
Cdd:TIGR00864 958 -------------------------------------TAMNHVSNLTEDFNVTVDRLNPMQGLQVKGVPAVLPPGATLAL 1000
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1080 TAGVLVDSAVEVAFLWTFGDGEQALHQFQPPYNESFPVPDPSVAQVLVEHNVMHTYAAPGEYLLTVLASNAFENLTQQVP 1159
Cdd:TIGR00864 1001 TAGVLIDMAVEAAFLWSFGDGEQALFEFKPPYNESFPCPDPSPAQVLLEHNVMHIYAAPGEYLATVLASNAFENISQQIN 1080
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1160 VSVRASLPSVAVGVSDGVLVAGRPVTFYPHPLPSPGGVLYTWDFGDGSPVLTQSQPAANHTYASRGTYHVRLEVNNTVSG 1239
Cdd:TIGR00864 1081 MSVRAILPRVAIGTEDGLLLAGKPADFEAHPLPSPGGIHYEWDFGDGSALLQGRQPAAAHTFAKRGPFHVCLEVNNTISG 1160
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1240 AAAQADVRVFEELRGLSVDMSLAVEQGAPVVVSAAVQTGDNITWTFDMGDGTVLSGPEATVEHVYLRAQNCTVTVGAASP 1319
Cdd:TIGR00864 1161 AAACADMFAFEEIEGLSADMSLATELGAATTVRAALQSGDNITWTFDMGDGKSLSGPEATVEHKYAKAGNCTVNIGAANA 1240
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1320 AGHLARSLHVLVFVLEVLRVEPAACIPTQPDARLTAYVTGNPAHYLFDWTFGDGSSNTTVRGCPTVTHNFTRSGTFPLAL 1399
Cdd:TIGR00864 1241 AGHGARIIHVEVFVFEVAGIEPAACIGEHADANFRARVSGNAAHYLFDWSFGDGSPNETHHGCPGISHNFRGNGTFPLAL 1320
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1400 VLSSRVNRAHYFTSICVEPEVGNVTLQPERQFVQLGDEAWLVACAWPPFPYRYTWDFGTEEAAPTRARGPEVTFIYRDPG 1479
Cdd:TIGR00864 1321 TISSGVNKAHFFTQICVEPELGKISLQAEKQFFALGDEAQFQACAEPEFNYRYEWDFGGEEAAPLPAAGAEVTFIYNDPG 1400
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1480 SYLVTVTASNNISAANDSALVEVQEPVLVTSIKVNGSLG--LELQQPYLFSAVGRGRPASYLWDLGDGGWLEGPEVTHAY 1557
Cdd:TIGR00864 1401 CYLVTVAASNNISAANDSALIEVLEPVGATSFKHNGSHGnnLELGQPYLFSAFGRARNASYLWDFGDGGLLEGPEILHAF 1480
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1558 NSTGDFTVRVAGWNEVSRSEAWLNVTVKRRVRGLVVNASRTVVPLNGSVSFSTSLEAGSDVRYSWVLCDRCTPIPGGPTI 1637
Cdd:TIGR00864 1481 NSPGDFNIRLAAANEVGKNEATLNVAVKARVRGLTINASLTNVPLNGSVHFEAHLDAGDDVRFSWILCDHCTPIFGGNTI 1560
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1638 SYTFRSVGTFNIIVTAENEVGSAQDSIFVYVLQLIEGLQVVGG-------------GRYFPTNHTVQLQAVVRDGTNVSY 1704
Cdd:TIGR00864 1561 FYTFRSVGTFNIIVTAENDVGAAQASIFLFVLQEIEGLQILGEtaegggggvqeldGCYFETNHTVQFHAGFKDGTNLSF 1640
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1705 SWTAWRD---RGPALAGSGKGFSLTVLEAGTYHVQLRATNMLGSAWADCTMDFVEPVGWLMVAASPNPAAVNTSVTLSAE 1781
Cdd:TIGR00864 1641 SWNAILDnepDGPAFAGSGKGAKLNPLEAGPCDIFLQAANLLGQATADCTIDFLEPAGNLMLAASDNPAAVNALINLSAE 1720
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1782 LAGGSGVVYTWSLEEGLSWETSEPFTTHSFPTPGLHLVTMTAGNPLGSANATVEVDVQVPVSGLSIRASEPGGS-FVAAG 1860
Cdd:TIGR00864 1721 LAEGSGLQYRWFLEEGDDLETSEPFMSHSFPSAGLHLVTMKAFNELGSANASEEVDVQEPISGLKIRAADAGEQnFFAAD 1800
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1861 SSVPFWGQLATGTNVSWCWAVPGGSSKRGPHVTMVFPDAGTFSIRLNASNAVSWVSATYNLTAEEPIVGLVLWASSKVVA 1940
Cdd:TIGR00864 1801 SSVCFQGELATGTNVSWCWAIDGGSSKMGKHACMTFPDAGTFAIRLNASNAVSGKSASREFFAEEPIFGLELKASKKIAA 1880
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1941 PGQLVHFQILLAAGSAVTFRLQVGGANPEVL-PGPRFSHSFPRVGDHVVSVRGKNHVSWAQAQVRIVVLEAVSGLQVPNC 2019
Cdd:TIGR00864 1881 IGEKVEFQILLAAGSAVNFRLQIGGAAPEVLqPGPRFSHSFPRVDDHMVNLRAKNEVSCAQANLHIEVLEAVRGLQIPDC 1960
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2020 CEPGIATGTERNFTARVQRGSRVAYAWYFSLQKVQGDSLVILSGRDVTYTPVAAGLLEIQVRAFNALGSENRTLVLEVQD 2099
Cdd:TIGR00864 1961 CAAGIATGEEKNFTANVQRGKPVAFAWTFDLHHLHGDSLVIHMGKDVSYTAEAAGLLEIQLGAFNALGAENITLQLEAQD 2040
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2100 AVQYVALQSGP--CFTNRSAQFEAATSPSPRRVAYHWDFGDGSPGQDTDEPRAEHSYLRPGDYRVQVNASNLVSFFVAQA 2177
Cdd:TIGR00864 2041 ALMDAALQAGPqdCFTNKMAQFEAATSPKPNFMACHWDFGDGSAGQDTDEPRAEHEYLHPGDYRVQVNASNLVSFFSAHA 2120
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2178 TVTVQVLACREPEVDVVLPLQVLMRRSQRNYLEAHVDLRDCVTYQTEYRWEVYRTASCQRPGRPARVALPG--------- 2248
Cdd:TIGR00864 2121 EINVQVLACEEPEVDVVLALQLAIRRSQPNLLEAHVDLKDCLRYGAEYLWEILRAASCDNDGHFARGALNGatrsfpvip 2200
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2249 ----VDVSRPRLVLPRLALPVGHYCFVFVVSFGDTPLTQSIQANVTVAPERLVPIIEGGSYRVWSDTRDLVLDGSESYDP 2324
Cdd:TIGR00864 2201 lpaeVDVQRLQLSLPKLALAAGHYCFVFSLSFEDTPLKKAACANLGVAAARLMPIIEGGSYRVWSDTQDLQLDAEESYDP 2280
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2325 NLEDGDQTPLSFHWACVASTQREAGGCALNFGPRG-SSTVTIPRERLAAGVEYTFSLTVWKAGRKEEATNQTVLIRSGRV 2403
Cdd:TIGR00864 2281 NLDDDDQSLLHFHWACQASSKGEAGCCALNFGLGGkGPTLGIPGEELAAGIEYTFKLSIGKAGMKEEATNQTVLIQSGHI 2360
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2404 PIVSLECVSCKAQAVYEVSRSSYVYLEGRCLNCSSGSKRGRWAARTFSNKTLVLDETTTSTGSAGMRLVLRRGVLRDGEG 2483
Cdd:TIGR00864 2361 PIVSLECVSCKAQALYEVSQNSYVYLEGRCLNCQSGFHRGRWAARTFQNDTLVLDESSTSTGSAGMNLVLRQGVLHDGEG 2440
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2484 YTFTLTVLGRSGEEEGCASIRLSPNRPPLGGSCRLFPLG--------------AVHALTTKVHFECTGWHDAEDAGAPLV 2549
Cdd:TIGR00864 2441 YNFTLHVLDDSGDEEGAASIRLHHNMPPDGGECHLFPGGetgqehgdkedevwAIEALLDKVHFECSGWHDAEDAEAPLL 2520
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2550 YALLLRRCRQGHCEEFCVYKGSLSSYGAVLPPGFR-PHFEVGLAVVVQDQLGAAVVALNRSLAITLPEPNGSATGLTVWL 2628
Cdd:TIGR00864 2521 YALLLNRCRDDHCEEFCVYKGSLPEHGAFLPPGFRsAHFEVGLAITVEDHLGAAIRALNKSIAITLPDPNGEASGLPHWL 2600
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2629 HGLTASVLPGLLRQADPQHVIEYSLALVTVLNEYERALDVAAEPKHERQHRAQIRKNITETLVSLRVHTVDDIQQIAAAL 2708
Cdd:TIGR00864 2601 HDLIASKLKGLLDQADFQHVIELSLALITVLNEYEQALDSAAEPKHERGHRAQIRKNITEALTALDLHTVDDIQQIAAAL 2680
|
2730 2740 2750 2760 2770 2780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2709 AQCMGPSRELVCRSCLKQTLHKLEAMMLILQAETTAGTVTPTAIGDSILNITGDLIHLAS 2768
Cdd:TIGR00864 2681 AQCMAPSREFICEECLKQTLHKLEAMLEILQADTKAGIVTPTAIADNILNIMGDLIHLAS 2740
|
|
| REJ |
pfam02010 |
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ... |
2211-2654 |
9.89e-133 |
|
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor for egg jelly Swiss:Q26627. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains.
Pssm-ID: 366875 [Multi-domain] Cd Length: 448 Bit Score: 425.38 E-value: 9.89e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2211 AHVDLRDCV-TYQTEYRWEVYRTASC---QRPGRPARVALPGVDvsrprlvLPRLALPVGHYCFVFVVSFGDTP-LTQSI 2285
Cdd:pfam02010 1 ASVELNGCFsAYTIDYLWSVFTVSSNlnlQTISSPKDLVLPQLT-------IPSGTLPYGTYVFTLTVSLSSTPsLAGTD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2286 QANVTVAPERLVPIIEGGSYRVWSDTRDLVLDGSESYDPNLEDGDQTPLSFHWACVAST------QREAGGCA-----LN 2354
Cdd:pfam02010 74 IITVTVQPSPLVAVIDGGSSRVVGYNQDLTLDGSESYDPDVDPGSSSGLTYLWSCRRSSsgdnplLNNDPVCFsdqneGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2355 FGPRGSSTVTIPRERLAAGVEYTFSLTVWKAGRKEEATNQTVLIRSGRVPIVSLECVSCKAQAVYEVSRssYVYLEGRCL 2434
Cdd:pfam02010 154 LLQSTSSSLTIPASTLQANVTYTFKLTVSKGSRNSASTTQTILVVDGNPPIIILSCISNCNRKNNPVDR--LVLLASTCL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2435 NCSSGSKRG--RWAARTFSNKTLVLD--ETTTSTGSAGMRLVLRRGVLRDGEGYTFTLTVLGRSGEEEGCASIRLSPNRP 2510
Cdd:pfam02010 232 NCSSDLSDVtyRWLSLGSENTSLVLDqlNSQTSTGRSGPYLVIKAGVLQSGVSYRFTLIVTVYPGLVSGLASISFITNAP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2511 PLGGSCRLFPLGAvHALTTKVHFECTGWHDAEDagaPLVYALLLRRCRQGHCEEFCVYKGSLS-SYGAVLPPGFRPH-FE 2588
Cdd:pfam02010 312 PTGGTCSVTPTEG-TALETKFTVTCQGWTDDDL---PLTYQFGDISFREASEEWFLLYEGSSQiSISTFLPPGLPANdYQ 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370468559 2589 VGLAVVVQDQLGAAvVALNRSLAITLPEPNGSatglTVWLHGLTASVLPGLLRQADPQHVIEYSLA 2654
Cdd:pfam02010 388 VTVVVVVYDSLGAA-TSVSLTITVTPPSSSDE----LLYFLLGTTSDLSALLQSGDPQQAAQLILA 448
|
|
| PLAT_polycystin |
cd01752 |
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ... |
3158-3277 |
9.70e-58 |
|
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: 196.34 E-value: 9.70e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 3158 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLDGD--RAFHRNSLDIFRIATPHSLGSVWKIRVWHDNKGLSPAW 3235
Cdd:cd01752 1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPekPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1370468559 3236 FLQHVIVRDLQTARSAFFLVNDWLSVETEanGGLVEKEVLAA 3277
Cdd:cd01752 81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEG--DGTVERTFPVA 120
|
|
| Polycystin_dom |
pfam20519 |
Polycystin domain; This domain represents the polycystin domain from group II of Transient ... |
3753-3931 |
5.40e-56 |
|
Polycystin domain; This domain represents the polycystin domain from group II of Transient receptor potential (TRP) channels (TRPP) including PKD1, PKD2, PKD2L and mucolipins. The polycystin domain display a sandwich-like shape with five beta-sheets in the tilted middle layer, three alpha-helices on one side and a large loop with two short antiparallel beta-sheets on the other.
Pssm-ID: 466668 Cd Length: 199 Bit Score: 194.56 E-value: 5.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 3753 AFLAITRSEELWPWMAHVLLPYVHGNQS------------SPELGPPRLRQVRLQEA--LYPDPPGPRVHTCSAAGGFST 3818
Cdd:pfam20519 1 GLLTVTDLDDIWDWLSSVLLPALHSNKTpsglpgsfiayeSLLLGVPRLRQLRVRNSscLVHDKFVREINECHAGYSPPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 3819 SDY----DVGWESPHNGSGTW-AYSAPDLL-GAWSWGSCAVYDSGGYVQELGLSLEESRDRLRFLQLHNWLDNRSRAVFL 3892
Cdd:pfam20519 81 EDRklysALPYKPVHYGSKYWfIYTPPGLLmGYDHWGHLASYPSGGYVVLLPSSREESLKRLAYLQDNNWLDRGTRAVFV 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1370468559 3893 ELTRYSPAVGLHAAVTLRLEFPAAGRALAALSVRPFALR 3931
Cdd:pfam20519 161 DFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVKLL 199
|
|
| PKD_channel |
pfam08016 |
Polycystin cation channel; This family contains the cation channel region from group II of ... |
3932-4153 |
7.50e-44 |
|
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: 160.52 E-value: 7.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 3932 RLSAGLSLPLLT-SVCLLLFAVHFAVAEARTWHREGR------WRVLRLgawarwLLVALTAATALVRLAQLGAADRQWT 4004
Cdd:pfam08016 1 RYVTNRSLFILLcEIVFVVFFLYFVVEEILKIRKHRPsylrsvWNLLDL------AIVILSVVLIVLNIYRDFLADRLIK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 4005 rFVRGRPRRFTSFDQVAQLSSAARGLAASLLFLLLVKAAQQLRFVRQWSVFGKTLCRALPELLGVTLGLVVLGVAYAQLA 4084
Cdd:pfam08016 75 -SVEASPVTFIDFDRVAQLDNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370468559 4085 ILLVSSCVDSLWSVAQALLVLCPgtglsTLCPAESWH--------LSPLLCVGLWALRLWGALRLGAVILRWRYHAL 4153
Cdd:pfam08016 154 YLLFGTQAPNFSNFVKSILTLFR-----TILGDFGYNeifsgnrvLGPLLFLTFVFLVIFILLNLFLAIINDSYVEV 225
|
|
| WSC |
smart00321 |
present in yeast cell wall integrity and stress response component proteins; Domain present in ... |
177-271 |
3.51e-24 |
|
present in yeast cell wall integrity and stress response component proteins; Domain present in WSC proteins, polycystin and fungal exoglucanase
Pssm-ID: 214616 [Multi-domain] Cd Length: 95 Bit Score: 99.47 E-value: 3.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 177 GEEYVACLPDNSSGTVAAVSFSAAHegLLQPEACSAFCFSTGQGLAALSEQGWCLCGAAQPSSA-----SFACLSLCSGp 251
Cdd:smart00321 1 GATYVGCYSDNSSRTLAAVSSYAYH--NMSVEACSNFCFSAGYALAALENGNECYCGDSLPSTSvsasdSSQCSTTCSG- 77
|
90 100
....*....|....*....|
gi 1370468559 252 ppPPAPTCRGPTLLQHVFPA 271
Cdd:smart00321 78 --YPAEVCGGPNRLSVYVLA 95
|
|
| PLAT |
pfam01477 |
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ... |
3160-3263 |
2.86e-23 |
|
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: 97.50 E-value: 2.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 3160 YEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLDGDR-AFHRNSLDIFRIATPHSLGSVWKIRVWHDNKGLSPAWFLQ 3238
Cdd:pfam01477 1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNpDFERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEWFLK 80
|
90 100
....*....|....*....|....*.
gi 1370468559 3239 HVIV-RDLQTARSAFFLVNDWLSVET 3263
Cdd:pfam01477 81 SITVeVPGETGGKYTFPCNSWVYGSK 106
|
|
| LH2 |
smart00308 |
Lipoxygenase homology 2 (beta barrel) domain; |
3158-3260 |
1.97e-19 |
|
Lipoxygenase homology 2 (beta barrel) domain;
Pssm-ID: 214608 [Multi-domain] Cd Length: 105 Bit Score: 86.16 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 3158 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLD--GDRAFHRNSLDIFRIATPHSLGSVWKIRVWHDNKglSPAW 3235
Cdd:smart00308 1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDylFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR--HPEW 78
|
90 100
....*....|....*....|....*
gi 1370468559 3236 FLQHVIVRDLQTARSAFFLVNDWLS 3260
Cdd:smart00308 79 FLKSITVKDLPTGGKYHFPCNSWVY 103
|
|
| CLECT |
cd00037 |
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ... |
418-531 |
1.02e-16 |
|
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: 78.82 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 418 HCYRLVVEKAAWLQAQEQCQAWaGAALAMVDSPAVQRFLVSRVTRSL--DVWIGFSTVQGVEVGPAPQGEAFSleSCQNW 495
Cdd:cd00037 1 SCYKFSTEKLTWEEAQEYCRSL-GGHLASIHSEEENDFLASLLKKSSssDVWIGLNDLSSEGTWKWSDGSPLV--DYTNW 77
|
90 100 110
....*....|....*....|....*....|....*...
gi 1370468559 496 LPGEPHPATAEHCVRL--GPTGWCNTDLCSAPHSYVCE 531
Cdd:cd00037 78 APGEPNPGGSEDCVVLssSSDGKWNDVSCSSKLPFICE 115
|
|
| COG3291 |
COG3291 |
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
1509-1815 |
1.11e-12 |
|
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 72.78 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1509 TSIKVNGSLGLELQqpylFSAVGRGRPASYLWDLGDGGWLEGPEVTHAYNSTGDFTVRVAGWNEV-SRSEAWLNVTVKRR 1587
Cdd:COG3291 2 TATPTSGCAPLTVQ----FTDTSSGNATSYEWDFGDGTTSTEANPSHTYTTPGTYTVTLTVTDAAgCSDTTTKTITVGAP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1588 VRGLVVNASRTVVPLNGSVSFSTSLEAGSDVrYSWVLCDRCTPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQDSIFVY 1667
Cdd:COG3291 78 NPGVTTVTTSTTVTTLANTANGGATTVVAGS-TVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1668 VLQLIEGLQVVGGGRYFPTNHTVQLQAVVRDGTNVSYSWTAWRDRGPALAGSGKGFSLTVLEAGTYHVQLRATNMLGSAW 1747
Cdd:COG3291 157 TSVSTTDVTSDGTTSASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDVTLT 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370468559 1748 ADCTMDFVEPVGWLMVAASPNPAAVNTSVTLSAELAGGSGVVYTWSLEEGLSWETSEPFTTHSFPTPG 1815
Cdd:COG3291 237 GISTGDAGTPGTNTVTTSGANTAGTSTITGGTSGVVTTSAATGTSTNGTGGLGTTTAITPGNVSTTAD 304
|
|
| GPS |
smart00303 |
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ... |
3051-3100 |
3.65e-10 |
|
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: 57.78 E-value: 3.65e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1370468559 3051 YTSLCQYFSEEDMVWRTEGLLPLEETSpRQAVCLTRHLTAFGASLFVPPS 3100
Cdd:smart00303 1 FNPICVFWDESSGEWSTRGCELLETNG-THTTCSCNHLTTFAVLMDVPPI 49
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
54-127 |
6.41e-09 |
|
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.
Pssm-ID: 411060 [Multi-domain] Cd Length: 220 Bit Score: 59.41 E-value: 6.41e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370468559 54 RGLRTLGPALRIpadataLDVSHNLLRALDVglLANLSALAELDISNNKISTLEE--GIFANLFNLSEINLSGNPF 127
Cdd:cd21340 113 RSLAALSNSLRV------LNISGNNIDSLEP--LAPLRNLEQLDASNNQISDLEEllDLLSSWPSLRELDLTGNPV 180
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
48-128 |
4.88e-08 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 58.79 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 48 RVNCSGRGLRTLGPALRIPADATALDVSHNLLRALDVGLlANLSALAELDISNNKISTLEEGIfANLFNLSEINLSGNPF 127
Cdd:COG4886 117 SLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPL-GNLTNLKSLDLSNNQLTDLPEEL-GNLTNLKELDLSNNQI 194
|
.
gi 1370468559 128 E 128
Cdd:COG4886 195 T 195
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
496-791 |
3.67e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 47.24 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 496 LPGEPHPATAEHCVrlgPTGWCnTDLCSAPHSYVCELQPGGPVQDAENLLVGAPSGDLQGPLTPLA-----------QQD 564
Cdd:PHA03247 2555 LPPAAPPAAPDRSV---PPPRP-APRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPlppdthapdppPPS 2630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 565 GLSAPHEPVEVMVFPGL------------------RLSREAFLTTAEFGTQELRRPAqLRLQVYRLLSTAGTPENGSEPE 626
Cdd:PHA03247 2631 PSPAANEPDPHPPPTVPpperprddpapgrvsrprRARRLGRAAQASSPPQRPRRRA-ARPTVGSLTSLADPPPPPPTPE 2709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 627 SRsPDNRTQLAPAcMPGGRWCPGANICLPLDASCHPQACANGCTSGPGLPGAPYALWREFLFSVPAGPP----------- 695
Cdd:PHA03247 2710 PA-PHALVSATPL-PPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAagpprrltrpa 2787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 696 -AQYSVTLHGQDVLMLPGDLVGLQHDAGPGALLHCSPAPGHPGPRAPYLSANASSWLPHLPAQLEGTWACPACALRLLAA 774
Cdd:PHA03247 2788 vASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPP 2867
|
330
....*....|....*..
gi 1370468559 775 TEQLTVLLGLRPNPGLR 791
Cdd:PHA03247 2868 SRSPAAKPAAPARPPVR 2884
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PCC |
TIGR00864 |
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ... |
97-2768 |
0e+00 |
|
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: 4844.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 97 DISNNKISTLEEGIFANLFNLSEINLSGNPFECDCGLAWLPRWAEEQQVRVVQPEAATCAGPGSLAGQPLLGIPLLDSGC 176
Cdd:TIGR00864 1 DISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPEAALCAGPGALAGQPLLGIPLLDSGC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 177 GEEYVACLPDNSSGTVAAVS----FSAAHEGLLQPEACSAFCFSTGQGLAALSEQGWCLCGAAQPSSASFACLSLCSGPP 252
Cdd:TIGR00864 81 DEEYVACLKDNSSGGGAARSelviFSAAHEGLFQPEACNAFCFSAGHGLAALGEQGECLCGAAQPSEANFACESLCSGPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 253 PPPAPTCRGPTLLQHVFPASPGATLVGPHGPLASGQLAAFHIAAPLPVTATRWDFGDGSAEVDAAGP----AASHRYVLP 328
Cdd:TIGR00864 161 PPPAAACRGPQLLEHIFPALPGAPIQGPHGPIASGQLAAFHAAAPLAPTAMRWDFGDGSAEVDAAGAggttAASHKYGHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 329 GRYHVTAVLALGAGSALLGTDVQVEAAPAALELVCPSSVQSDESLDLSIQNRGGSGLEAAYSIVALGEEPARAVHPLCPS 408
Cdd:TIGR00864 241 GRYHVSAMGALGAGKALAGGDVQVEAAPAALELHCPSLVQADESLDLSIQNRGGSDLDAAWKITAHGEEPAKASHPHCPK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 409 DTEIFPGNGHCYRLVVEKAAWLQAQEQCQAWAGAALAMVDSPAVQRFLVSRVTRSLD--VWIGFSTVQGVEVGPAPQGEA 486
Cdd:TIGR00864 321 DGEIFEENGHCFQIVPEEAAWLDAQEQCLARAGAALAIVDNDALQNFLARKVTHSLDrgVWIGFSDVNGAEKGPAHQGEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 487 FSLESCQNWLPGEPHPATAEHCVRLGPTGWCNTDLCSAPHSYVCELQPGGPVQDAENLLVGAPSGDLQGPLTPLAQQDGL 566
Cdd:TIGR00864 401 FEAEECEEGLAGEPHPARAEHCVRLDPRGQCNSDLCNAPHAYVCELNPGGPVPDAENFAMGAASFDLHGLLQALAAMDGL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 567 SAP-HEPVEVMVFPGLRLSREAFLTTAEFGTQELRRPAQLRLQVYRL---LSTAGTPENGSEPESRSPDNRTQLAPACMP 642
Cdd:TIGR00864 481 PAPpHEGVEVLLFPALRFSRAAFLSSAEFGTQELRRPAHILFQIYRLrcrLPGAGGPACGPEAECRPPDNRSADAPACMK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 643 GGRWCPGANICLPLDASCHPQACANGCTSGPGLPGAP----YALWREFLFSVPAGPPAQYSVTLHGQDVLMLPGDLVGLQ 718
Cdd:TIGR00864 561 GEQWCPFAHICLPLDAPCHPQACANGCSQGHGLPGAArmplYALQREFLFSLPAGPAAHVLLQDHGEDLLMLPGDLIALQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 719 HDAGPGALLHCSPAPGHPGPRAPYLSANASSWLPH------------------------LPAQLEGTWA----CPACALR 770
Cdd:TIGR00864 641 HDAGPAALIHCQPAPGHPGPRAPVFAANASEWFGHnntpvppdnlagdgadplpdpeldLKALLEGTRAswleCAACAIR 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 771 LLAATEQLTVLLGLRPNPGLRLPGRYEVRAEVGNGVSRHNLSCSFDVVSPVAGLRVIYPAPRDGRLYVPTNGSALVLQVD 850
Cdd:TIGR00864 721 LLAAGEQETRLLGAELNAGLPLPGLYELLAESAKGSDLHNASCSFDVLPPLAGLRVIHPAPQDGRLFLESNGSALLLQVD 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 851 SGANATATARWPGGSVSARFENVCPALVA-------TFVPGCPWETNDTLFSVVALPWLSEGEHV----VDVVVENSASR 919
Cdd:TIGR00864 801 SGANAEAKAFWPGGNSSARFENVCPAEFAsrlchpsTFEGGCAEEAEDSLFAVLALNWLKEGEHTgpvqVDLMAENNASE 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 920 ANLSLRVTAEEPICGLRATPSPEARVLQGVLVRYSPVVEAGSDMVFRWTINDKQSLTFQNVVFNVIYQSAAVFKLSVggr 999
Cdd:TIGR00864 881 ANLSLLVQAEEPICGLRAQPHPAARVLMESLVRYSASVEAGSDMTFKWTIDDKPFFTFQNTVFNVIYQHAAVFKLSL--- 957
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1000 gwggegmgrgragagstftsafcsasccprtlpwlwlTASNHVSNVTVNYNVTVERMNRMQGLQVSTVPAVLSPNATLAL 1079
Cdd:TIGR00864 958 -------------------------------------TAMNHVSNLTEDFNVTVDRLNPMQGLQVKGVPAVLPPGATLAL 1000
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1080 TAGVLVDSAVEVAFLWTFGDGEQALHQFQPPYNESFPVPDPSVAQVLVEHNVMHTYAAPGEYLLTVLASNAFENLTQQVP 1159
Cdd:TIGR00864 1001 TAGVLIDMAVEAAFLWSFGDGEQALFEFKPPYNESFPCPDPSPAQVLLEHNVMHIYAAPGEYLATVLASNAFENISQQIN 1080
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1160 VSVRASLPSVAVGVSDGVLVAGRPVTFYPHPLPSPGGVLYTWDFGDGSPVLTQSQPAANHTYASRGTYHVRLEVNNTVSG 1239
Cdd:TIGR00864 1081 MSVRAILPRVAIGTEDGLLLAGKPADFEAHPLPSPGGIHYEWDFGDGSALLQGRQPAAAHTFAKRGPFHVCLEVNNTISG 1160
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1240 AAAQADVRVFEELRGLSVDMSLAVEQGAPVVVSAAVQTGDNITWTFDMGDGTVLSGPEATVEHVYLRAQNCTVTVGAASP 1319
Cdd:TIGR00864 1161 AAACADMFAFEEIEGLSADMSLATELGAATTVRAALQSGDNITWTFDMGDGKSLSGPEATVEHKYAKAGNCTVNIGAANA 1240
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1320 AGHLARSLHVLVFVLEVLRVEPAACIPTQPDARLTAYVTGNPAHYLFDWTFGDGSSNTTVRGCPTVTHNFTRSGTFPLAL 1399
Cdd:TIGR00864 1241 AGHGARIIHVEVFVFEVAGIEPAACIGEHADANFRARVSGNAAHYLFDWSFGDGSPNETHHGCPGISHNFRGNGTFPLAL 1320
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1400 VLSSRVNRAHYFTSICVEPEVGNVTLQPERQFVQLGDEAWLVACAWPPFPYRYTWDFGTEEAAPTRARGPEVTFIYRDPG 1479
Cdd:TIGR00864 1321 TISSGVNKAHFFTQICVEPELGKISLQAEKQFFALGDEAQFQACAEPEFNYRYEWDFGGEEAAPLPAAGAEVTFIYNDPG 1400
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1480 SYLVTVTASNNISAANDSALVEVQEPVLVTSIKVNGSLG--LELQQPYLFSAVGRGRPASYLWDLGDGGWLEGPEVTHAY 1557
Cdd:TIGR00864 1401 CYLVTVAASNNISAANDSALIEVLEPVGATSFKHNGSHGnnLELGQPYLFSAFGRARNASYLWDFGDGGLLEGPEILHAF 1480
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1558 NSTGDFTVRVAGWNEVSRSEAWLNVTVKRRVRGLVVNASRTVVPLNGSVSFSTSLEAGSDVRYSWVLCDRCTPIPGGPTI 1637
Cdd:TIGR00864 1481 NSPGDFNIRLAAANEVGKNEATLNVAVKARVRGLTINASLTNVPLNGSVHFEAHLDAGDDVRFSWILCDHCTPIFGGNTI 1560
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1638 SYTFRSVGTFNIIVTAENEVGSAQDSIFVYVLQLIEGLQVVGG-------------GRYFPTNHTVQLQAVVRDGTNVSY 1704
Cdd:TIGR00864 1561 FYTFRSVGTFNIIVTAENDVGAAQASIFLFVLQEIEGLQILGEtaegggggvqeldGCYFETNHTVQFHAGFKDGTNLSF 1640
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1705 SWTAWRD---RGPALAGSGKGFSLTVLEAGTYHVQLRATNMLGSAWADCTMDFVEPVGWLMVAASPNPAAVNTSVTLSAE 1781
Cdd:TIGR00864 1641 SWNAILDnepDGPAFAGSGKGAKLNPLEAGPCDIFLQAANLLGQATADCTIDFLEPAGNLMLAASDNPAAVNALINLSAE 1720
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1782 LAGGSGVVYTWSLEEGLSWETSEPFTTHSFPTPGLHLVTMTAGNPLGSANATVEVDVQVPVSGLSIRASEPGGS-FVAAG 1860
Cdd:TIGR00864 1721 LAEGSGLQYRWFLEEGDDLETSEPFMSHSFPSAGLHLVTMKAFNELGSANASEEVDVQEPISGLKIRAADAGEQnFFAAD 1800
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1861 SSVPFWGQLATGTNVSWCWAVPGGSSKRGPHVTMVFPDAGTFSIRLNASNAVSWVSATYNLTAEEPIVGLVLWASSKVVA 1940
Cdd:TIGR00864 1801 SSVCFQGELATGTNVSWCWAIDGGSSKMGKHACMTFPDAGTFAIRLNASNAVSGKSASREFFAEEPIFGLELKASKKIAA 1880
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1941 PGQLVHFQILLAAGSAVTFRLQVGGANPEVL-PGPRFSHSFPRVGDHVVSVRGKNHVSWAQAQVRIVVLEAVSGLQVPNC 2019
Cdd:TIGR00864 1881 IGEKVEFQILLAAGSAVNFRLQIGGAAPEVLqPGPRFSHSFPRVDDHMVNLRAKNEVSCAQANLHIEVLEAVRGLQIPDC 1960
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2020 CEPGIATGTERNFTARVQRGSRVAYAWYFSLQKVQGDSLVILSGRDVTYTPVAAGLLEIQVRAFNALGSENRTLVLEVQD 2099
Cdd:TIGR00864 1961 CAAGIATGEEKNFTANVQRGKPVAFAWTFDLHHLHGDSLVIHMGKDVSYTAEAAGLLEIQLGAFNALGAENITLQLEAQD 2040
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2100 AVQYVALQSGP--CFTNRSAQFEAATSPSPRRVAYHWDFGDGSPGQDTDEPRAEHSYLRPGDYRVQVNASNLVSFFVAQA 2177
Cdd:TIGR00864 2041 ALMDAALQAGPqdCFTNKMAQFEAATSPKPNFMACHWDFGDGSAGQDTDEPRAEHEYLHPGDYRVQVNASNLVSFFSAHA 2120
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2178 TVTVQVLACREPEVDVVLPLQVLMRRSQRNYLEAHVDLRDCVTYQTEYRWEVYRTASCQRPGRPARVALPG--------- 2248
Cdd:TIGR00864 2121 EINVQVLACEEPEVDVVLALQLAIRRSQPNLLEAHVDLKDCLRYGAEYLWEILRAASCDNDGHFARGALNGatrsfpvip 2200
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2249 ----VDVSRPRLVLPRLALPVGHYCFVFVVSFGDTPLTQSIQANVTVAPERLVPIIEGGSYRVWSDTRDLVLDGSESYDP 2324
Cdd:TIGR00864 2201 lpaeVDVQRLQLSLPKLALAAGHYCFVFSLSFEDTPLKKAACANLGVAAARLMPIIEGGSYRVWSDTQDLQLDAEESYDP 2280
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2325 NLEDGDQTPLSFHWACVASTQREAGGCALNFGPRG-SSTVTIPRERLAAGVEYTFSLTVWKAGRKEEATNQTVLIRSGRV 2403
Cdd:TIGR00864 2281 NLDDDDQSLLHFHWACQASSKGEAGCCALNFGLGGkGPTLGIPGEELAAGIEYTFKLSIGKAGMKEEATNQTVLIQSGHI 2360
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2404 PIVSLECVSCKAQAVYEVSRSSYVYLEGRCLNCSSGSKRGRWAARTFSNKTLVLDETTTSTGSAGMRLVLRRGVLRDGEG 2483
Cdd:TIGR00864 2361 PIVSLECVSCKAQALYEVSQNSYVYLEGRCLNCQSGFHRGRWAARTFQNDTLVLDESSTSTGSAGMNLVLRQGVLHDGEG 2440
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2484 YTFTLTVLGRSGEEEGCASIRLSPNRPPLGGSCRLFPLG--------------AVHALTTKVHFECTGWHDAEDAGAPLV 2549
Cdd:TIGR00864 2441 YNFTLHVLDDSGDEEGAASIRLHHNMPPDGGECHLFPGGetgqehgdkedevwAIEALLDKVHFECSGWHDAEDAEAPLL 2520
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2550 YALLLRRCRQGHCEEFCVYKGSLSSYGAVLPPGFR-PHFEVGLAVVVQDQLGAAVVALNRSLAITLPEPNGSATGLTVWL 2628
Cdd:TIGR00864 2521 YALLLNRCRDDHCEEFCVYKGSLPEHGAFLPPGFRsAHFEVGLAITVEDHLGAAIRALNKSIAITLPDPNGEASGLPHWL 2600
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2629 HGLTASVLPGLLRQADPQHVIEYSLALVTVLNEYERALDVAAEPKHERQHRAQIRKNITETLVSLRVHTVDDIQQIAAAL 2708
Cdd:TIGR00864 2601 HDLIASKLKGLLDQADFQHVIELSLALITVLNEYEQALDSAAEPKHERGHRAQIRKNITEALTALDLHTVDDIQQIAAAL 2680
|
2730 2740 2750 2760 2770 2780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2709 AQCMGPSRELVCRSCLKQTLHKLEAMMLILQAETTAGTVTPTAIGDSILNITGDLIHLAS 2768
Cdd:TIGR00864 2681 AQCMAPSREFICEECLKQTLHKLEAMLEILQADTKAGIVTPTAIADNILNIMGDLIHLAS 2740
|
|
| REJ |
pfam02010 |
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ... |
2211-2654 |
9.89e-133 |
|
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor for egg jelly Swiss:Q26627. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains.
Pssm-ID: 366875 [Multi-domain] Cd Length: 448 Bit Score: 425.38 E-value: 9.89e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2211 AHVDLRDCV-TYQTEYRWEVYRTASC---QRPGRPARVALPGVDvsrprlvLPRLALPVGHYCFVFVVSFGDTP-LTQSI 2285
Cdd:pfam02010 1 ASVELNGCFsAYTIDYLWSVFTVSSNlnlQTISSPKDLVLPQLT-------IPSGTLPYGTYVFTLTVSLSSTPsLAGTD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2286 QANVTVAPERLVPIIEGGSYRVWSDTRDLVLDGSESYDPNLEDGDQTPLSFHWACVAST------QREAGGCA-----LN 2354
Cdd:pfam02010 74 IITVTVQPSPLVAVIDGGSSRVVGYNQDLTLDGSESYDPDVDPGSSSGLTYLWSCRRSSsgdnplLNNDPVCFsdqneGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2355 FGPRGSSTVTIPRERLAAGVEYTFSLTVWKAGRKEEATNQTVLIRSGRVPIVSLECVSCKAQAVYEVSRssYVYLEGRCL 2434
Cdd:pfam02010 154 LLQSTSSSLTIPASTLQANVTYTFKLTVSKGSRNSASTTQTILVVDGNPPIIILSCISNCNRKNNPVDR--LVLLASTCL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2435 NCSSGSKRG--RWAARTFSNKTLVLD--ETTTSTGSAGMRLVLRRGVLRDGEGYTFTLTVLGRSGEEEGCASIRLSPNRP 2510
Cdd:pfam02010 232 NCSSDLSDVtyRWLSLGSENTSLVLDqlNSQTSTGRSGPYLVIKAGVLQSGVSYRFTLIVTVYPGLVSGLASISFITNAP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2511 PLGGSCRLFPLGAvHALTTKVHFECTGWHDAEDagaPLVYALLLRRCRQGHCEEFCVYKGSLS-SYGAVLPPGFRPH-FE 2588
Cdd:pfam02010 312 PTGGTCSVTPTEG-TALETKFTVTCQGWTDDDL---PLTYQFGDISFREASEEWFLLYEGSSQiSISTFLPPGLPANdYQ 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370468559 2589 VGLAVVVQDQLGAAvVALNRSLAITLPEPNGSatglTVWLHGLTASVLPGLLRQADPQHVIEYSLA 2654
Cdd:pfam02010 388 VTVVVVVYDSLGAA-TSVSLTITVTPPSSSDE----LLYFLLGTTSDLSALLQSGDPQQAAQLILA 448
|
|
| PLAT_polycystin |
cd01752 |
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ... |
3158-3277 |
9.70e-58 |
|
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: 196.34 E-value: 9.70e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 3158 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLDGD--RAFHRNSLDIFRIATPHSLGSVWKIRVWHDNKGLSPAW 3235
Cdd:cd01752 1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPekPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1370468559 3236 FLQHVIVRDLQTARSAFFLVNDWLSVETEanGGLVEKEVLAA 3277
Cdd:cd01752 81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEG--DGTVERTFPVA 120
|
|
| Polycystin_dom |
pfam20519 |
Polycystin domain; This domain represents the polycystin domain from group II of Transient ... |
3753-3931 |
5.40e-56 |
|
Polycystin domain; This domain represents the polycystin domain from group II of Transient receptor potential (TRP) channels (TRPP) including PKD1, PKD2, PKD2L and mucolipins. The polycystin domain display a sandwich-like shape with five beta-sheets in the tilted middle layer, three alpha-helices on one side and a large loop with two short antiparallel beta-sheets on the other.
Pssm-ID: 466668 Cd Length: 199 Bit Score: 194.56 E-value: 5.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 3753 AFLAITRSEELWPWMAHVLLPYVHGNQS------------SPELGPPRLRQVRLQEA--LYPDPPGPRVHTCSAAGGFST 3818
Cdd:pfam20519 1 GLLTVTDLDDIWDWLSSVLLPALHSNKTpsglpgsfiayeSLLLGVPRLRQLRVRNSscLVHDKFVREINECHAGYSPPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 3819 SDY----DVGWESPHNGSGTW-AYSAPDLL-GAWSWGSCAVYDSGGYVQELGLSLEESRDRLRFLQLHNWLDNRSRAVFL 3892
Cdd:pfam20519 81 EDRklysALPYKPVHYGSKYWfIYTPPGLLmGYDHWGHLASYPSGGYVVLLPSSREESLKRLAYLQDNNWLDRGTRAVFV 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1370468559 3893 ELTRYSPAVGLHAAVTLRLEFPAAGRALAALSVRPFALR 3931
Cdd:pfam20519 161 DFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVKLL 199
|
|
| PKD_channel |
pfam08016 |
Polycystin cation channel; This family contains the cation channel region from group II of ... |
3932-4153 |
7.50e-44 |
|
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: 160.52 E-value: 7.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 3932 RLSAGLSLPLLT-SVCLLLFAVHFAVAEARTWHREGR------WRVLRLgawarwLLVALTAATALVRLAQLGAADRQWT 4004
Cdd:pfam08016 1 RYVTNRSLFILLcEIVFVVFFLYFVVEEILKIRKHRPsylrsvWNLLDL------AIVILSVVLIVLNIYRDFLADRLIK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 4005 rFVRGRPRRFTSFDQVAQLSSAARGLAASLLFLLLVKAAQQLRFVRQWSVFGKTLCRALPELLGVTLGLVVLGVAYAQLA 4084
Cdd:pfam08016 75 -SVEASPVTFIDFDRVAQLDNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370468559 4085 ILLVSSCVDSLWSVAQALLVLCPgtglsTLCPAESWH--------LSPLLCVGLWALRLWGALRLGAVILRWRYHAL 4153
Cdd:pfam08016 154 YLLFGTQAPNFSNFVKSILTLFR-----TILGDFGYNeifsgnrvLGPLLFLTFVFLVIFILLNLFLAIINDSYVEV 225
|
|
| PLAT_repeat |
cd01756 |
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ... |
3158-3277 |
6.31e-28 |
|
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: 111.11 E-value: 6.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 3158 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLD---GDRAFHRNSLDIFRIATPhSLGSVWKIRVWHDNKGLSPA 3234
Cdd:cd01756 1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKksnNKNKFERGQTDKFTVEAV-DLGKLKKIRIGHDNSGLGAG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1370468559 3235 WFLQHVIVRDLQTARSAFFLVNDWLSveTEANGGLVEKEVLAA 3277
Cdd:cd01756 80 WFLDKVEIREPGTGDEYTFPCNRWLD--KDEDDGQIVRELYPS 120
|
|
| WSC |
smart00321 |
present in yeast cell wall integrity and stress response component proteins; Domain present in ... |
177-271 |
3.51e-24 |
|
present in yeast cell wall integrity and stress response component proteins; Domain present in WSC proteins, polycystin and fungal exoglucanase
Pssm-ID: 214616 [Multi-domain] Cd Length: 95 Bit Score: 99.47 E-value: 3.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 177 GEEYVACLPDNSSGTVAAVSFSAAHegLLQPEACSAFCFSTGQGLAALSEQGWCLCGAAQPSSA-----SFACLSLCSGp 251
Cdd:smart00321 1 GATYVGCYSDNSSRTLAAVSSYAYH--NMSVEACSNFCFSAGYALAALENGNECYCGDSLPSTSvsasdSSQCSTTCSG- 77
|
90 100
....*....|....*....|
gi 1370468559 252 ppPPAPTCRGPTLLQHVFPA 271
Cdd:smart00321 78 --YPAEVCGGPNRLSVYVLA 95
|
|
| PLAT |
pfam01477 |
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ... |
3160-3263 |
2.86e-23 |
|
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: 97.50 E-value: 2.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 3160 YEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLDGDR-AFHRNSLDIFRIATPHSLGSVWKIRVWHDNKGLSPAWFLQ 3238
Cdd:pfam01477 1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNpDFERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEWFLK 80
|
90 100
....*....|....*....|....*.
gi 1370468559 3239 HVIV-RDLQTARSAFFLVNDWLSVET 3263
Cdd:pfam01477 81 SITVeVPGETGGKYTFPCNSWVYGSK 106
|
|
| LH2 |
smart00308 |
Lipoxygenase homology 2 (beta barrel) domain; |
3158-3260 |
1.97e-19 |
|
Lipoxygenase homology 2 (beta barrel) domain;
Pssm-ID: 214608 [Multi-domain] Cd Length: 105 Bit Score: 86.16 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 3158 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLD--GDRAFHRNSLDIFRIATPHSLGSVWKIRVWHDNKglSPAW 3235
Cdd:smart00308 1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDylFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR--HPEW 78
|
90 100
....*....|....*....|....*
gi 1370468559 3236 FLQHVIVRDLQTARSAFFLVNDWLS 3260
Cdd:smart00308 79 FLKSITVKDLPTGGKYHFPCNSWVY 103
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1763-1832 |
1.41e-17 |
|
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.
Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 79.74 E-value: 1.41e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1763 VAASPNPAAVNTSVTLSAELAGGSGVVYTWSLEEGLSWETSEPFTTHSFPTPGLHLVTMTAGNPLGSANA 1832
Cdd:pfam00801 1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
|
|
| CLECT |
smart00034 |
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ... |
406-531 |
1.52e-17 |
|
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: 81.49 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 406 CPSDTEIFpgNGHCYRLVVEKAAWLQAQEQCQAwAGAALAMVDSPAVQRFL---VSRVTRSLDVWIGFSTVQGVEVGPAP 482
Cdd:smart00034 1 CPSGWISY--GGKCYKFSTEKKTWEDAQAFCQS-LGGHLASIHSEAENDFVaslLKNSGSSDYYWIGLSDPDSNGSWQWS 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1370468559 483 QGeaFSLESCQNWLPGEPhPATAEHCVRLGPTGWC-NTDLCSAPHSYVCE 531
Cdd:smart00034 78 DG--SGPVSYSNWAPGEP-NNSSGDCVVLSTSGGKwNDVSCTSKLPFVCE 124
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1168-1249 |
6.69e-17 |
|
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.
Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 78.26 E-value: 6.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1168 SVAVGVSDGVLVAGRPVTFYPHPLPSPGGVLYTWDFGDGSpvlTQSQPAANHTYASRGTYHVRLEVNNTVSGAAAQADVR 1247
Cdd:smart00089 1 VADVSASPTVGVAGESVTFTATSSDDGSIVSYTWDFGDGT---SSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVV 77
|
..
gi 1370468559 1248 VF 1249
Cdd:smart00089 78 VQ 79
|
|
| CLECT |
cd00037 |
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ... |
418-531 |
1.02e-16 |
|
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: 78.82 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 418 HCYRLVVEKAAWLQAQEQCQAWaGAALAMVDSPAVQRFLVSRVTRSL--DVWIGFSTVQGVEVGPAPQGEAFSleSCQNW 495
Cdd:cd00037 1 SCYKFSTEKLTWEEAQEYCRSL-GGHLASIHSEEENDFLASLLKKSSssDVWIGLNDLSSEGTWKWSDGSPLV--DYTNW 77
|
90 100 110
....*....|....*....|....*....|....*...
gi 1370468559 496 LPGEPHPATAEHCVRL--GPTGWCNTDLCSAPHSYVCE 531
Cdd:cd00037 78 APGEPNPGGSEDCVVLssSSDGKWNDVSCSSKLPFICE 115
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1932-2001 |
1.50e-16 |
|
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.
Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 76.66 E-value: 1.50e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1932 LWASSKVVAPGQLVHFQILLAAGSAVTFRLQVGGANPEVLPGPRFSHSFPRVGDHVVSVRGKNHVSWAQA 2001
Cdd:pfam00801 1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1677-1748 |
2.03e-16 |
|
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.
Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 76.27 E-value: 2.03e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370468559 1677 VVGGGRYFPTNHTVQLQAVVRDGTNVSYSWTAWRdrGPALAGSGKGFSLTVLEAGTYHVQLRATNMLGSAWA 1748
Cdd:pfam00801 1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFGD--SPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
|
|
| PLAT |
cd00113 |
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ... |
3159-3260 |
2.24e-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: 77.76 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 3159 KYEILVKTGWGRGSGTTAHVGIMLYGVD-SRSGHRHLDGDRAFHRNSLDIFRIATPHSLGSVWKIRVWHDNKGLSPAWFL 3237
Cdd:cd00113 2 RYTVTIKTGDKKGAGTDSNISLALYGENgNSSDIPILDGPGSFERGSTDTFQIDLKLDIGDITKVYLRRDGSGLSDGWYC 81
|
90 100
....*....|....*....|...
gi 1370468559 3238 QHVIVRDLQTARSAFFLVNDWLS 3260
Cdd:cd00113 82 ESITVQALGTKKVYTFPVNRWVL 104
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1593-1662 |
3.00e-16 |
|
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.
Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 75.89 E-value: 3.00e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1593 VNASRTVVPLNGSVSFSTSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQD 1662
Cdd:pfam00801 1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
2108-2175 |
3.98e-16 |
|
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.
Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 75.50 E-value: 3.98e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370468559 2108 SGPCFTNRSAQFEAaTSPSPRRVAYHWDFGDgSPGQDTDEPRAEHSYLRPGDYRVQVNASNLVSFFVA 2175
Cdd:pfam00801 5 GTVVAAGQPVTFTA-TLADGSNVTYTWDFGD-SPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1171-1242 |
4.94e-16 |
|
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.
Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 75.12 E-value: 4.94e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370468559 1171 VGVSDGVLVAGRPVTFYPHpLPSPGGVLYTWDFGDgSPVLTQSQPAANHTYASRGTYHVRLEVNNTVSGAAA 1242
Cdd:pfam00801 1 VSASGTVVAAGQPVTFTAT-LADGSNVTYTWDFGD-SPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1425-1496 |
9.87e-16 |
|
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.
Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 74.35 E-value: 9.87e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370468559 1425 LQPERQFVQLGDEAWLVACAWPPFPYRYTWDFGteEAAPTRARGPEVTFIYRDPGSYLVTVTASNNISAAND 1496
Cdd:pfam00801 1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFG--DSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
2100-2182 |
2.99e-15 |
|
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.
Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 73.25 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 2100 AVQYVALQSGPcfTNRSAQFEAATSPSPRRVAYHWDFGDGSpgqDTDEPRAEHSYLRPGDYRVQVNASNLVSFFVAQATV 2179
Cdd:smart00089 2 ADVSASPTVGV--AGESVTFTATSSDDGSIVSYTWDFGDGT---SSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTV 76
|
...
gi 1370468559 2180 TVQ 2182
Cdd:smart00089 77 VVQ 79
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1260-1325 |
7.87e-15 |
|
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.
Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 72.03 E-value: 7.87e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370468559 1260 SLAVEQGAPVVVSAAVQTGDNITWTFDMGDGTVLSGPEATVEHVYLRAQNCTVTVGAASPAGHLAR 1325
Cdd:pfam00801 5 GTVVAAGQPVTFTATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1852-1917 |
9.66e-15 |
|
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.
Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 71.65 E-value: 9.66e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370468559 1852 PGGSFVAAGSSVPFWGQLATGTNVSWCWAVPG--GSSKRGPHVTMVFPDAGTFSIRLNASNAVSWVSA 1917
Cdd:pfam00801 3 ASGTVVAAGQPVTFTATLADGSNVTYTWDFGDspGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1169-1243 |
3.51e-14 |
|
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.
Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 70.60 E-value: 3.51e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370468559 1169 VAVGVSDGVLV-AGRPVTFYPHPLPSPGGVLYTWDFGDGSpVLTQSQPAANHTYASRGTYHVRLEVNNTVSGAAAQ 1243
Cdd:cd00146 1 PTASVSAPPVAeLGASVTFSASDSSGGSIVSYKWDFGDGE-VSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTK 75
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1590-1668 |
1.14e-13 |
|
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.
Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 69.02 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1590 GLVVNASRTVVPLNGSVSFS-TSLEAGSDVRYSWVLCDRctPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQDSIFVYV 1668
Cdd:smart00089 1 VADVSASPTVGVAGESVTFTaTSSDDGSIVSYTWDFGDG--TSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVV 78
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1508-1585 |
2.76e-13 |
|
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.
Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 67.86 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1508 VTSIKVNGSLGLeLQQPYLFSAV--GRGRPASYLWDLGDGGWLEGPEVTHAYNSTGDFTVRVAGWNEVSRSEAWLNVTVK 1585
Cdd:smart00089 1 VADVSASPTVGV-AGESVTFTATssDDGSIVSYTWDFGDGTSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
|
|
| COG3291 |
COG3291 |
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
1509-1815 |
1.11e-12 |
|
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 72.78 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1509 TSIKVNGSLGLELQqpylFSAVGRGRPASYLWDLGDGGWLEGPEVTHAYNSTGDFTVRVAGWNEV-SRSEAWLNVTVKRR 1587
Cdd:COG3291 2 TATPTSGCAPLTVQ----FTDTSSGNATSYEWDFGDGTTSTEANPSHTYTTPGTYTVTLTVTDAAgCSDTTTKTITVGAP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1588 VRGLVVNASRTVVPLNGSVSFSTSLEAGSDVrYSWVLCDRCTPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQDSIFVY 1667
Cdd:COG3291 78 NPGVTTVTTSTTVTTLANTANGGATTVVAGS-TVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1668 VLQLIEGLQVVGGGRYFPTNHTVQLQAVVRDGTNVSYSWTAWRDRGPALAGSGKGFSLTVLEAGTYHVQLRATNMLGSAW 1747
Cdd:COG3291 157 TSVSTTDVTSDGTTSASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDVTLT 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370468559 1748 ADCTMDFVEPVGWLMVAASPNPAAVNTSVTLSAELAGGSGVVYTWSLEEGLSWETSEPFTTHSFPTPG 1815
Cdd:COG3291 237 GISTGDAGTPGTNTVTTSGANTAGTSTITGGTSGVVTTSAATGTSTNGTGGLGTTTAITPGNVSTTAD 304
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1765-1839 |
2.36e-12 |
|
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.
Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 65.17 E-value: 2.36e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370468559 1765 ASPNPAAVNTSVTLSAELAG-GSGVVYTWSLEEGLSWetSEPFTTHSFPTPGLHLVTMTAGNPLGSANATVEVDVQ 1839
Cdd:smart00089 6 ASPTVGVAGESVTFTATSSDdGSIVSYTWDFGDGTSS--TGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1513-1578 |
2.40e-12 |
|
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.
Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 64.72 E-value: 2.40e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370468559 1513 VNGSLGLELQQPYLFSA-VGRGRPASYLWDLGD--GGWLEGPEVTHAYNSTGDFTVRVAGWNEVSRSEA 1578
Cdd:pfam00801 2 SASGTVVAAGQPVTFTAtLADGSNVTYTWDFGDspGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1859-1918 |
3.73e-12 |
|
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.
Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 64.78 E-value: 3.73e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370468559 1859 AGSSVPFWGQLAT-GTNVSWCWAVPGGSSKRGPHVTMVFPDAGTFSIRLNASNAVSWVSAT 1918
Cdd:smart00089 13 AGESVTFTATSSDdGSIVSYTWDFGDGTSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASAT 73
|
|
| WSC |
pfam01822 |
WSC domain; This domain is involved in carbohydrate binding. |
180-250 |
8.73e-12 |
|
WSC domain; This domain is involved in carbohydrate binding.
Pssm-ID: 460348 Cd Length: 82 Bit Score: 63.63 E-value: 8.73e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370468559 180 YVACLPDNSsGTVAAVSFSAAHEGLLQPEACSAFCFSTGQGLAALSEQGWCLCGAAQPSSASFA----CLSLCSG 250
Cdd:pfam01822 1 YLGCYSDGT-GGRRLLLGSSGDYDDMTPEKCIAFCSAAGYTYAGLEYGGECYCGNSLPSGSALAdssdCNTPCPG 74
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
70-127 |
1.23e-11 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 62.54 E-value: 1.23e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1370468559 70 TALDVSHNLLRALDVGLLANLSALAELDISNNKISTLEEGIFANLFNLSEINLSGNPF 127
Cdd:pfam13855 4 RSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
2020-2091 |
1.90e-11 |
|
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.
Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 62.40 E-value: 1.90e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370468559 2020 CEPGIATGTERNFTARVQRGSRVAYAWYFslqkvqGDSLV-ILSGRDVTYTPVAAGLLEIQVRAFNALGSENR 2091
Cdd:pfam00801 4 SGTVVAAGQPVTFTATLADGSNVTYTWDF------GDSPGtSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
2113-2183 |
1.95e-11 |
|
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.
Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 62.51 E-value: 1.95e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370468559 2113 TNRSAQFEAATSPSPRRVAYHWDFGDGSpGQDTDEPRAEHSYLRPGDYRVQVNASNLVSfFVAQATVTVQV 2183
Cdd:cd00146 13 LGASVTFSASDSSGGSIVSYKWDFGDGE-VSSSGEPTVTHTYTKPGTYTVTLTVTNAVG-SSSTKTTTVVV 81
|
|
| LRRCT |
smart00082 |
Leucine rich repeat C-terminal domain; |
125-177 |
2.77e-11 |
|
Leucine rich repeat C-terminal domain;
Pssm-ID: 214507 [Multi-domain] Cd Length: 51 Bit Score: 61.29 E-value: 2.77e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1370468559 125 NPFECDCGLAWLPRWAeEQQVRVVQPEAATCAGPGSLAGqPLLGIPLLDSGCG 177
Cdd:smart00082 1 NPFICDCELRWLLRWL-QANEHLQDPVDLRCASPSSLRG-PLLELLHSEFKCP 51
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1592-1668 |
5.13e-11 |
|
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.
Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 61.36 E-value: 5.13e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370468559 1592 VVNASRTVVPLNGSVSFS-TSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQ-DSIFVYV 1668
Cdd:cd00146 3 ASVSAPPVAELGASVTFSaSDSSGGSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSStKTTTVVV 81
|
|
| CLECT_DC-SIGN_like |
cd03590 |
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ... |
406-531 |
5.43e-11 |
|
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: 62.71 E-value: 5.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 406 CPSDTEIFpgNGHCYRLVVEKAAWLQAQEQCQAwAGAALAMVDSPAVQRFLVSRVTRSLDVWIGFStVQGVE-----V-G 479
Cdd:cd03590 1 CPTNWKSF--QSSCYFFSTEKKSWEESRQFCED-MGAHLVIINSQEEQEFISKILSGNRSYWIGLS-DEETEgewkwVdG 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370468559 480 PAPqgeafsLESCQNWLPGEP--HPATAEHCVRLGPT--GWcNTDLCSAPHSYVCE 531
Cdd:cd03590 77 TPL------NSSKTFWHPGEPnnWGGGGEDCAELVYDsgGW-NDVPCNLEYRWICE 125
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
277-344 |
1.07e-10 |
|
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.
Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 60.09 E-value: 1.07e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370468559 277 LVGPHGPLASGQLAAFHIA-APLPVTATRWDFGDgSAEVDAAGPAASHRYVLPGRYHVTAVLALGAGSA 344
Cdd:pfam00801 1 VSASGTVVAAGQPVTFTATlADGSNVTYTWDFGD-SPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSA 68
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1336-1417 |
1.91e-10 |
|
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.
Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 59.77 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1336 VLRVEPAACIPTQP-DARLTAYVTGNPAHYLFDWTFGDGssnTTVRGcPTVTHNFTRSGTFPLALVLSSRVNRAHYFTSI 1414
Cdd:smart00089 1 VADVSASPTVGVAGeSVTFTATSSDDGSIVSYTWDFGDG---TSSTG-PTVTHTYTKPGTYTVTLTVTNAVGSASATVTV 76
|
...
gi 1370468559 1415 CVE 1417
Cdd:smart00089 77 VVQ 79
|
|
| GPS |
smart00303 |
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ... |
3051-3100 |
3.65e-10 |
|
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: 57.78 E-value: 3.65e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1370468559 3051 YTSLCQYFSEEDMVWRTEGLLPLEETSpRQAVCLTRHLTAFGASLFVPPS 3100
Cdd:smart00303 1 FNPICVFWDESSGEWSTRGCELLETNG-THTTCSCNHLTTFAVLMDVPPI 49
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1447-1503 |
4.59e-10 |
|
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.
Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 58.62 E-value: 4.59e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370468559 1447 PFPYRYTWDFGTEeaapTRARGPEVTFIYRDPGSYLVTVTASNNISAANDSALVEVQ 1503
Cdd:smart00089 27 GSIVSYTWDFGDG----TSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1685-1752 |
3.68e-09 |
|
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.
Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 55.92 E-value: 3.68e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370468559 1685 PTNHTVQLQAVVR-DGTNVSYSWtawrDRGPALAGSGKGFSLTVLEAGTYHVQLRATNMLGSAWADCTM 1752
Cdd:smart00089 12 VAGESVTFTATSSdDGSIVSYTW----DFGDGTSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTV 76
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1262-1321 |
5.05e-09 |
|
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.
Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 55.97 E-value: 5.05e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370468559 1262 AVEQGAPVVVSAAVQ-TGDNITWTFDMGDGTVLSGPEATVEHVYLRAQNCTVTVGAASPAG 1321
Cdd:cd00146 10 VAELGASVTFSASDSsGGSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVG 70
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
54-127 |
6.41e-09 |
|
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.
Pssm-ID: 411060 [Multi-domain] Cd Length: 220 Bit Score: 59.41 E-value: 6.41e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370468559 54 RGLRTLGPALRIpadataLDVSHNLLRALDVglLANLSALAELDISNNKISTLEE--GIFANLFNLSEINLSGNPF 127
Cdd:cd21340 113 RSLAALSNSLRV------LNISGNNIDSLEP--LAPLRNLEQLDASNNQISDLEEllDLLSSWPSLRELDLTGNPV 180
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1266-1332 |
8.52e-09 |
|
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.
Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 55.15 E-value: 8.52e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370468559 1266 GAPVVVSAAVQT-GDNITWTFDMGDGTVLSGPeaTVEHVYLRAQNCTVTVGAASPAGHLARSLHVLVF 1332
Cdd:smart00089 14 GESVTFTATSSDdGSIVSYTWDFGDGTSSTGP--TVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
|
|
| CLECT_REG-1_like |
cd03594 |
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ... |
406-531 |
8.58e-09 |
|
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: 56.61 E-value: 8.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 406 CPSDTeiFPGNGHCYRLVVEKAAWLQAQEQCQAW-AGAALAMVDSPAVQRFLVSRV----TRSLDVWIGFSTVQGVEVGP 480
Cdd:cd03594 1 CPKGW--LPYKGNCYGYFRQPLSWSDAELFCQKYgPGAHLASIHSPAEAAAIASLIssyqKAYQPVWIGLHDPQQSRGWE 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1370468559 481 APQGEAFSLEScqnWLPGEPHPaTAEHCVRL-GPTG---WcNTDLCSAPHSYVCE 531
Cdd:cd03594 79 WSDGSKLDYRS---WDRNPPYA-RGGYCAELsRSTGflkW-NDANCEERNPFICK 128
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
70-128 |
1.69e-08 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 60.33 E-value: 1.69e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370468559 70 TALDVSHNLLRALDVGLlANLSALAELDISNNKISTLEEgiFANLFNLSEINLSGNPFE 128
Cdd:COG4886 208 EELDLSGNQLTDLPEPL-ANLTNLETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLT 263
|
|
| COG3291 |
COG3291 |
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
1180-1390 |
2.44e-08 |
|
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 59.30 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1180 AGRPVTFYPHplpSPGGVL-YTWDFGDGSpvlTQSQPAANHTYASRGTYHVRLEVNNTV-SGAAAQADVRVFEELRGLSV 1257
Cdd:COG3291 10 APLTVQFTDT---SSGNATsYEWDFGDGT---TSTEANPSHTYTTPGTYTVTLTVTDAAgCSDTTTKTITVGAPNPGVTT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1258 DMSLAVEQGAPVVVSAAVQTGDNITWTFDMGDGTVLSGPEATVEHVYLRAQNCTVTVGAASPAGHLARSLHVLVFVLEVL 1337
Cdd:COG3291 84 VTTSTTVTTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVTTSVSTTD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1370468559 1338 RVEPAACIPTQPDARLTAYVTGNPAHYLFDWTFGDGSSNTTVRGCPTVTHNFT 1390
Cdd:COG3291 164 VTSDGTTSASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTAGVTTGATS 216
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1520-1584 |
2.85e-08 |
|
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.
Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 53.65 E-value: 2.85e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1520 ELQQPYLFSAV--GRGRPASYLWDLGDGGWL--EGPEVTHAYNSTGDFTVRVAGWNEVSRSEA-WLNVTV 1584
Cdd:cd00146 12 ELGASVTFSASdsSGGSIVSYKWDFGDGEVSssGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTkTTTVVV 81
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1847-1918 |
3.36e-08 |
|
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.
Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 53.27 E-value: 3.36e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370468559 1847 IRASEPGGSFVAAGSSVPFWGQLATG---TNVSWCWAVPGGSSKRGPHVTMVFPDAGTFSIRLNASNAVSWVSAT 1918
Cdd:cd00146 1 PTASVSAPPVAELGASVTFSASDSSGgsiVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTK 75
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1064-1156 |
4.38e-08 |
|
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.
Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 52.77 E-value: 4.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1064 VSTVPAVLSPNATLALTAGVLvdSAVEVAFLWTFGDgeqalhqfqppynesfpvpdpSVAQVLVEHNVMHTYAAPGEYLL 1143
Cdd:pfam00801 1 VSASGTVVAAGQPVTFTATLA--DGSNVTYTWDFGD---------------------SPGTSGSGPTVTHTYLSPGTYTV 57
|
90
....*....|...
gi 1370468559 1144 TVLASNAFENLTQ 1156
Cdd:pfam00801 58 TLTASNAVGSANA 70
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
48-128 |
4.88e-08 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 58.79 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 48 RVNCSGRGLRTLGPALRIPADATALDVSHNLLRALDVGLlANLSALAELDISNNKISTLEEGIfANLFNLSEINLSGNPF 127
Cdd:COG4886 117 SLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPL-GNLTNLKSLDLSNNQLTDLPEEL-GNLTNLKELDLSNNQI 194
|
.
gi 1370468559 128 E 128
Cdd:COG4886 195 T 195
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
48-128 |
5.05e-08 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 58.79 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 48 RVNCSGRGLRTLGPALripADATAL---DVSHNLLRALDVGLlANLSALAELDISNNKISTLEEGIfANLFNLSEINLSG 124
Cdd:COG4886 140 ELDLSNNQLTDLPEPL---GNLTNLkslDLSNNQLTDLPEEL-GNLTNLKELDLSNNQITDLPEPL-GNLTNLEELDLSG 214
|
....
gi 1370468559 125 NPFE 128
Cdd:COG4886 215 NQLT 218
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1763-1836 |
7.71e-08 |
|
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.
Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 52.50 E-value: 7.71e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370468559 1763 VAASPNPAA-VNTSVTLSAE-LAGGSGVVYTWSLEEGLSWETSEPFTTHSFPTPGLHLVTMTAGNPLGSAN---ATVEV 1836
Cdd:cd00146 3 ASVSAPPVAeLGASVTFSASdSSGGSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSStktTTVVV 81
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1061-1162 |
8.90e-08 |
|
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.
Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 52.07 E-value: 8.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1061 GLQVSTVPAVLSPNATLALTAGVLVDSAVeVAFLWTFGDGeqalhqfqppynesfpvpdpsvaQVLVEHNVMHTYAAPGE 1140
Cdd:smart00089 1 VADVSASPTVGVAGESVTFTATSSDDGSI-VSYTWDFGDG-----------------------TSSTGPTVTHTYTKPGT 56
|
90 100
....*....|....*....|..
gi 1370468559 1141 YLLTVLASNAFENLTQQVPVSV 1162
Cdd:smart00089 57 YTVTLTVTNAVGSASATVTVVV 78
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
70-128 |
9.04e-08 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 58.02 E-value: 9.04e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370468559 70 TALDVSHNLLRALDVglLANLSALAELDISNNKISTLEEgiFANLFNLSEINLSGNPFE 128
Cdd:COG4886 231 ETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLTDLPP--LANLTNLKTLDLSNNQLT 285
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
72-128 |
1.19e-07 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 57.64 E-value: 1.19e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370468559 72 LDVSHNLLRALDVGLlANLSALAELDISNNKISTLEEGIfANLFNLSEINLSGNPFE 128
Cdd:COG4886 187 LDLSNNQITDLPEPL-GNLTNLEELDLSGNQLTDLPEPL-ANLTNLETLDLSNNQLT 241
|
|
| PLAT_plant_stress |
cd01754 |
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ... |
3160-3267 |
1.61e-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: 52.93 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 3160 YEILVKTGWGRGSGTTAHVGIMLYGVDSRS---------GHRHLDGDRAFHRNSLDIFRIATPHSLGSVWKIRVWHDNKG 3230
Cdd:cd01754 3 YTIYVQTGSIWKAGTDSRISLQIYDADGPGlrianleawGGLMGAGHDYFERGNLDRFSGRGPCLPSPPCWMNLTSDGTG 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1370468559 3231 LSPAWFLQHVIVRDL-QTARSA--FFLVNDWLSVETEANG 3267
Cdd:cd01754 83 NHPGWYVNYVEVTQAgQHAPCMqhLFAVEQWLATDESPYM 122
|
|
| PKD_4 |
pfam18911 |
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins. |
1192-1248 |
1.88e-07 |
|
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
Pssm-ID: 436824 [Multi-domain] Cd Length: 85 Bit Score: 51.50 E-value: 1.88e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1370468559 1192 PSPGGVL-YTWDFGDGSpvlTQSQPAANHTYASRGTYHVRLEVNNTVSGAAAQADVRV 1248
Cdd:pfam18911 29 DPDGDILsYRWDFGDGT---TATGANVSHTYAAPGTYTVTLTVTDDSGASNSTATDTV 83
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1347-1420 |
2.33e-07 |
|
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.
Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 50.96 E-value: 2.33e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370468559 1347 TQPDARLTAYVTGNPAHYLFDWTFGDGssNTTVRGCPTVTHNFTRSGTFPLALVLSSRVNRAhyfTSICVEPEV 1420
Cdd:cd00146 13 LGASVTFSASDSSGGSIVSYKWDFGDG--EVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSS---STKTTTVVV 81
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1344-1409 |
2.81e-07 |
|
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.
Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 50.46 E-value: 2.81e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370468559 1344 CIPTQPDARLTAYV-TGNPAHYLfdWTFGDgsSNTTVRGCPTVTHNFTRSGTFPLALVLSSRVNRAH 1409
Cdd:pfam00801 7 VVAAGQPVTFTATLaDGSNVTYT--WDFGD--SPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSAN 69
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1928-2007 |
3.40e-07 |
|
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.
Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 50.53 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1928 VGLVLWASSKVVApGQLVHFQI-LLAAGSAVTFRLQVGgaNPEVLPGPRFSHSFPRVGDHVVSVRGKNHVSWAQAQVRIV 2006
Cdd:smart00089 1 VADVSASPTVGVA-GESVTFTAtSSDDGSIVSYTWDFG--DGTSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVV 77
|
.
gi 1370468559 2007 V 2007
Cdd:smart00089 78 V 78
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1449-1502 |
8.97e-07 |
|
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.
Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 49.42 E-value: 8.97e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1370468559 1449 PYRYTWDFGTEEAAPTRarGPEVTFIYRDPGSYLVTVTASNNISAAN-DSALVEV 1502
Cdd:cd00146 29 IVSYKWDFGDGEVSSSG--EPTVTHTYTKPGTYTVTLTVTNAVGSSStKTTTVVV 81
|
|
| COG3291 |
COG3291 |
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
1765-1942 |
2.12e-06 |
|
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 53.14 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1765 ASPNPAAVNTSVTLSAeLAGGSGVVYTWSLEEGLSweTSEPFTTHSFPTPGLHLVTMTAGNPLGSANA-----TVEVDVQ 1839
Cdd:COG3291 3 ATPTSGCAPLTVQFTD-TSSGNATSYEWDFGDGTT--STEANPSHTYTTPGTYTVTLTVTDAAGCSDTttktiTVGAPNP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1840 VPVSGLSIRASEPGGSFVAAGSSVPFWGQLATGTNVSWCWAVPGGSSKRGPHVTMVFPDAGTFSIRLNASNAVSWVSATY 1919
Cdd:COG3291 80 GVTTVTTSTTVTTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVTTSV 159
|
170 180
....*....|....*....|...
gi 1370468559 1920 NLTAEEPIVGLVLWASSKVVAPG 1942
Cdd:COG3291 160 STTDVTSDGTTSASTNPSVTTDT 182
|
|
| PKD_4 |
pfam18911 |
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins. |
1527-1567 |
2.43e-06 |
|
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
Pssm-ID: 436824 [Multi-domain] Cd Length: 85 Bit Score: 48.42 E-value: 2.43e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1370468559 1527 FSAVGRGRPASYLWDLGDGGWLEGPEVTHAYNSTGDFTVRV 1567
Cdd:pfam18911 26 ASDDPDGDILSYRWDFGDGTTATGANVSHTYAAPGTYTVTL 66
|
|
| COG3291 |
COG3291 |
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
1448-1749 |
4.48e-06 |
|
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 51.98 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1448 FPYRYTWDFGTeeaaPTRARGPEVTFIYRDPGSYLVTVTASNNI-SAANDSALVEVQEPVLVTSIKVNGSlglelqqpYL 1526
Cdd:COG3291 23 NATSYEWDFGD----GTTSTEANPSHTYTTPGTYTVTLTVTDAAgCSDTTTKTITVGAPNPGVTTVTTST--------TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1527 FSAVGRGRPASYLWDLGDGGWLEGPEVTHAYNSTGDFTVRVAGWNEVSRSEAWLNVTVKRRVRGLVVNASRTVVPLNGSV 1606
Cdd:COG3291 91 TTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1607 SFSTSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQDSIFVYVLQLIEGLQVVGGGRYFPT 1686
Cdd:COG3291 171 SASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNT 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370468559 1687 NHTVQLQAVVRDGTNVSYSWTAWRDRGPALAGSGKGFSLTVLEAGTYHVQLRATNMLGSAWAD 1749
Cdd:COG3291 251 VTTSGANTAGTSTITGGTSGVVTTSAATGTSTNGTGGLGTTTAITPGNVSTTADVTGGTATLA 313
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
276-348 |
5.43e-06 |
|
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.
Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 47.11 E-value: 5.43e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370468559 276 TLVGPHGPLAS-GQLAAFHIAAPLP--VTATRWDFGDGSAEVdAAGPAASHRYVLPGRYHVTAVLALGAGSALLGT 348
Cdd:cd00146 2 TASVSAPPVAElGASVTFSASDSSGgsIVSYKWDFGDGEVSS-SGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKT 76
|
|
| COG3291 |
COG3291 |
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
1065-1424 |
1.76e-05 |
|
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 50.44 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1065 STVPAVLSPNATLALTAgvlVDSAVEVAFLWTFGDGEQAlhqfqppynesfpvpdpsvaqvlVEHNVMHTYAAPGEYLLT 1144
Cdd:COG3291 2 TATPTSGCAPLTVQFTD---TSSGNATSYEWDFGDGTTS-----------------------TEANPSHTYTTPGTYTVT 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1145 VLASNAF-ENLTQQVPVSVRASLPSVAVGVSDGVLVAGRPVTFYPHPLPSPGGVLYTWDFGDGSPVLTQSQPAANHTYAS 1223
Cdd:COG3291 56 LTVTDAAgCSDTTTKTITVGAPNPGVTTVTTSTTVTTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTTTT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1224 RGTYHVRLEVNNTVSGAAAQADVRVFEELRGLSVDmslaveqGAPVVVSAAVQTGDNITWTFDMGDGTVLSGPEATVEHV 1303
Cdd:COG3291 136 TGTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTT-------SASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1304 YLRAQNCTVTVGAASPAGHLARSLHVLVFVLEVLRVEPAACIPTQPDARLTAYVTGNPAHYLFDWTFGDGSSNTTVRGCP 1383
Cdd:COG3291 209 GVTTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNTVTTSGANTAGTSTITGGTSGVVTTSAATGTSTNGTGGL 288
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1370468559 1384 TVTHNFTRSGTFPLALVLSSRVNRAHYFTSICVEPEVGNVT 1424
Cdd:COG3291 289 GTTTAITPGNVSTTADVTGGTATLAVSSTLTTNDTTGSSST 329
|
|
| PKD_4 |
pfam18911 |
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins. |
300-344 |
2.26e-05 |
|
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
Pssm-ID: 436824 [Multi-domain] Cd Length: 85 Bit Score: 45.34 E-value: 2.26e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1370468559 300 VTATRWDFGDGSAevdAAGPAASHRYVLPGRYHVTAVLALGAGSA 344
Cdd:pfam18911 34 ILSYRWDFGDGTT---ATGANVSHTYAAPGTYTVTLTVTDDSGAS 75
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
70-128 |
2.36e-05 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 50.32 E-value: 2.36e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370468559 70 TALDVSHNLLraldvglLANLSALAELDISNNKISTLEEGIfANLFNLSEINLSGNPFE 128
Cdd:COG4886 99 TELDLSGNEE-------LSNLTNLESLDLSGNQLTDLPEEL-ANLTNLKELDLSNNQLT 149
|
|
| PKD_4 |
pfam18911 |
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins. |
1451-1502 |
2.40e-05 |
|
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
Pssm-ID: 436824 [Multi-domain] Cd Length: 85 Bit Score: 45.34 E-value: 2.40e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1370468559 1451 RYTWDFGTEeaapTRARGPEVTFIYRDPGSYLVTVTASNNISAANDSALVEV 1502
Cdd:pfam18911 36 SYRWDFGDG----TTATGANVSHTYAAPGTYTVTLTVTDDSGASNSTATDTV 83
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
301-353 |
2.64e-05 |
|
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.
Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 45.13 E-value: 2.64e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1370468559 301 TATRWDFGDGSaevDAAGPAASHRYVLPGRYHVTAVLALGAGSALLGTDVQVE 353
Cdd:smart00089 30 VSYTWDFGDGT---SSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
2022-2098 |
2.70e-05 |
|
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.
Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 45.13 E-value: 2.70e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370468559 2022 PGIATGTERNFTARVQR-GSRVAYAWYFslqkvqGDSLViLSGRDVTYTPVAAGLLEIQVRAFNALGSENRTLVLEVQ 2098
Cdd:smart00089 9 TVGVAGESVTFTATSSDdGSIVSYTWDF------GDGTS-STGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1931-2007 |
3.73e-05 |
|
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.
Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 44.79 E-value: 3.73e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370468559 1931 VLWASSKVVAPGQLVHFQI-LLAAGSAVTFRLQVGGANPEVLPGPRFSHSFPRVGDHVVSVRGKNHVSWAQAQVRIVV 2007
Cdd:cd00146 3 ASVSAPPVAELGASVTFSAsDSSGGSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTTTVV 80
|
|
| COG3291 |
COG3291 |
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
2116-2182 |
4.35e-05 |
|
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 48.90 E-value: 4.35e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370468559 2116 SAQFEAATSPSPrrVAYHWDFGDGSpgqDTDEPRAEHSYLRPGDYRVQVNASNLV-SFFVAQATVTVQ 2182
Cdd:COG3291 13 TVQFTDTSSGNA--TSYEWDFGDGT---TSTEANPSHTYTTPGTYTVTLTVTDAAgCSDTTTKTITVG 75
|
|
| CLECT_NK_receptors_like |
cd03593 |
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ... |
406-531 |
5.11e-05 |
|
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: 45.40 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 406 CPSDTEIFpgNGHCYRLVVEKAAWLQAQEQCQAwAGAALAMVDSPAVQRFLvSRVTRSLDVWIGFSTVQGVEVGPAPQGE 485
Cdd:cd03593 1 CPKDWICY--GNKCYYFSMEKKTWNESKEACSS-KNSSLLKIDDEEELEFL-QSQIGSSSYWIGLSREKSEKPWKWIDGS 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1370468559 486 AFSlescqNWLpgEPHPATAE-HCVRLGPTGwCNTDLCSAPHSYVCE 531
Cdd:cd03593 77 PLN-----NLF--NIRGSTKSgNCAYLSSTG-IYSEDCSTKKRWICE 115
|
|
| PKD_4 |
pfam18911 |
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins. |
2116-2168 |
8.38e-05 |
|
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
Pssm-ID: 436824 [Multi-domain] Cd Length: 85 Bit Score: 43.80 E-value: 8.38e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1370468559 2116 SAQFEAATS--PSPRRVAYHWDFGDGSPGqdtDEPRAEHSYLRPGDYRVQVNASN 2168
Cdd:pfam18911 19 TVTFDASASddPDGDILSYRWDFGDGTTA---TGANVSHTYAAPGTYTVTLTVTD 70
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
3796-4321 |
1.37e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 48.33 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 3796 EALYPDPPGPRV--------HTCSAAGGFSTSDYDVGWESPHNGSGTWAYSAPDLLGAWSWGSCAVYDSGGYVQELGLSL 3867
Cdd:COG3321 850 SALYPGRGRRRVplptypfqREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAAL 929
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 3868 EESRDRLRFLQLHNWLDNRSRAVFLELTRYSPAVGLHAAVTLRLEFPAAGRALAALSVRPFALRRLSAGLSLPLLTSVCL 3947
Cdd:COG3321 930 LALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAA 1009
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 3948 LLFAVHFAVAEARTWHREGRWRVLRLGAWARWLLVALTAATALVRLAQLGAADRQWTRFVRGRPRRFTSFDQVAQLSSAA 4027
Cdd:COG3321 1010 LLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAA 1089
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 4028 RGLAASLLFLLLVKAAQQLRFVRQWSVFGKTLCRALPELLGVTLGLVVLGVAYAQLAILLVSSCVDSLWSVAQALLVLCP 4107
Cdd:COG3321 1090 LAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLA 1169
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 4108 GTGLSTLCPAESWHLSPLLCVGLWALRLWGALRLGAVILRWRYHALRGELYRPAWEPQDYEMVELFLRRLRLWMGLSKVK 4187
Cdd:COG3321 1170 AAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALA 1249
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 4188 EFRHKVRFEGMEPLPSRSSRGSKVSPDVPPPSAGSDASHPSTSSSQLDGLSVSLGRLGTRCEPEPSRLQAVFEALLTQFD 4267
Cdd:COG3321 1250 AAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAA 1329
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1370468559 4268 RLNQA-TEDVYQLEQQLHSLQGRRSSRAPAGSSRGPSPGLRPALPSRLARASRGV 4321
Cdd:COG3321 1330 LAALAaAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAA 1384
|
|
| CLECT_CEL-1_like |
cd03589 |
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ... |
406-532 |
1.66e-04 |
|
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: 44.66 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 406 CPSDTEIFpgNGHCYRLVVEKAAWLQAQEQCQAWAG----AALAMVDSPAVQRFL------VSRVTRSLDVWIGFStvQG 475
Cdd:cd03589 1 CPTFWTAF--GGYCYRFFGDRLTWEEAELRCRSFSIpgliAHLVSIHSQEENDFVydlfesSRGPDTPYGLWIGLH--DR 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370468559 476 VEVGPA--PQGEAFSLEscqNWLPGEPHPA-TAEHCVRLGPTG-----WcNTDLCSAPHSYVCEL 532
Cdd:cd03589 77 TSEGPFewTDGSPVDFT---KWAGGQPDNYgGNEDCVQMWRRGdagqsW-NDMPCDAVFPYICKM 137
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
496-791 |
3.67e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 47.24 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 496 LPGEPHPATAEHCVrlgPTGWCnTDLCSAPHSYVCELQPGGPVQDAENLLVGAPSGDLQGPLTPLA-----------QQD 564
Cdd:PHA03247 2555 LPPAAPPAAPDRSV---PPPRP-APRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPlppdthapdppPPS 2630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 565 GLSAPHEPVEVMVFPGL------------------RLSREAFLTTAEFGTQELRRPAqLRLQVYRLLSTAGTPENGSEPE 626
Cdd:PHA03247 2631 PSPAANEPDPHPPPTVPpperprddpapgrvsrprRARRLGRAAQASSPPQRPRRRA-ARPTVGSLTSLADPPPPPPTPE 2709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 627 SRsPDNRTQLAPAcMPGGRWCPGANICLPLDASCHPQACANGCTSGPGLPGAPYALWREFLFSVPAGPP----------- 695
Cdd:PHA03247 2710 PA-PHALVSATPL-PPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAagpprrltrpa 2787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 696 -AQYSVTLHGQDVLMLPGDLVGLQHDAGPGALLHCSPAPGHPGPRAPYLSANASSWLPHLPAQLEGTWACPACALRLLAA 774
Cdd:PHA03247 2788 vASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPP 2867
|
330
....*....|....*..
gi 1370468559 775 TEQLTVLLGLRPNPGLR 791
Cdd:PHA03247 2868 SRSPAAKPAAPARPPVR 2884
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1683-1755 |
6.57e-04 |
|
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.
Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 41.33 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1683 YFPTNHTVQLQAVVR-------DGTNVSYSWTaWRDrGPALAGSGKGFSLTVLEAGTYHVQLRATNMLGSAWADCTMDFV 1755
Cdd:cd00146 4 SVSAPPVAELGASVTfsasdssGGSIVSYKWD-FGD-GEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTTTVVV 81
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
93-125 |
1.25e-03 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 39.82 E-value: 1.25e-03
10 20 30
....*....|....*....|....*....|...
gi 1370468559 93 LAELDISNNKISTLEEGIFANLFNLSEINLSGN 125
Cdd:pfam13855 3 LRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNN 35
|
|
| PKD_4 |
pfam18911 |
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins. |
1763-1840 |
2.24e-03 |
|
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
Pssm-ID: 436824 [Multi-domain] Cd Length: 85 Bit Score: 39.95 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468559 1763 VAASPNPAAVNTSVTLSAE---LAGGSGVVYTWSLEEGLSWETSEPftTHSFPTPGLHLVTMTAGNPLGSANATVEVDVQ 1839
Cdd:pfam18911 7 DAGGDRIVAEGETVTFDASasdDPDGDILSYRWDFGDGTTATGANV--SHTYAAPGTYTVTLTVTDDSGASNSTATDTVT 84
|
.
gi 1370468559 1840 V 1840
Cdd:pfam18911 85 V 85
|
|
| |
