|
Name |
Accession |
Description |
Interval |
E-value |
| PCC |
TIGR00864 |
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ... |
97-2728 |
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: 4862.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 97 DISNNKISTLEEGIFANLFNLSEINLSGNPFECDCGLAWLPRWAEEQQVRVVQPEAATCAGPGSLAGQPLLGIPLLDSGC 176
Cdd:TIGR00864 1 DISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPEAALCAGPGALAGQPLLGIPLLDSGC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 177 GEEYVACLPDNSSGTVAAVS----FSAAHEGLLQPEACSAFCFSTGQGLAALSEQGWCLCGAAQPSSASFACLSLCSGPP 252
Cdd:TIGR00864 81 DEEYVACLKDNSSGGGAARSelviFSAAHEGLFQPEACNAFCFSAGHGLAALGEQGECLCGAAQPSEANFACESLCSGPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 253 PPPAPTCRGPTLLQHVFPASPGATLVGPHGPLASGQLAAFHIAAPLPVTATRWDFGDGSAEVDAAGP----AASHRYVLP 328
Cdd:TIGR00864 161 PPPAAACRGPQLLEHIFPALPGAPIQGPHGPIASGQLAAFHAAAPLAPTAMRWDFGDGSAEVDAAGAggttAASHKYGHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 329 GRYHVTAVLALGAGSALLGTDVQVEAAPAALELVCPSSVQSDESLDLSIQNRGGSGLEAAYSIVALGEEPARAVHPLCPS 408
Cdd:TIGR00864 241 GRYHVSAMGALGAGKALAGGDVQVEAAPAALELHCPSLVQADESLDLSIQNRGGSDLDAAWKITAHGEEPAKASHPHCPK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 409 DTEIFPGNGHCYRLVVEKAAWLQAQEQCQAWAGAALAMVDSPAVQRFLVSRVTRSLD--VWIGFSTVQGVEVGPAPQGEA 486
Cdd:TIGR00864 321 DGEIFEENGHCFQIVPEEAAWLDAQEQCLARAGAALAIVDNDALQNFLARKVTHSLDrgVWIGFSDVNGAEKGPAHQGEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 487 FSLESCQNWLPGEPHPATAEHCVRLGPTGWCNTDLCSAPHSYVCELQPGGPVQDAENLLVGAPSGDLQGPLTPLAQQDGL 566
Cdd:TIGR00864 401 FEAEECEEGLAGEPHPARAEHCVRLDPRGQCNSDLCNAPHAYVCELNPGGPVPDAENFAMGAASFDLHGLLQALAAMDGL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 567 SAP-HEPVEVMVFPGLRLSREAFLTTAEFGTQELRRPAQLRLQVYRL---LSTAGTPENGSEPESRSPDNRTQLAPACMP 642
Cdd:TIGR00864 481 PAPpHEGVEVLLFPALRFSRAAFLSSAEFGTQELRRPAHILFQIYRLrcrLPGAGGPACGPEAECRPPDNRSADAPACMK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 643 GGRWCPGANICLPLDASCHPQACANGCTSGPGLPGAP----YALWREFLFSVPAGPPAQYSVTLHGQDVLMLPGDLVGLQ 718
Cdd:TIGR00864 561 GEQWCPFAHICLPLDAPCHPQACANGCSQGHGLPGAArmplYALQREFLFSLPAGPAAHVLLQDHGEDLLMLPGDLIALQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 719 HDAGPGALLHCSPAPGHPGPQAPYLSANASSWLPH------------------------LPAQLEGTWA----CPACALR 770
Cdd:TIGR00864 641 HDAGPAALIHCQPAPGHPGPRAPVFAANASEWFGHnntpvppdnlagdgadplpdpeldLKALLEGTRAswleCAACAIR 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 771 LLAATEQLTVLLGLRPNPGLRLPGRYEVRAEVGNGVSRHNLSCSFDVVSPVAGLRVIYPAPRDGRLYVPTNGSALVLQVD 850
Cdd:TIGR00864 721 LLAAGEQETRLLGAELNAGLPLPGLYELLAESAKGSDLHNASCSFDVLPPLAGLRVIHPAPQDGRLFLESNGSALLLQVD 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 851 SGANATATARWPGGSVSARFENVCPALVA-------TFVPGCPWETNDTLFSVVALPWLSEGEHV----VDVVVENSASR 919
Cdd:TIGR00864 801 SGANAEAKAFWPGGNSSARFENVCPAEFAsrlchpsTFEGGCAEEAEDSLFAVLALNWLKEGEHTgpvqVDLMAENNASE 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 920 ANLSLRVTAEEPICGLRATPSPEARVLQGVLVRYSPVVEAGSDMVFRWTINDKQSLTFQNVVFNVIYQSAAVFKLSLTAS 999
Cdd:TIGR00864 881 ANLSLLVQAEEPICGLRAQPHPAARVLMESLVRYSASVEAGSDMTFKWTIDDKPFFTFQNTVFNVIYQHAAVFKLSLTAM 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1000 NHVSNVTVNYNVTVERMNRMQGLQVSTVPAVLSPNATLALTAGVLVDSAVEVAFLWTFGDGEQALHQFQPPYNESFPVPD 1079
Cdd:TIGR00864 961 NHVSNLTEDFNVTVDRLNPMQGLQVKGVPAVLPPGATLALTAGVLIDMAVEAAFLWSFGDGEQALFEFKPPYNESFPCPD 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1080 PSVAQVLVEHNVMHTYAAPGEYLLTVLASNAFENLTQQVPVSVRASLPSVAVGVSDGVLVAGRPVTFYPHPLPSPGGVLY 1159
Cdd:TIGR00864 1041 PSPAQVLLEHNVMHIYAAPGEYLATVLASNAFENISQQINMSVRAILPRVAIGTEDGLLLAGKPADFEAHPLPSPGGIHY 1120
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1160 TWDFGDGSPVLTQSQPAANHTYASRGTYHVRLEVNNTVSGAAAQADVRVFEELRGLSVDMSLAVEQGAPVVVSAAVQTGD 1239
Cdd:TIGR00864 1121 EWDFGDGSALLQGRQPAAAHTFAKRGPFHVCLEVNNTISGAAACADMFAFEEIEGLSADMSLATELGAATTVRAALQSGD 1200
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1240 NITWTFDMGDGTVLSGPEATVEHVYLRAQNCTVTVGAASPAGHLARSLHVLVFVLEVLRVEPAACIPTQPDARLTAYVTG 1319
Cdd:TIGR00864 1201 NITWTFDMGDGKSLSGPEATVEHKYAKAGNCTVNIGAANAAGHGARIIHVEVFVFEVAGIEPAACIGEHADANFRARVSG 1280
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1320 NPAHYLFDWTFGDGSSNTTVRGCPTVTHNFTRSGTFPLALVLSSRVNRAHYFTSICVEPEVGNVTLQPERQFVQLGDEAW 1399
Cdd:TIGR00864 1281 NAAHYLFDWSFGDGSPNETHHGCPGISHNFRGNGTFPLALTISSGVNKAHFFTQICVEPELGKISLQAEKQFFALGDEAQ 1360
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1400 LVACAWPPFPYRYTWDFGTEEAAPTRARGPEVTFIYRDPGSYLVTVTASNNISAANDSALVEVQEPVLVTSIKVNGSLG- 1478
Cdd:TIGR00864 1361 FQACAEPEFNYRYEWDFGGEEAAPLPAAGAEVTFIYNDPGCYLVTVAASNNISAANDSALIEVLEPVGATSFKHNGSHGn 1440
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1479 -LELQQPYLFSAVGRGRPASYLWDLGDGGWLEGPEVTHAYNSTGDFTVRVAGWNEVSRSEAWLNVTVKRRVRGLVVNASR 1557
Cdd:TIGR00864 1441 nLELGQPYLFSAFGRARNASYLWDFGDGGLLEGPEILHAFNSPGDFNIRLAAANEVGKNEATLNVAVKARVRGLTINASL 1520
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1558 TVVPLNGSVSFSTSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQDSIFVYVLQLIEGLQV 1637
Cdd:TIGR00864 1521 TNVPLNGSVHFEAHLDAGDDVRFSWILCDHCTPIFGGNTIFYTFRSVGTFNIIVTAENDVGAAQASIFLFVLQEIEGLQI 1600
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1638 VGG-------------GRYFPTNHTVQLQAVVRDGTNVSYSWTAWRD---RGPALAGSGKGFSLTVLEAGTYHVQLRATN 1701
Cdd:TIGR00864 1601 LGEtaegggggvqeldGCYFETNHTVQFHAGFKDGTNLSFSWNAILDnepDGPAFAGSGKGAKLNPLEAGPCDIFLQAAN 1680
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1702 MLGSAWADCTMDFVEPVGWLMVAASPNPAAVNTSVTLSAELAGGSGVVYTWSLEEGLSWETSEPFTTHSFPTPGLHLVTM 1781
Cdd:TIGR00864 1681 LLGQATADCTIDFLEPAGNLMLAASDNPAAVNALINLSAELAEGSGLQYRWFLEEGDDLETSEPFMSHSFPSAGLHLVTM 1760
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1782 TAGNPLGSANATVEVDVQVPVSGLSIRASEPGGS-FVAAGSSVPFWGQLATGTNVSWCWAVPGGSSKRGPHVTMVFPDAG 1860
Cdd:TIGR00864 1761 KAFNELGSANASEEVDVQEPISGLKIRAADAGEQnFFAADSSVCFQGELATGTNVSWCWAIDGGSSKMGKHACMTFPDAG 1840
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1861 TFSIRLNASNAVSWVSATYNLTAEEPIVGLVLWASSKVVAPGQLVHFQILLAAGSAVTFRLQVGGANPEVL-PGPRFSHS 1939
Cdd:TIGR00864 1841 TFAIRLNASNAVSGKSASREFFAEEPIFGLELKASKKIAAIGEKVEFQILLAAGSAVNFRLQIGGAAPEVLqPGPRFSHS 1920
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1940 FPRVGDHVVSVRGKNHVSWAQAQVRIVVLEAVSGLQVPNCCEPGIATGTERNFTARVQRGSRVAYAWYFSLQKVQGDSLV 2019
Cdd:TIGR00864 1921 FPRVDDHMVNLRAKNEVSCAQANLHIEVLEAVRGLQIPDCCAAGIATGEEKNFTANVQRGKPVAFAWTFDLHHLHGDSLV 2000
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2020 ILSGRDVTYTPVAAGLLEIQVRAFNALGSENRTLVLEVQDAVQYVALQSGP--CFTNRSAQFEAATSPSPRRVAYHWDFG 2097
Cdd:TIGR00864 2001 IHMGKDVSYTAEAAGLLEIQLGAFNALGAENITLQLEAQDALMDAALQAGPqdCFTNKMAQFEAATSPKPNFMACHWDFG 2080
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2098 DGSPGQDTDEPRAEHSYLRPGDYRVQVNASNLVSFFVAQATVTVQVLACREPEVDVVLPLQVLMRRSQRNYLEAHVDLRD 2177
Cdd:TIGR00864 2081 DGSAGQDTDEPRAEHEYLHPGDYRVQVNASNLVSFFSAHAEINVQVLACEEPEVDVVLALQLAIRRSQPNLLEAHVDLKD 2160
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2178 CVTYQTEYRWEVYRTASCQRPGRPARVALPG-------------VDVSRPRLVLPRLALPVGHYCFVFVVSFGDTPLTQS 2244
Cdd:TIGR00864 2161 CLRYGAEYLWEILRAASCDNDGHFARGALNGatrsfpviplpaeVDVQRLQLSLPKLALAAGHYCFVFSLSFEDTPLKKA 2240
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2245 IQANVTVAPERLVPIIEGGSYRVWSDTRDLVLDGSESYDPNLEDGDQTPLSFHWACVASTQREAGGCALNFGPRG-SSTV 2323
Cdd:TIGR00864 2241 ACANLGVAAARLMPIIEGGSYRVWSDTQDLQLDAEESYDPNLDDDDQSLLHFHWACQASSKGEAGCCALNFGLGGkGPTL 2320
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2324 TIPRERLAAGVEYTFSLTVWKAGRKEEATNQTVLIRSGRVPIVSLECVSCKAQAVYEVSRSSYVYLEGRCLNCSSGSKRG 2403
Cdd:TIGR00864 2321 GIPGEELAAGIEYTFKLSIGKAGMKEEATNQTVLIQSGHIPIVSLECVSCKAQALYEVSQNSYVYLEGRCLNCQSGFHRG 2400
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2404 RWAARTFSNKTLVLDETTTSTGSAGMRLVLRRGVLRDGEGYTFTLTVLGRSGEEEGCASIRLSPNRPPLGGSCRLFPLG- 2482
Cdd:TIGR00864 2401 RWAARTFQNDTLVLDESSTSTGSAGMNLVLRQGVLHDGEGYNFTLHVLDDSGDEEGAASIRLHHNMPPDGGECHLFPGGe 2480
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2483 -------------AVHALTTKVHFECTGWHDAEDAGAPLVYALLLRRCRQGHCEEFCVYKGSLSSYGAVLPPGFR-PHFE 2548
Cdd:TIGR00864 2481 tgqehgdkedevwAIEALLDKVHFECSGWHDAEDAEAPLLYALLLNRCRDDHCEEFCVYKGSLPEHGAFLPPGFRsAHFE 2560
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2549 VGLAVVVQDQLGAAVVALNRSLAITLPEPNGSATGLTVWLHGLTASVLPGLLRQADPQHVIEYSLALVTVLNEYERALDV 2628
Cdd:TIGR00864 2561 VGLAITVEDHLGAAIRALNKSIAITLPDPNGEASGLPHWLHDLIASKLKGLLDQADFQHVIELSLALITVLNEYEQALDS 2640
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2629 AAEPKHERQHRAQIRKNITETLVSLRVHTVDDIQQIAAALAQCMGPSRELVCRSCLKQTLHKLEAMMLILQAETTAGTVT 2708
Cdd:TIGR00864 2641 AAEPKHERGHRAQIRKNITEALTALDLHTVDDIQQIAAALAQCMAPSREFICEECLKQTLHKLEAMLEILQADTKAGIVT 2720
|
2730 2740
....*....|....*....|
gi 119605959 2709 PTAIGDSILNITGDLIHLAS 2728
Cdd:TIGR00864 2721 PTAIADNILNIMGDLIHLAS 2740
|
|
| REJ |
pfam02010 |
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ... |
2171-2614 |
7.84e-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: 425.76 E-value: 7.84e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2171 AHVDLRDCV-TYQTEYRWEVYRTASC---QRPGRPARVALPGVDvsrprlvLPRLALPVGHYCFVFVVSFGDTP-LTQSI 2245
Cdd:pfam02010 1 ASVELNGCFsAYTIDYLWSVFTVSSNlnlQTISSPKDLVLPQLT-------IPSGTLPYGTYVFTLTVSLSSTPsLAGTD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2246 QANVTVAPERLVPIIEGGSYRVWSDTRDLVLDGSESYDPNLEDGDQTPLSFHWACVAST------QREAGGCA-----LN 2314
Cdd:pfam02010 74 IITVTVQPSPLVAVIDGGSSRVVGYNQDLTLDGSESYDPDVDPGSSSGLTYLWSCRRSSsgdnplLNNDPVCFsdqneGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2315 FGPRGSSTVTIPRERLAAGVEYTFSLTVWKAGRKEEATNQTVLIRSGRVPIVSLECVSCKAQAVYEVSRssYVYLEGRCL 2394
Cdd:pfam02010 154 LLQSTSSSLTIPASTLQANVTYTFKLTVSKGSRNSASTTQTILVVDGNPPIIILSCISNCNRKNNPVDR--LVLLASTCL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2395 NCSSGSKRG--RWAARTFSNKTLVLD--ETTTSTGSAGMRLVLRRGVLRDGEGYTFTLTVLGRSGEEEGCASIRLSPNRP 2470
Cdd:pfam02010 232 NCSSDLSDVtyRWLSLGSENTSLVLDqlNSQTSTGRSGPYLVIKAGVLQSGVSYRFTLIVTVYPGLVSGLASISFITNAP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2471 PLGGSCRLFPLGAvHALTTKVHFECTGWHDAEDagaPLVYALLLRRCRQGHCEEFCVYKGSLS-SYGAVLPPGFRPH-FE 2548
Cdd:pfam02010 312 PTGGTCSVTPTEG-TALETKFTVTCQGWTDDDL---PLTYQFGDISFREASEEWFLLYEGSSQiSISTFLPPGLPANdYQ 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119605959 2549 VGLAVVVQDQLGAAvVALNRSLAITLPEPNGSatglTVWLHGLTASVLPGLLRQADPQHVIEYSLA 2614
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 ... |
3118-3237 |
8.80e-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: 8.80e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3118 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLDGD--RAFHRNSLDIFRIATPHSLGSVWKIRVWHDNKGLSPAW 3195
Cdd:cd01752 1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPekPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 119605959 3196 FLQHVIVRDLQTARSAFFLVNDWLSVETEanGGLVEKEVLAA 3237
Cdd:cd01752 81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEG--DGTVERTFPVA 120
|
|
| Polycystin_dom |
pfam20519 |
Polycystin domain; This domain represents the polycystin domain from group II of Transient ... |
3713-3891 |
5.05e-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: 5.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3713 AFLAITRSEELWPWMAHVLLPYVHGNQS------------SPELGPPRLRQVRLQEA--LYPDPPGPRVHTCSAAGGFST 3778
Cdd:pfam20519 1 GLLTVTDLDDIWDWLSSVLLPALHSNKTpsglpgsfiayeSLLLGVPRLRQLRVRNSscLVHDKFVREINECHAGYSPPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3779 SDY----DVGWESPHNGSGTW-AYSAPDLL-GAWSWGSCAVYDSGGYVQELGLSLEESRDRLRFLQLHNWLDNRSRAVFL 3852
Cdd:pfam20519 81 EDRklysALPYKPVHYGSKYWfIYTPPGLLmGYDHWGHLASYPSGGYVVLLPSSREESLKRLAYLQDNNWLDRGTRAVFV 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 119605959 3853 ELTRYSPAVGLHAAVTLRLEFPAAGRALAALSVRPFALR 3891
Cdd:pfam20519 161 DFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVKLL 199
|
|
| PKD_channel |
pfam08016 |
Polycystin cation channel; This family contains the cation channel region from group II of ... |
3892-4113 |
6.81e-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: 160.91 E-value: 6.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3892 RLSAGLSLPLLT-SVCLLLFAVHFAVAEARTWHREGR------WRVLRLgawarwLLVALTAATALVRLAQLGAADRQWT 3964
Cdd:pfam08016 1 RYVTNRSLFILLcEIVFVVFFLYFVVEEILKIRKHRPsylrsvWNLLDL------AIVILSVVLIVLNIYRDFLADRLIK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3965 rFVRGRPRRFTSFDQVAQLSSAARGLAASLLFLLLVKAAQQLRFVRQWSVFGKTLCRALPELLGVTLGLVVLGVAYAQLA 4044
Cdd:pfam08016 75 -SVEASPVTFIDFDRVAQLDNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119605959 4045 ILLVSSCVDSLWSVAQALLVLCPgtglsTLCPAESWH--------LSPLLCVGLWALRLWGALRLGAVILRWRYHAL 4113
Cdd:pfam08016 154 YLLFGTQAPNFSNFVKSILTLFR-----TILGDFGYNeifsgnrvLGPLLFLTFVFLVIFILLNLFLAIINDSYVEV 225
|
|
| WSC |
smart00321 |
present in yeast cell wall integrity and stress response component proteins; Domain present in ... |
177-271 |
2.95e-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: 2.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 177 GEEYVACLPDNSSGTVAAVSFSAAHegLLQPEACSAFCFSTGQGLAALSEQGWCLCGAAQPSSA-----SFACLSLCSGp 251
Cdd:smart00321 1 GATYVGCYSDNSSRTLAAVSSYAYH--NMSVEACSNFCFSAGYALAALENGNECYCGDSLPSTSvsasdSSQCSTTCSG- 77
|
90 100
....*....|....*....|
gi 119605959 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. ... |
3120-3223 |
2.84e-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: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3120 YEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLDGDR-AFHRNSLDIFRIATPHSLGSVWKIRVWHDNKGLSPAWFLQ 3198
Cdd:pfam01477 1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNpDFERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEWFLK 80
|
90 100
....*....|....*....|....*.
gi 119605959 3199 HVIV-RDLQTARSAFFLVNDWLSVET 3223
Cdd:pfam01477 81 SITVeVPGETGGKYTFPCNSWVYGSK 106
|
|
| LH2 |
smart00308 |
Lipoxygenase homology 2 (beta barrel) domain; |
3118-3220 |
1.95e-19 |
|
Lipoxygenase homology 2 (beta barrel) domain;
Pssm-ID: 214608 [Multi-domain] Cd Length: 105 Bit Score: 86.16 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3118 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLD--GDRAFHRNSLDIFRIATPHSLGSVWKIRVWHDNKglSPAW 3195
Cdd:smart00308 1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDylFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR--HPEW 78
|
90 100
....*....|....*....|....*
gi 119605959 3196 FLQHVIVRDLQTARSAFFLVNDWLS 3220
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 |
1.01e-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: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 418 HCYRLVVEKAAWLQAQEQCQAWaGAALAMVDSPAVQRFLVSRVTRSL--DVWIGFSTVQGVEVGPAPQGEAFSleSCQNW 495
Cdd:cd00037 1 SCYKFSTEKLTWEEAQEYCRSL-GGHLASIHSEEENDFLASLLKKSSssDVWIGLNDLSSEGTWKWSDGSPLV--DYTNW 77
|
90 100 110
....*....|....*....|....*....|....*...
gi 119605959 496 LPGEPHPATAEHCVRL--GPTGWCNTDLCSAPHSYVCE 531
Cdd:cd00037 78 APGEPNPGGSEDCVVLssSSDGKWNDVSCSSKLPFICE 115
|
|
| COG3291 |
COG3291 |
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
1469-1775 |
1.09e-12 |
|
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 72.78 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1469 TSIKVNGSLGLELQqpylFSAVGRGRPASYLWDLGDGGWLEGPEVTHAYNSTGDFTVRVAGWNEV-SRSEAWLNVTVKRR 1547
Cdd:COG3291 2 TATPTSGCAPLTVQ----FTDTSSGNATSYEWDFGDGTTSTEANPSHTYTTPGTYTVTLTVTDAAgCSDTTTKTITVGAP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1548 VRGLVVNASRTVVPLNGSVSFSTSLEAGSDVrYSWVLCDRCTPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQDSIFVY 1627
Cdd:COG3291 78 NPGVTTVTTSTTVTTLANTANGGATTVVAGS-TVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1628 VLQLIEGLQVVGGGRYFPTNHTVQLQAVVRDGTNVSYSWTAWRDRGPALAGSGKGFSLTVLEAGTYHVQLRATNMLGSAW 1707
Cdd:COG3291 157 TSVSTTDVTSDGTTSASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDVTLT 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119605959 1708 ADCTMDFVEPVGWLMVAASPNPAAVNTSVTLSAELAGGSGVVYTWSLEEGLSWETSEPFTTHSFPTPG 1775
Cdd:COG3291 237 GISTGDAGTPGTNTVTTSGANTAGTSTITGGTSGVVTTSAATGTSTNGTGGLGTTTAITPGNVSTTAD 304
|
|
| GPS |
smart00303 |
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ... |
3011-3060 |
3.22e-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: 58.17 E-value: 3.22e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 119605959 3011 YTSLCQYFSEEDMVWRTEGLLPLEETSpRQAVCLTRHLTAFGASLFVPPS 3060
Cdd:smart00303 1 FNPICVFWDESSGEWSTRGCELLETNG-THTTCSCNHLTTFAVLMDVPPI 49
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
54-127 |
6.35e-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: 6.35e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119605959 54 RGLRTLGPALRIpadataLDVSHNLLRALDVglLANLSALAELDISNNKISTLEE--GIFANLFNLSEINLSGNPF 127
Cdd:cd21340 113 RSLAALSNSLRV------LNISGNNIDSLEP--LAPLRNLEQLDASNNQISDLEEllDLLSSWPSLRELDLTGNPV 180
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
48-128 |
4.83e-08 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 58.79 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 48 RVNCSGRGLRTLGPALRIPADATALDVSHNLLRALDVGLlANLSALAELDISNNKISTLEEGIfANLFNLSEINLSGNPF 127
Cdd:COG4886 117 SLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPL-GNLTNLKSLDLSNNQLTDLPEEL-GNLTNLKELDLSNNQI 194
|
.
gi 119605959 128 E 128
Cdd:COG4886 195 T 195
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
496-791 |
3.18e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 47.24 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 496 LPGEPHPATAEHCVrlgPTGWCnTDLCSAPHSYVCELQPGGPVQDAENLLVGAPSGDLQGPLTPLA-----------QQD 564
Cdd:PHA03247 2555 LPPAAPPAAPDRSV---PPPRP-APRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPlppdthapdppPPS 2630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 565 GLSAPHEPVEVMVFPGL------------------RLSREAFLTTAEFGTQELRRPAqLRLQVYRLLSTAGTPENGSEPE 626
Cdd:PHA03247 2631 PSPAANEPDPHPPPTVPpperprddpapgrvsrprRARRLGRAAQASSPPQRPRRRA-ARPTVGSLTSLADPPPPPPTPE 2709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 627 SRsPDNRTQLAPAcMPGGRWCPGANICLPLDASCHPQACANGCTSGPGLPGAPYALWREFLFSVPAGPP----------- 695
Cdd:PHA03247 2710 PA-PHALVSATPL-PPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAagpprrltrpa 2787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 696 -AQYSVTLHGQDVLMLPGDLVGLQHDAGPGALLHCSPAPGHPGPQAPYLSANASSWLPHLPAQLEGTWACPACALRLLAA 774
Cdd:PHA03247 2788 vASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPP 2867
|
330
....*....|....*..
gi 119605959 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) ... |
97-2728 |
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: 4862.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 97 DISNNKISTLEEGIFANLFNLSEINLSGNPFECDCGLAWLPRWAEEQQVRVVQPEAATCAGPGSLAGQPLLGIPLLDSGC 176
Cdd:TIGR00864 1 DISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPEAALCAGPGALAGQPLLGIPLLDSGC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 177 GEEYVACLPDNSSGTVAAVS----FSAAHEGLLQPEACSAFCFSTGQGLAALSEQGWCLCGAAQPSSASFACLSLCSGPP 252
Cdd:TIGR00864 81 DEEYVACLKDNSSGGGAARSelviFSAAHEGLFQPEACNAFCFSAGHGLAALGEQGECLCGAAQPSEANFACESLCSGPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 253 PPPAPTCRGPTLLQHVFPASPGATLVGPHGPLASGQLAAFHIAAPLPVTATRWDFGDGSAEVDAAGP----AASHRYVLP 328
Cdd:TIGR00864 161 PPPAAACRGPQLLEHIFPALPGAPIQGPHGPIASGQLAAFHAAAPLAPTAMRWDFGDGSAEVDAAGAggttAASHKYGHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 329 GRYHVTAVLALGAGSALLGTDVQVEAAPAALELVCPSSVQSDESLDLSIQNRGGSGLEAAYSIVALGEEPARAVHPLCPS 408
Cdd:TIGR00864 241 GRYHVSAMGALGAGKALAGGDVQVEAAPAALELHCPSLVQADESLDLSIQNRGGSDLDAAWKITAHGEEPAKASHPHCPK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 409 DTEIFPGNGHCYRLVVEKAAWLQAQEQCQAWAGAALAMVDSPAVQRFLVSRVTRSLD--VWIGFSTVQGVEVGPAPQGEA 486
Cdd:TIGR00864 321 DGEIFEENGHCFQIVPEEAAWLDAQEQCLARAGAALAIVDNDALQNFLARKVTHSLDrgVWIGFSDVNGAEKGPAHQGEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 487 FSLESCQNWLPGEPHPATAEHCVRLGPTGWCNTDLCSAPHSYVCELQPGGPVQDAENLLVGAPSGDLQGPLTPLAQQDGL 566
Cdd:TIGR00864 401 FEAEECEEGLAGEPHPARAEHCVRLDPRGQCNSDLCNAPHAYVCELNPGGPVPDAENFAMGAASFDLHGLLQALAAMDGL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 567 SAP-HEPVEVMVFPGLRLSREAFLTTAEFGTQELRRPAQLRLQVYRL---LSTAGTPENGSEPESRSPDNRTQLAPACMP 642
Cdd:TIGR00864 481 PAPpHEGVEVLLFPALRFSRAAFLSSAEFGTQELRRPAHILFQIYRLrcrLPGAGGPACGPEAECRPPDNRSADAPACMK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 643 GGRWCPGANICLPLDASCHPQACANGCTSGPGLPGAP----YALWREFLFSVPAGPPAQYSVTLHGQDVLMLPGDLVGLQ 718
Cdd:TIGR00864 561 GEQWCPFAHICLPLDAPCHPQACANGCSQGHGLPGAArmplYALQREFLFSLPAGPAAHVLLQDHGEDLLMLPGDLIALQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 719 HDAGPGALLHCSPAPGHPGPQAPYLSANASSWLPH------------------------LPAQLEGTWA----CPACALR 770
Cdd:TIGR00864 641 HDAGPAALIHCQPAPGHPGPRAPVFAANASEWFGHnntpvppdnlagdgadplpdpeldLKALLEGTRAswleCAACAIR 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 771 LLAATEQLTVLLGLRPNPGLRLPGRYEVRAEVGNGVSRHNLSCSFDVVSPVAGLRVIYPAPRDGRLYVPTNGSALVLQVD 850
Cdd:TIGR00864 721 LLAAGEQETRLLGAELNAGLPLPGLYELLAESAKGSDLHNASCSFDVLPPLAGLRVIHPAPQDGRLFLESNGSALLLQVD 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 851 SGANATATARWPGGSVSARFENVCPALVA-------TFVPGCPWETNDTLFSVVALPWLSEGEHV----VDVVVENSASR 919
Cdd:TIGR00864 801 SGANAEAKAFWPGGNSSARFENVCPAEFAsrlchpsTFEGGCAEEAEDSLFAVLALNWLKEGEHTgpvqVDLMAENNASE 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 920 ANLSLRVTAEEPICGLRATPSPEARVLQGVLVRYSPVVEAGSDMVFRWTINDKQSLTFQNVVFNVIYQSAAVFKLSLTAS 999
Cdd:TIGR00864 881 ANLSLLVQAEEPICGLRAQPHPAARVLMESLVRYSASVEAGSDMTFKWTIDDKPFFTFQNTVFNVIYQHAAVFKLSLTAM 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1000 NHVSNVTVNYNVTVERMNRMQGLQVSTVPAVLSPNATLALTAGVLVDSAVEVAFLWTFGDGEQALHQFQPPYNESFPVPD 1079
Cdd:TIGR00864 961 NHVSNLTEDFNVTVDRLNPMQGLQVKGVPAVLPPGATLALTAGVLIDMAVEAAFLWSFGDGEQALFEFKPPYNESFPCPD 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1080 PSVAQVLVEHNVMHTYAAPGEYLLTVLASNAFENLTQQVPVSVRASLPSVAVGVSDGVLVAGRPVTFYPHPLPSPGGVLY 1159
Cdd:TIGR00864 1041 PSPAQVLLEHNVMHIYAAPGEYLATVLASNAFENISQQINMSVRAILPRVAIGTEDGLLLAGKPADFEAHPLPSPGGIHY 1120
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1160 TWDFGDGSPVLTQSQPAANHTYASRGTYHVRLEVNNTVSGAAAQADVRVFEELRGLSVDMSLAVEQGAPVVVSAAVQTGD 1239
Cdd:TIGR00864 1121 EWDFGDGSALLQGRQPAAAHTFAKRGPFHVCLEVNNTISGAAACADMFAFEEIEGLSADMSLATELGAATTVRAALQSGD 1200
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1240 NITWTFDMGDGTVLSGPEATVEHVYLRAQNCTVTVGAASPAGHLARSLHVLVFVLEVLRVEPAACIPTQPDARLTAYVTG 1319
Cdd:TIGR00864 1201 NITWTFDMGDGKSLSGPEATVEHKYAKAGNCTVNIGAANAAGHGARIIHVEVFVFEVAGIEPAACIGEHADANFRARVSG 1280
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1320 NPAHYLFDWTFGDGSSNTTVRGCPTVTHNFTRSGTFPLALVLSSRVNRAHYFTSICVEPEVGNVTLQPERQFVQLGDEAW 1399
Cdd:TIGR00864 1281 NAAHYLFDWSFGDGSPNETHHGCPGISHNFRGNGTFPLALTISSGVNKAHFFTQICVEPELGKISLQAEKQFFALGDEAQ 1360
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1400 LVACAWPPFPYRYTWDFGTEEAAPTRARGPEVTFIYRDPGSYLVTVTASNNISAANDSALVEVQEPVLVTSIKVNGSLG- 1478
Cdd:TIGR00864 1361 FQACAEPEFNYRYEWDFGGEEAAPLPAAGAEVTFIYNDPGCYLVTVAASNNISAANDSALIEVLEPVGATSFKHNGSHGn 1440
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1479 -LELQQPYLFSAVGRGRPASYLWDLGDGGWLEGPEVTHAYNSTGDFTVRVAGWNEVSRSEAWLNVTVKRRVRGLVVNASR 1557
Cdd:TIGR00864 1441 nLELGQPYLFSAFGRARNASYLWDFGDGGLLEGPEILHAFNSPGDFNIRLAAANEVGKNEATLNVAVKARVRGLTINASL 1520
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1558 TVVPLNGSVSFSTSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQDSIFVYVLQLIEGLQV 1637
Cdd:TIGR00864 1521 TNVPLNGSVHFEAHLDAGDDVRFSWILCDHCTPIFGGNTIFYTFRSVGTFNIIVTAENDVGAAQASIFLFVLQEIEGLQI 1600
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1638 VGG-------------GRYFPTNHTVQLQAVVRDGTNVSYSWTAWRD---RGPALAGSGKGFSLTVLEAGTYHVQLRATN 1701
Cdd:TIGR00864 1601 LGEtaegggggvqeldGCYFETNHTVQFHAGFKDGTNLSFSWNAILDnepDGPAFAGSGKGAKLNPLEAGPCDIFLQAAN 1680
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1702 MLGSAWADCTMDFVEPVGWLMVAASPNPAAVNTSVTLSAELAGGSGVVYTWSLEEGLSWETSEPFTTHSFPTPGLHLVTM 1781
Cdd:TIGR00864 1681 LLGQATADCTIDFLEPAGNLMLAASDNPAAVNALINLSAELAEGSGLQYRWFLEEGDDLETSEPFMSHSFPSAGLHLVTM 1760
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1782 TAGNPLGSANATVEVDVQVPVSGLSIRASEPGGS-FVAAGSSVPFWGQLATGTNVSWCWAVPGGSSKRGPHVTMVFPDAG 1860
Cdd:TIGR00864 1761 KAFNELGSANASEEVDVQEPISGLKIRAADAGEQnFFAADSSVCFQGELATGTNVSWCWAIDGGSSKMGKHACMTFPDAG 1840
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1861 TFSIRLNASNAVSWVSATYNLTAEEPIVGLVLWASSKVVAPGQLVHFQILLAAGSAVTFRLQVGGANPEVL-PGPRFSHS 1939
Cdd:TIGR00864 1841 TFAIRLNASNAVSGKSASREFFAEEPIFGLELKASKKIAAIGEKVEFQILLAAGSAVNFRLQIGGAAPEVLqPGPRFSHS 1920
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1940 FPRVGDHVVSVRGKNHVSWAQAQVRIVVLEAVSGLQVPNCCEPGIATGTERNFTARVQRGSRVAYAWYFSLQKVQGDSLV 2019
Cdd:TIGR00864 1921 FPRVDDHMVNLRAKNEVSCAQANLHIEVLEAVRGLQIPDCCAAGIATGEEKNFTANVQRGKPVAFAWTFDLHHLHGDSLV 2000
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2020 ILSGRDVTYTPVAAGLLEIQVRAFNALGSENRTLVLEVQDAVQYVALQSGP--CFTNRSAQFEAATSPSPRRVAYHWDFG 2097
Cdd:TIGR00864 2001 IHMGKDVSYTAEAAGLLEIQLGAFNALGAENITLQLEAQDALMDAALQAGPqdCFTNKMAQFEAATSPKPNFMACHWDFG 2080
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2098 DGSPGQDTDEPRAEHSYLRPGDYRVQVNASNLVSFFVAQATVTVQVLACREPEVDVVLPLQVLMRRSQRNYLEAHVDLRD 2177
Cdd:TIGR00864 2081 DGSAGQDTDEPRAEHEYLHPGDYRVQVNASNLVSFFSAHAEINVQVLACEEPEVDVVLALQLAIRRSQPNLLEAHVDLKD 2160
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2178 CVTYQTEYRWEVYRTASCQRPGRPARVALPG-------------VDVSRPRLVLPRLALPVGHYCFVFVVSFGDTPLTQS 2244
Cdd:TIGR00864 2161 CLRYGAEYLWEILRAASCDNDGHFARGALNGatrsfpviplpaeVDVQRLQLSLPKLALAAGHYCFVFSLSFEDTPLKKA 2240
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2245 IQANVTVAPERLVPIIEGGSYRVWSDTRDLVLDGSESYDPNLEDGDQTPLSFHWACVASTQREAGGCALNFGPRG-SSTV 2323
Cdd:TIGR00864 2241 ACANLGVAAARLMPIIEGGSYRVWSDTQDLQLDAEESYDPNLDDDDQSLLHFHWACQASSKGEAGCCALNFGLGGkGPTL 2320
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2324 TIPRERLAAGVEYTFSLTVWKAGRKEEATNQTVLIRSGRVPIVSLECVSCKAQAVYEVSRSSYVYLEGRCLNCSSGSKRG 2403
Cdd:TIGR00864 2321 GIPGEELAAGIEYTFKLSIGKAGMKEEATNQTVLIQSGHIPIVSLECVSCKAQALYEVSQNSYVYLEGRCLNCQSGFHRG 2400
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2404 RWAARTFSNKTLVLDETTTSTGSAGMRLVLRRGVLRDGEGYTFTLTVLGRSGEEEGCASIRLSPNRPPLGGSCRLFPLG- 2482
Cdd:TIGR00864 2401 RWAARTFQNDTLVLDESSTSTGSAGMNLVLRQGVLHDGEGYNFTLHVLDDSGDEEGAASIRLHHNMPPDGGECHLFPGGe 2480
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2483 -------------AVHALTTKVHFECTGWHDAEDAGAPLVYALLLRRCRQGHCEEFCVYKGSLSSYGAVLPPGFR-PHFE 2548
Cdd:TIGR00864 2481 tgqehgdkedevwAIEALLDKVHFECSGWHDAEDAEAPLLYALLLNRCRDDHCEEFCVYKGSLPEHGAFLPPGFRsAHFE 2560
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2549 VGLAVVVQDQLGAAVVALNRSLAITLPEPNGSATGLTVWLHGLTASVLPGLLRQADPQHVIEYSLALVTVLNEYERALDV 2628
Cdd:TIGR00864 2561 VGLAITVEDHLGAAIRALNKSIAITLPDPNGEASGLPHWLHDLIASKLKGLLDQADFQHVIELSLALITVLNEYEQALDS 2640
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2629 AAEPKHERQHRAQIRKNITETLVSLRVHTVDDIQQIAAALAQCMGPSRELVCRSCLKQTLHKLEAMMLILQAETTAGTVT 2708
Cdd:TIGR00864 2641 AAEPKHERGHRAQIRKNITEALTALDLHTVDDIQQIAAALAQCMAPSREFICEECLKQTLHKLEAMLEILQADTKAGIVT 2720
|
2730 2740
....*....|....*....|
gi 119605959 2709 PTAIGDSILNITGDLIHLAS 2728
Cdd:TIGR00864 2721 PTAIADNILNIMGDLIHLAS 2740
|
|
| REJ |
pfam02010 |
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ... |
2171-2614 |
7.84e-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: 425.76 E-value: 7.84e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2171 AHVDLRDCV-TYQTEYRWEVYRTASC---QRPGRPARVALPGVDvsrprlvLPRLALPVGHYCFVFVVSFGDTP-LTQSI 2245
Cdd:pfam02010 1 ASVELNGCFsAYTIDYLWSVFTVSSNlnlQTISSPKDLVLPQLT-------IPSGTLPYGTYVFTLTVSLSSTPsLAGTD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2246 QANVTVAPERLVPIIEGGSYRVWSDTRDLVLDGSESYDPNLEDGDQTPLSFHWACVAST------QREAGGCA-----LN 2314
Cdd:pfam02010 74 IITVTVQPSPLVAVIDGGSSRVVGYNQDLTLDGSESYDPDVDPGSSSGLTYLWSCRRSSsgdnplLNNDPVCFsdqneGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2315 FGPRGSSTVTIPRERLAAGVEYTFSLTVWKAGRKEEATNQTVLIRSGRVPIVSLECVSCKAQAVYEVSRssYVYLEGRCL 2394
Cdd:pfam02010 154 LLQSTSSSLTIPASTLQANVTYTFKLTVSKGSRNSASTTQTILVVDGNPPIIILSCISNCNRKNNPVDR--LVLLASTCL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2395 NCSSGSKRG--RWAARTFSNKTLVLD--ETTTSTGSAGMRLVLRRGVLRDGEGYTFTLTVLGRSGEEEGCASIRLSPNRP 2470
Cdd:pfam02010 232 NCSSDLSDVtyRWLSLGSENTSLVLDqlNSQTSTGRSGPYLVIKAGVLQSGVSYRFTLIVTVYPGLVSGLASISFITNAP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2471 PLGGSCRLFPLGAvHALTTKVHFECTGWHDAEDagaPLVYALLLRRCRQGHCEEFCVYKGSLS-SYGAVLPPGFRPH-FE 2548
Cdd:pfam02010 312 PTGGTCSVTPTEG-TALETKFTVTCQGWTDDDL---PLTYQFGDISFREASEEWFLLYEGSSQiSISTFLPPGLPANdYQ 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119605959 2549 VGLAVVVQDQLGAAvVALNRSLAITLPEPNGSatglTVWLHGLTASVLPGLLRQADPQHVIEYSLA 2614
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 ... |
3118-3237 |
8.80e-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: 8.80e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3118 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLDGD--RAFHRNSLDIFRIATPHSLGSVWKIRVWHDNKGLSPAW 3195
Cdd:cd01752 1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPekPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 119605959 3196 FLQHVIVRDLQTARSAFFLVNDWLSVETEanGGLVEKEVLAA 3237
Cdd:cd01752 81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEG--DGTVERTFPVA 120
|
|
| Polycystin_dom |
pfam20519 |
Polycystin domain; This domain represents the polycystin domain from group II of Transient ... |
3713-3891 |
5.05e-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: 5.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3713 AFLAITRSEELWPWMAHVLLPYVHGNQS------------SPELGPPRLRQVRLQEA--LYPDPPGPRVHTCSAAGGFST 3778
Cdd:pfam20519 1 GLLTVTDLDDIWDWLSSVLLPALHSNKTpsglpgsfiayeSLLLGVPRLRQLRVRNSscLVHDKFVREINECHAGYSPPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3779 SDY----DVGWESPHNGSGTW-AYSAPDLL-GAWSWGSCAVYDSGGYVQELGLSLEESRDRLRFLQLHNWLDNRSRAVFL 3852
Cdd:pfam20519 81 EDRklysALPYKPVHYGSKYWfIYTPPGLLmGYDHWGHLASYPSGGYVVLLPSSREESLKRLAYLQDNNWLDRGTRAVFV 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 119605959 3853 ELTRYSPAVGLHAAVTLRLEFPAAGRALAALSVRPFALR 3891
Cdd:pfam20519 161 DFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVKLL 199
|
|
| PKD_channel |
pfam08016 |
Polycystin cation channel; This family contains the cation channel region from group II of ... |
3892-4113 |
6.81e-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: 160.91 E-value: 6.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3892 RLSAGLSLPLLT-SVCLLLFAVHFAVAEARTWHREGR------WRVLRLgawarwLLVALTAATALVRLAQLGAADRQWT 3964
Cdd:pfam08016 1 RYVTNRSLFILLcEIVFVVFFLYFVVEEILKIRKHRPsylrsvWNLLDL------AIVILSVVLIVLNIYRDFLADRLIK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3965 rFVRGRPRRFTSFDQVAQLSSAARGLAASLLFLLLVKAAQQLRFVRQWSVFGKTLCRALPELLGVTLGLVVLGVAYAQLA 4044
Cdd:pfam08016 75 -SVEASPVTFIDFDRVAQLDNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119605959 4045 ILLVSSCVDSLWSVAQALLVLCPgtglsTLCPAESWH--------LSPLLCVGLWALRLWGALRLGAVILRWRYHAL 4113
Cdd:pfam08016 154 YLLFGTQAPNFSNFVKSILTLFR-----TILGDFGYNeifsgnrvLGPLLFLTFVFLVIFILLNLFLAIINDSYVEV 225
|
|
| PLAT_repeat |
cd01756 |
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ... |
3118-3237 |
6.25e-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: 6.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3118 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLD---GDRAFHRNSLDIFRIATPhSLGSVWKIRVWHDNKGLSPA 3194
Cdd:cd01756 1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKksnNKNKFERGQTDKFTVEAV-DLGKLKKIRIGHDNSGLGAG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 119605959 3195 WFLQHVIVRDLQTARSAFFLVNDWLSveTEANGGLVEKEVLAA 3237
Cdd:cd01756 80 WFLDKVEIREPGTGDEYTFPCNRWLD--KDEDDGQIVRELYPS 120
|
|
| WSC |
smart00321 |
present in yeast cell wall integrity and stress response component proteins; Domain present in ... |
177-271 |
2.95e-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: 2.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 177 GEEYVACLPDNSSGTVAAVSFSAAHegLLQPEACSAFCFSTGQGLAALSEQGWCLCGAAQPSSA-----SFACLSLCSGp 251
Cdd:smart00321 1 GATYVGCYSDNSSRTLAAVSSYAYH--NMSVEACSNFCFSAGYALAALENGNECYCGDSLPSTSvsasdSSQCSTTCSG- 77
|
90 100
....*....|....*....|
gi 119605959 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. ... |
3120-3223 |
2.84e-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: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3120 YEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLDGDR-AFHRNSLDIFRIATPHSLGSVWKIRVWHDNKGLSPAWFLQ 3198
Cdd:pfam01477 1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNpDFERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEWFLK 80
|
90 100
....*....|....*....|....*.
gi 119605959 3199 HVIV-RDLQTARSAFFLVNDWLSVET 3223
Cdd:pfam01477 81 SITVeVPGETGGKYTFPCNSWVYGSK 106
|
|
| LH2 |
smart00308 |
Lipoxygenase homology 2 (beta barrel) domain; |
3118-3220 |
1.95e-19 |
|
Lipoxygenase homology 2 (beta barrel) domain;
Pssm-ID: 214608 [Multi-domain] Cd Length: 105 Bit Score: 86.16 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3118 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLD--GDRAFHRNSLDIFRIATPHSLGSVWKIRVWHDNKglSPAW 3195
Cdd:smart00308 1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDylFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR--HPEW 78
|
90 100
....*....|....*....|....*
gi 119605959 3196 FLQHVIVRDLQTARSAFFLVNDWLS 3220
Cdd:smart00308 79 FLKSITVKDLPTGGKYHFPCNSWVY 103
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1723-1792 |
1.30e-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: 1.30e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1723 VAASPNPAAVNTSVTLSAELAGGSGVVYTWSLEEGLSWETSEPFTTHSFPTPGLHLVTMTAGNPLGSANA 1792
Cdd:pfam00801 1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
|
|
| CLECT |
smart00034 |
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ... |
406-531 |
1.51e-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: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 406 CPSDTEIFpgNGHCYRLVVEKAAWLQAQEQCQAwAGAALAMVDSPAVQRFL---VSRVTRSLDVWIGFSTVQGVEVGPAP 482
Cdd:smart00034 1 CPSGWISY--GGKCYKFSTEKKTWEDAQAFCQS-LGGHLASIHSEAENDFVaslLKNSGSSDYYWIGLSDPDSNGSWQWS 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 119605959 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 ... |
1128-1209 |
6.44e-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: 6.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1128 SVAVGVSDGVLVAGRPVTFYPHPLPSPGGVLYTWDFGDGSpvlTQSQPAANHTYASRGTYHVRLEVNNTVSGAAAQADVR 1207
Cdd:smart00089 1 VADVSASPTVGVAGESVTFTATSSDDGSIVSYTWDFGDGT---SSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVV 77
|
..
gi 119605959 1208 VF 1209
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 |
1.01e-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: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 418 HCYRLVVEKAAWLQAQEQCQAWaGAALAMVDSPAVQRFLVSRVTRSL--DVWIGFSTVQGVEVGPAPQGEAFSleSCQNW 495
Cdd:cd00037 1 SCYKFSTEKLTWEEAQEYCRSL-GGHLASIHSEEENDFLASLLKKSSssDVWIGLNDLSSEGTWKWSDGSPLV--DYTNW 77
|
90 100 110
....*....|....*....|....*....|....*...
gi 119605959 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. ... |
1892-1961 |
1.43e-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: 1.43e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1892 LWASSKVVAPGQLVHFQILLAAGSAVTFRLQVGGANPEVLPGPRFSHSFPRVGDHVVSVRGKNHVSWAQA 1961
Cdd:pfam00801 1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1637-1708 |
1.92e-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: 1.92e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119605959 1637 VVGGGRYFPTNHTVQLQAVVRDGTNVSYSWTAWRdrGPALAGSGKGFSLTVLEAGTYHVQLRATNMLGSAWA 1708
Cdd:pfam00801 1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFGD--SPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
|
|
| PLAT |
cd00113 |
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ... |
3119-3220 |
2.22e-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: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3119 KYEILVKTGWGRGSGTTAHVGIMLYGVD-SRSGHRHLDGDRAFHRNSLDIFRIATPHSLGSVWKIRVWHDNKGLSPAWFL 3197
Cdd:cd00113 2 RYTVTIKTGDKKGAGTDSNISLALYGENgNSSDIPILDGPGSFERGSTDTFQIDLKLDIGDITKVYLRRDGSGLSDGWYC 81
|
90 100
....*....|....*....|...
gi 119605959 3198 QHVIVRDLQTARSAFFLVNDWLS 3220
Cdd:cd00113 82 ESITVQALGTKKVYTFPVNRWVL 104
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1553-1622 |
2.86e-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: 2.86e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1553 VNASRTVVPLNGSVSFSTSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQD 1622
Cdd:pfam00801 1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
2068-2135 |
3.83e-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: 3.83e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119605959 2068 SGPCFTNRSAQFEAaTSPSPRRVAYHWDFGDgSPGQDTDEPRAEHSYLRPGDYRVQVNASNLVSFFVA 2135
Cdd:pfam00801 5 GTVVAAGQPVTFTA-TLADGSNVTYTWDFGD-SPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1131-1202 |
4.66e-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: 4.66e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119605959 1131 VGVSDGVLVAGRPVTFYPHpLPSPGGVLYTWDFGDgSPVLTQSQPAANHTYASRGTYHVRLEVNNTVSGAAA 1202
Cdd:pfam00801 1 VSASGTVVAAGQPVTFTAT-LADGSNVTYTWDFGD-SPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1385-1456 |
9.49e-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: 9.49e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119605959 1385 LQPERQFVQLGDEAWLVACAWPPFPYRYTWDFGteEAAPTRARGPEVTFIYRDPGSYLVTVTASNNISAAND 1456
Cdd:pfam00801 1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFG--DSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
2060-2142 |
2.93e-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: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 2060 AVQYVALQSGPcfTNRSAQFEAATSPSPRRVAYHWDFGDGSpgqDTDEPRAEHSYLRPGDYRVQVNASNLVSFFVAQATV 2139
Cdd:smart00089 2 ADVSASPTVGV--AGESVTFTATSSDDGSIVSYTWDFGDGT---SSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTV 76
|
...
gi 119605959 2140 TVQ 2142
Cdd:smart00089 77 VVQ 79
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1220-1285 |
7.43e-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: 7.43e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119605959 1220 SLAVEQGAPVVVSAAVQTGDNITWTFDMGDGTVLSGPEATVEHVYLRAQNCTVTVGAASPAGHLAR 1285
Cdd:pfam00801 5 GTVVAAGQPVTFTATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1812-1877 |
9.39e-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: 9.39e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119605959 1812 PGGSFVAAGSSVPFWGQLATGTNVSWCWAVPG--GSSKRGPHVTMVFPDAGTFSIRLNASNAVSWVSA 1877
Cdd:pfam00801 3 ASGTVVAAGQPVTFTATLADGSNVTYTWDFGDspGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1129-1203 |
3.38e-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: 3.38e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119605959 1129 VAVGVSDGVLV-AGRPVTFYPHPLPSPGGVLYTWDFGDGSpVLTQSQPAANHTYASRGTYHVRLEVNNTVSGAAAQ 1203
Cdd:cd00146 1 PTASVSAPPVAeLGASVTFSASDSSGGSIVSYKWDFGDGE-VSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTK 75
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1550-1628 |
1.08e-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: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1550 GLVVNASRTVVPLNGSVSFS-TSLEAGSDVRYSWVLCDRctPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQDSIFVYV 1628
Cdd:smart00089 1 VADVSASPTVGVAGESVTFTaTSSDDGSIVSYTWDFGDG--TSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVV 78
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1468-1545 |
2.65e-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: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1468 VTSIKVNGSLGLeLQQPYLFSAV--GRGRPASYLWDLGDGGWLEGPEVTHAYNSTGDFTVRVAGWNEVSRSEAWLNVTVK 1545
Cdd:smart00089 1 VADVSASPTVGV-AGESVTFTATssDDGSIVSYTWDFGDGTSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
|
|
| COG3291 |
COG3291 |
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
1469-1775 |
1.09e-12 |
|
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 72.78 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1469 TSIKVNGSLGLELQqpylFSAVGRGRPASYLWDLGDGGWLEGPEVTHAYNSTGDFTVRVAGWNEV-SRSEAWLNVTVKRR 1547
Cdd:COG3291 2 TATPTSGCAPLTVQ----FTDTSSGNATSYEWDFGDGTTSTEANPSHTYTTPGTYTVTLTVTDAAgCSDTTTKTITVGAP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1548 VRGLVVNASRTVVPLNGSVSFSTSLEAGSDVrYSWVLCDRCTPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQDSIFVY 1627
Cdd:COG3291 78 NPGVTTVTTSTTVTTLANTANGGATTVVAGS-TVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1628 VLQLIEGLQVVGGGRYFPTNHTVQLQAVVRDGTNVSYSWTAWRDRGPALAGSGKGFSLTVLEAGTYHVQLRATNMLGSAW 1707
Cdd:COG3291 157 TSVSTTDVTSDGTTSASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDVTLT 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119605959 1708 ADCTMDFVEPVGWLMVAASPNPAAVNTSVTLSAELAGGSGVVYTWSLEEGLSWETSEPFTTHSFPTPG 1775
Cdd:COG3291 237 GISTGDAGTPGTNTVTTSGANTAGTSTITGGTSGVVTTSAATGTSTNGTGGLGTTTAITPGNVSTTAD 304
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1473-1538 |
2.24e-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: 2.24e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119605959 1473 VNGSLGLELQQPYLFSA-VGRGRPASYLWDLGD--GGWLEGPEVTHAYNSTGDFTVRVAGWNEVSRSEA 1538
Cdd:pfam00801 2 SASGTVVAAGQPVTFTAtLADGSNVTYTWDFGDspGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1725-1799 |
2.34e-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: 2.34e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119605959 1725 ASPNPAAVNTSVTLSAELAG-GSGVVYTWSLEEGLSWetSEPFTTHSFPTPGLHLVTMTAGNPLGSANATVEVDVQ 1799
Cdd:smart00089 6 ASPTVGVAGESVTFTATSSDdGSIVSYTWDFGDGTSS--TGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1819-1878 |
3.70e-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: 3.70e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119605959 1819 AGSSVPFWGQLAT-GTNVSWCWAVPGGSSKRGPHVTMVFPDAGTFSIRLNASNAVSWVSAT 1878
Cdd:smart00089 13 AGESVTFTATSSDdGSIVSYTWDFGDGTSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASAT 73
|
|
| WSC |
pfam01822 |
WSC domain; This domain is involved in carbohydrate binding. |
180-250 |
8.00e-12 |
|
WSC domain; This domain is involved in carbohydrate binding.
Pssm-ID: 460348 Cd Length: 82 Bit Score: 63.63 E-value: 8.00e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119605959 180 YVACLPDNSsGTVAAVSFSAAHEGLLQPEACSAFCFSTGQGLAALSEQGWCLCGAAQPSSASFA----CLSLCSG 250
Cdd:pfam01822 1 YLGCYSDGT-GGRRLLLGSSGDYDDMTPEKCIAFCSAAGYTYAGLEYGGECYCGNSLPSGSALAdssdCNTPCPG 74
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
70-127 |
1.21e-11 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 62.54 E-value: 1.21e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 119605959 70 TALDVSHNLLRALDVGLLANLSALAELDISNNKISTLEEGIFANLFNLSEINLSGNPF 127
Cdd:pfam13855 4 RSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1980-2051 |
1.79e-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: 1.79e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119605959 1980 CEPGIATGTERNFTARVQRGSRVAYAWYFslqkvqGDSLV-ILSGRDVTYTPVAAGLLEIQVRAFNALGSENR 2051
Cdd:pfam00801 4 SGTVVAAGQPVTFTATLADGSNVTYTWDF------GDSPGtSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
2073-2143 |
1.86e-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: 1.86e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119605959 2073 TNRSAQFEAATSPSPRRVAYHWDFGDGSpGQDTDEPRAEHSYLRPGDYRVQVNASNLVSfFVAQATVTVQV 2143
Cdd:cd00146 13 LGASVTFSASDSSGGSIVSYKWDFGDGE-VSSSGEPTVTHTYTKPGTYTVTLTVTNAVG-SSSTKTTTVVV 81
|
|
| LRRCT |
smart00082 |
Leucine rich repeat C-terminal domain; |
125-177 |
2.41e-11 |
|
Leucine rich repeat C-terminal domain;
Pssm-ID: 214507 [Multi-domain] Cd Length: 51 Bit Score: 61.29 E-value: 2.41e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 119605959 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 ... |
1552-1628 |
4.94e-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: 4.94e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119605959 1552 VVNASRTVVPLNGSVSFS-TSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQ-DSIFVYV 1628
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 |
5.38e-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: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 406 CPSDTEIFpgNGHCYRLVVEKAAWLQAQEQCQAwAGAALAMVDSPAVQRFLVSRVTRSLDVWIGFStVQGVE-----V-G 479
Cdd:cd03590 1 CPTNWKSF--QSSCYFFSTEKKSWEESRQFCED-MGAHLVIINSQEEQEFISKILSGNRSYWIGLS-DEETEgewkwVdG 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 119605959 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 |
1.01e-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: 1.01e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119605959 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 ... |
1296-1377 |
1.85e-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: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1296 VLRVEPAACIPTQP-DARLTAYVTGNPAHYLFDWTFGDGssnTTVRGcPTVTHNFTRSGTFPLALVLSSRVNRAHYFTSI 1374
Cdd:smart00089 1 VADVSASPTVGVAGeSVTFTATSSDDGSIVSYTWDFGDG---TSSTG-PTVTHTYTKPGTYTVTLTVTNAVGSASATVTV 76
|
...
gi 119605959 1375 CVE 1377
Cdd:smart00089 77 VVQ 79
|
|
| GPS |
smart00303 |
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ... |
3011-3060 |
3.22e-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: 58.17 E-value: 3.22e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 119605959 3011 YTSLCQYFSEEDMVWRTEGLLPLEETSpRQAVCLTRHLTAFGASLFVPPS 3060
Cdd:smart00303 1 FNPICVFWDESSGEWSTRGCELLETNG-THTTCSCNHLTTFAVLMDVPPI 49
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1407-1463 |
4.51e-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: 4.51e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 119605959 1407 PFPYRYTWDFGTEeaapTRARGPEVTFIYRDPGSYLVTVTASNNISAANDSALVEVQ 1463
Cdd:smart00089 27 GSIVSYTWDFGDG----TSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1645-1712 |
3.57e-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: 56.31 E-value: 3.57e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119605959 1645 PTNHTVQLQAVVR-DGTNVSYSWtawrDRGPALAGSGKGFSLTVLEAGTYHVQLRATNMLGSAWADCTM 1712
Cdd:smart00089 12 VAGESVTFTATSSdDGSIVSYTW----DFGDGTSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTV 76
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1222-1281 |
4.95e-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: 4.95e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119605959 1222 AVEQGAPVVVSAAVQ-TGDNITWTFDMGDGTVLSGPEATVEHVYLRAQNCTVTVGAASPAG 1281
Cdd:cd00146 10 VAELGASVTFSASDSsGGSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVG 70
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
54-127 |
6.35e-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: 6.35e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119605959 54 RGLRTLGPALRIpadataLDVSHNLLRALDVglLANLSALAELDISNNKISTLEE--GIFANLFNLSEINLSGNPF 127
Cdd:cd21340 113 RSLAALSNSLRV------LNISGNNIDSLEP--LAPLRNLEQLDASNNQISDLEEllDLLSSWPSLRELDLTGNPV 180
|
|
| 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 |
7.35e-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: 57.00 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 406 CPSDTeiFPGNGHCYRLVVEKAAWLQAQEQCQAW-AGAALAMVDSPAVQRFLVSRV----TRSLDVWIGFSTVQGVEVGP 480
Cdd:cd03594 1 CPKGW--LPYKGNCYGYFRQPLSWSDAELFCQKYgPGAHLASIHSPAEAAAIASLIssyqKAYQPVWIGLHDPQQSRGWE 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 119605959 481 APQGEAFSLEScqnWLPGEPHPaTAEHCVRL-GPTG---WcNTDLCSAPHSYVCE 531
Cdd:cd03594 79 WSDGSKLDYRS---WDRNPPYA-RGGYCAELsRSTGflkW-NDANCEERNPFICK 128
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1226-1292 |
8.28e-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: 8.28e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119605959 1226 GAPVVVSAAVQT-GDNITWTFDMGDGTVLSGPeaTVEHVYLRAQNCTVTVGAASPAGHLARSLHVLVF 1292
Cdd:smart00089 14 GESVTFTATSSDdGSIVSYTWDFGDGTSSTGP--TVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
70-128 |
1.67e-08 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 60.33 E-value: 1.67e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 119605959 70 TALDVSHNLLRALDVGLlANLSALAELDISNNKISTLEEgiFANLFNLSEINLSGNPFE 128
Cdd:COG4886 208 EELDLSGNQLTDLPEPL-ANLTNLETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLT 263
|
|
| COG3291 |
COG3291 |
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
1140-1350 |
2.29e-08 |
|
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 59.30 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1140 AGRPVTFYPHplpSPGGVL-YTWDFGDGSpvlTQSQPAANHTYASRGTYHVRLEVNNTV-SGAAAQADVRVFEELRGLSV 1217
Cdd:COG3291 10 APLTVQFTDT---SSGNATsYEWDFGDGT---TSTEANPSHTYTTPGTYTVTLTVTDAAgCSDTTTKTITVGAPNPGVTT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1218 DMSLAVEQGAPVVVSAAVQTGDNITWTFDMGDGTVLSGPEATVEHVYLRAQNCTVTVGAASPAGHLARSLHVLVFVLEVL 1297
Cdd:COG3291 84 VTTSTTVTTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVTTSVSTTD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 119605959 1298 RVEPAACIPTQPDARLTAYVTGNPAHYLFDWTFGDGSSNTTVRGCPTVTHNFT 1350
Cdd:COG3291 164 VTSDGTTSASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTAGVTTGATS 216
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1480-1544 |
2.79e-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: 2.79e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1480 ELQQPYLFSAV--GRGRPASYLWDLGDGGWL--EGPEVTHAYNSTGDFTVRVAGWNEVSRSEA-WLNVTV 1544
Cdd:cd00146 12 ELGASVTFSASdsSGGSIVSYKWDFGDGEVSssGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTkTTTVVV 81
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1807-1878 |
3.33e-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: 3.33e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119605959 1807 IRASEPGGSFVAAGSSVPFWGQLATG---TNVSWCWAVPGGSSKRGPHVTMVFPDAGTFSIRLNASNAVSWVSAT 1878
Cdd:cd00146 1 PTASVSAPPVAELGASVTFSASDSSGgsiVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTK 75
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1024-1116 |
4.17e-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: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1024 VSTVPAVLSPNATLALTAGVLvdSAVEVAFLWTFGDgeqalhqfqppynesfpvpdpSVAQVLVEHNVMHTYAAPGEYLL 1103
Cdd:pfam00801 1 VSASGTVVAAGQPVTFTATLA--DGSNVTYTWDFGD---------------------SPGTSGSGPTVTHTYLSPGTYTV 57
|
90
....*....|...
gi 119605959 1104 TVLASNAFENLTQ 1116
Cdd:pfam00801 58 TLTASNAVGSANA 70
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
48-128 |
4.83e-08 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 58.79 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 48 RVNCSGRGLRTLGPALRIPADATALDVSHNLLRALDVGLlANLSALAELDISNNKISTLEEGIfANLFNLSEINLSGNPF 127
Cdd:COG4886 117 SLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPL-GNLTNLKSLDLSNNQLTDLPEEL-GNLTNLKELDLSNNQI 194
|
.
gi 119605959 128 E 128
Cdd:COG4886 195 T 195
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
48-128 |
5.00e-08 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 58.79 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 48 RVNCSGRGLRTLGPALripADATAL---DVSHNLLRALDVGLlANLSALAELDISNNKISTLEEGIfANLFNLSEINLSG 124
Cdd:COG4886 140 ELDLSNNQLTDLPEPL---GNLTNLkslDLSNNQLTDLPEEL-GNLTNLKELDLSNNQITDLPEPL-GNLTNLEELDLSG 214
|
....
gi 119605959 125 NPFE 128
Cdd:COG4886 215 NQLT 218
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1723-1796 |
7.49e-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: 7.49e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119605959 1723 VAASPNPAA-VNTSVTLSAE-LAGGSGVVYTWSLEEGLSWETSEPFTTHSFPTPGLHLVTMTAGNPLGSAN---ATVEV 1796
Cdd:cd00146 3 ASVSAPPVAeLGASVTFSASdSSGGSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSStktTTVVV 81
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1021-1122 |
8.65e-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: 8.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1021 GLQVSTVPAVLSPNATLALTAGVLVDSAVeVAFLWTFGDGeqalhqfqppynesfpvpdpsvaQVLVEHNVMHTYAAPGE 1100
Cdd:smart00089 1 VADVSASPTVGVAGESVTFTATSSDDGSI-VSYTWDFGDG-----------------------TSSTGPTVTHTYTKPGT 56
|
90 100
....*....|....*....|..
gi 119605959 1101 YLLTVLASNAFENLTQQVPVSV 1122
Cdd:smart00089 57 YTVTLTVTNAVGSASATVTVVV 78
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
70-128 |
8.95e-08 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 58.02 E-value: 8.95e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 119605959 70 TALDVSHNLLRALDVglLANLSALAELDISNNKISTLEEgiFANLFNLSEINLSGNPFE 128
Cdd:COG4886 231 ETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLTDLPP--LANLTNLKTLDLSNNQLT 285
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
72-128 |
1.18e-07 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 57.64 E-value: 1.18e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 119605959 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 ... |
3120-3227 |
1.53e-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: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3120 YEILVKTGWGRGSGTTAHVGIMLYGVDSRS---------GHRHLDGDRAFHRNSLDIFRIATPHSLGSVWKIRVWHDNKG 3190
Cdd:cd01754 3 YTIYVQTGSIWKAGTDSRISLQIYDADGPGlrianleawGGLMGAGHDYFERGNLDRFSGRGPCLPSPPCWMNLTSDGTG 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 119605959 3191 LSPAWFLQHVIVRDL-QTARSA--FFLVNDWLSVETEANG 3227
Cdd:cd01754 83 NHPGWYVNYVEVTQAgQHAPCMqhLFAVEQWLATDESPYM 122
|
|
| PKD_4 |
pfam18911 |
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins. |
1152-1208 |
1.86e-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: 1.86e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 119605959 1152 PSPGGVL-YTWDFGDGSpvlTQSQPAANHTYASRGTYHVRLEVNNTVSGAAAQADVRV 1208
Cdd:pfam18911 29 DPDGDILsYRWDFGDGT---TATGANVSHTYAAPGTYTVTLTVTDDSGASNSTATDTV 83
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1307-1380 |
2.24e-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: 2.24e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119605959 1307 TQPDARLTAYVTGNPAHYLFDWTFGDGssNTTVRGCPTVTHNFTRSGTFPLALVLSSRVNRAhyfTSICVEPEV 1380
Cdd:cd00146 13 LGASVTFSASDSSGGSIVSYKWDFGDG--EVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSS---STKTTTVVV 81
|
|
| PKD |
pfam00801 |
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1304-1369 |
2.63e-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: 2.63e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119605959 1304 CIPTQPDARLTAYV-TGNPAHYLfdWTFGDgsSNTTVRGCPTVTHNFTRSGTFPLALVLSSRVNRAH 1369
Cdd:pfam00801 7 VVAAGQPVTFTATLaDGSNVTYT--WDFGD--SPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSAN 69
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1888-1967 |
3.37e-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: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1888 VGLVLWASSKVVApGQLVHFQI-LLAAGSAVTFRLQVGgaNPEVLPGPRFSHSFPRVGDHVVSVRGKNHVSWAQAQVRIV 1966
Cdd:smart00089 1 VADVSASPTVGVA-GESVTFTAtSSDDGSIVSYTWDFG--DGTSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVV 77
|
.
gi 119605959 1967 V 1967
Cdd:smart00089 78 V 78
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1409-1462 |
8.80e-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: 8.80e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 119605959 1409 PYRYTWDFGTEEAAPTRarGPEVTFIYRDPGSYLVTVTASNNISAAN-DSALVEV 1462
Cdd:cd00146 29 IVSYKWDFGDGEVSSSG--EPTVTHTYTKPGTYTVTLTVTNAVGSSStKTTTVVV 81
|
|
| COG3291 |
COG3291 |
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
1725-1902 |
1.92e-06 |
|
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 53.14 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1725 ASPNPAAVNTSVTLSAeLAGGSGVVYTWSLEEGLSweTSEPFTTHSFPTPGLHLVTMTAGNPLGSANA-----TVEVDVQ 1799
Cdd:COG3291 3 ATPTSGCAPLTVQFTD-TSSGNATSYEWDFGDGTT--STEANPSHTYTTPGTYTVTLTVTDAAGCSDTttktiTVGAPNP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1800 VPVSGLSIRASEPGGSFVAAGSSVPFWGQLATGTNVSWCWAVPGGSSKRGPHVTMVFPDAGTFSIRLNASNAVSWVSATY 1879
Cdd:COG3291 80 GVTTVTTSTTVTTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVTTSV 159
|
170 180
....*....|....*....|...
gi 119605959 1880 NLTAEEPIVGLVLWASSKVVAPG 1902
Cdd:COG3291 160 STTDVTSDGTTSASTNPSVTTDT 182
|
|
| PKD_4 |
pfam18911 |
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins. |
1487-1527 |
2.41e-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: 2.41e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 119605959 1487 FSAVGRGRPASYLWDLGDGGWLEGPEVTHAYNSTGDFTVRV 1527
Cdd:pfam18911 26 ASDDPDGDILSYRWDFGDGTTATGANVSHTYAAPGTYTVTL 66
|
|
| COG3291 |
COG3291 |
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
1408-1709 |
4.24e-06 |
|
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 52.36 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1408 FPYRYTWDFGTeeaaPTRARGPEVTFIYRDPGSYLVTVTASNNI-SAANDSALVEVQEPVLVTSIKVNGSlglelqqpYL 1486
Cdd:COG3291 23 NATSYEWDFGD----GTTSTEANPSHTYTTPGTYTVTLTVTDAAgCSDTTTKTITVGAPNPGVTTVTTST--------TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1487 FSAVGRGRPASYLWDLGDGGWLEGPEVTHAYNSTGDFTVRVAGWNEVSRSEAWLNVTVKRRVRGLVVNASRTVVPLNGSV 1566
Cdd:COG3291 91 TTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1567 SFSTSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQDSIFVYVLQLIEGLQVVGGGRYFPT 1646
Cdd:COG3291 171 SASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNT 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119605959 1647 NHTVQLQAVVRDGTNVSYSWTAWRDRGPALAGSGKGFSLTVLEAGTYHVQLRATNMLGSAWAD 1709
Cdd:COG3291 251 VTTSGANTAGTSTITGGTSGVVTTSAATGTSTNGTGGLGTTTAITPGNVSTTADVTGGTATLA 313
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
276-348 |
5.32e-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: 5.32e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119605959 276 TLVGPHGPLAS-GQLAAFHIAAPLP--VTATRWDFGDGSAEVdAAGPAASHRYVLPGRYHVTAVLALGAGSALLGT 348
Cdd:cd00146 2 TASVSAPPVAElGASVTFSASDSSGgsIVSYKWDFGDGEVSS-SGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKT 76
|
|
| COG3291 |
COG3291 |
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
1025-1384 |
1.72e-05 |
|
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 50.44 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1025 STVPAVLSPNATLALTAgvlVDSAVEVAFLWTFGDGEQAlhqfqppynesfpvpdpsvaqvlVEHNVMHTYAAPGEYLLT 1104
Cdd:COG3291 2 TATPTSGCAPLTVQFTD---TSSGNATSYEWDFGDGTTS-----------------------TEANPSHTYTTPGTYTVT 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1105 VLASNAF-ENLTQQVPVSVRASLPSVAVGVSDGVLVAGRPVTFYPHPLPSPGGVLYTWDFGDGSPVLTQSQPAANHTYAS 1183
Cdd:COG3291 56 LTVTDAAgCSDTTTKTITVGAPNPGVTTVTTSTTVTTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTTTT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1184 RGTYHVRLEVNNTVSGAAAQADVRVFEELRGLSVDmslaveqGAPVVVSAAVQTGDNITWTFDMGDGTVLSGPEATVEHV 1263
Cdd:COG3291 136 TGTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTT-------SASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1264 YLRAQNCTVTVGAASPAGHLARSLHVLVFVLEVLRVEPAACIPTQPDARLTAYVTGNPAHYLFDWTFGDGSSNTTVRGCP 1343
Cdd:COG3291 209 GVTTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNTVTTSGANTAGTSTITGGTSGVVTTSAATGTSTNGTGGL 288
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 119605959 1344 TVTHNFTRSGTFPLALVLSSRVNRAHYFTSICVEPEVGNVT 1384
Cdd:COG3291 289 GTTTAITPGNVSTTADVTGGTATLAVSSTLTTNDTTGSSST 329
|
|
| PKD_4 |
pfam18911 |
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins. |
300-344 |
2.24e-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: 2.24e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 119605959 300 VTATRWDFGDGSAevdAAGPAASHRYVLPGRYHVTAVLALGAGSA 344
Cdd:pfam18911 34 ILSYRWDFGDGTT---ATGANVSHTYAAPGTYTVTLTVTDDSGAS 75
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
70-128 |
2.34e-05 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 50.32 E-value: 2.34e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 119605959 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. |
1411-1462 |
2.37e-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: 2.37e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 119605959 1411 RYTWDFGTEeaapTRARGPEVTFIYRDPGSYLVTVTASNNISAANDSALVEV 1462
Cdd:pfam18911 36 SYRWDFGDG----TTATGANVSHTYAAPGTYTVTLTVTDDSGASNSTATDTV 83
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1972-2058 |
2.59e-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: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1972 SGLQVPNCCEPgiATGTERNFTARVQR-GSRVAYAWYFslqkvqGDSLViLSGRDVTYTPVAAGLLEIQVRAFNALGSEN 2050
Cdd:smart00089 1 VADVSASPTVG--VAGESVTFTATSSDdGSIVSYTWDF------GDGTS-STGPTVTHTYTKPGTYTVTLTVTNAVGSAS 71
|
....*...
gi 119605959 2051 RTLVLEVQ 2058
Cdd:smart00089 72 ATVTVVVQ 79
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
301-353 |
2.62e-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: 2.62e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 119605959 301 TATRWDFGDGSaevDAAGPAASHRYVLPGRYHVTAVLALGAGSALLGTDVQVE 353
Cdd:smart00089 30 VSYTWDFGDGT---SSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1891-1967 |
3.70e-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: 3.70e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119605959 1891 VLWASSKVVAPGQLVHFQI-LLAAGSAVTFRLQVGGANPEVLPGPRFSHSFPRVGDHVVSVRGKNHVSWAQAQVRIVV 1967
Cdd:cd00146 3 ASVSAPPVAELGASVTFSAsDSSGGSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTTTVV 80
|
|
| COG3291 |
COG3291 |
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
2076-2142 |
4.24e-05 |
|
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 48.90 E-value: 4.24e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119605959 2076 SAQFEAATSPSPrrVAYHWDFGDGSpgqDTDEPRAEHSYLRPGDYRVQVNASNLV-SFFVAQATVTVQ 2142
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 |
5.07e-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: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 406 CPSDTEIFpgNGHCYRLVVEKAAWLQAQEQCQAwAGAALAMVDSPAVQRFLvSRVTRSLDVWIGFSTVQGVEVGPAPQGE 485
Cdd:cd03593 1 CPKDWICY--GNKCYYFSMEKKTWNESKEACSS-KNSSLLKIDDEEELEFL-QSQIGSSSYWIGLSREKSEKPWKWIDGS 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 119605959 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. |
2076-2128 |
8.30e-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: 8.30e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 119605959 2076 SAQFEAATS--PSPRRVAYHWDFGDGSPGqdtDEPRAEHSYLRPGDYRVQVNASN 2128
Cdd:pfam18911 19 TVTFDASASddPDGDILSYRWDFGDGTTA---TGANVSHTYAAPGTYTVTLTVTD 70
|
|
| CLECT_CEL-1_like |
cd03589 |
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ... |
406-532 |
1.42e-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: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 406 CPSDTEIFpgNGHCYRLVVEKAAWLQAQEQCQAWAG----AALAMVDSPAVQRFL------VSRVTRSLDVWIGFStvQG 475
Cdd:cd03589 1 CPTFWTAF--GGYCYRFFGDRLTWEEAELRCRSFSIpgliAHLVSIHSQEENDFVydlfesSRGPDTPYGLWIGLH--DR 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119605959 476 VEVGPA--PQGEAFSLEscqNWLPGEPHPA-TAEHCVRLGPTG-----WcNTDLCSAPHSYVCEL 532
Cdd:cd03589 77 TSEGPFewTDGSPVDFT---KWAGGQPDNYgGNEDCVQMWRRGdagqsW-NDMPCDAVFPYICKM 137
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
3756-4281 |
1.42e-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: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3756 EALYPDPPGPRV--------HTCSAAGGFSTSDYDVGWESPHNGSGTWAYSAPDLLGAWSWGSCAVYDSGGYVQELGLSL 3827
Cdd:COG3321 850 SALYPGRGRRRVplptypfqREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAAL 929
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3828 EESRDRLRFLQLHNWLDNRSRAVFLELTRYSPAVGLHAAVTLRLEFPAAGRALAALSVRPFALRRLSAGLSLPLLTSVCL 3907
Cdd:COG3321 930 LALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAA 1009
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3908 LLFAVHFAVAEARTWHREGRWRVLRLGAWARWLLVALTAATALVRLAQLGAADRQWTRFVRGRPRRFTSFDQVAQLSSAA 3987
Cdd:COG3321 1010 LLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAA 1089
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 3988 RGLAASLLFLLLVKAAQQLRFVRQWSVFGKTLCRALPELLGVTLGLVVLGVAYAQLAILLVSSCVDSLWSVAQALLVLCP 4067
Cdd:COG3321 1090 LAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLA 1169
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 4068 GTGLSTLCPAESWHLSPLLCVGLWALRLWGALRLGAVILRWRYHALRGELYRPAWEPQDYEMVELFLRRLRLWMGLSKVK 4147
Cdd:COG3321 1170 AAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALA 1249
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 4148 EFRHKVRFEGMEPLPSRSSRGSKVSPDVPPPSAGSDASHPSTSSSQLDGLSVSLGRLGTRCEPEPSRLQAVFEALLTQFD 4227
Cdd:COG3321 1250 AAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAA 1329
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 119605959 4228 RLNQA-TEDVYQLEQQLHSLQGRRSSRAPAGSSRGPSPGLRPALPSRLARASRGV 4281
Cdd:COG3321 1330 LAALAaAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAA 1384
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
496-791 |
3.18e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 47.24 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 496 LPGEPHPATAEHCVrlgPTGWCnTDLCSAPHSYVCELQPGGPVQDAENLLVGAPSGDLQGPLTPLA-----------QQD 564
Cdd:PHA03247 2555 LPPAAPPAAPDRSV---PPPRP-APRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPlppdthapdppPPS 2630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 565 GLSAPHEPVEVMVFPGL------------------RLSREAFLTTAEFGTQELRRPAqLRLQVYRLLSTAGTPENGSEPE 626
Cdd:PHA03247 2631 PSPAANEPDPHPPPTVPpperprddpapgrvsrprRARRLGRAAQASSPPQRPRRRA-ARPTVGSLTSLADPPPPPPTPE 2709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 627 SRsPDNRTQLAPAcMPGGRWCPGANICLPLDASCHPQACANGCTSGPGLPGAPYALWREFLFSVPAGPP----------- 695
Cdd:PHA03247 2710 PA-PHALVSATPL-PPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAagpprrltrpa 2787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 696 -AQYSVTLHGQDVLMLPGDLVGLQHDAGPGALLHCSPAPGHPGPQAPYLSANASSWLPHLPAQLEGTWACPACALRLLAA 774
Cdd:PHA03247 2788 vASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPP 2867
|
330
....*....|....*..
gi 119605959 775 TEQLTVLLGLRPNPGLR 791
Cdd:PHA03247 2868 SRSPAAKPAAPARPPVR 2884
|
|
| PKD |
smart00089 |
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
934-1014 |
5.62e-04 |
|
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: 41.28 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 934 GLRATPSPEARVLQGVLVRYSPVVEAGSDMVFRWTINDKQSLTFQNVVFnvIYQSAAVFKLSLTASNHVSNVTVNYNVTV 1013
Cdd:smart00089 1 VADVSASPTVGVAGESVTFTATSSDDGSIVSYTWDFGDGTSSTGPTVTH--TYTKPGTYTVTLTVTNAVGSASATVTVVV 78
|
.
gi 119605959 1014 E 1014
Cdd:smart00089 79 Q 79
|
|
| PKD |
cd00146 |
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1643-1715 |
6.39e-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: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1643 YFPTNHTVQLQAVVR-------DGTNVSYSWTaWRDrGPALAGSGKGFSLTVLEAGTYHVQLRATNMLGSAWADCTMDFV 1715
Cdd:cd00146 4 SVSAPPVAELGASVTfsasdssGGSIVSYKWD-FGD-GEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTTTVVV 81
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
93-125 |
1.24e-03 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 39.82 E-value: 1.24e-03
10 20 30
....*....|....*....|....*....|...
gi 119605959 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. |
1723-1800 |
2.22e-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: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119605959 1723 VAASPNPAAVNTSVTLSAE---LAGGSGVVYTWSLEEGLSWETSEPftTHSFPTPGLHLVTMTAGNPLGSANATVEVDVQ 1799
Cdd:pfam18911 7 DAGGDRIVAEGETVTFDASasdDPDGDILSYRWDFGDGTTATGANV--SHTYAAPGTYTVTLTVTDDSGASNSTATDTVT 84
|
.
gi 119605959 1800 V 1800
Cdd:pfam18911 85 V 85
|
|
| |
