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Conserved domains on  [gi|1622916324|ref|XP_028697316|]
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polycystin-1 isoform X9 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PCC super family cl28216
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
99-2476 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.


The actual alignment was detected with superfamily member TIGR00864:

Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 3375.51  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324   99 DISNNKISTLEEGIFANLFNLSEINLSGNPFECDCGLVWLPRWAEEQQVRVVQPEAATCAGPGSLAGQPLLGIPLLDSDC 178
Cdd:TIGR00864    1 DISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPEAALCAGPGALAGQPLLGIPLLDSGC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  179 GEEYIACLPDNSSGTVAAVA----FSAAHEGLLQPEACSAFCFSTGRGLAALSEQGWCLCGAAQPSSASFACLSF----- 249
Cdd:TIGR00864   81 DEEYVACLKDNSSGGGAARSelviFSAAHEGLFQPEACNAFCFSAGHGLAALGEQGECLCGAAQPSEANFACESLcsgpp 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  250 ------CSGP-------PPPPALDCGGPtllqHVFPASPGAALVGPHGPLAS-------GQLAA-FHIAAPLPVTATRWD 308
Cdd:TIGR00864  161 pppaaaCRGPqllehifPALPGAPIQGP----HGPIASGQLAAFHAAAPLAPtamrwdfGDGSAeVDAAGAGGTTAASHK 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  309 FG-DGSPEVDAAGPAASHRYVLPGRYHVTA------------VVA-------------LGVSSALLGTNVQVEAAPAALE 362
Cdd:TIGR00864  237 YGhPGRYHVSAMGALGAGKALAGGDVQVEAapaalelhcpslVQAdesldlsiqnrggSDLDAAWKITAHGEEPAKASHP 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  363 LvCPSSV----QSDESLKLSI------------QNRGGSGLEAAYSIVALGEELARVVHPLcpsDTEIFPGNGHCYRLVV 426
Cdd:TIGR00864  317 H-CPKDGeifeENGHCFQIVPeeaawldaqeqcLARAGAALAIVDNDALQNFLARKVTHSL---DRGVWIGFSDVNGAEK 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  427 EKAAWLQAQ--EQCRAWagaaLAMVDSPAVQRFLVS--------------------------RVTRSLDVWIGFST--VQ 476
Cdd:TIGR00864  393 GPAHQGEAFeaEECEEG----LAGEPHPARAEHCVRldprgqcnsdlcnaphayvcelnpggPVPDAENFAMGAASfdLH 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  477 GPETGLAPQG----------------------EAF--SLESCQNWL--------------------------------PG 500
Cdd:TIGR00864  469 GLLQALAAMDglpapphegvevllfpalrfsrAAFlsSAEFGTQELrrpahilfqiyrlrcrlpgaggpacgpeaecrPP 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  501 EPHPATAEHCVRLGPtgWCN-----------------TDLCSAPHSYVCELR--------------PGGP-----VQD-A 543
Cdd:TIGR00864  549 DNRSADAPACMKGEQ--WCPfahiclpldapchpqacANGCSQGHGLPGAARmplyalqreflfslPAGPaahvlLQDhG 626
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  544 ENLLVGapSGDL------QGP--LTPLTPQDGLSAPHEPV--------------------------EVMVFPGLSLSHEA 589
Cdd:TIGR00864  627 EDLLML--PGDLialqhdAGPaaLIHCQPAPGHPGPRAPVfaanasewfghnntpvppdnlagdgaDPLPDPELDLKALL 704
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  590 FLTTAE------------FGTQELRRPAQLRLQ-------VYRLLSTAGtpeNGSEPESRS------------------- 631
Cdd:TIGR00864  705 EGTRASwlecaacairllAAGEQETRLLGAELNaglplpgLYELLAESA---KGSDLHNAScsfdvlpplaglrvihpap 781
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  632 -------PDNRTQLVPECMPGGRWCPAA------------NVCVPLDAS--CHPQangcTSGPGLP----GALYAL---- 682
Cdd:TIGR00864  782 qdgrlflESNGSALLLQVDSGANAEAKAfwpggnssarfeNVCPAEFASrlCHPS----TFEGGCAeeaeDSLFAVlaln 857
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  683 W-------------------------------REFLFSVPAGP-PAQ------YSRYSPVVEAGSDVVFRWTINDKQSLT 724
Cdd:TIGR00864  858 WlkegehtgpvqvdlmaennaseanlsllvqaEEPICGLRAQPhPAArvlmesLVRYSASVEAGSDMTFKWTIDDKPFFT 937
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  725 FQNVVFNVIYQSAAVFKLSLTASNHVSNVTVNYNVTVERMNRMQGLWVSTVPAVLPPNATLALTAGVLVDSAVEVAFLWT 804
Cdd:TIGR00864  938 FQNTVFNVIYQHAAVFKLSLTAMNHVSNLTEDFNVTVDRLNPMQGLQVKGVPAVLPPGATLALTAGVLIDMAVEAAFLWS 1017
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  805 FGDGEQALRQFHPPYNESFPVPDPSVAQVLVEHNVTHTYAAPGEYILTVLTSNAFENLTQQVPVSVRAALPSMAVGVSDS 884
Cdd:TIGR00864 1018 FGDGEQALFEFKPPYNESFPCPDPSPAQVLLEHNVMHIYAAPGEYLATVLASNAFENISQQINMSVRAILPRVAIGTEDG 1097
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  885 VLVAGRPITFYPHPLPSPGGVLYTWDFGDSSPVLTQSQPTANHTYASRGTYRVHLEVNNTVSSALAQADVRVFEELRGLS 964
Cdd:TIGR00864 1098 LLLAGKPADFEAHPLPSPGGIHYEWDFGDGSALLQGRQPAAAHTFAKRGPFHVCLEVNNTISGAAACADMFAFEEIEGLS 1177
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  965 VNMSLAVEQGAPVVVSAAVQTGDDITWTFDMGDGTVLSGPEDTVEHVYLRAQNCTVTVGAASPAGRLAQSLHVLVFVLEV 1044
Cdd:TIGR00864 1178 ADMSLATELGAATTVRAALQSGDNITWTFDMGDGKSLSGPEATVEHKYAKAGNCTVNIGAANAAGHGARIIHVEVFVFEV 1257
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1045 LRIEPAACIPTQPDARLTAYVTGNPAHYLFDWTFGDGSSNTTVRGRPTVTHNFTRSGTFPLALVLSSPVNKAHYFTSICV 1124
Cdd:TIGR00864 1258 AGIEPAACIGEHADANFRARVSGNAAHYLFDWSFGDGSPNETHHGCPGISHNFRGNGTFPLALTISSGVNKAHFFTQICV 1337
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1125 EPEVGNVTLQPERQFVQLGDEVRLVACVWPPFPYRYAWDFGTEEAAPARAGGPEVTFTYRDPGSYLVTVTASNNVSAAND 1204
Cdd:TIGR00864 1338 EPELGKISLQAEKQFFALGDEAQFQACAEPEFNYRYEWDFGGEEAAPLPAAGAEVTFIYNDPGCYLVTVAASNNISAAND 1417
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1205 SALVEVQEPVVVTDIKVNSSL--VLELQQPYLFSAVGRGRPASYLWDLGDGGRLEGPEVTHAYNSIGDFTVRVAGWNDVS 1282
Cdd:TIGR00864 1418 SALIEVLEPVGATSFKHNGSHgnNLELGQPYLFSAFGRARNASYLWDFGDGGLLEGPEILHAFNSPGDFNIRLAAANEVG 1497
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1283 RSEAWLNVTVKRRVRGLVVNASRTVVPLNGSVSFSTSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFSIIVTAE 1362
Cdd:TIGR00864 1498 KNEATLNVAVKARVRGLTINASLTNVPLNGSVHFEAHLDAGDDVRFSWILCDHCTPIFGGNTIFYTFRSVGTFNIIVTAE 1577
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1363 NEVGSAQDSIFVYVLQLIEGLQVAG-------------CGSYFPTNHTAQLQAVVRDGTNVSYSWTAWWD---RGPALAG 1426
Cdd:TIGR00864 1578 NDVGAAQASIFLFVLQEIEGLQILGetaegggggvqelDGCYFETNHTVQFHAGFKDGTNLSFSWNAILDnepDGPAFAG 1657
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1427 SGKGFSLTALEAGTYHVQLRATNMLGSAWADCTVDFVEPVGWLMVTASPNPAAVNTSVTLSAKLAGGSGVLYTWSLEEGL 1506
Cdd:TIGR00864 1658 SGKGAKLNPLEAGPCDIFLQAANLLGQATADCTIDFLEPAGNLMLAASDNPAAVNALINLSAELAEGSGLQYRWFLEEGD 1737
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1507 SWETPEPFTTHSFPTPGLHLVTVTAGNPLGSASATVEVGVQVPVSGLSIRASESGGS-FVAAGSSVPFWGQLATGTNVSW 1585
Cdd:TIGR00864 1738 DLETSEPFMSHSFPSAGLHLVTMKAFNELGSANASEEVDVQEPISGLKIRAADAGEQnFFAADSSVCFQGELATGTNVSW 1817
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1586 CWAVPGGSSKRGPHVTMVFPDAGTFSVQLNASNAVSWVSATHNLTVEEPIVGLVLWASSKVVAPGQLVHFQILLAAGSAV 1665
Cdd:TIGR00864 1818 CWAIDGGSSKMGKHACMTFPDAGTFAIRLNASNAVSGKSASREFFAEEPIFGLELKASKKIAAIGEKVEFQILLAAGSAV 1897
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1666 TFRLQVGGASPAVL-PGPRFSHSFPRVGDHVVSVQGENHVSWAQAQVRIVVLEAVSGLQVPNCCEPGIATGTERNFTARV 1744
Cdd:TIGR00864 1898 NFRLQIGGAAPEVLqPGPRFSHSFPRVDDHMVNLRAKNEVSCAQANLHIEVLEAVRGLQIPDCCAAGIATGEEKNFTANV 1977
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1745 QRGSRVAYAWYFSLQKVQGDSLVILSGRDVTYTPVAAGLLEIQVRAFNALGSENRTLVLEVQDAVQYVALRSGP--CFTN 1822
Cdd:TIGR00864 1978 QRGKPVAFAWTFDLHHLHGDSLVIHMGKDVSYTAEAAGLLEIQLGAFNALGAENITLQLEAQDALMDAALQAGPqdCFTN 2057
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1823 RSAWFEAATSPSPRRVAYHWDFGDGAPGQDTDEPRAEHCYLRPGDYRVQVNASNLVSFFVAQATVTVQVLACREPEVDVV 1902
Cdd:TIGR00864 2058 KMAQFEAATSPKPNFMACHWDFGDGSAGQDTDEPRAEHEYLHPGDYRVQVNASNLVSFFSAHAEINVQVLACEEPEVDVV 2137
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1903 LPLQVLMRRSQRNYLEAHVDLRDCVTYQTEYRWEVYRTASCQRPGRPTRVALPG-------------VDVSRPQLVLPRL 1969
Cdd:TIGR00864 2138 LALQLAIRRSQPNLLEAHVDLKDCLRYGAEYLWEILRAASCDNDGHFARGALNGatrsfpviplpaeVDVQRLQLSLPKL 2217
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1970 ALPVGHYCFVFVVSFGDTPLARSIQANVTVAPERLVPIIEGGSYRVWSDTQDLVLDGSESYDPNLEDGDQTPLSFHWACV 2049
Cdd:TIGR00864 2218 ALAAGHYCFVFSLSFEDTPLKKAACANLGVAAARLMPIIEGGSYRVWSDTQDLQLDAEESYDPNLDDDDQSLLHFHWACQ 2297
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2050 ASTQREAGGCALNFGPRG-SSVVTIPRERLAAGVEYTFSLTVWKAGRKEEATNQTVLIRRGRVPIVSLECVSCKAQAVYE 2128
Cdd:TIGR00864 2298 ASSKGEAGCCALNFGLGGkGPTLGIPGEELAAGIEYTFKLSIGKAGMKEEATNQTVLIQSGHIPIVSLECVSCKAQALYE 2377
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2129 VSRSSYVYLEGRCLNCSSGSKRGRWAARTFSNKTLVLDETTTSTGSAGMRLVLRRGVLRDGEGYTFTLTVLGHSGEEEGC 2208
Cdd:TIGR00864 2378 VSQNSYVYLEGRCLNCQSGFHRGRWAARTFQNDTLVLDESSTSTGSAGMNLVLRQGVLHDGEGYNFTLHVLDDSGDEEGA 2457
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2209 ASIRLSPNRPPLGGSCRLFPLGN--------------VHALTTKVHFECTGWHDAEDAGAPLVYALLLRRCRQGHCEEFC 2274
Cdd:TIGR00864 2458 ASIRLHHNMPPDGGECHLFPGGEtgqehgdkedevwaIEALLDKVHFECSGWHDAEDAEAPLLYALLLNRCRDDHCEEFC 2537
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2275 VYKGSLSSYGAVLPPGFR-PHFEVGLAVVVQDQLGAAVVALNRSLAIALPEPSGGTTGLTVWLHGLTASVLPGLLRQADP 2353
Cdd:TIGR00864 2538 VYKGSLPEHGAFLPPGFRsAHFEVGLAITVEDHLGAAIRALNKSIAITLPDPNGEASGLPHWLHDLIASKLKGLLDQADF 2617
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2354 QHVIEYSLALVTVLNEYEQALDVAAEPEHERQRRAQIRKNVTQTLVSLRVHTVDDIQQIAAALAQSMGPSRELVCRSCLK 2433
Cdd:TIGR00864 2618 QHVIELSLALITVLNEYEQALDSAAEPKHERGHRAQIRKNITEALTALDLHTVDDIQQIAAALAQCMAPSREFICEECLK 2697
                         2730      2740      2750      2760
                   ....*....|....*....|....*....|....*....|...
gi 1622916324 2434 QTLHKLEAMMRILQAETTAGTVTPTAIGDSILNITGDLIHLAS 2476
Cdd:TIGR00864 2698 QTLHKLEAMLEILQADTKAGIVTPTAIADNILNIMGDLIHLAS 2740
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
2863-2982 1.79e-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: 198.27  E-value: 1.79e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2863 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLDGD--RAFHRNSLDIFQIATPHSLGSVWKIRVWHDNKGLSPAW 2940
Cdd:cd01752      1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPekPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1622916324 2941 FLQHVIVRDLQTARSAFFLVNDWLSVETEanGGLVEKEVLVA 2982
Cdd:cd01752     81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEG--DGTVERTFPVA 120
Polycystin_dom super family cl48672
Polycystin domain; This domain represents the polycystin domain from group II of Transient ...
3464-3648 7.86e-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.


The actual alignment was detected with superfamily member pfam20519:

Pssm-ID: 466668  Cd Length: 199  Bit Score: 193.79  E-value: 7.86e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 3464 FLAITRSEELWPWMAHVLLPYVHGNQS------------SPELGPPRLRQVRLQEALC--PDPPGPRVHTCSAAGGFSTS 3529
Cdd:pfam20519    2 LLTVTDLDDIWDWLSSVLLPALHSNKTpsglpgsfiayeSLLLGVPRLRQLRVRNSSClvHDKFVREINECHAGYSPPSE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 3530 DY----DVGWESPHNGSGTW-AYSAPDLL-GAWSWGSCAVYDSGGYVQELGLSLEESRDRLRFLQLHNWLDnsdphplRR 3603
Cdd:pfam20519   82 DRklysALPYKPVHYGSKYWfIYTPPGLLmGYDHWGHLASYPSGGYVVLLPSSREESLKRLAYLQDNNWLD-------RG 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1622916324 3604 SRAVFVELTRYSPAVGLHAAVTLRLEFPAAGRALAALSVRPFALR 3648
Cdd:pfam20519  155 TRAVFVDFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVKLL 199
PKD_channel super family cl37568
Polycystin cation channel; This family contains the cation channel region from group II of ...
3649-3870 1.05e-43

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


The actual alignment was detected with superfamily member pfam08016:

Pssm-ID: 462341 [Multi-domain]  Cd Length: 225  Bit Score: 160.13  E-value: 1.05e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 3649 RLSAGLSLPLLT-SVCLLLFALHFAVAEARTWHREGCwHVLRpRAW--ARWLLVVLTAATALVRLAQLGAADRQWTrFVR 3725
Cdd:pfam08016    1 RYVTNRSLFILLcEIVFVVFFLYFVVEEILKIRKHRP-SYLR-SVWnlLDLAIVILSVVLIVLNIYRDFLADRLIK-SVE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 3726 GRPRRFTSFDQVAQLSSAARGLAASLLFLLLVKAAQQLRFVRQWSVFGKTLFRALPELLGATLGLVVLGVAYAQLAVLLV 3805
Cdd:pfam08016   78 ASPVTFIDFDRVAQLDNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFGYLLF 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622916324 3806 SSCVDSLWSVAQALLVLCsgtglSTLCPAESWH--------LSPLLCVGLWALRLWGALRLGAVILRWRYHAL 3870
Cdd:pfam08016  158 GTQAPNFSNFVKSILTLF-----RTILGDFGYNeifsgnrvLGPLLFLTFVFLVIFILLNLFLAIINDSYVEV 225
GPS super family cl02559
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
2756-2805 6.51e-10

GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for auto-proteolysis, so is thus named, GPS. The GPS motif is a conserved sequence of ~40 amino acids containing canonical cysteine and tryptophan residues, and is the most highly conserved part of the domain. In most, if not all, cell-adhesion GPCRs these undergo autoproteolysis in the GPS between a conserved aliphatic residue (usually a leucine) and a threonine, serine, or cysteine residue. In higher eukaryotes this motif is found embedded in the C-terminal beta-stranded part of a GAIN domain - GPCR-Autoproteolysis INducing (GAIN). The GAIN-GPS domain adopts a fold in which the GPS motif, at the C-terminus, forms five beta-strands that are tightly integrated into the overall GAIN domain. The GPS motif, evolutionarily conserved from tetrahymena to mammals, is the only extracellular domain shared by all human cell-adhesion GPCRs and PKD proteins, and is the locus of multiple human disease mutations. The GAIN-GPS domain is both necessary and sufficient functionally for autoproteolysis, suggesting an autoproteolytic mechanism whereby the overall GAIN domain fine-tunes the chemical environment in the GPS to catalyze peptide bond hydrolysis. In the cell-adhesion GPCRs and PKD proteins, the GPS motif is always located at the end of their long N-terminal extracellular regions, immediately before the first transmembrane helix of the respective protein.


The actual alignment was detected with superfamily member smart00303:

Pssm-ID: 470616  Cd Length: 49  Bit Score: 57.01  E-value: 6.51e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1622916324  2756 YTSLCQYFSEENMVWRTEGLLPLEETSPHqAVCLTRHLTAFGASLFVPPS 2805
Cdd:smart00303    1 FNPICVFWDESSGEWSTRGCELLETNGTH-TTCSCNHLTTFAVLMDVPPI 49
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
56-129 2.48e-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.


The actual alignment was detected with superfamily member cd21340:

Pssm-ID: 455733 [Multi-domain]  Cd Length: 220  Bit Score: 60.57  E-value: 2.48e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916324   56 RGLRTLGPALRIpadataLDVSHNLLRALDVglLANLSQLSELDISNNKISTLEE--GIFANLFNLSEINLSGNPF 129
Cdd:cd21340    113 RSLAALSNSLRV------LNISGNNIDSLEP--LAPLRNLEQLDASNNQISDLEEllDLLSSWPSLRELDLTGNPV 180
LRRNT smart00013
Leucine rich repeat N-terminal domain;
34-73 7.88e-04

Leucine rich repeat N-terminal domain;


:

Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 39.61  E-value: 7.88e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1622916324    34 PCAPPCLCGPapgaaCRVNCSGRGLRTLgpALRIPADATA 73
Cdd:smart00013    1 ACPAPCNCSG-----TAVDCSGRGLTEV--PLDLPPDTTL 33
 
Name Accession Description Interval E-value
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
99-2476 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: 3375.51  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324   99 DISNNKISTLEEGIFANLFNLSEINLSGNPFECDCGLVWLPRWAEEQQVRVVQPEAATCAGPGSLAGQPLLGIPLLDSDC 178
Cdd:TIGR00864    1 DISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPEAALCAGPGALAGQPLLGIPLLDSGC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  179 GEEYIACLPDNSSGTVAAVA----FSAAHEGLLQPEACSAFCFSTGRGLAALSEQGWCLCGAAQPSSASFACLSF----- 249
Cdd:TIGR00864   81 DEEYVACLKDNSSGGGAARSelviFSAAHEGLFQPEACNAFCFSAGHGLAALGEQGECLCGAAQPSEANFACESLcsgpp 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  250 ------CSGP-------PPPPALDCGGPtllqHVFPASPGAALVGPHGPLAS-------GQLAA-FHIAAPLPVTATRWD 308
Cdd:TIGR00864  161 pppaaaCRGPqllehifPALPGAPIQGP----HGPIASGQLAAFHAAAPLAPtamrwdfGDGSAeVDAAGAGGTTAASHK 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  309 FG-DGSPEVDAAGPAASHRYVLPGRYHVTA------------VVA-------------LGVSSALLGTNVQVEAAPAALE 362
Cdd:TIGR00864  237 YGhPGRYHVSAMGALGAGKALAGGDVQVEAapaalelhcpslVQAdesldlsiqnrggSDLDAAWKITAHGEEPAKASHP 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  363 LvCPSSV----QSDESLKLSI------------QNRGGSGLEAAYSIVALGEELARVVHPLcpsDTEIFPGNGHCYRLVV 426
Cdd:TIGR00864  317 H-CPKDGeifeENGHCFQIVPeeaawldaqeqcLARAGAALAIVDNDALQNFLARKVTHSL---DRGVWIGFSDVNGAEK 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  427 EKAAWLQAQ--EQCRAWagaaLAMVDSPAVQRFLVS--------------------------RVTRSLDVWIGFST--VQ 476
Cdd:TIGR00864  393 GPAHQGEAFeaEECEEG----LAGEPHPARAEHCVRldprgqcnsdlcnaphayvcelnpggPVPDAENFAMGAASfdLH 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  477 GPETGLAPQG----------------------EAF--SLESCQNWL--------------------------------PG 500
Cdd:TIGR00864  469 GLLQALAAMDglpapphegvevllfpalrfsrAAFlsSAEFGTQELrrpahilfqiyrlrcrlpgaggpacgpeaecrPP 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  501 EPHPATAEHCVRLGPtgWCN-----------------TDLCSAPHSYVCELR--------------PGGP-----VQD-A 543
Cdd:TIGR00864  549 DNRSADAPACMKGEQ--WCPfahiclpldapchpqacANGCSQGHGLPGAARmplyalqreflfslPAGPaahvlLQDhG 626
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  544 ENLLVGapSGDL------QGP--LTPLTPQDGLSAPHEPV--------------------------EVMVFPGLSLSHEA 589
Cdd:TIGR00864  627 EDLLML--PGDLialqhdAGPaaLIHCQPAPGHPGPRAPVfaanasewfghnntpvppdnlagdgaDPLPDPELDLKALL 704
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  590 FLTTAE------------FGTQELRRPAQLRLQ-------VYRLLSTAGtpeNGSEPESRS------------------- 631
Cdd:TIGR00864  705 EGTRASwlecaacairllAAGEQETRLLGAELNaglplpgLYELLAESA---KGSDLHNAScsfdvlpplaglrvihpap 781
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  632 -------PDNRTQLVPECMPGGRWCPAA------------NVCVPLDAS--CHPQangcTSGPGLP----GALYAL---- 682
Cdd:TIGR00864  782 qdgrlflESNGSALLLQVDSGANAEAKAfwpggnssarfeNVCPAEFASrlCHPS----TFEGGCAeeaeDSLFAVlaln 857
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  683 W-------------------------------REFLFSVPAGP-PAQ------YSRYSPVVEAGSDVVFRWTINDKQSLT 724
Cdd:TIGR00864  858 WlkegehtgpvqvdlmaennaseanlsllvqaEEPICGLRAQPhPAArvlmesLVRYSASVEAGSDMTFKWTIDDKPFFT 937
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  725 FQNVVFNVIYQSAAVFKLSLTASNHVSNVTVNYNVTVERMNRMQGLWVSTVPAVLPPNATLALTAGVLVDSAVEVAFLWT 804
Cdd:TIGR00864  938 FQNTVFNVIYQHAAVFKLSLTAMNHVSNLTEDFNVTVDRLNPMQGLQVKGVPAVLPPGATLALTAGVLIDMAVEAAFLWS 1017
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  805 FGDGEQALRQFHPPYNESFPVPDPSVAQVLVEHNVTHTYAAPGEYILTVLTSNAFENLTQQVPVSVRAALPSMAVGVSDS 884
Cdd:TIGR00864 1018 FGDGEQALFEFKPPYNESFPCPDPSPAQVLLEHNVMHIYAAPGEYLATVLASNAFENISQQINMSVRAILPRVAIGTEDG 1097
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  885 VLVAGRPITFYPHPLPSPGGVLYTWDFGDSSPVLTQSQPTANHTYASRGTYRVHLEVNNTVSSALAQADVRVFEELRGLS 964
Cdd:TIGR00864 1098 LLLAGKPADFEAHPLPSPGGIHYEWDFGDGSALLQGRQPAAAHTFAKRGPFHVCLEVNNTISGAAACADMFAFEEIEGLS 1177
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  965 VNMSLAVEQGAPVVVSAAVQTGDDITWTFDMGDGTVLSGPEDTVEHVYLRAQNCTVTVGAASPAGRLAQSLHVLVFVLEV 1044
Cdd:TIGR00864 1178 ADMSLATELGAATTVRAALQSGDNITWTFDMGDGKSLSGPEATVEHKYAKAGNCTVNIGAANAAGHGARIIHVEVFVFEV 1257
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1045 LRIEPAACIPTQPDARLTAYVTGNPAHYLFDWTFGDGSSNTTVRGRPTVTHNFTRSGTFPLALVLSSPVNKAHYFTSICV 1124
Cdd:TIGR00864 1258 AGIEPAACIGEHADANFRARVSGNAAHYLFDWSFGDGSPNETHHGCPGISHNFRGNGTFPLALTISSGVNKAHFFTQICV 1337
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1125 EPEVGNVTLQPERQFVQLGDEVRLVACVWPPFPYRYAWDFGTEEAAPARAGGPEVTFTYRDPGSYLVTVTASNNVSAAND 1204
Cdd:TIGR00864 1338 EPELGKISLQAEKQFFALGDEAQFQACAEPEFNYRYEWDFGGEEAAPLPAAGAEVTFIYNDPGCYLVTVAASNNISAAND 1417
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1205 SALVEVQEPVVVTDIKVNSSL--VLELQQPYLFSAVGRGRPASYLWDLGDGGRLEGPEVTHAYNSIGDFTVRVAGWNDVS 1282
Cdd:TIGR00864 1418 SALIEVLEPVGATSFKHNGSHgnNLELGQPYLFSAFGRARNASYLWDFGDGGLLEGPEILHAFNSPGDFNIRLAAANEVG 1497
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1283 RSEAWLNVTVKRRVRGLVVNASRTVVPLNGSVSFSTSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFSIIVTAE 1362
Cdd:TIGR00864 1498 KNEATLNVAVKARVRGLTINASLTNVPLNGSVHFEAHLDAGDDVRFSWILCDHCTPIFGGNTIFYTFRSVGTFNIIVTAE 1577
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1363 NEVGSAQDSIFVYVLQLIEGLQVAG-------------CGSYFPTNHTAQLQAVVRDGTNVSYSWTAWWD---RGPALAG 1426
Cdd:TIGR00864 1578 NDVGAAQASIFLFVLQEIEGLQILGetaegggggvqelDGCYFETNHTVQFHAGFKDGTNLSFSWNAILDnepDGPAFAG 1657
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1427 SGKGFSLTALEAGTYHVQLRATNMLGSAWADCTVDFVEPVGWLMVTASPNPAAVNTSVTLSAKLAGGSGVLYTWSLEEGL 1506
Cdd:TIGR00864 1658 SGKGAKLNPLEAGPCDIFLQAANLLGQATADCTIDFLEPAGNLMLAASDNPAAVNALINLSAELAEGSGLQYRWFLEEGD 1737
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1507 SWETPEPFTTHSFPTPGLHLVTVTAGNPLGSASATVEVGVQVPVSGLSIRASESGGS-FVAAGSSVPFWGQLATGTNVSW 1585
Cdd:TIGR00864 1738 DLETSEPFMSHSFPSAGLHLVTMKAFNELGSANASEEVDVQEPISGLKIRAADAGEQnFFAADSSVCFQGELATGTNVSW 1817
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1586 CWAVPGGSSKRGPHVTMVFPDAGTFSVQLNASNAVSWVSATHNLTVEEPIVGLVLWASSKVVAPGQLVHFQILLAAGSAV 1665
Cdd:TIGR00864 1818 CWAIDGGSSKMGKHACMTFPDAGTFAIRLNASNAVSGKSASREFFAEEPIFGLELKASKKIAAIGEKVEFQILLAAGSAV 1897
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1666 TFRLQVGGASPAVL-PGPRFSHSFPRVGDHVVSVQGENHVSWAQAQVRIVVLEAVSGLQVPNCCEPGIATGTERNFTARV 1744
Cdd:TIGR00864 1898 NFRLQIGGAAPEVLqPGPRFSHSFPRVDDHMVNLRAKNEVSCAQANLHIEVLEAVRGLQIPDCCAAGIATGEEKNFTANV 1977
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1745 QRGSRVAYAWYFSLQKVQGDSLVILSGRDVTYTPVAAGLLEIQVRAFNALGSENRTLVLEVQDAVQYVALRSGP--CFTN 1822
Cdd:TIGR00864 1978 QRGKPVAFAWTFDLHHLHGDSLVIHMGKDVSYTAEAAGLLEIQLGAFNALGAENITLQLEAQDALMDAALQAGPqdCFTN 2057
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1823 RSAWFEAATSPSPRRVAYHWDFGDGAPGQDTDEPRAEHCYLRPGDYRVQVNASNLVSFFVAQATVTVQVLACREPEVDVV 1902
Cdd:TIGR00864 2058 KMAQFEAATSPKPNFMACHWDFGDGSAGQDTDEPRAEHEYLHPGDYRVQVNASNLVSFFSAHAEINVQVLACEEPEVDVV 2137
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1903 LPLQVLMRRSQRNYLEAHVDLRDCVTYQTEYRWEVYRTASCQRPGRPTRVALPG-------------VDVSRPQLVLPRL 1969
Cdd:TIGR00864 2138 LALQLAIRRSQPNLLEAHVDLKDCLRYGAEYLWEILRAASCDNDGHFARGALNGatrsfpviplpaeVDVQRLQLSLPKL 2217
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1970 ALPVGHYCFVFVVSFGDTPLARSIQANVTVAPERLVPIIEGGSYRVWSDTQDLVLDGSESYDPNLEDGDQTPLSFHWACV 2049
Cdd:TIGR00864 2218 ALAAGHYCFVFSLSFEDTPLKKAACANLGVAAARLMPIIEGGSYRVWSDTQDLQLDAEESYDPNLDDDDQSLLHFHWACQ 2297
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2050 ASTQREAGGCALNFGPRG-SSVVTIPRERLAAGVEYTFSLTVWKAGRKEEATNQTVLIRRGRVPIVSLECVSCKAQAVYE 2128
Cdd:TIGR00864 2298 ASSKGEAGCCALNFGLGGkGPTLGIPGEELAAGIEYTFKLSIGKAGMKEEATNQTVLIQSGHIPIVSLECVSCKAQALYE 2377
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2129 VSRSSYVYLEGRCLNCSSGSKRGRWAARTFSNKTLVLDETTTSTGSAGMRLVLRRGVLRDGEGYTFTLTVLGHSGEEEGC 2208
Cdd:TIGR00864 2378 VSQNSYVYLEGRCLNCQSGFHRGRWAARTFQNDTLVLDESSTSTGSAGMNLVLRQGVLHDGEGYNFTLHVLDDSGDEEGA 2457
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2209 ASIRLSPNRPPLGGSCRLFPLGN--------------VHALTTKVHFECTGWHDAEDAGAPLVYALLLRRCRQGHCEEFC 2274
Cdd:TIGR00864 2458 ASIRLHHNMPPDGGECHLFPGGEtgqehgdkedevwaIEALLDKVHFECSGWHDAEDAEAPLLYALLLNRCRDDHCEEFC 2537
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2275 VYKGSLSSYGAVLPPGFR-PHFEVGLAVVVQDQLGAAVVALNRSLAIALPEPSGGTTGLTVWLHGLTASVLPGLLRQADP 2353
Cdd:TIGR00864 2538 VYKGSLPEHGAFLPPGFRsAHFEVGLAITVEDHLGAAIRALNKSIAITLPDPNGEASGLPHWLHDLIASKLKGLLDQADF 2617
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2354 QHVIEYSLALVTVLNEYEQALDVAAEPEHERQRRAQIRKNVTQTLVSLRVHTVDDIQQIAAALAQSMGPSRELVCRSCLK 2433
Cdd:TIGR00864 2618 QHVIELSLALITVLNEYEQALDSAAEPKHERGHRAQIRKNITEALTALDLHTVDDIQQIAAALAQCMAPSREFICEECLK 2697
                         2730      2740      2750      2760
                   ....*....|....*....|....*....|....*....|...
gi 1622916324 2434 QTLHKLEAMMRILQAETTAGTVTPTAIGDSILNITGDLIHLAS 2476
Cdd:TIGR00864 2698 QTLHKLEAMLEILQADTKAGIVTPTAIADNILNIMGDLIHLAS 2740
REJ pfam02010
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
1919-2362 1.52e-131

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: 421.91  E-value: 1.52e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1919 AHVDLRDCV-TYQTEYRWEVYRTASCqrpGRPTRVALPgVDVSRPQLVLPRLALPVGHYCFVFVVSFGDTP-LARSIQAN 1996
Cdd:pfam02010    1 ASVELNGCFsAYTIDYLWSVFTVSSN---LNLQTISSP-KDLVLPQLTIPSGTLPYGTYVFTLTVSLSSTPsLAGTDIIT 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1997 VTVAPERLVPIIEGGSYRVWSDTQDLVLDGSESYDPNLEDGDQTPLSFHWACVAST------QREAGGCA-----LNFGP 2065
Cdd:pfam02010   77 VTVQPSPLVAVIDGGSSRVVGYNQDLTLDGSESYDPDVDPGSSSGLTYLWSCRRSSsgdnplLNNDPVCFsdqneGTLLQ 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2066 RGSSVVTIPRERLAAGVEYTFSLTVWKAGRKEEATNQTVLIRRGRVPIVSLECVSCKAQAVYEVSRssYVYLEGRCLNCS 2145
Cdd:pfam02010  157 STSSSLTIPASTLQANVTYTFKLTVSKGSRNSASTTQTILVVDGNPPIIILSCISNCNRKNNPVDR--LVLLASTCLNCS 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2146 SGSKRG--RWAARTFSNKTLVLD--ETTTSTGSAGMRLVLRRGVLRDGEGYTFTLTVLGHSGEEEGCASIRLSPNRPPLG 2221
Cdd:pfam02010  235 SDLSDVtyRWLSLGSENTSLVLDqlNSQTSTGRSGPYLVIKAGVLQSGVSYRFTLIVTVYPGLVSGLASISFITNAPPTG 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2222 GSCRLFPLGNvHALTTKVHFECTGWHDAEDagaPLVYALLLRRCRQGHCEEFCVYKGSLS-SYGAVLPPGFRPH-FEVGL 2299
Cdd:pfam02010  315 GTCSVTPTEG-TALETKFTVTCQGWTDDDL---PLTYQFGDISFREASEEWFLLYEGSSQiSISTFLPPGLPANdYQVTV 390
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622916324 2300 AVVVQDQLGAAvVALNRSLAIALPEPSGGttglTVWLHGLTASVLPGLLRQADPQHVIEYSLA 2362
Cdd:pfam02010  391 VVVVYDSLGAA-TSVSLTITVTPPSSSDE----LLYFLLGTTSDLSALLQSGDPQQAAQLILA 448
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
2863-2982 1.79e-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: 198.27  E-value: 1.79e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2863 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLDGD--RAFHRNSLDIFQIATPHSLGSVWKIRVWHDNKGLSPAW 2940
Cdd:cd01752      1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPekPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1622916324 2941 FLQHVIVRDLQTARSAFFLVNDWLSVETEanGGLVEKEVLVA 2982
Cdd:cd01752     81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEG--DGTVERTFPVA 120
Polycystin_dom pfam20519
Polycystin domain; This domain represents the polycystin domain from group II of Transient ...
3464-3648 7.86e-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: 193.79  E-value: 7.86e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 3464 FLAITRSEELWPWMAHVLLPYVHGNQS------------SPELGPPRLRQVRLQEALC--PDPPGPRVHTCSAAGGFSTS 3529
Cdd:pfam20519    2 LLTVTDLDDIWDWLSSVLLPALHSNKTpsglpgsfiayeSLLLGVPRLRQLRVRNSSClvHDKFVREINECHAGYSPPSE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 3530 DY----DVGWESPHNGSGTW-AYSAPDLL-GAWSWGSCAVYDSGGYVQELGLSLEESRDRLRFLQLHNWLDnsdphplRR 3603
Cdd:pfam20519   82 DRklysALPYKPVHYGSKYWfIYTPPGLLmGYDHWGHLASYPSGGYVVLLPSSREESLKRLAYLQDNNWLD-------RG 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1622916324 3604 SRAVFVELTRYSPAVGLHAAVTLRLEFPAAGRALAALSVRPFALR 3648
Cdd:pfam20519  155 TRAVFVDFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVKLL 199
PKD_channel pfam08016
Polycystin cation channel; This family contains the cation channel region from group II of ...
3649-3870 1.05e-43

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: 160.13  E-value: 1.05e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 3649 RLSAGLSLPLLT-SVCLLLFALHFAVAEARTWHREGCwHVLRpRAW--ARWLLVVLTAATALVRLAQLGAADRQWTrFVR 3725
Cdd:pfam08016    1 RYVTNRSLFILLcEIVFVVFFLYFVVEEILKIRKHRP-SYLR-SVWnlLDLAIVILSVVLIVLNIYRDFLADRLIK-SVE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 3726 GRPRRFTSFDQVAQLSSAARGLAASLLFLLLVKAAQQLRFVRQWSVFGKTLFRALPELLGATLGLVVLGVAYAQLAVLLV 3805
Cdd:pfam08016   78 ASPVTFIDFDRVAQLDNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFGYLLF 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622916324 3806 SSCVDSLWSVAQALLVLCsgtglSTLCPAESWH--------LSPLLCVGLWALRLWGALRLGAVILRWRYHAL 3870
Cdd:pfam08016  158 GTQAPNFSNFVKSILTLF-----RTILGDFGYNeifsgnrvLGPLLFLTFVFLVIFILLNLFLAIINDSYVEV 225
WSC smart00321
present in yeast cell wall integrity and stress response component proteins; Domain present in ...
179-273 1.52e-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: 100.24  E-value: 1.52e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324   179 GEEYIACLPDNSSGTVAAVAFSAAHegLLQPEACSAFCFSTGRGLAALSEQGWCLCGAAQPSSA-----SFACLSFCSGp 253
Cdd:smart00321    1 GATYVGCYSDNSSRTLAAVSSYAYH--NMSVEACSNFCFSAGYALAALENGNECYCGDSLPSTSvsasdSSQCSTTCSG- 77
                            90       100
                    ....*....|....*....|
gi 1622916324   254 ppPPALDCGGPTLLQHVFPA 273
Cdd:smart00321   78 --YPAEVCGGPNRLSVYVLA 95
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
2865-2968 3.90e-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: 97.12  E-value: 3.90e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2865 YEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLDGDR-AFHRNSLDIFQIATPHSLGSVWKIRVWHDNKGLSPAWFLQ 2943
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNpDFERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEWFLK 80
                           90       100
                   ....*....|....*....|....*.
gi 1622916324 2944 HVIV-RDLQTARSAFFLVNDWLSVET 2968
Cdd:pfam01477   81 SITVeVPGETGGKYTFPCNSWVYGSK 106
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
2863-2965 4.38e-19

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 85.00  E-value: 4.38e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  2863 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLD--GDRAFHRNSLDIFQIATPHSLGSVWKIRVWHDNKglSPAW 2940
Cdd:smart00308    1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDylFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR--HPEW 78
                            90       100
                    ....*....|....*....|....*
gi 1622916324  2941 FLQHVIVRDLQTARSAFFLVNDWLS 2965
Cdd:smart00308   79 FLKSITVKDLPTGGKYHFPCNSWVY 103
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
420-533 4.43e-18

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: 82.67  E-value: 4.43e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  420 HCYRLVVEKAAWLQAQEQCRAWaGAALAMVDSPAVQRFLVSRVTRSL--DVWIGFSTVQGPETGLAPQGEAFSleSCQNW 497
Cdd:cd00037      1 SCYKFSTEKLTWEEAQEYCRSL-GGHLASIHSEEENDFLASLLKKSSssDVWIGLNDLSSEGTWKWSDGSPLV--DYTNW 77
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1622916324  498 LPGEPHPATAEHCVRL--GPTGWCNTDLCSAPHSYVCE 533
Cdd:cd00037     78 APGEPNPGGSEDCVVLssSSDGKWNDVSCSSKLPFICE 115
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
1235-1552 1.29e-10

Uncharacterized conserved protein, PKD repeat domain [Function unknown];


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 66.23  E-value: 1.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1235 FSAVGRGRPASYLWDLGDGGRLEGPEVTHAYNSIGDFTVRVAGWNDV-SRSEAWLNVTVKRRVRGLVVNASRTVVPLNGS 1313
Cdd:COG3291     16 FTDTSSGNATSYEWDFGDGTTSTEANPSHTYTTPGTYTVTLTVTDAAgCSDTTTKTITVGAPNPGVTTVTTSTTVTTLAN 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1314 VSFSTSLEAGSDVrYSWVLCDRCTPIPGGPTISYTFRSVGTFSIIVTAENEVGSAQDSIFVYVLQLIEGLQVAGCGSYFP 1393
Cdd:COG3291     96 TANGGATTVVAGS-TVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTTSAST 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1394 TNHTAQLQAVVRDGTNVSYSWTAWWDRGPALAGSGKGFSLTALEAGTYHVQLRATNMLGSAWADCTVDFVEPVGWLMVTA 1473
Cdd:COG3291    175 NPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNTVTTS 254
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916324 1474 SPNPAAVNTSVTLSAKLAGGSGVLYTWSLEEGLSWETPEPFTTHSFPTPGLHLVTVTAGNPLGSASATVEVGVQVPVSG 1552
Cdd:COG3291    255 GANTAGTSTITGGTSGVVTTSAATGTSTNGTGGLGTTTAITPGNVSTTADVTGGTATLAVSSTLTTNDTTGSSSTGTVF 333
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
2756-2805 6.51e-10

G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin REJ and polycystin.


Pssm-ID: 197639  Cd Length: 49  Bit Score: 57.01  E-value: 6.51e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1622916324  2756 YTSLCQYFSEENMVWRTEGLLPLEETSPHqAVCLTRHLTAFGASLFVPPS 2805
Cdd:smart00303    1 FNPICVFWDESSGEWSTRGCELLETNGTH-TTCSCNHLTTFAVLMDVPPI 49
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
56-129 2.48e-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: 60.57  E-value: 2.48e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916324   56 RGLRTLGPALRIpadataLDVSHNLLRALDVglLANLSQLSELDISNNKISTLEE--GIFANLFNLSEINLSGNPF 129
Cdd:cd21340    113 RSLAALSNSLRV------LNISGNNIDSLEP--LAPLRNLEQLDASNNQISDLEEllDLLSSWPSLRELDLTGNPV 180
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
50-130 1.03e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 60.72  E-value: 1.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324   50 RVNCSGRGLRTLGPALripADATAL---DVSHNLLRALDVGLlANLSQLSELDISNNKISTLEEGIfANLFNLSEINLSG 126
Cdd:COG4886    140 ELDLSNNQLTDLPEPL---GNLTNLkslDLSNNQLTDLPEEL-GNLTNLKELDLSNNQITDLPEPL-GNLTNLEELDLSG 214

                   ....
gi 1622916324  127 NPFE 130
Cdd:COG4886    215 NQLT 218
LRRNT smart00013
Leucine rich repeat N-terminal domain;
34-73 7.88e-04

Leucine rich repeat N-terminal domain;


Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 39.61  E-value: 7.88e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1622916324    34 PCAPPCLCGPapgaaCRVNCSGRGLRTLgpALRIPADATA 73
Cdd:smart00013    1 ACPAPCNCSG-----TAVDCSGRGLTEV--PLDLPPDTTL 33
 
Name Accession Description Interval E-value
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
99-2476 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: 3375.51  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324   99 DISNNKISTLEEGIFANLFNLSEINLSGNPFECDCGLVWLPRWAEEQQVRVVQPEAATCAGPGSLAGQPLLGIPLLDSDC 178
Cdd:TIGR00864    1 DISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPEAALCAGPGALAGQPLLGIPLLDSGC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  179 GEEYIACLPDNSSGTVAAVA----FSAAHEGLLQPEACSAFCFSTGRGLAALSEQGWCLCGAAQPSSASFACLSF----- 249
Cdd:TIGR00864   81 DEEYVACLKDNSSGGGAARSelviFSAAHEGLFQPEACNAFCFSAGHGLAALGEQGECLCGAAQPSEANFACESLcsgpp 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  250 ------CSGP-------PPPPALDCGGPtllqHVFPASPGAALVGPHGPLAS-------GQLAA-FHIAAPLPVTATRWD 308
Cdd:TIGR00864  161 pppaaaCRGPqllehifPALPGAPIQGP----HGPIASGQLAAFHAAAPLAPtamrwdfGDGSAeVDAAGAGGTTAASHK 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  309 FG-DGSPEVDAAGPAASHRYVLPGRYHVTA------------VVA-------------LGVSSALLGTNVQVEAAPAALE 362
Cdd:TIGR00864  237 YGhPGRYHVSAMGALGAGKALAGGDVQVEAapaalelhcpslVQAdesldlsiqnrggSDLDAAWKITAHGEEPAKASHP 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  363 LvCPSSV----QSDESLKLSI------------QNRGGSGLEAAYSIVALGEELARVVHPLcpsDTEIFPGNGHCYRLVV 426
Cdd:TIGR00864  317 H-CPKDGeifeENGHCFQIVPeeaawldaqeqcLARAGAALAIVDNDALQNFLARKVTHSL---DRGVWIGFSDVNGAEK 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  427 EKAAWLQAQ--EQCRAWagaaLAMVDSPAVQRFLVS--------------------------RVTRSLDVWIGFST--VQ 476
Cdd:TIGR00864  393 GPAHQGEAFeaEECEEG----LAGEPHPARAEHCVRldprgqcnsdlcnaphayvcelnpggPVPDAENFAMGAASfdLH 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  477 GPETGLAPQG----------------------EAF--SLESCQNWL--------------------------------PG 500
Cdd:TIGR00864  469 GLLQALAAMDglpapphegvevllfpalrfsrAAFlsSAEFGTQELrrpahilfqiyrlrcrlpgaggpacgpeaecrPP 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  501 EPHPATAEHCVRLGPtgWCN-----------------TDLCSAPHSYVCELR--------------PGGP-----VQD-A 543
Cdd:TIGR00864  549 DNRSADAPACMKGEQ--WCPfahiclpldapchpqacANGCSQGHGLPGAARmplyalqreflfslPAGPaahvlLQDhG 626
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  544 ENLLVGapSGDL------QGP--LTPLTPQDGLSAPHEPV--------------------------EVMVFPGLSLSHEA 589
Cdd:TIGR00864  627 EDLLML--PGDLialqhdAGPaaLIHCQPAPGHPGPRAPVfaanasewfghnntpvppdnlagdgaDPLPDPELDLKALL 704
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  590 FLTTAE------------FGTQELRRPAQLRLQ-------VYRLLSTAGtpeNGSEPESRS------------------- 631
Cdd:TIGR00864  705 EGTRASwlecaacairllAAGEQETRLLGAELNaglplpgLYELLAESA---KGSDLHNAScsfdvlpplaglrvihpap 781
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  632 -------PDNRTQLVPECMPGGRWCPAA------------NVCVPLDAS--CHPQangcTSGPGLP----GALYAL---- 682
Cdd:TIGR00864  782 qdgrlflESNGSALLLQVDSGANAEAKAfwpggnssarfeNVCPAEFASrlCHPS----TFEGGCAeeaeDSLFAVlaln 857
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  683 W-------------------------------REFLFSVPAGP-PAQ------YSRYSPVVEAGSDVVFRWTINDKQSLT 724
Cdd:TIGR00864  858 WlkegehtgpvqvdlmaennaseanlsllvqaEEPICGLRAQPhPAArvlmesLVRYSASVEAGSDMTFKWTIDDKPFFT 937
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  725 FQNVVFNVIYQSAAVFKLSLTASNHVSNVTVNYNVTVERMNRMQGLWVSTVPAVLPPNATLALTAGVLVDSAVEVAFLWT 804
Cdd:TIGR00864  938 FQNTVFNVIYQHAAVFKLSLTAMNHVSNLTEDFNVTVDRLNPMQGLQVKGVPAVLPPGATLALTAGVLIDMAVEAAFLWS 1017
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  805 FGDGEQALRQFHPPYNESFPVPDPSVAQVLVEHNVTHTYAAPGEYILTVLTSNAFENLTQQVPVSVRAALPSMAVGVSDS 884
Cdd:TIGR00864 1018 FGDGEQALFEFKPPYNESFPCPDPSPAQVLLEHNVMHIYAAPGEYLATVLASNAFENISQQINMSVRAILPRVAIGTEDG 1097
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  885 VLVAGRPITFYPHPLPSPGGVLYTWDFGDSSPVLTQSQPTANHTYASRGTYRVHLEVNNTVSSALAQADVRVFEELRGLS 964
Cdd:TIGR00864 1098 LLLAGKPADFEAHPLPSPGGIHYEWDFGDGSALLQGRQPAAAHTFAKRGPFHVCLEVNNTISGAAACADMFAFEEIEGLS 1177
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  965 VNMSLAVEQGAPVVVSAAVQTGDDITWTFDMGDGTVLSGPEDTVEHVYLRAQNCTVTVGAASPAGRLAQSLHVLVFVLEV 1044
Cdd:TIGR00864 1178 ADMSLATELGAATTVRAALQSGDNITWTFDMGDGKSLSGPEATVEHKYAKAGNCTVNIGAANAAGHGARIIHVEVFVFEV 1257
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1045 LRIEPAACIPTQPDARLTAYVTGNPAHYLFDWTFGDGSSNTTVRGRPTVTHNFTRSGTFPLALVLSSPVNKAHYFTSICV 1124
Cdd:TIGR00864 1258 AGIEPAACIGEHADANFRARVSGNAAHYLFDWSFGDGSPNETHHGCPGISHNFRGNGTFPLALTISSGVNKAHFFTQICV 1337
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1125 EPEVGNVTLQPERQFVQLGDEVRLVACVWPPFPYRYAWDFGTEEAAPARAGGPEVTFTYRDPGSYLVTVTASNNVSAAND 1204
Cdd:TIGR00864 1338 EPELGKISLQAEKQFFALGDEAQFQACAEPEFNYRYEWDFGGEEAAPLPAAGAEVTFIYNDPGCYLVTVAASNNISAAND 1417
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1205 SALVEVQEPVVVTDIKVNSSL--VLELQQPYLFSAVGRGRPASYLWDLGDGGRLEGPEVTHAYNSIGDFTVRVAGWNDVS 1282
Cdd:TIGR00864 1418 SALIEVLEPVGATSFKHNGSHgnNLELGQPYLFSAFGRARNASYLWDFGDGGLLEGPEILHAFNSPGDFNIRLAAANEVG 1497
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1283 RSEAWLNVTVKRRVRGLVVNASRTVVPLNGSVSFSTSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFSIIVTAE 1362
Cdd:TIGR00864 1498 KNEATLNVAVKARVRGLTINASLTNVPLNGSVHFEAHLDAGDDVRFSWILCDHCTPIFGGNTIFYTFRSVGTFNIIVTAE 1577
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1363 NEVGSAQDSIFVYVLQLIEGLQVAG-------------CGSYFPTNHTAQLQAVVRDGTNVSYSWTAWWD---RGPALAG 1426
Cdd:TIGR00864 1578 NDVGAAQASIFLFVLQEIEGLQILGetaegggggvqelDGCYFETNHTVQFHAGFKDGTNLSFSWNAILDnepDGPAFAG 1657
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1427 SGKGFSLTALEAGTYHVQLRATNMLGSAWADCTVDFVEPVGWLMVTASPNPAAVNTSVTLSAKLAGGSGVLYTWSLEEGL 1506
Cdd:TIGR00864 1658 SGKGAKLNPLEAGPCDIFLQAANLLGQATADCTIDFLEPAGNLMLAASDNPAAVNALINLSAELAEGSGLQYRWFLEEGD 1737
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1507 SWETPEPFTTHSFPTPGLHLVTVTAGNPLGSASATVEVGVQVPVSGLSIRASESGGS-FVAAGSSVPFWGQLATGTNVSW 1585
Cdd:TIGR00864 1738 DLETSEPFMSHSFPSAGLHLVTMKAFNELGSANASEEVDVQEPISGLKIRAADAGEQnFFAADSSVCFQGELATGTNVSW 1817
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1586 CWAVPGGSSKRGPHVTMVFPDAGTFSVQLNASNAVSWVSATHNLTVEEPIVGLVLWASSKVVAPGQLVHFQILLAAGSAV 1665
Cdd:TIGR00864 1818 CWAIDGGSSKMGKHACMTFPDAGTFAIRLNASNAVSGKSASREFFAEEPIFGLELKASKKIAAIGEKVEFQILLAAGSAV 1897
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1666 TFRLQVGGASPAVL-PGPRFSHSFPRVGDHVVSVQGENHVSWAQAQVRIVVLEAVSGLQVPNCCEPGIATGTERNFTARV 1744
Cdd:TIGR00864 1898 NFRLQIGGAAPEVLqPGPRFSHSFPRVDDHMVNLRAKNEVSCAQANLHIEVLEAVRGLQIPDCCAAGIATGEEKNFTANV 1977
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1745 QRGSRVAYAWYFSLQKVQGDSLVILSGRDVTYTPVAAGLLEIQVRAFNALGSENRTLVLEVQDAVQYVALRSGP--CFTN 1822
Cdd:TIGR00864 1978 QRGKPVAFAWTFDLHHLHGDSLVIHMGKDVSYTAEAAGLLEIQLGAFNALGAENITLQLEAQDALMDAALQAGPqdCFTN 2057
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1823 RSAWFEAATSPSPRRVAYHWDFGDGAPGQDTDEPRAEHCYLRPGDYRVQVNASNLVSFFVAQATVTVQVLACREPEVDVV 1902
Cdd:TIGR00864 2058 KMAQFEAATSPKPNFMACHWDFGDGSAGQDTDEPRAEHEYLHPGDYRVQVNASNLVSFFSAHAEINVQVLACEEPEVDVV 2137
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1903 LPLQVLMRRSQRNYLEAHVDLRDCVTYQTEYRWEVYRTASCQRPGRPTRVALPG-------------VDVSRPQLVLPRL 1969
Cdd:TIGR00864 2138 LALQLAIRRSQPNLLEAHVDLKDCLRYGAEYLWEILRAASCDNDGHFARGALNGatrsfpviplpaeVDVQRLQLSLPKL 2217
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1970 ALPVGHYCFVFVVSFGDTPLARSIQANVTVAPERLVPIIEGGSYRVWSDTQDLVLDGSESYDPNLEDGDQTPLSFHWACV 2049
Cdd:TIGR00864 2218 ALAAGHYCFVFSLSFEDTPLKKAACANLGVAAARLMPIIEGGSYRVWSDTQDLQLDAEESYDPNLDDDDQSLLHFHWACQ 2297
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2050 ASTQREAGGCALNFGPRG-SSVVTIPRERLAAGVEYTFSLTVWKAGRKEEATNQTVLIRRGRVPIVSLECVSCKAQAVYE 2128
Cdd:TIGR00864 2298 ASSKGEAGCCALNFGLGGkGPTLGIPGEELAAGIEYTFKLSIGKAGMKEEATNQTVLIQSGHIPIVSLECVSCKAQALYE 2377
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2129 VSRSSYVYLEGRCLNCSSGSKRGRWAARTFSNKTLVLDETTTSTGSAGMRLVLRRGVLRDGEGYTFTLTVLGHSGEEEGC 2208
Cdd:TIGR00864 2378 VSQNSYVYLEGRCLNCQSGFHRGRWAARTFQNDTLVLDESSTSTGSAGMNLVLRQGVLHDGEGYNFTLHVLDDSGDEEGA 2457
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2209 ASIRLSPNRPPLGGSCRLFPLGN--------------VHALTTKVHFECTGWHDAEDAGAPLVYALLLRRCRQGHCEEFC 2274
Cdd:TIGR00864 2458 ASIRLHHNMPPDGGECHLFPGGEtgqehgdkedevwaIEALLDKVHFECSGWHDAEDAEAPLLYALLLNRCRDDHCEEFC 2537
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2275 VYKGSLSSYGAVLPPGFR-PHFEVGLAVVVQDQLGAAVVALNRSLAIALPEPSGGTTGLTVWLHGLTASVLPGLLRQADP 2353
Cdd:TIGR00864 2538 VYKGSLPEHGAFLPPGFRsAHFEVGLAITVEDHLGAAIRALNKSIAITLPDPNGEASGLPHWLHDLIASKLKGLLDQADF 2617
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2354 QHVIEYSLALVTVLNEYEQALDVAAEPEHERQRRAQIRKNVTQTLVSLRVHTVDDIQQIAAALAQSMGPSRELVCRSCLK 2433
Cdd:TIGR00864 2618 QHVIELSLALITVLNEYEQALDSAAEPKHERGHRAQIRKNITEALTALDLHTVDDIQQIAAALAQCMAPSREFICEECLK 2697
                         2730      2740      2750      2760
                   ....*....|....*....|....*....|....*....|...
gi 1622916324 2434 QTLHKLEAMMRILQAETTAGTVTPTAIGDSILNITGDLIHLAS 2476
Cdd:TIGR00864 2698 QTLHKLEAMLEILQADTKAGIVTPTAIADNILNIMGDLIHLAS 2740
REJ pfam02010
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
1919-2362 1.52e-131

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: 421.91  E-value: 1.52e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1919 AHVDLRDCV-TYQTEYRWEVYRTASCqrpGRPTRVALPgVDVSRPQLVLPRLALPVGHYCFVFVVSFGDTP-LARSIQAN 1996
Cdd:pfam02010    1 ASVELNGCFsAYTIDYLWSVFTVSSN---LNLQTISSP-KDLVLPQLTIPSGTLPYGTYVFTLTVSLSSTPsLAGTDIIT 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1997 VTVAPERLVPIIEGGSYRVWSDTQDLVLDGSESYDPNLEDGDQTPLSFHWACVAST------QREAGGCA-----LNFGP 2065
Cdd:pfam02010   77 VTVQPSPLVAVIDGGSSRVVGYNQDLTLDGSESYDPDVDPGSSSGLTYLWSCRRSSsgdnplLNNDPVCFsdqneGTLLQ 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2066 RGSSVVTIPRERLAAGVEYTFSLTVWKAGRKEEATNQTVLIRRGRVPIVSLECVSCKAQAVYEVSRssYVYLEGRCLNCS 2145
Cdd:pfam02010  157 STSSSLTIPASTLQANVTYTFKLTVSKGSRNSASTTQTILVVDGNPPIIILSCISNCNRKNNPVDR--LVLLASTCLNCS 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2146 SGSKRG--RWAARTFSNKTLVLD--ETTTSTGSAGMRLVLRRGVLRDGEGYTFTLTVLGHSGEEEGCASIRLSPNRPPLG 2221
Cdd:pfam02010  235 SDLSDVtyRWLSLGSENTSLVLDqlNSQTSTGRSGPYLVIKAGVLQSGVSYRFTLIVTVYPGLVSGLASISFITNAPPTG 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2222 GSCRLFPLGNvHALTTKVHFECTGWHDAEDagaPLVYALLLRRCRQGHCEEFCVYKGSLS-SYGAVLPPGFRPH-FEVGL 2299
Cdd:pfam02010  315 GTCSVTPTEG-TALETKFTVTCQGWTDDDL---PLTYQFGDISFREASEEWFLLYEGSSQiSISTFLPPGLPANdYQVTV 390
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622916324 2300 AVVVQDQLGAAvVALNRSLAIALPEPSGGttglTVWLHGLTASVLPGLLRQADPQHVIEYSLA 2362
Cdd:pfam02010  391 VVVVYDSLGAA-TSVSLTITVTPPSSSDE----LLYFLLGTTSDLSALLQSGDPQQAAQLILA 448
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
2863-2982 1.79e-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: 198.27  E-value: 1.79e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2863 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLDGD--RAFHRNSLDIFQIATPHSLGSVWKIRVWHDNKGLSPAW 2940
Cdd:cd01752      1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPekPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1622916324 2941 FLQHVIVRDLQTARSAFFLVNDWLSVETEanGGLVEKEVLVA 2982
Cdd:cd01752     81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEG--DGTVERTFPVA 120
Polycystin_dom pfam20519
Polycystin domain; This domain represents the polycystin domain from group II of Transient ...
3464-3648 7.86e-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: 193.79  E-value: 7.86e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 3464 FLAITRSEELWPWMAHVLLPYVHGNQS------------SPELGPPRLRQVRLQEALC--PDPPGPRVHTCSAAGGFSTS 3529
Cdd:pfam20519    2 LLTVTDLDDIWDWLSSVLLPALHSNKTpsglpgsfiayeSLLLGVPRLRQLRVRNSSClvHDKFVREINECHAGYSPPSE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 3530 DY----DVGWESPHNGSGTW-AYSAPDLL-GAWSWGSCAVYDSGGYVQELGLSLEESRDRLRFLQLHNWLDnsdphplRR 3603
Cdd:pfam20519   82 DRklysALPYKPVHYGSKYWfIYTPPGLLmGYDHWGHLASYPSGGYVVLLPSSREESLKRLAYLQDNNWLD-------RG 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1622916324 3604 SRAVFVELTRYSPAVGLHAAVTLRLEFPAAGRALAALSVRPFALR 3648
Cdd:pfam20519  155 TRAVFVDFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVKLL 199
PKD_channel pfam08016
Polycystin cation channel; This family contains the cation channel region from group II of ...
3649-3870 1.05e-43

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: 160.13  E-value: 1.05e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 3649 RLSAGLSLPLLT-SVCLLLFALHFAVAEARTWHREGCwHVLRpRAW--ARWLLVVLTAATALVRLAQLGAADRQWTrFVR 3725
Cdd:pfam08016    1 RYVTNRSLFILLcEIVFVVFFLYFVVEEILKIRKHRP-SYLR-SVWnlLDLAIVILSVVLIVLNIYRDFLADRLIK-SVE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 3726 GRPRRFTSFDQVAQLSSAARGLAASLLFLLLVKAAQQLRFVRQWSVFGKTLFRALPELLGATLGLVVLGVAYAQLAVLLV 3805
Cdd:pfam08016   78 ASPVTFIDFDRVAQLDNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFGYLLF 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622916324 3806 SSCVDSLWSVAQALLVLCsgtglSTLCPAESWH--------LSPLLCVGLWALRLWGALRLGAVILRWRYHAL 3870
Cdd:pfam08016  158 GTQAPNFSNFVKSILTLF-----RTILGDFGYNeifsgnrvLGPLLFLTFVFLVIFILLNLFLAIINDSYVEV 225
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
2863-2982 4.85e-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: 4.85e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2863 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLD---GDRAFHRNSLDIFQIATPhSLGSVWKIRVWHDNKGLSPA 2939
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKksnNKNKFERGQTDKFTVEAV-DLGKLKKIRIGHDNSGLGAG 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1622916324 2940 WFLQHVIVRDLQTARSAFFLVNDWLSveTEANGGLVEKEVLVA 2982
Cdd:cd01756     80 WFLDKVEIREPGTGDEYTFPCNRWLD--KDEDDGQIVRELYPS 120
WSC smart00321
present in yeast cell wall integrity and stress response component proteins; Domain present in ...
179-273 1.52e-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: 100.24  E-value: 1.52e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324   179 GEEYIACLPDNSSGTVAAVAFSAAHegLLQPEACSAFCFSTGRGLAALSEQGWCLCGAAQPSSA-----SFACLSFCSGp 253
Cdd:smart00321    1 GATYVGCYSDNSSRTLAAVSSYAYH--NMSVEACSNFCFSAGYALAALENGNECYCGDSLPSTSvsasdSSQCSTTCSG- 77
                            90       100
                    ....*....|....*....|
gi 1622916324   254 ppPPALDCGGPTLLQHVFPA 273
Cdd:smart00321   78 --YPAEVCGGPNRLSVYVLA 95
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
2865-2968 3.90e-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: 97.12  E-value: 3.90e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2865 YEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLDGDR-AFHRNSLDIFQIATPHSLGSVWKIRVWHDNKGLSPAWFLQ 2943
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNpDFERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEWFLK 80
                           90       100
                   ....*....|....*....|....*.
gi 1622916324 2944 HVIV-RDLQTARSAFFLVNDWLSVET 2968
Cdd:pfam01477   81 SITVeVPGETGGKYTFPCNSWVYGSK 106
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
2863-2965 4.38e-19

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 85.00  E-value: 4.38e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  2863 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLD--GDRAFHRNSLDIFQIATPHSLGSVWKIRVWHDNKglSPAW 2940
Cdd:smart00308    1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDylFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR--HPEW 78
                            90       100
                    ....*....|....*....|....*
gi 1622916324  2941 FLQHVIVRDLQTARSAFFLVNDWLS 2965
Cdd:smart00308   79 FLKSITVKDLPTGGKYHFPCNSWVY 103
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
408-533 7.44e-19

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: 85.34  E-value: 7.44e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324   408 CPSDTEIFpgNGHCYRLVVEKAAWLQAQEQCRAwAGAALAMVDSPAVQRFL---VSRVTRSLDVWIGFSTVQGPETGLAP 484
Cdd:smart00034    1 CPSGWISY--GGKCYKFSTEKKTWEDAQAFCQS-LGGHLASIHSEAENDFVaslLKNSGSSDYYWIGLSDPDSNGSWQWS 77
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 1622916324   485 QGeaFSLESCQNWLPGEPhPATAEHCVRLGPTGWC-NTDLCSAPHSYVCE 533
Cdd:smart00034   78 DG--SGPVSYSNWAPGEP-NNSSGDCVVLSTSGGKwNDVSCTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
420-533 4.43e-18

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: 82.67  E-value: 4.43e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  420 HCYRLVVEKAAWLQAQEQCRAWaGAALAMVDSPAVQRFLVSRVTRSL--DVWIGFSTVQGPETGLAPQGEAFSleSCQNW 497
Cdd:cd00037      1 SCYKFSTEKLTWEEAQEYCRSL-GGHLASIHSEEENDFLASLLKKSSssDVWIGLNDLSSEGTWKWSDGSPLV--DYTNW 77
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1622916324  498 LPGEPHPATAEHCVRL--GPTGWCNTDLCSAPHSYVCE 533
Cdd:cd00037     78 APGEPNPGGSEDCVVLssSSDGKWNDVSCSSKLPFICE 115
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1471-1540 6.13e-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: 77.81  E-value: 6.13e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1471 VTASPNPAAVNTSVTLSAKLAGGSGVLYTWSLEEGLSWETPEPFTTHSFPTPGLHLVTVTAGNPLGSASA 1540
Cdd:pfam00801    1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
2864-2965 8.08e-17

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: 78.92  E-value: 8.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2864 KYEILVKTGWGRGSGTTAHVGIMLYGVD-SRSGHRHLDGDRAFHRNSLDIFQIATPHSLGSVWKIRVWHDNKGLSPAWFL 2942
Cdd:cd00113      2 RYTVTIKTGDKKGAGTDSNISLALYGENgNSSDIPILDGPGSFERGSTDTFQIDLKLDIGDITKVYLRRDGSGLSDGWYC 81
                           90       100
                   ....*....|....*....|...
gi 1622916324 2943 QHVIVRDLQTARSAFFLVNDWLS 2965
Cdd:cd00113     82 ESITVQALGTKKVYTFPVNRWVL 104
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
879-957 3.31e-16

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: 75.95  E-value: 3.31e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916324   879 VGVSDSVLVAGRPITFYPHPLPSPGGVLYTWDFGDSSpvlTQSQPTANHTYASRGTYRVHLEVNNTVSSALAQADVRVF 957
Cdd:smart00089    4 VSASPTVGVAGESVTFTATSSDDGSIVSYTWDFGDGT---SSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1301-1370 4.71e-16

PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.


Pssm-ID: 395646 [Multi-domain]  Cd Length: 70  Bit Score: 75.12  E-value: 4.71e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1301 VNASRTVVPLNGSVSFSTSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFSIIVTAENEVGSAQD 1370
Cdd:pfam00801    1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1640-1709 6.43e-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: 74.73  E-value: 6.43e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1640 LWASSKVVAPGQLVHFQILLAAGSAVTFRLQVGGASPAVLPGPRFSHSFPRVGDHVVSVQGENHVSWAQA 1709
Cdd:pfam00801    1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1133-1204 7.97e-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: 74.73  E-value: 7.97e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622916324 1133 LQPERQFVQLGDEVRLVACVWPPFPYRYAWDFGteEAAPARAGGPEVTFTYRDPGSYLVTVTASNNVSAAND 1204
Cdd:pfam00801    1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFG--DSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1385-1456 1.14e-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: 74.35  E-value: 1.14e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622916324 1385 VAGCGSYFPTNHTAQLQAVVRDGTNVSYSWTAWwdRGPALAGSGKGFSLTALEAGTYHVQLRATNMLGSAWA 1456
Cdd:pfam00801    1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFG--DSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1561-1625 4.65e-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: 72.42  E-value: 4.65e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622916324 1561 GGSFVAAGSSVPFWGQLATGTNVSWCWAVPG--GSSKRGPHVTMVFPDAGTFSVQLNASNAVSWVSA 1625
Cdd:pfam00801    4 SGTVVAAGQPVTFTATLADGSNVTYTWDFGDspGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
879-950 4.70e-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: 72.42  E-value: 4.70e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622916324  879 VGVSDSVLVAGRPITFYPHpLPSPGGVLYTWDFGDSsPVLTQSQPTANHTYASRGTYRVHLEVNNTVSSALA 950
Cdd:pfam00801    1 VSASGTVVAAGQPVTFTAT-LADGSNVTYTWDFGDS-PGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1816-1883 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 1622916324 1816 SGPCFTNRSAWFEAaTSPSPRRVAYHWDFGDGaPGQDTDEPRAEHCYLRPGDYRVQVNASNLVSFFVA 1883
Cdd:pfam00801    5 GTVVAAGQPVTFTA-TLADGSNVTYTWDFGDS-PGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
968-1033 3.94e-14

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: 69.72  E-value: 3.94e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916324  968 SLAVEQGAPVVVSAAVQTGDDITWTFDMGDGTVLSGPEDTVEHVYLRAQNCTVTVGAASPAGRLAQ 1033
Cdd:pfam00801    5 GTVVAAGQPVTFTATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1471-1547 1.17e-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: 68.63  E-value: 1.17e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622916324  1471 VTASPNPAAVNTSVTLSAKLAG-GSGVLYTWSLEEGLSWEtpEPFTTHSFPTPGLHLVTVTAGNPLGSASATVEVGVQ 1547
Cdd:smart00089    4 VSASPTVGVAGESVTFTATSSDdGSIVSYTWDFGDGTSST--GPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1567-1632 1.35e-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: 68.63  E-value: 1.35e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622916324  1567 AGSSVPFWGQLAT-GTNVSWCWAVPGGSSKRGPHVTMVFPDAGTFSVQLNASNAVSWVSATHNLTVE 1632
Cdd:smart00089   13 AGESVTFTATSSDdGSIVSYTWDFGDGTSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1808-1890 2.23e-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: 2.23e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  1808 AVQYVALRSGPcfTNRSAWFEAATSPSPRRVAYHWDFGDGapgQDTDEPRAEHCYLRPGDYRVQVNASNLVSFFVAQATV 1887
Cdd:smart00089    2 ADVSASPTVGV--AGESVTFTATSSDDGSIVSYTWDFGDG---TSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTV 76

                    ...
gi 1622916324  1888 TVQ 1890
Cdd:smart00089   77 VVQ 79
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1298-1376 2.29e-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: 2.29e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  1298 GLVVNASRTVVPLNGSVSFS-TSLEAGSDVRYSWVLCDRctPIPGGPTISYTFRSVGTFSIIVTAENEVGSAQDSIFVYV 1376
Cdd:smart00089    1 VADVSASPTVGVAGESVTFTaTSSDDGSIVSYTWDFGDG--TSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVV 78
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1216-1293 3.45e-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: 67.48  E-value: 3.45e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  1216 VTDIKVNSSlVLELQQPYLFSAV--GRGRPASYLWDLGDGGRLEGPEVTHAYNSIGDFTVRVAGWNDVSRSEAWLNVTVK 1293
Cdd:smart00089    1 VADVSASPT-VGVAGESVTFTATssDDGSIVSYTWDFGDGTSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
884-951 8.12e-13

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: 66.37  E-value: 8.12e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622916324  884 SVLVAGRPITFYPHPLPSPGGVLYTWDFGDSSpVLTQSQPTANHTYASRGTYRVHLEVNNTVSSALAQ 951
Cdd:cd00146      9 PVAELGASVTFSASDSSGGSIVSYKWDFGDGE-VSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTK 75
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1221-1286 4.75e-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: 63.94  E-value: 4.75e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916324 1221 VNSSLVLELQQPYLFSA-VGRGRPASYLWDLGD--GGRLEGPEVTHAYNSIGDFTVRVAGWNDVSRSEA 1286
Cdd:pfam00801    2 SASGTVVAAGQPVTFTAtLADGSNVTYTWDFGDspGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
LRR_8 pfam13855
Leucine rich repeat;
72-129 1.23e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 62.54  E-value: 1.23e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622916324   72 TALDVSHNLLRALDVGLLANLSQLSELDISNNKISTLEEGIFANLFNLSEINLSGNPF 129
Cdd:pfam13855    4 RSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
279-346 1.30e-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: 62.79  E-value: 1.30e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916324  279 LVGPHGPLASGQLAAFHIA-APLPVTATRWDFGDgSPEVDAAGPAASHRYVLPGRYHVTAVVALGVSSA 346
Cdd:pfam00801    1 VSASGTVVAAGQPVTFTATlADGSNVTYTWDFGD-SPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSA 68
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1728-1799 2.20e-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: 62.02  E-value: 2.20e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622916324 1728 CEPGIATGTERNFTARVQRGSRVAYAWYFslqkvqGDSLV-ILSGRDVTYTPVAAGLLEIQVRAFNALGSENR 1799
Cdd:pfam00801    4 SGTVVAAGQPVTFTATLADGSNVTYTWDF------GDSPGtSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
WSC pfam01822
WSC domain; This domain is involved in carbohydrate binding.
182-263 2.34e-11

WSC domain; This domain is involved in carbohydrate binding.


Pssm-ID: 460348  Cd Length: 82  Bit Score: 62.48  E-value: 2.34e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  182 YIACLPDNSsGTVAAVAFSAAHEGLLQPEACSAFCFSTGRGLAALSEQGWCLCGAAQPSSASFA----CLSFCSGPPPPP 257
Cdd:pfam01822    1 YLGCYSDGT-GGRRLLLGSSGDYDDMTPEKCIAFCSAAGYTYAGLEYGGECYCGNSLPSGSALAdssdCNTPCPGDSSQT 79

                   ....*.
gi 1622916324  258 aldCGG 263
Cdd:pfam01822   80 ---CGG 82
LRRCT smart00082
Leucine rich repeat C-terminal domain;
127-179 6.17e-11

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 60.14  E-value: 6.17e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1622916324   127 NPFECDCGLVWLPRWAeEQQVRVVQPEAATCAGPGSLAGqPLLGIPLLDSDCG 179
Cdd:smart00082    1 NPFICDCELRWLLRWL-QANEHLQDPVDLRCASPSSLRG-PLLELLHSEFKCP 51
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1300-1376 9.49e-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: 60.59  E-value: 9.49e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916324 1300 VVNASRTVVPLNGSVSFS-TSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFSIIVTAENEVGSAQ-DSIFVYV 1376
Cdd:cd00146      3 ASVSAPPVAELGASVTFSaSDSSGGSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSStKTTTVVV 81
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
1235-1552 1.29e-10

Uncharacterized conserved protein, PKD repeat domain [Function unknown];


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 66.23  E-value: 1.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1235 FSAVGRGRPASYLWDLGDGGRLEGPEVTHAYNSIGDFTVRVAGWNDV-SRSEAWLNVTVKRRVRGLVVNASRTVVPLNGS 1313
Cdd:COG3291     16 FTDTSSGNATSYEWDFGDGTTSTEANPSHTYTTPGTYTVTLTVTDAAgCSDTTTKTITVGAPNPGVTTVTTSTTVTTLAN 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1314 VSFSTSLEAGSDVrYSWVLCDRCTPIPGGPTISYTFRSVGTFSIIVTAENEVGSAQDSIFVYVLQLIEGLQVAGCGSYFP 1393
Cdd:COG3291     96 TANGGATTVVAGS-TVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTTSAST 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1394 TNHTAQLQAVVRDGTNVSYSWTAWWDRGPALAGSGKGFSLTALEAGTYHVQLRATNMLGSAWADCTVDFVEPVGWLMVTA 1473
Cdd:COG3291    175 NPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNTVTTS 254
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916324 1474 SPNPAAVNTSVTLSAKLAGGSGVLYTWSLEEGLSWETPEPFTTHSFPTPGLHLVTVTAGNPLGSASATVEVGVQVPVSG 1552
Cdd:COG3291    255 GANTAGTSTITGGTSGVVTTSAATGTSTNGTGGLGTTTAITPGNVSTTADVTGGTATLAVSSTLTTNDTTGSSSTGTVF 333
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
408-533 1.50e-10

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: 61.55  E-value: 1.50e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  408 CPSDTEIFpgNGHCYRLVVEKAAWLQAQEQCRAwAGAALAMVDSPAVQRFLVSRVTRSLDVWIGFSTvqgPETglapQGE 487
Cdd:cd03590      1 CPTNWKSF--QSSCYFFSTEKKSWEESRQFCED-MGAHLVIINSQEEQEFISKILSGNRSYWIGLSD---EET----EGE 70
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622916324  488 -------AFSLEScQNWLPGEP--HPATAEHCVRLGPT--GWcNTDLCSAPHSYVCE 533
Cdd:cd03590     71 wkwvdgtPLNSSK-TFWHPGEPnnWGGGGEDCAELVYDsgGW-NDVPCNLEYRWICE 125
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1128-1211 1.98e-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: 1.98e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  1128 VGNVTLQPERqfVQLGDEVRLVACVWP-PFPYRYAWDFGTEEAAParagGPEVTFTYRDPGSYLVTVTASNNVSAANDSA 1206
Cdd:smart00089    1 VADVSASPTV--GVAGESVTFTATSSDdGSIVSYTWDFGDGTSST----GPTVTHTYTKPGTYTVTLTVTNAVGSASATV 74

                    ....*
gi 1622916324  1207 LVEVQ 1211
Cdd:smart00089   75 TVVVQ 79
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1044-1125 2.23e-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: 59.39  E-value: 2.23e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  1044 VLRIEPAACIPTQP-DARLTAYVTGNPAHYLFDWTFGDGssnTTVRGrPTVTHNFTRSGTFPLALVLSSPVNKAHYFTSI 1122
Cdd:smart00089    1 VADVSASPTVGVAGeSVTFTATSSDDGSIVSYTWDFGDG---TSSTG-PTVTHTYTKPGTYTVTLTVTNAVGSASATVTV 76

                    ...
gi 1622916324  1123 CVE 1125
Cdd:smart00089   77 VVQ 79
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
2756-2805 6.51e-10

G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin REJ and polycystin.


Pssm-ID: 197639  Cd Length: 49  Bit Score: 57.01  E-value: 6.51e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1622916324  2756 YTSLCQYFSEENMVWRTEGLLPLEETSPHqAVCLTRHLTAFGASLFVPPS 2805
Cdd:smart00303    1 FNPICVFWDESSGEWSTRGCELLETNGTH-TTCSCNHLTTFAVLMDVPPI 49
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1821-1891 1.81e-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: 57.12  E-value: 1.81e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622916324 1821 TNRSAWFEAATSPSPRRVAYHWDFGDGaPGQDTDEPRAEHCYLRPGDYRVQVNASNLVSfFVAQATVTVQV 1891
Cdd:cd00146     13 LGASVTFSASDSSGGSIVSYKWDFGDG-EVSSSGEPTVTHTYTKPGTYTVTLTVTNAVG-SSSTKTTTVVV 81
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
56-129 2.48e-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: 60.57  E-value: 2.48e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916324   56 RGLRTLGPALRIpadataLDVSHNLLRALDVglLANLSQLSELDISNNKISTLEE--GIFANLFNLSEINLSGNPF 129
Cdd:cd21340    113 RSLAALSNSLRV------LNISGNNIDSLEP--LAPLRNLEQLDASNNQISDLEEllDLLSSWPSLRELDLTGNPV 180
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1473-1546 4.00e-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: 4.00e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916324 1473 ASPNPAAVNTSVTLSAK-LAGGSGVLYTWSLEEGLSWETPEPFTTHSFPTPGLHLVTVTAGNPLGSASA-TVEVGV 1546
Cdd:cd00146      6 SAPPVAELGASVTFSASdSSGGSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTkTTTVVV 81
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
72-130 4.80e-09

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 61.87  E-value: 4.80e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916324   72 TALDVSHNLLRALDVGLlANLSQLSELDISNNKISTLEEgiFANLFNLSEINLSGNPFE 130
Cdd:COG4886    208 EELDLSGNQLTDLPEPL-ANLTNLETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLT 263
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1555-1627 5.15e-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: 55.58  E-value: 5.15e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916324 1555 IRASESGGSFVAAGSSVPFWGQLATG---TNVSWCWAVPGGSSKRGPHVTMVFPDAGTFSVQLNASNAVSWVSATH 1627
Cdd:cd00146      1 PTASVSAPPVAELGASVTFSASDSSGgsiVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKT 76
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
970-1041 5.62e-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: 55.58  E-value: 5.62e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622916324  970 AVEQGAPVVVSAAVQ-TGDDITWTFDMGDGTVLSGPEDTVEHVYLRAQNCTVTVGAASPAGRlAQSLHVLVFV 1041
Cdd:cd00146     10 VAELGASVTFSASDSsGGSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGS-SSTKTTTVVV 81
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
408-533 6.87e-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: 6.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  408 CPSDTeiFPGNGHCYRLVVEKAAWLQAQEQCRAW-AGAALAMVDSPAVQRFLVSRV----TRSLDVWIGFSTVQGPETGL 482
Cdd:cd03594      1 CPKGW--LPYKGNCYGYFRQPLSWSDAELFCQKYgPGAHLASIHSPAEAAAIASLIssyqKAYQPVWIGLHDPQQSRGWE 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622916324  483 APQGEAFSLEScqnWLPGEPHPaTAEHCVRL-GPTG---WcNTDLCSAPHSYVCE 533
Cdd:cd03594     79 WSDGSKLDYRS---WDRNPPYA-RGGYCAELsRSTGflkW-NDANCEERNPFICK 128
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
50-130 1.03e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 60.72  E-value: 1.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324   50 RVNCSGRGLRTLGPALripADATAL---DVSHNLLRALDVGLlANLSQLSELDISNNKISTLEEGIfANLFNLSEINLSG 126
Cdd:COG4886    140 ELDLSNNQLTDLPEPL---GNLTNLkslDLSNNQLTDLPEEL-GNLTNLKELDLSNNQITDLPEPL-GNLTNLEELDLSG 214

                   ....
gi 1622916324  127 NPFE 130
Cdd:COG4886    215 NQLT 218
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
974-1040 1.71e-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: 53.99  E-value: 1.71e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622916324   974 GAPVVVSAAVQT-GDDITWTFDMGDGTVLSGPedTVEHVYLRAQNCTVTVGAASPAGRLAQSLHVLVF 1040
Cdd:smart00089   14 GESVTFTATSSDdGSIVSYTWDFGDGTSSTGP--TVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
74-130 3.24e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 59.18  E-value: 3.24e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622916324   74 LDVSHNLLRALDVGLlANLSQLSELDISNNKISTLEEGIfANLFNLSEINLSGNPFE 130
Cdd:COG4886    187 LDLSNNQITDLPEPL-GNLTNLEELDLSGNQLTDLPEPL-ANLTNLETLDLSNNQLT 241
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
72-130 3.72e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 59.18  E-value: 3.72e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916324   72 TALDVSHNLLRALDVglLANLSQLSELDISNNKISTLEEgiFANLFNLSEINLSGNPFE 130
Cdd:COG4886    231 ETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLTDLPP--LANLTNLKTLDLSNNQLT 285
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1393-1460 5.62e-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: 52.84  E-value: 5.62e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916324  1393 PTNHTAQLQAVVR-DGTNVSYSWtawwDRGPALAGSGKGFSLTALEAGTYHVQLRATNMLGSAWADCTV 1460
Cdd:smart00089   12 VAGESVTFTATSSdDGSIVSYTW----DFGDGTSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTV 76
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1135-1210 6.66e-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: 6.66e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622916324 1135 PERQFVQLGDEVRLVACVWP-PFPYRYAWDFGTEEAAPAraGGPEVTFTYRDPGSYLVTVTASNNVSAAN-DSALVEV 1210
Cdd:cd00146      6 SAPPVAELGASVTFSASDSSgGSIVSYKWDFGDGEVSSS--GEPTVTHTYTKPGTYTVTLTVTNAVGSSStKTTTVVV 81
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
772-870 9.26e-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: 9.26e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324   772 VSTVPAVLPPNATLALTAGVLVDSAVeVAFLWTFGDGeqalrqfhppynesfpvpdpsvaQVLVEHNVTHTYAAPGEYIL 851
Cdd:smart00089    4 VSASPTVGVAGESVTFTATSSDDGSI-VSYTWDFGDG-----------------------TSSTGPTVTHTYTKPGTYTV 59
                            90
                    ....*....|....*....
gi 1622916324   852 TVLTSNAFENLTQQVPVSV 870
Cdd:smart00089   60 TLTVTNAVGSASATVTVVV 78
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
772-864 1.07e-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: 51.62  E-value: 1.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  772 VSTVPAVLPPNATLALTAGVLvdSAVEVAFLWTFGDgeqalrqfhppynesfpvpdpSVAQVLVEHNVTHTYAAPGEYIL 851
Cdd:pfam00801    1 VSASGTVVAAGQPVTFTATLA--DGSNVTYTWDFGD---------------------SPGTSGSGPTVTHTYLSPGTYTV 57
                           90
                   ....*....|...
gi 1622916324  852 TVLTSNAFENLTQ 864
Cdd:pfam00801   58 TLTASNAVGSANA 70
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
72-130 1.72e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 56.87  E-value: 1.72e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916324   72 TALDVSHNLLRALDVGLlANLSQLSELDISNNKISTLEEGIfANLFNLSEINLSGNPFE 130
Cdd:COG4886    116 ESLDLSGNQLTDLPEEL-ANLTNLKELDLSNNQLTDLPEPL-GNLTNLKSLDLSNNQLT 172
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1055-1128 3.03e-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: 50.57  E-value: 3.03e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622916324 1055 TQPDARLTAYVTGNPAHYLFDWTFGDGssNTTVRGRPTVTHNFTRSGTFPLALVLSSPVNKAhyfTSICVEPEV 1128
Cdd:cd00146     13 LGASVTFSASDSSGGSIVSYKWDFGDG--EVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSS---STKTTTVVV 81
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
907-1206 3.50e-07

Uncharacterized conserved protein, PKD repeat domain [Function unknown];


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 55.45  E-value: 3.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  907 YTWDFGDSSpvlTQSQPTANHTYASRGTYRVHLEVNNTV-SSALAQADVRVFEELRGLSVNMSLAVEQGAPVVVSAAVQT 985
Cdd:COG3291     27 YEWDFGDGT---TSTEANPSHTYTTPGTYTVTLTVTDAAgCSDTTTKTITVGAPNPGVTTVTTSTTVTTLANTANGGATT 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  986 GDDITWTFDMGDGTVLSGPEDTVEHVYLRAQNCTVTVGAASPAGRLAQSLHVLVFVLEVLRIEPAACIPTQPDARLTAYV 1065
Cdd:COG3291    104 VVAGSTVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTTSASTNPSVTTDTV 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1066 TGNPAHYLFDWTFGDGSSNTTVR-GRPTVTHNFTRSGTFPLALVLSSPVNKAHYFTSICVEPEVGNVTLQPERQFVQLGD 1144
Cdd:COG3291    184 TTLTGSYTGTIVGGSGSGTVTSGtAGVTTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNTVTTSGANTAGTST 263
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916324 1145 EVRLVACVWPPF----PYRYAWDFGTEEAAPARAGGPEVTFTYRDPGSYLVTVTASNNVSAANDSA 1206
Cdd:COG3291    264 ITGGTSGVVTTSaatgTSTNGTGGLGTTTAITPGNVSTTADVTGGTATLAVSSTLTTNDTTGSSST 329
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
2865-2972 4.02e-07

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


Pssm-ID: 238852  Cd Length: 129  Bit Score: 51.77  E-value: 4.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 2865 YEILVKTGWGRGSGTTAHVGIMLYGVDSRS---------GHRHLDGDRAFHRNSLDIFQIATPHSLGSVWKIRVWHDNKG 2935
Cdd:cd01754      3 YTIYVQTGSIWKAGTDSRISLQIYDADGPGlrianleawGGLMGAGHDYFERGNLDRFSGRGPCLPSPPCWMNLTSDGTG 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1622916324 2936 LSPAWFLQHVIVRDL-QTARSA--FFLVNDWLSVETEANG 2972
Cdd:cd01754     83 NHPGWYVNYVEVTQAgQHAPCMqhLFAVEQWLATDESPYM 122
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
1156-1476 4.03e-07

Uncharacterized conserved protein, PKD repeat domain [Function unknown];


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 55.45  E-value: 4.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1156 FPYRYAWDFGTeeaaPARAGGPEVTFTYRDPGSYLVTVTASNNV-SAANDSALVEVQEPVVVTDIKVNSSLVlelqqpyl 1234
Cdd:COG3291     23 NATSYEWDFGD----GTTSTEANPSHTYTTPGTYTVTLTVTDAAgCSDTTTKTITVGAPNPGVTTVTTSTTV-------- 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1235 FSAVGRGRPASYLWDLGDGGRLEGPEVTHAYNSIGDFTVRVAGWNDVSRSEAWLNVTVKRRVRGLVVNASRTVVPLNGSV 1314
Cdd:COG3291     91 TTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTT 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1315 SFSTSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFSIIVTAENEVGSAQDSIFVYVLQLIEGLQVAGCGSYFPT 1394
Cdd:COG3291    171 SASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNT 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1395 NHTAQLQAVVRDGTNVSYSWTAWWDRGPALAGSGKGFSLTALEAGTYHVQLRATNMLGSAWADCTVDFVEPVGWLMVTAS 1474
Cdd:COG3291    251 VTTSGANTAGTSTITGGTSGVVTTSAATGTSTNGTGGLGTTTAITPGNVSTTADVTGGTATLAVSSTLTTNDTTGSSSTG 330

                   ..
gi 1622916324 1475 PN 1476
Cdd:COG3291    331 TV 332
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1226-1292 4.57e-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: 50.19  E-value: 4.57e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622916324 1226 VLELQQPYLFSAV--GRGRPASYLWDLGDGGRL--EGPEVTHAYNSIGDFTVRVAGWNDVSRSEA-WLNVTV 1292
Cdd:cd00146     10 VAELGASVTFSASdsSGGSIVSYKWDFGDGEVSssGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTkTTTVVV 81
PKD_4 pfam18911
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
1235-1292 1.26e-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: 48.81  E-value: 1.26e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1235 FSAVGRGRPASYLWDLGDGGRLEGPEVTHAYNSIGDFTVRVAGWND--VSRSEAWLNVTV 1292
Cdd:pfam18911   26 ASDDPDGDILSYRWDFGDGTTATGANVSHTYAAPGTYTVTLTVTDDsgASNSTATDTVTV 85
PKD_4 pfam18911
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
900-956 1.26e-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: 48.81  E-value: 1.26e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  900 PSPGGVL-YTWDFGDSSpvlTQSQPTANHTYASRGTYRVHLEVNNT--VSSALAQADVRV 956
Cdd:pfam18911   29 DPDGDILsYRWDFGDGT---TATGANVSHTYAAPGTYTVTLTVTDDsgASNSTATDTVTV 85
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
303-355 2.06e-06

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: 48.22  E-value: 2.06e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1622916324   303 TATRWDFGDGSpevDAAGPAASHRYVLPGRYHVTAVVALGVSSALLGTNVQVE 355
Cdd:smart00089   30 VSYTWDFGDGT---SSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
408-533 2.26e-06

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


Pssm-ID: 153063  Cd Length: 116  Bit Score: 49.25  E-value: 2.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  408 CPSDTEIFpgNGHCYRLVVEKAAWLQAQEQCRAwAGAALAMVDSPAVQRFLvSRVTRSLDVWIGFSTVQGPETGLAPQGE 487
Cdd:cd03593      1 CPKDWICY--GNKCYYFSMEKKTWNESKEACSS-KNSSLLKIDDEEELEFL-QSQIGSSSYWIGLSREKSEKPWKWIDGS 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1622916324  488 AFSlescqNWLpgEPHPATAE-HCVRLGPTGwCNTDLCSAPHSYVCE 533
Cdd:cd03593     77 PLN-----NLF--NIRGSTKSgNCAYLSSTG-IYSEDCSTKKRWICE 115
YjdB COG5492
Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction ...
1174-1651 2.49e-06

Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction only];


Pssm-ID: 444243 [Multi-domain]  Cd Length: 613  Bit Score: 53.54  E-value: 2.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1174 AGGPEVTFTYRDPGSYLVTVTASNNVSAANDSALVEVQEPVVVTDIKVNSSLVLELQQPYLFSAVGRGRPASYLWDLGDG 1253
Cdd:COG5492    144 TAAVAVGSVGVASAGTSVTTTVATATSASLVSTLVVTSVGLTTASGSLNTVVVTSVVGNGATDASTASAVVAAVTAVTSA 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1254 GRLEGPEVTHAYNSIGDFTVRVAGWNDVSrSEAWLNVTVKRRVRGLVVNASRTVVPLNGSVSFSTSLEAGSDVRYSWVLc 1333
Cdd:COG5492    224 GSLTSAASVTTAGDDGTGVVATTVTTTIS-TSSSTTLTVTGATSSASTLGSGSTTSTNTVTAGVGDTGVSVAVASSSAA- 301
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1334 drcTPIPGGPTISYTFRSVGTFSIIVTAENEVGSAQDSIFVYVLQLIEGLQVAGCGSYFPTNHTAQLQAVVR--DGTNVS 1411
Cdd:COG5492    302 ---TTSAVVGTLSSSGGGGGVVTAAATTGVTVVTASSVATTVDVVPVTGVTLNPTSVTLAVGQTLTLTATVTpaNATNKN 378
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1412 YSWTawwDRGPALAG---SGKgfsLTALEAGTYHVQLRATNmlGSAWADCTV---DFVEPVGWLMVTASPNPAAVNTSVT 1485
Cdd:COG5492    379 VTWS---SSDPSVATvdsNGL---VTAVAAGTATITATTKD--GGKTATCTVtvtAAGSTGTVVVVSLAATSAVSASVVL 450
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1486 LSAKLAGGSGVLYTWSLEEGLSWETPEPFTTHSFPTPGLHLVTVTAGNPLGSASATVEVGVQVPVSGLSIRASESGGSFV 1565
Cdd:COG5492    451 TPAGTVNAGASTASLNVNATDGVSTTVGVANVVSAVTVTASVAEVATSVGGGATVTVTVSTAATVTVTVGVKSTGIAVAG 530
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1566 AAGSSVPFWGQLATGTNVSWCWAVPGGSSkrgphVTMVFPDAGTFSVQLNASNAVSWVSATHNLTVEEPIVGLVLWASSK 1645
Cdd:COG5492    531 STGILAGIVLSGSAKGDVAGGATLVDAGT-----ADVGGTTSTTTSVTDASVVSLTGSTSSTGVGVGGTTATGTAVAALV 605

                   ....*.
gi 1622916324 1646 VVAPGQ 1651
Cdd:COG5492    606 TGTGAT 611
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1052-1114 2.65e-06

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: 47.77  E-value: 2.65e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622916324 1052 CIPTQPDARLTAYV-TGNPAHYLfdWTFGDgsSNTTVRGRPTVTHNFTRSGTFPLALVLSSPVN 1114
Cdd:pfam00801    7 VVAAGQPVTFTATLaDGSNVTYT--WDFGD--SPGTSGSGPTVTHTYLSPGTYTVTLTASNAVG 66
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
431-533 2.82e-06

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 48.63  E-value: 2.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  431 WLQAQEQCRAwAGAALAMVDSPAVQRFLVSRVT-RSLDVWIGFSTVQGPETGLAPQGEAFSLEscqNWLPGEPHPATAEH 509
Cdd:pfam00059    4 WDEAREACRK-LGGHLVSINSAEELDFLSSTLKkSNKYFWIGLTDRKNEGTWKWVDGSPVNYT---NWAPEPNNNGENED 79
                           90       100
                   ....*....|....*....|....*.
gi 1622916324  510 CVRLGPT--GWcNTDLCSAPHSYVCE 533
Cdd:pfam00059   80 CVELSSSsgKW-NDENCNSKNPFVCE 104
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1636-1715 4.59e-06

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: 47.06  E-value: 4.59e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  1636 VGLVLWASSKVVApGQLVHFQI-LLAAGSAVTFRLQVGGASpaVLPGPRFSHSFPRVGDHVVSVQGENHVSWAQAQVRIV 1714
Cdd:smart00089    1 VADVSASPTVGVA-GESVTFTAtSSDDGSIVSYTWDFGDGT--SSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVV 77

                    .
gi 1622916324  1715 V 1715
Cdd:smart00089   78 V 78
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
282-354 5.43e-06

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 47.11  E-value: 5.43e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622916324  282 PHGPLAS-GQLAAFHIAAPLP--VTATRWDFGDGSPEVdAAGPAASHRYVLPGRYHVTAVVALGVSSALLGT-NVQV 354
Cdd:cd00146      6 SAPPVAElGASVTFSASDSSGgsIVSYKWDFGDGEVSS-SGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTtTVVV 81
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
72-130 7.55e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 51.86  E-value: 7.55e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916324   72 TALDVSHNLLraldvglLANLSQLSELDISNNKISTLEEGIfANLFNLSEINLSGNPFE 130
Cdd:COG4886     99 TELDLSGNEE-------LSNLTNLESLDLSGNQLTDLPEEL-ANLTNLKELDLSNNQLT 149
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1730-1806 3.31e-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: 44.75  E-value: 3.31e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622916324  1730 PGIATGTERNFTARVQR-GSRVAYAWYFslqkvqGDSLViLSGRDVTYTPVAAGLLEIQVRAFNALGSENRTLVLEVQ 1806
Cdd:smart00089    9 TVGVAGESVTFTATSSDdGSIVSYTWDF------GDGTS-STGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
PKD_4 pfam18911
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
302-339 3.65e-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: 44.95  E-value: 3.65e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1622916324  302 VTATRWDFGDGSPevdAAGPAASHRYVLPGRYHVTAVV 339
Cdd:pfam18911   34 ILSYRWDFGDGTT---ATGANVSHTYAAPGTYTVTLTV 68
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
773-1132 4.13e-05

Uncharacterized conserved protein, PKD repeat domain [Function unknown];


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 48.90  E-value: 4.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  773 STVPAVLPPNATLALTAgvlVDSAVEVAFLWTFGDGEQAlrqfhppynesfpvpdpsvaqvlVEHNVTHTYAAPGEYI-- 850
Cdd:COG3291      2 TATPTSGCAPLTVQFTD---TSSGNATSYEWDFGDGTTS-----------------------TEANPSHTYTTPGTYTvt 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  851 LTVlTSNAFENLTQQVPVSVRAALPSMAVGVSDSVLVAGRPITFYPHPLPSPGGVLYTWDFGDSSPVLTQSQPTANHTYA 930
Cdd:COG3291     56 LTV-TDAAGCSDTTTKTITVGAPNPGVTTVTTSTTVTTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTTT 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  931 SRGTYRVHLEVNNTVSSALAQADVRVFEELRGLSVNmslaveqGAPVVVSAAVQTGDDITWTFDMGDGTVLSGPEDTVEH 1010
Cdd:COG3291    135 TTGTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTT-------SASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGT 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1011 VYLRAQNCTVTVGAASPAGRLAQSLHVLVFVLEVLRIEPAACIPTQPDARLTAYVTGNPAHYLFDWTFGDGSSNTTVRGR 1090
Cdd:COG3291    208 AGVTTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNTVTTSGANTAGTSTITGGTSGVVTTSAATGTSTNGTGG 287
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1622916324 1091 PTVTHNFTRSGTFPLALVLSSPVNKAHYFTSICVEPEVGNVT 1132
Cdd:COG3291    288 LGTTTAITPGNVSTTADVTGGTATLAVSSTLTTNDTTGSSST 329
PKD_4 pfam18911
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
1159-1210 5.84e-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: 44.18  E-value: 5.84e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622916324 1159 RYAWDF--GTEeaaparAGGPEVTFTYRDPGSYLVTVTASNNVSAANDSALVEV 1210
Cdd:pfam18911   36 SYRWDFgdGTT------ATGANVSHTYAAPGTYTVTLTVTDDSGASNSTATDTV 83
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
1302-1643 1.30e-04

Uncharacterized conserved protein, PKD repeat domain [Function unknown];


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 47.36  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1302 NASRTVVPLNGSVSFsTSLEAGSDVRYSWVLCDRCTPipGGPTISYTFRSVGTFSIIVTAENEVG-SAQDSIFVYVLQLI 1380
Cdd:COG3291      2 TATPTSGCAPLTVQF-TDTSSGNATSYEWDFGDGTTS--TEANPSHTYTTPGTYTVTLTVTDAAGcSDTTTKTITVGAPN 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1381 EGLQVAGCGSYFPTNHTAQLQAVVRDGTNVSYSWTAWWDRGPALAGSGKGFSLTALEAGTYHVqlrATNMLGSAWADCTV 1460
Cdd:COG3291     79 PGVTTVTTSTTVTTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTG---LTGSTGTASDTATV 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1461 DFVEPVGWLMVTASPNPAAVNTSVTLSAKLAGGSGVLYTWSLeeGLSWETPEPFTTHSFPTPGLHLVTVTAGNPLGSASA 1540
Cdd:COG3291    156 TTSVSTTDVTSDGTTSASTNPSVTTDTVTTLTGSYTGTIVGG--SGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDV 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1541 TVEVGVQVPVSGLSIRASESGGSFVAAGSSVPFWGqlaTGTNVSWCWAVPGGSSKRGPHVTMVFPDAGTFSVQLNASNAV 1620
Cdd:COG3291    234 TLTGISTGDAGTPGTNTVTTSGANTAGTSTITGGT---SGVVTTSAATGTSTNGTGGLGTTTAITPGNVSTTADVTGGTA 310
                          330       340
                   ....*....|....*....|...
gi 1622916324 1621 SWVSATHNLTVEEPIVGLVLWAS 1643
Cdd:COG3291    311 TLAVSSTLTTNDTTGSSSTGTVF 333
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
408-534 2.02e-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: 44.27  E-value: 2.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  408 CPSDTEIFpgNGHCYRLVVEKAAWLQAQEQCRAWAG----AALAMVDSPAVQRFL------VSRVTRSLDVWIGF--STV 475
Cdd:cd03589      1 CPTFWTAF--GGYCYRFFGDRLTWEEAELRCRSFSIpgliAHLVSIHSQEENDFVydlfesSRGPDTPYGLWIGLhdRTS 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622916324  476 QGPETGLAPQGEAFSlescqNWLPGEPHPA-TAEHCVRLGPTG-----WcNTDLCSAPHSYVCEL 534
Cdd:cd03589     79 EGPFEWTDGSPVDFT-----KWAGGQPDNYgGNEDCVQMWRRGdagqsW-NDMPCDAVFPYICKM 137
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
701-762 3.19e-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: 42.05  E-value: 3.19e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622916324   701 YSPVVEAGSDVVFRWTINDKQSLTFQNVVFnvIYQSAAVFKLSLTASNHVSNVTVNYNVTVE 762
Cdd:smart00089   20 TATSSDDGSIVSYTWDFGDGTSSTGPTVTH--TYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
LRR_8 pfam13855
Leucine rich repeat;
93-127 4.03e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.97  E-value: 4.03e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1622916324   93 SQLSELDISNNKISTLEEGIFANLFNLSEINLSGN 127
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNN 35
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1391-1459 5.46e-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: 5.46e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916324 1391 YFPTNHTAQLQAVVR-------DGTNVSYSWTawWDRGPALAGSGKGFSLTALEAGTYHVQLRATNMLGSAWADCT 1459
Cdd:cd00146      4 SVSAPPVAELGASVTfsasdssGGSIVSYKWD--FGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTT 77
LRRNT smart00013
Leucine rich repeat N-terminal domain;
34-73 7.88e-04

Leucine rich repeat N-terminal domain;


Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 39.61  E-value: 7.88e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1622916324    34 PCAPPCLCGPapgaaCRVNCSGRGLRTLgpALRIPADATA 73
Cdd:smart00013    1 ACPAPCNCSG-----TAVDCSGRGLTEV--PLDLPPDTTL 33
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
419-511 8.38e-04

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


Pssm-ID: 153058  Cd Length: 124  Bit Score: 42.18  E-value: 8.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  419 GHCYRLVVEKAAWLQAQEQCRAwAGAALAMVDSPAVQRFlVSRVTRSLDvWIGFS--TVQGPETGlaPQGEAFSLEscqN 496
Cdd:cd03588     10 GHCYRHFPDRETWEDAERRCRE-QQGHLSSIVTPEEQEF-VNNNAQDYQ-WIGLNdrTIEGDFRW--SDGHPLQFE---N 81
                           90
                   ....*....|....*..
gi 1622916324  497 WLPGEPHP--ATAEHCV 511
Cdd:cd03588     82 WRPNQPDNffATGEDCV 98
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
975-1224 9.11e-04

Uncharacterized conserved protein, PKD repeat domain [Function unknown];


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 44.66  E-value: 9.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  975 APVVVS-AAVQTGDDITWTFDMGDGTVLSGPedTVEHVYLRAQNCTVTVGAASPAGRLAqSLHVLVFVLEVLRIEPAACI 1053
Cdd:COG3291     10 APLTVQfTDTSSGNATSYEWDFGDGTTSTEA--NPSHTYTTPGTYTVTLTVTDAAGCSD-TTTKTITVGAPNPGVTTVTT 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1054 PTQPDARLTAYVTGNPAHYLFDWTFGDGSSNTTVRGRPTVTHNFTRSGTFPLALVLSSPVNKAHYFTSICVEPEVGNVTL 1133
Cdd:COG3291     87 STTVTTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVTTSVSTTDVTS 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324 1134 QPERQFVQLGDEVRLVACVWPPFPYRYAWDFGTEEAAPARAGGPEVTFTYRDPGSYLVTVTASNNVSAANDSALVEVQEP 1213
Cdd:COG3291    167 DGTTSASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTP 246
                          250
                   ....*....|.
gi 1622916324 1214 VVVTDIKVNSS 1224
Cdd:COG3291    247 GTNTVTTSGAN 257
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
782-870 1.23e-03

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: 40.56  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  782 NATLALTAGVLVDSAVeVAFLWTFGDGEQALRQfhppynesfpvpdpsvaqvlvEHNVTHTYAAPGEYILTV-LTSNAFE 860
Cdd:cd00146     14 GASVTFSASDSSGGSI-VSYKWDFGDGEVSSSG---------------------EPTVTHTYTKPGTYTVTLtVTNAVGS 71
                           90
                   ....*....|
gi 1622916324  861 NLTQQVPVSV 870
Cdd:cd00146     72 SSTKTTTVVV 81
PKD_4 pfam18911
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
1838-1876 1.40e-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: 40.33  E-value: 1.40e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1622916324 1838 VAYHWDFGDGAPGqdtDEPRAEHCYLRPGDYRVQVNASN 1876
Cdd:pfam18911   35 LSYRWDFGDGTTA---TGANVSHTYAAPGTYTVTLTVTD 70
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1639-1715 1.70e-03

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: 40.17  E-value: 1.70e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622916324 1639 VLWASSKVVAPGQLVHFQI-LLAAGSAVTFRLQVGGASPAVLPGPRFSHSFPRVGDHVVSVQGENHVSWAQAQVRIVV 1715
Cdd:cd00146      3 ASVSAPPVAELGASVTFSAsDSSGGSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTTTVV 80
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
690-754 4.08e-03

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: 38.52  E-value: 4.08e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622916324  690 VPAGPPAQYSrysPVVEAGSDVVFRWTINDKQSLTFQNVVFNVIYQSAAVFKLSLTASNHVSNVT 754
Cdd:pfam00801    8 VAAGQPVTFT---ATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSAN 69
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
1827-1890 4.37e-03

Uncharacterized conserved protein, PKD repeat domain [Function unknown];


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 42.73  E-value: 4.37e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622916324 1827 FEAATSPSPrrVAYHWDFGDGApgqDTDEPRAEHCYLRPGDYRVQVNASNLV-SFFVAQATVTVQ 1890
Cdd:COG3291     16 FTDTSSGNA--TSYEWDFGDGT---TSTEANPSHTYTTPGTYTVTLTVTDAAgCSDTTTKTITVG 75
CLECT_TC14_like cd03601
C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 ...
437-533 5.37e-03

C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm; CLECT_TC14_like: C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TC14 is homodimeric. The CTLD of TC14 binds D-galactose and D-fucose. TC14 is expressed constitutively by multipotent epithelial and mesenchymal cells and plays in role during budding, in inducing the aggregation of undifferentiated mesenchymal cells to give rise to epithelial forming tissue. TC14-2 and TC14-3 shows calcium-dependent galactose binding activity. TC14-3 is a cytostatic factor which blocks cell growth and dedifferentiation of the atrial epithelium during asexual reproduction. It may also act as a differentiation inducing factor. Galactose inhibits the cytostatic activity of TC14-3. The gene for Acorn worm PfG6 is gill-specific; PfG6 may be a secreted protein.


Pssm-ID: 153071  Cd Length: 119  Bit Score: 39.82  E-value: 5.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916324  437 QCRAWAGAALAMVDSPAVQRFLVSRVTRSLDVWIGFSTVQGPETG-LAPQGEAFSLEScQNWLPGEP-HPATAEHCVRLg 514
Cdd:cd03601     20 RSRGMRLASLAMRDSEMRDAILAFTLVKGHGYWVGADNLQDGEYDfLWNDGVSLPTDS-DLWAPNEPsNPQSRQLCVQL- 97
                           90       100
                   ....*....|....*....|....
gi 1622916324  515 ptgWCNTDL-----CSAPHSYVCE 533
Cdd:cd03601     98 ---WSKYNLlddeyCGRAKRVICE 118
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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