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Conserved domains on  [gi|1622916307|ref|XP_028697312|]
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polycystin-1 isoform X3 [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) ...
99-2728 0e+00

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


The actual alignment was detected with superfamily member TIGR00864:

Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 4618.93  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307   99 DISNNKISTLEEGIFANLFNLSEINLSGNPFECDCGLVWLPRWAEEQQVRVVQPEAATCAGPGSLAGQPLLGIPLLDSDC 178
Cdd:TIGR00864    1 DISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPEAALCAGPGALAGQPLLGIPLLDSGC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  179 GEEYIACLPDNSSGTVAAVA----FSAAHEGLLQPEACSAFCFSTGRGLAALSEQGWCLCGAAQPSSASFACLSFCSGPP 254
Cdd:TIGR00864   81 DEEYVACLKDNSSGGGAARSelviFSAAHEGLFQPEACNAFCFSAGHGLAALGEQGECLCGAAQPSEANFACESLCSGPP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  255 PPPALDCGGPTLLQHVFPASPGAALVGPHGPLASGQLAAFHIAAPLPVTATRWDFGDGSPEVDAAGP----AASHRYVLP 330
Cdd:TIGR00864  161 PPPAAACRGPQLLEHIFPALPGAPIQGPHGPIASGQLAAFHAAAPLAPTAMRWDFGDGSAEVDAAGAggttAASHKYGHP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  331 GRYHVTAVVALGVSSALLGTNVQVEAAPAALELVCPSSVQSDESLKLSIQNRGGSGLEAAYSIVALGEELARVVHPLCPS 410
Cdd:TIGR00864  241 GRYHVSAMGALGAGKALAGGDVQVEAAPAALELHCPSLVQADESLDLSIQNRGGSDLDAAWKITAHGEEPAKASHPHCPK 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  411 DTEIFPGNGHCYRLVVEKAAWLQAQEQCRAWAGAALAMVDSPAVQRFLVSRVTRSLD--VWIGFSTVQGPETGLAPQGEA 488
Cdd:TIGR00864  321 DGEIFEENGHCFQIVPEEAAWLDAQEQCLARAGAALAIVDNDALQNFLARKVTHSLDrgVWIGFSDVNGAEKGPAHQGEA 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  489 FSLESCQNWLPGEPHPATAEHCVRLGPTGWCNTDLCSAPHSYVCELRPGGPVQDAENLLVGAPSGDLQGPLTPLTPQDGL 568
Cdd:TIGR00864  401 FEAEECEEGLAGEPHPARAEHCVRLDPRGQCNSDLCNAPHAYVCELNPGGPVPDAENFAMGAASFDLHGLLQALAAMDGL 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  569 SAP-HEPVEVMVFPGLSLSHEAFLTTAEFGTQELRRPAQLRLQVYRL---LSTAGTPENGSEPESRSPDNRTQLVPECMP 644
Cdd:TIGR00864  481 PAPpHEGVEVLLFPALRFSRAAFLSSAEFGTQELRRPAHILFQIYRLrcrLPGAGGPACGPEAECRPPDNRSADAPACMK 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  645 GGRWCPAANVCVPLDASCHPQA--NGCTSGPGLPGA----LYALWREFLFSVPAGPPAQYSVTLHGQDVLMLPGDLVGLQ 718
Cdd:TIGR00864  561 GEQWCPFAHICLPLDAPCHPQAcaNGCSQGHGLPGAarmpLYALQREFLFSLPAGPAAHVLLQDHGEDLLMLPGDLIALQ 640
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  719 HDAGPGALLHCSPAPGHPGPQALYLSANASAWLPH------------------------LPAQLEGTR----DCPACALR 770
Cdd:TIGR00864  641 HDAGPAALIHCQPAPGHPGPRAPVFAANASEWFGHnntpvppdnlagdgadplpdpeldLKALLEGTRaswlECAACAIR 720
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  771 LLAATEQLTVLLGLRPNPGLRLPGRYEVRAEVGNGVSRHNLSCSFNVVSPVAGLRVIYPAPHNGHLYVPTNGSALVLQVD 850
Cdd:TIGR00864  721 LLAAGEQETRLLGAELNAGLPLPGLYELLAESAKGSDLHNASCSFDVLPPLAGLRVIHPAPQDGRLFLESNGSALLLQVD 800
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  851 SGANATATARWPGGNVSTRFEAACPALVA-------TLLPGCPWETNDTQFSVVALPWLSEGEHV----VEVVAENSASQ 919
Cdd:TIGR00864  801 SGANAEAKAFWPGGNSSARFENVCPAEFAsrlchpsTFEGGCAEEAEDSLFAVLALNWLKEGEHTgpvqVDLMAENNASE 880
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  920 ANLSLRVTAEEPICGLRATPSPEARVLQGVLVRYSPVVEAGSDVVFRWTINDKQSLTFQNVVFNVIYQSAAVFKLSLTAS 999
Cdd:TIGR00864  881 ANLSLLVQAEEPICGLRAQPHPAARVLMESLVRYSASVEAGSDMTFKWTIDDKPFFTFQNTVFNVIYQHAAVFKLSLTAM 960
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1000 NHVSNVTVNYNVTVERMNRMQGLWVSTVPAVLPPNATLALTAGVLVDSAVEVAFLWTFGDGEQALRQFHPPYNESFPVPD 1079
Cdd:TIGR00864  961 NHVSNLTEDFNVTVDRLNPMQGLQVKGVPAVLPPGATLALTAGVLIDMAVEAAFLWSFGDGEQALFEFKPPYNESFPCPD 1040
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1080 PSVAQVLVEHNVTHTYAAPGEYILTVLTSNAFENLTQQVPVSVRAALPSMAVGVSDSVLVAGRPITFYPHPLPSPGGVLY 1159
Cdd:TIGR00864 1041 PSPAQVLLEHNVMHIYAAPGEYLATVLASNAFENISQQINMSVRAILPRVAIGTEDGLLLAGKPADFEAHPLPSPGGIHY 1120
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1160 TWDFGDSSPVLTQSQPTANHTYASRGTYRVHLEVNNTVSSALAQADVRVFEELRGLSVNMSLAVEQGAPVVVSAAVQTGD 1239
Cdd:TIGR00864 1121 EWDFGDGSALLQGRQPAAAHTFAKRGPFHVCLEVNNTISGAAACADMFAFEEIEGLSADMSLATELGAATTVRAALQSGD 1200
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1240 DITWTFDMGDGTVLSGPEDTVEHVYLRAQNCTVTVGAASPAGRLAQSLHVLVFVLEVLRIEPAACIPTQPDARLTAYVTG 1319
Cdd:TIGR00864 1201 NITWTFDMGDGKSLSGPEATVEHKYAKAGNCTVNIGAANAAGHGARIIHVEVFVFEVAGIEPAACIGEHADANFRARVSG 1280
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1320 NPAHYLFDWTFGDGSSNTTVRGRPTVTHNFTRSGTFPLALVLSSPVNKAHYFTSICVEPEVGNVTLQPERQFVQLGDEVR 1399
Cdd:TIGR00864 1281 NAAHYLFDWSFGDGSPNETHHGCPGISHNFRGNGTFPLALTISSGVNKAHFFTQICVEPELGKISLQAEKQFFALGDEAQ 1360
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1400 LVACVWPPFPYRYAWDFGTEEAAPARAGGPEVTFTYRDPGSYLVTVTASNNVSAANDSALVEVQEPVVVTDIKVNSSL-- 1477
Cdd:TIGR00864 1361 FQACAEPEFNYRYEWDFGGEEAAPLPAAGAEVTFIYNDPGCYLVTVAASNNISAANDSALIEVLEPVGATSFKHNGSHgn 1440
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1478 VLELQQPYLFSAVGRGRPASYLWDLGDGGRLEGPEVTHAYNSIGDFTVRVAGWNDVSRSEAWLNVTVKRRVRGLVVNASR 1557
Cdd:TIGR00864 1441 NLELGQPYLFSAFGRARNASYLWDFGDGGLLEGPEILHAFNSPGDFNIRLAAANEVGKNEATLNVAVKARVRGLTINASL 1520
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1558 TVVPLNGSVSFSTSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFSIIVTAENEVGSAQDSIFVYVLQLIEGLQV 1637
Cdd:TIGR00864 1521 TNVPLNGSVHFEAHLDAGDDVRFSWILCDHCTPIFGGNTIFYTFRSVGTFNIIVTAENDVGAAQASIFLFVLQEIEGLQI 1600
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1638 AG-------------CGSYFPTNHTAQLQAVVRDGTNVSYSWTAWWD---RGPALAGSGKGFSLTALEAGTYHVQLRATN 1701
Cdd:TIGR00864 1601 LGetaegggggvqelDGCYFETNHTVQFHAGFKDGTNLSFSWNAILDnepDGPAFAGSGKGAKLNPLEAGPCDIFLQAAN 1680
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1702 MLGSAWADCTVDFVEPVGWLMVTASPNPAAVNTSVTLSAKLAGGSGVLYTWSLEEGLSWETPEPFTTHSFPTPGLHLVTV 1781
Cdd:TIGR00864 1681 LLGQATADCTIDFLEPAGNLMLAASDNPAAVNALINLSAELAEGSGLQYRWFLEEGDDLETSEPFMSHSFPSAGLHLVTM 1760
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1782 TAGNPLGSASATVEVGVQVPVSGLSIRASESGGS-FVAAGSSVPFWGQLATGTNVSWCWAVPGGSSKRGPHVTMVFPDAG 1860
Cdd:TIGR00864 1761 KAFNELGSANASEEVDVQEPISGLKIRAADAGEQnFFAADSSVCFQGELATGTNVSWCWAIDGGSSKMGKHACMTFPDAG 1840
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1861 TFSVQLNASNAVSWVSATHNLTVEEPIVGLVLWASSKVVAPGQLVHFQILLAAGSAVTFRLQVGGASPAVL-PGPRFSHS 1939
Cdd:TIGR00864 1841 TFAIRLNASNAVSGKSASREFFAEEPIFGLELKASKKIAAIGEKVEFQILLAAGSAVNFRLQIGGAAPEVLqPGPRFSHS 1920
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1940 FPRVGDHVVSVQGENHVSWAQAQVRIVVLEAVSGLQVPNCCEPGIATGTERNFTARVQRGSRVAYAWYFSLQKVQGDSLV 2019
Cdd:TIGR00864 1921 FPRVDDHMVNLRAKNEVSCAQANLHIEVLEAVRGLQIPDCCAAGIATGEEKNFTANVQRGKPVAFAWTFDLHHLHGDSLV 2000
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2020 ILSGRDVTYTPVAAGLLEIQVRAFNALGSENRTLVLEVQDAVQYVALRSGP--CFTNRSAWFEAATSPSPRRVAYHWDFG 2097
Cdd:TIGR00864 2001 IHMGKDVSYTAEAAGLLEIQLGAFNALGAENITLQLEAQDALMDAALQAGPqdCFTNKMAQFEAATSPKPNFMACHWDFG 2080
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2098 DGAPGQDTDEPRAEHCYLRPGDYRVQVNASNLVSFFVAQATVTVQVLACREPEVDVVLPLQVLMRRSQRNYLEAHVDLRD 2177
Cdd:TIGR00864 2081 DGSAGQDTDEPRAEHEYLHPGDYRVQVNASNLVSFFSAHAEINVQVLACEEPEVDVVLALQLAIRRSQPNLLEAHVDLKD 2160
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2178 CVTYQTEYRWEVYRTASCQRPGRPTRVALPG-------------VDVSRPQLVLPRLALPVGHYCFVFVVSFGDTPLARS 2244
Cdd:TIGR00864 2161 CLRYGAEYLWEILRAASCDNDGHFARGALNGatrsfpviplpaeVDVQRLQLSLPKLALAAGHYCFVFSLSFEDTPLKKA 2240
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2245 IQANVTVAPERLVPIIEGGSYRVWSDTQDLVLDGSESYDPNLEDGDQTPLSFHWACVASTQREAGGCALNFGPRG-SSVV 2323
Cdd:TIGR00864 2241 ACANLGVAAARLMPIIEGGSYRVWSDTQDLQLDAEESYDPNLDDDDQSLLHFHWACQASSKGEAGCCALNFGLGGkGPTL 2320
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2324 TIPRERLAAGVEYTFSLTVWKAGRKEEATNQTVLIRRGRVPIVSLECVSCKAQAVYEVSRSSYVYLEGRCLNCSSGSKRG 2403
Cdd:TIGR00864 2321 GIPGEELAAGIEYTFKLSIGKAGMKEEATNQTVLIQSGHIPIVSLECVSCKAQALYEVSQNSYVYLEGRCLNCQSGFHRG 2400
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2404 RWAARTFSNKTLVLDETTTSTGSAGMRLVLRRGVLRDGEGYTFTLTVLGHSGEEEGCASIRLSPNRPPLGGSCRLFPLGN 2483
Cdd:TIGR00864 2401 RWAARTFQNDTLVLDESSTSTGSAGMNLVLRQGVLHDGEGYNFTLHVLDDSGDEEGAASIRLHHNMPPDGGECHLFPGGE 2480
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2484 --------------VHALTTKVHFECTGWHDAEDAGAPLVYALLLRRCRQGHCEEFCVYKGSLSSYGAVLPPGFR-PHFE 2548
Cdd:TIGR00864 2481 tgqehgdkedevwaIEALLDKVHFECSGWHDAEDAEAPLLYALLLNRCRDDHCEEFCVYKGSLPEHGAFLPPGFRsAHFE 2560
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2549 VGLAVVVQDQLGAAVVALNRSLAIALPEPSGGTTGLTVWLHGLTASVLPGLLRQADPQHVIEYSLALVTVLNEYEQALDV 2628
Cdd:TIGR00864 2561 VGLAITVEDHLGAAIRALNKSIAITLPDPNGEASGLPHWLHDLIASKLKGLLDQADFQHVIELSLALITVLNEYEQALDS 2640
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2629 AAEPEHERQRRAQIRKNVTQTLVSLRVHTVDDIQQIAAALAQSMGPSRELVCRSCLKQTLHKLEAMMRILQAETTAGTVT 2708
Cdd:TIGR00864 2641 AAEPKHERGHRAQIRKNITEALTALDLHTVDDIQQIAAALAQCMAPSREFICEECLKQTLHKLEAMLEILQADTKAGIVT 2720
                         2730      2740
                   ....*....|....*....|
gi 1622916307 2709 PTAIGDSILNITGDLIHLAS 2728
Cdd:TIGR00864 2721 PTAIADNILNIMGDLIHLAS 2740
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
3115-3234 1.40e-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: 198.65  E-value: 1.40e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 3115 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLDGD--RAFHRNSLDIFQIATPHSLGSVWKIRVWHDNKGLSPAW 3192
Cdd:cd01752      1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPekPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1622916307 3193 FLQHVIVRDLQTARSAFFLVNDWLSVETEanGGLVEKEVLVA 3234
Cdd:cd01752     81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEG--DGTVERTFPVA 120
Polycystin_dom super family cl48672
Polycystin domain; This domain represents the polycystin domain from group II of Transient ...
3710-3894 7.02e-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: 194.18  E-value: 7.02e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 3710 FLAITRSEELWPWMAHVLLPYVHGNQS------------SPELGPPRLRQVRLQEALC--PDPPGPRVHTCSAAGGFSTS 3775
Cdd:pfam20519    2 LLTVTDLDDIWDWLSSVLLPALHSNKTpsglpgsfiayeSLLLGVPRLRQLRVRNSSClvHDKFVREINECHAGYSPPSE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 3776 DY----DVGWESPHNGSGTW-AYSAPDLL-GAWSWGSCAVYDSGGYVQELGLSLEESRDRLRFLQLHNWLDnsdphplRR 3849
Cdd:pfam20519   82 DRklysALPYKPVHYGSKYWfIYTPPGLLmGYDHWGHLASYPSGGYVVLLPSSREESLKRLAYLQDNNWLD-------RG 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1622916307 3850 SRAVFVELTRYSPAVGLHAAVTLRLEFPAAGRALAALSVRPFALR 3894
Cdd:pfam20519  155 TRAVFVDFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVKLL 199
PKD_channel super family cl37568
Polycystin cation channel; This family contains the cation channel region from group II of ...
3895-4116 6.49e-44

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


The actual alignment was detected with superfamily member pfam08016:

Pssm-ID: 462341 [Multi-domain]  Cd Length: 225  Bit Score: 160.91  E-value: 6.49e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 3895 RLSAGLSLPLLT-SVCLLLFALHFAVAEARTWHREGCwHVLRpRAW--ARWLLVVLTAATALVRLAQLGAADRQWTrFVR 3971
Cdd:pfam08016    1 RYVTNRSLFILLcEIVFVVFFLYFVVEEILKIRKHRP-SYLR-SVWnlLDLAIVILSVVLIVLNIYRDFLADRLIK-SVE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 3972 GRPRRFTSFDQVAQLSSAARGLAASLLFLLLVKAAQQLRFVRQWSVFGKTLFRALPELLGATLGLVVLGVAYAQLAVLLV 4051
Cdd:pfam08016   78 ASPVTFIDFDRVAQLDNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFGYLLF 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622916307 4052 SSCVDSLWSVAQALLVLCsgtglSTLCPAESWH--------LSPLLCVGLWALRLWGALRLGAVILRWRYHAL 4116
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 ...
3008-3057 6.64e-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: 6.64e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1622916307  3008 YTSLCQYFSEENMVWRTEGLLPLEETSPHqAVCLTRHLTAFGASLFVPPS 3057
Cdd:smart00303    1 FNPICVFWDESSGEWSTRGCELLETNGTH-TTCSCNHLTTFAVLMDVPPI 49
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
56-129 2.63e-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: 2.63e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916307   56 RGLRTLGPALRIpadataLDVSHNLLRALDVglLANLSQLSELDISNNKISTLEE--GIFANLFNLSEINLSGNPF 129
Cdd:cd21340    113 RSLAALSNSLRV------LNISGNNIDSLEP--LAPLRNLEQLDASNNQISDLEEllDLLSSWPSLRELDLTGNPV 180
LRRNT smart00013
Leucine rich repeat N-terminal domain;
34-73 9.68e-04

Leucine rich repeat N-terminal domain;


:

Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 39.22  E-value: 9.68e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1622916307    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) ...
99-2728 0e+00

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 4618.93  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307   99 DISNNKISTLEEGIFANLFNLSEINLSGNPFECDCGLVWLPRWAEEQQVRVVQPEAATCAGPGSLAGQPLLGIPLLDSDC 178
Cdd:TIGR00864    1 DISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPEAALCAGPGALAGQPLLGIPLLDSGC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  179 GEEYIACLPDNSSGTVAAVA----FSAAHEGLLQPEACSAFCFSTGRGLAALSEQGWCLCGAAQPSSASFACLSFCSGPP 254
Cdd:TIGR00864   81 DEEYVACLKDNSSGGGAARSelviFSAAHEGLFQPEACNAFCFSAGHGLAALGEQGECLCGAAQPSEANFACESLCSGPP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  255 PPPALDCGGPTLLQHVFPASPGAALVGPHGPLASGQLAAFHIAAPLPVTATRWDFGDGSPEVDAAGP----AASHRYVLP 330
Cdd:TIGR00864  161 PPPAAACRGPQLLEHIFPALPGAPIQGPHGPIASGQLAAFHAAAPLAPTAMRWDFGDGSAEVDAAGAggttAASHKYGHP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  331 GRYHVTAVVALGVSSALLGTNVQVEAAPAALELVCPSSVQSDESLKLSIQNRGGSGLEAAYSIVALGEELARVVHPLCPS 410
Cdd:TIGR00864  241 GRYHVSAMGALGAGKALAGGDVQVEAAPAALELHCPSLVQADESLDLSIQNRGGSDLDAAWKITAHGEEPAKASHPHCPK 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  411 DTEIFPGNGHCYRLVVEKAAWLQAQEQCRAWAGAALAMVDSPAVQRFLVSRVTRSLD--VWIGFSTVQGPETGLAPQGEA 488
Cdd:TIGR00864  321 DGEIFEENGHCFQIVPEEAAWLDAQEQCLARAGAALAIVDNDALQNFLARKVTHSLDrgVWIGFSDVNGAEKGPAHQGEA 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  489 FSLESCQNWLPGEPHPATAEHCVRLGPTGWCNTDLCSAPHSYVCELRPGGPVQDAENLLVGAPSGDLQGPLTPLTPQDGL 568
Cdd:TIGR00864  401 FEAEECEEGLAGEPHPARAEHCVRLDPRGQCNSDLCNAPHAYVCELNPGGPVPDAENFAMGAASFDLHGLLQALAAMDGL 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  569 SAP-HEPVEVMVFPGLSLSHEAFLTTAEFGTQELRRPAQLRLQVYRL---LSTAGTPENGSEPESRSPDNRTQLVPECMP 644
Cdd:TIGR00864  481 PAPpHEGVEVLLFPALRFSRAAFLSSAEFGTQELRRPAHILFQIYRLrcrLPGAGGPACGPEAECRPPDNRSADAPACMK 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  645 GGRWCPAANVCVPLDASCHPQA--NGCTSGPGLPGA----LYALWREFLFSVPAGPPAQYSVTLHGQDVLMLPGDLVGLQ 718
Cdd:TIGR00864  561 GEQWCPFAHICLPLDAPCHPQAcaNGCSQGHGLPGAarmpLYALQREFLFSLPAGPAAHVLLQDHGEDLLMLPGDLIALQ 640
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  719 HDAGPGALLHCSPAPGHPGPQALYLSANASAWLPH------------------------LPAQLEGTR----DCPACALR 770
Cdd:TIGR00864  641 HDAGPAALIHCQPAPGHPGPRAPVFAANASEWFGHnntpvppdnlagdgadplpdpeldLKALLEGTRaswlECAACAIR 720
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  771 LLAATEQLTVLLGLRPNPGLRLPGRYEVRAEVGNGVSRHNLSCSFNVVSPVAGLRVIYPAPHNGHLYVPTNGSALVLQVD 850
Cdd:TIGR00864  721 LLAAGEQETRLLGAELNAGLPLPGLYELLAESAKGSDLHNASCSFDVLPPLAGLRVIHPAPQDGRLFLESNGSALLLQVD 800
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  851 SGANATATARWPGGNVSTRFEAACPALVA-------TLLPGCPWETNDTQFSVVALPWLSEGEHV----VEVVAENSASQ 919
Cdd:TIGR00864  801 SGANAEAKAFWPGGNSSARFENVCPAEFAsrlchpsTFEGGCAEEAEDSLFAVLALNWLKEGEHTgpvqVDLMAENNASE 880
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  920 ANLSLRVTAEEPICGLRATPSPEARVLQGVLVRYSPVVEAGSDVVFRWTINDKQSLTFQNVVFNVIYQSAAVFKLSLTAS 999
Cdd:TIGR00864  881 ANLSLLVQAEEPICGLRAQPHPAARVLMESLVRYSASVEAGSDMTFKWTIDDKPFFTFQNTVFNVIYQHAAVFKLSLTAM 960
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1000 NHVSNVTVNYNVTVERMNRMQGLWVSTVPAVLPPNATLALTAGVLVDSAVEVAFLWTFGDGEQALRQFHPPYNESFPVPD 1079
Cdd:TIGR00864  961 NHVSNLTEDFNVTVDRLNPMQGLQVKGVPAVLPPGATLALTAGVLIDMAVEAAFLWSFGDGEQALFEFKPPYNESFPCPD 1040
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1080 PSVAQVLVEHNVTHTYAAPGEYILTVLTSNAFENLTQQVPVSVRAALPSMAVGVSDSVLVAGRPITFYPHPLPSPGGVLY 1159
Cdd:TIGR00864 1041 PSPAQVLLEHNVMHIYAAPGEYLATVLASNAFENISQQINMSVRAILPRVAIGTEDGLLLAGKPADFEAHPLPSPGGIHY 1120
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1160 TWDFGDSSPVLTQSQPTANHTYASRGTYRVHLEVNNTVSSALAQADVRVFEELRGLSVNMSLAVEQGAPVVVSAAVQTGD 1239
Cdd:TIGR00864 1121 EWDFGDGSALLQGRQPAAAHTFAKRGPFHVCLEVNNTISGAAACADMFAFEEIEGLSADMSLATELGAATTVRAALQSGD 1200
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1240 DITWTFDMGDGTVLSGPEDTVEHVYLRAQNCTVTVGAASPAGRLAQSLHVLVFVLEVLRIEPAACIPTQPDARLTAYVTG 1319
Cdd:TIGR00864 1201 NITWTFDMGDGKSLSGPEATVEHKYAKAGNCTVNIGAANAAGHGARIIHVEVFVFEVAGIEPAACIGEHADANFRARVSG 1280
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1320 NPAHYLFDWTFGDGSSNTTVRGRPTVTHNFTRSGTFPLALVLSSPVNKAHYFTSICVEPEVGNVTLQPERQFVQLGDEVR 1399
Cdd:TIGR00864 1281 NAAHYLFDWSFGDGSPNETHHGCPGISHNFRGNGTFPLALTISSGVNKAHFFTQICVEPELGKISLQAEKQFFALGDEAQ 1360
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1400 LVACVWPPFPYRYAWDFGTEEAAPARAGGPEVTFTYRDPGSYLVTVTASNNVSAANDSALVEVQEPVVVTDIKVNSSL-- 1477
Cdd:TIGR00864 1361 FQACAEPEFNYRYEWDFGGEEAAPLPAAGAEVTFIYNDPGCYLVTVAASNNISAANDSALIEVLEPVGATSFKHNGSHgn 1440
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1478 VLELQQPYLFSAVGRGRPASYLWDLGDGGRLEGPEVTHAYNSIGDFTVRVAGWNDVSRSEAWLNVTVKRRVRGLVVNASR 1557
Cdd:TIGR00864 1441 NLELGQPYLFSAFGRARNASYLWDFGDGGLLEGPEILHAFNSPGDFNIRLAAANEVGKNEATLNVAVKARVRGLTINASL 1520
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1558 TVVPLNGSVSFSTSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFSIIVTAENEVGSAQDSIFVYVLQLIEGLQV 1637
Cdd:TIGR00864 1521 TNVPLNGSVHFEAHLDAGDDVRFSWILCDHCTPIFGGNTIFYTFRSVGTFNIIVTAENDVGAAQASIFLFVLQEIEGLQI 1600
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1638 AG-------------CGSYFPTNHTAQLQAVVRDGTNVSYSWTAWWD---RGPALAGSGKGFSLTALEAGTYHVQLRATN 1701
Cdd:TIGR00864 1601 LGetaegggggvqelDGCYFETNHTVQFHAGFKDGTNLSFSWNAILDnepDGPAFAGSGKGAKLNPLEAGPCDIFLQAAN 1680
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1702 MLGSAWADCTVDFVEPVGWLMVTASPNPAAVNTSVTLSAKLAGGSGVLYTWSLEEGLSWETPEPFTTHSFPTPGLHLVTV 1781
Cdd:TIGR00864 1681 LLGQATADCTIDFLEPAGNLMLAASDNPAAVNALINLSAELAEGSGLQYRWFLEEGDDLETSEPFMSHSFPSAGLHLVTM 1760
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1782 TAGNPLGSASATVEVGVQVPVSGLSIRASESGGS-FVAAGSSVPFWGQLATGTNVSWCWAVPGGSSKRGPHVTMVFPDAG 1860
Cdd:TIGR00864 1761 KAFNELGSANASEEVDVQEPISGLKIRAADAGEQnFFAADSSVCFQGELATGTNVSWCWAIDGGSSKMGKHACMTFPDAG 1840
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1861 TFSVQLNASNAVSWVSATHNLTVEEPIVGLVLWASSKVVAPGQLVHFQILLAAGSAVTFRLQVGGASPAVL-PGPRFSHS 1939
Cdd:TIGR00864 1841 TFAIRLNASNAVSGKSASREFFAEEPIFGLELKASKKIAAIGEKVEFQILLAAGSAVNFRLQIGGAAPEVLqPGPRFSHS 1920
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1940 FPRVGDHVVSVQGENHVSWAQAQVRIVVLEAVSGLQVPNCCEPGIATGTERNFTARVQRGSRVAYAWYFSLQKVQGDSLV 2019
Cdd:TIGR00864 1921 FPRVDDHMVNLRAKNEVSCAQANLHIEVLEAVRGLQIPDCCAAGIATGEEKNFTANVQRGKPVAFAWTFDLHHLHGDSLV 2000
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2020 ILSGRDVTYTPVAAGLLEIQVRAFNALGSENRTLVLEVQDAVQYVALRSGP--CFTNRSAWFEAATSPSPRRVAYHWDFG 2097
Cdd:TIGR00864 2001 IHMGKDVSYTAEAAGLLEIQLGAFNALGAENITLQLEAQDALMDAALQAGPqdCFTNKMAQFEAATSPKPNFMACHWDFG 2080
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2098 DGAPGQDTDEPRAEHCYLRPGDYRVQVNASNLVSFFVAQATVTVQVLACREPEVDVVLPLQVLMRRSQRNYLEAHVDLRD 2177
Cdd:TIGR00864 2081 DGSAGQDTDEPRAEHEYLHPGDYRVQVNASNLVSFFSAHAEINVQVLACEEPEVDVVLALQLAIRRSQPNLLEAHVDLKD 2160
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2178 CVTYQTEYRWEVYRTASCQRPGRPTRVALPG-------------VDVSRPQLVLPRLALPVGHYCFVFVVSFGDTPLARS 2244
Cdd:TIGR00864 2161 CLRYGAEYLWEILRAASCDNDGHFARGALNGatrsfpviplpaeVDVQRLQLSLPKLALAAGHYCFVFSLSFEDTPLKKA 2240
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2245 IQANVTVAPERLVPIIEGGSYRVWSDTQDLVLDGSESYDPNLEDGDQTPLSFHWACVASTQREAGGCALNFGPRG-SSVV 2323
Cdd:TIGR00864 2241 ACANLGVAAARLMPIIEGGSYRVWSDTQDLQLDAEESYDPNLDDDDQSLLHFHWACQASSKGEAGCCALNFGLGGkGPTL 2320
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2324 TIPRERLAAGVEYTFSLTVWKAGRKEEATNQTVLIRRGRVPIVSLECVSCKAQAVYEVSRSSYVYLEGRCLNCSSGSKRG 2403
Cdd:TIGR00864 2321 GIPGEELAAGIEYTFKLSIGKAGMKEEATNQTVLIQSGHIPIVSLECVSCKAQALYEVSQNSYVYLEGRCLNCQSGFHRG 2400
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2404 RWAARTFSNKTLVLDETTTSTGSAGMRLVLRRGVLRDGEGYTFTLTVLGHSGEEEGCASIRLSPNRPPLGGSCRLFPLGN 2483
Cdd:TIGR00864 2401 RWAARTFQNDTLVLDESSTSTGSAGMNLVLRQGVLHDGEGYNFTLHVLDDSGDEEGAASIRLHHNMPPDGGECHLFPGGE 2480
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2484 --------------VHALTTKVHFECTGWHDAEDAGAPLVYALLLRRCRQGHCEEFCVYKGSLSSYGAVLPPGFR-PHFE 2548
Cdd:TIGR00864 2481 tgqehgdkedevwaIEALLDKVHFECSGWHDAEDAEAPLLYALLLNRCRDDHCEEFCVYKGSLPEHGAFLPPGFRsAHFE 2560
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2549 VGLAVVVQDQLGAAVVALNRSLAIALPEPSGGTTGLTVWLHGLTASVLPGLLRQADPQHVIEYSLALVTVLNEYEQALDV 2628
Cdd:TIGR00864 2561 VGLAITVEDHLGAAIRALNKSIAITLPDPNGEASGLPHWLHDLIASKLKGLLDQADFQHVIELSLALITVLNEYEQALDS 2640
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2629 AAEPEHERQRRAQIRKNVTQTLVSLRVHTVDDIQQIAAALAQSMGPSRELVCRSCLKQTLHKLEAMMRILQAETTAGTVT 2708
Cdd:TIGR00864 2641 AAEPKHERGHRAQIRKNITEALTALDLHTVDDIQQIAAALAQCMAPSREFICEECLKQTLHKLEAMLEILQADTKAGIVT 2720
                         2730      2740
                   ....*....|....*....|
gi 1622916307 2709 PTAIGDSILNITGDLIHLAS 2728
Cdd:TIGR00864 2721 PTAIADNILNIMGDLIHLAS 2740
REJ pfam02010
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
2171-2614 9.34e-132

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: 422.68  E-value: 9.34e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2171 AHVDLRDCV-TYQTEYRWEVYRTASCqrpGRPTRVALPgVDVSRPQLVLPRLALPVGHYCFVFVVSFGDTP-LARSIQAN 2248
Cdd:pfam02010    1 ASVELNGCFsAYTIDYLWSVFTVSSN---LNLQTISSP-KDLVLPQLTIPSGTLPYGTYVFTLTVSLSSTPsLAGTDIIT 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2249 VTVAPERLVPIIEGGSYRVWSDTQDLVLDGSESYDPNLEDGDQTPLSFHWACVAST------QREAGGCA-----LNFGP 2317
Cdd:pfam02010   77 VTVQPSPLVAVIDGGSSRVVGYNQDLTLDGSESYDPDVDPGSSSGLTYLWSCRRSSsgdnplLNNDPVCFsdqneGTLLQ 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2318 RGSSVVTIPRERLAAGVEYTFSLTVWKAGRKEEATNQTVLIRRGRVPIVSLECVSCKAQAVYEVSRssYVYLEGRCLNCS 2397
Cdd:pfam02010  157 STSSSLTIPASTLQANVTYTFKLTVSKGSRNSASTTQTILVVDGNPPIIILSCISNCNRKNNPVDR--LVLLASTCLNCS 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2398 SGSKRG--RWAARTFSNKTLVLD--ETTTSTGSAGMRLVLRRGVLRDGEGYTFTLTVLGHSGEEEGCASIRLSPNRPPLG 2473
Cdd:pfam02010  235 SDLSDVtyRWLSLGSENTSLVLDqlNSQTSTGRSGPYLVIKAGVLQSGVSYRFTLIVTVYPGLVSGLASISFITNAPPTG 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2474 GSCRLFPLGNvHALTTKVHFECTGWHDAEDagaPLVYALLLRRCRQGHCEEFCVYKGSLS-SYGAVLPPGFRPH-FEVGL 2551
Cdd:pfam02010  315 GTCSVTPTEG-TALETKFTVTCQGWTDDDL---PLTYQFGDISFREASEEWFLLYEGSSQiSISTFLPPGLPANdYQVTV 390
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622916307 2552 AVVVQDQLGAAvVALNRSLAIALPEPSGGttglTVWLHGLTASVLPGLLRQADPQHVIEYSLA 2614
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 ...
3115-3234 1.40e-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: 198.65  E-value: 1.40e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 3115 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLDGD--RAFHRNSLDIFQIATPHSLGSVWKIRVWHDNKGLSPAW 3192
Cdd:cd01752      1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPekPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1622916307 3193 FLQHVIVRDLQTARSAFFLVNDWLSVETEanGGLVEKEVLVA 3234
Cdd:cd01752     81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEG--DGTVERTFPVA 120
Polycystin_dom pfam20519
Polycystin domain; This domain represents the polycystin domain from group II of Transient ...
3710-3894 7.02e-56

Polycystin domain; This domain represents the polycystin domain from group II of Transient receptor potential (TRP) channels (TRPP) including PKD1, PKD2, PKD2L and mucolipins. The polycystin domain display a sandwich-like shape with five beta-sheets in the tilted middle layer, three alpha-helices on one side and a large loop with two short antiparallel beta-sheets on the other.


Pssm-ID: 466668  Cd Length: 199  Bit Score: 194.18  E-value: 7.02e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 3710 FLAITRSEELWPWMAHVLLPYVHGNQS------------SPELGPPRLRQVRLQEALC--PDPPGPRVHTCSAAGGFSTS 3775
Cdd:pfam20519    2 LLTVTDLDDIWDWLSSVLLPALHSNKTpsglpgsfiayeSLLLGVPRLRQLRVRNSSClvHDKFVREINECHAGYSPPSE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 3776 DY----DVGWESPHNGSGTW-AYSAPDLL-GAWSWGSCAVYDSGGYVQELGLSLEESRDRLRFLQLHNWLDnsdphplRR 3849
Cdd:pfam20519   82 DRklysALPYKPVHYGSKYWfIYTPPGLLmGYDHWGHLASYPSGGYVVLLPSSREESLKRLAYLQDNNWLD-------RG 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1622916307 3850 SRAVFVELTRYSPAVGLHAAVTLRLEFPAAGRALAALSVRPFALR 3894
Cdd:pfam20519  155 TRAVFVDFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVKLL 199
PKD_channel pfam08016
Polycystin cation channel; This family contains the cation channel region from group II of ...
3895-4116 6.49e-44

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


Pssm-ID: 462341 [Multi-domain]  Cd Length: 225  Bit Score: 160.91  E-value: 6.49e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 3895 RLSAGLSLPLLT-SVCLLLFALHFAVAEARTWHREGCwHVLRpRAW--ARWLLVVLTAATALVRLAQLGAADRQWTrFVR 3971
Cdd:pfam08016    1 RYVTNRSLFILLcEIVFVVFFLYFVVEEILKIRKHRP-SYLR-SVWnlLDLAIVILSVVLIVLNIYRDFLADRLIK-SVE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 3972 GRPRRFTSFDQVAQLSSAARGLAASLLFLLLVKAAQQLRFVRQWSVFGKTLFRALPELLGATLGLVVLGVAYAQLAVLLV 4051
Cdd:pfam08016   78 ASPVTFIDFDRVAQLDNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFGYLLF 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622916307 4052 SSCVDSLWSVAQALLVLCsgtglSTLCPAESWH--------LSPLLCVGLWALRLWGALRLGAVILRWRYHAL 4116
Cdd:pfam08016  158 GTQAPNFSNFVKSILTLF-----RTILGDFGYNeifsgnrvLGPLLFLTFVFLVIFILLNLFLAIINDSYVEV 225
WSC smart00321
present in yeast cell wall integrity and stress response component proteins; Domain present in ...
179-273 1.78e-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: 1.78e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307   179 GEEYIACLPDNSSGTVAAVAFSAAHegLLQPEACSAFCFSTGRGLAALSEQGWCLCGAAQPSSA-----SFACLSFCSGp 253
Cdd:smart00321    1 GATYVGCYSDNSSRTLAAVSSYAYH--NMSVEACSNFCFSAGYALAALENGNECYCGDSLPSTSvsasdSSQCSTTCSG- 77
                            90       100
                    ....*....|....*....|
gi 1622916307   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. ...
3117-3220 4.14e-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: 4.14e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 3117 YEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLDGDR-AFHRNSLDIFQIATPHSLGSVWKIRVWHDNKGLSPAWFLQ 3195
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNpDFERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEWFLK 80
                           90       100
                   ....*....|....*....|....*.
gi 1622916307 3196 HVIV-RDLQTARSAFFLVNDWLSVET 3220
Cdd:pfam01477   81 SITVeVPGETGGKYTFPCNSWVYGSK 106
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
3115-3217 4.65e-19

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 85.00  E-value: 4.65e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  3115 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLD--GDRAFHRNSLDIFQIATPHSLGSVWKIRVWHDNKglSPAW 3192
Cdd:smart00308    1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDylFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR--HPEW 78
                            90       100
                    ....*....|....*....|....*
gi 1622916307  3193 FLQHVIVRDLQTARSAFFLVNDWLS 3217
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 4.70e-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: 4.70e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  420 HCYRLVVEKAAWLQAQEQCRAWaGAALAMVDSPAVQRFLVSRVTRSL--DVWIGFSTVQGPETGLAPQGEAFSleSCQNW 497
Cdd:cd00037      1 SCYKFSTEKLTWEEAQEYCRSL-GGHLASIHSEEENDFLASLLKKSSssDVWIGLNDLSSEGTWKWSDGSPLV--DYTNW 77
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1622916307  498 LPGEPHPATAEHCVRL--GPTGWCNTDLCSAPHSYVCE 533
Cdd:cd00037     78 APGEPNPGGSEDCVVLssSSDGKWNDVSCSSKLPFICE 115
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
1487-1804 1.10e-10

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


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 66.62  E-value: 1.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1487 FSAVGRGRPASYLWDLGDGGRLEGPEVTHAYNSIGDFTVRVAGWNDV-SRSEAWLNVTVKRRVRGLVVNASRTVVPLNGS 1565
Cdd:COG3291     16 FTDTSSGNATSYEWDFGDGTTSTEANPSHTYTTPGTYTVTLTVTDAAgCSDTTTKTITVGAPNPGVTTVTTSTTVTTLAN 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1566 VSFSTSLEAGSDVrYSWVLCDRCTPIPGGPTISYTFRSVGTFSIIVTAENEVGSAQDSIFVYVLQLIEGLQVAGCGSYFP 1645
Cdd:COG3291     96 TANGGATTVVAGS-TVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTTSAST 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1646 TNHTAQLQAVVRDGTNVSYSWTAWWDRGPALAGSGKGFSLTALEAGTYHVQLRATNMLGSAWADCTVDFVEPVGWLMVTA 1725
Cdd:COG3291    175 NPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNTVTTS 254
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916307 1726 SPNPAAVNTSVTLSAKLAGGSGVLYTWSLEEGLSWETPEPFTTHSFPTPGLHLVTVTAGNPLGSASATVEVGVQVPVSG 1804
Cdd:COG3291    255 GANTAGTSTITGGTSGVVTTSAATGTSTNGTGGLGTTTAITPGNVSTTADVTGGTATLAVSSTLTTNDTTGSSSTGTVF 333
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
3008-3057 6.64e-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: 6.64e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1622916307  3008 YTSLCQYFSEENMVWRTEGLLPLEETSPHqAVCLTRHLTAFGASLFVPPS 3057
Cdd:smart00303    1 FNPICVFWDESSGEWSTRGCELLETNGTH-TTCSCNHLTTFAVLMDVPPI 49
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
56-129 2.63e-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: 2.63e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916307   56 RGLRTLGPALRIpadataLDVSHNLLRALDVglLANLSQLSELDISNNKISTLEE--GIFANLFNLSEINLSGNPF 129
Cdd:cd21340    113 RSLAALSNSLRV------LNISGNNIDSLEP--LAPLRNLEQLDASNNQISDLEEllDLLSSWPSLRELDLTGNPV 180
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
50-130 1.10e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 60.72  E-value: 1.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307   50 RVNCSGRGLRTLGPALripADATAL---DVSHNLLRALDVGLlANLSQLSELDISNNKISTLEEGIfANLFNLSEINLSG 126
Cdd:COG4886    140 ELDLSNNQLTDLPEPL---GNLTNLkslDLSNNQLTDLPEEL-GNLTNLKELDLSNNQITDLPEPL-GNLTNLEELDLSG 214

                   ....
gi 1622916307  127 NPFE 130
Cdd:COG4886    215 NQLT 218
LRRNT smart00013
Leucine rich repeat N-terminal domain;
34-73 9.68e-04

Leucine rich repeat N-terminal domain;


Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 39.22  E-value: 9.68e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1622916307    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) ...
99-2728 0e+00

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 4618.93  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307   99 DISNNKISTLEEGIFANLFNLSEINLSGNPFECDCGLVWLPRWAEEQQVRVVQPEAATCAGPGSLAGQPLLGIPLLDSDC 178
Cdd:TIGR00864    1 DISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPEAALCAGPGALAGQPLLGIPLLDSGC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  179 GEEYIACLPDNSSGTVAAVA----FSAAHEGLLQPEACSAFCFSTGRGLAALSEQGWCLCGAAQPSSASFACLSFCSGPP 254
Cdd:TIGR00864   81 DEEYVACLKDNSSGGGAARSelviFSAAHEGLFQPEACNAFCFSAGHGLAALGEQGECLCGAAQPSEANFACESLCSGPP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  255 PPPALDCGGPTLLQHVFPASPGAALVGPHGPLASGQLAAFHIAAPLPVTATRWDFGDGSPEVDAAGP----AASHRYVLP 330
Cdd:TIGR00864  161 PPPAAACRGPQLLEHIFPALPGAPIQGPHGPIASGQLAAFHAAAPLAPTAMRWDFGDGSAEVDAAGAggttAASHKYGHP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  331 GRYHVTAVVALGVSSALLGTNVQVEAAPAALELVCPSSVQSDESLKLSIQNRGGSGLEAAYSIVALGEELARVVHPLCPS 410
Cdd:TIGR00864  241 GRYHVSAMGALGAGKALAGGDVQVEAAPAALELHCPSLVQADESLDLSIQNRGGSDLDAAWKITAHGEEPAKASHPHCPK 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  411 DTEIFPGNGHCYRLVVEKAAWLQAQEQCRAWAGAALAMVDSPAVQRFLVSRVTRSLD--VWIGFSTVQGPETGLAPQGEA 488
Cdd:TIGR00864  321 DGEIFEENGHCFQIVPEEAAWLDAQEQCLARAGAALAIVDNDALQNFLARKVTHSLDrgVWIGFSDVNGAEKGPAHQGEA 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  489 FSLESCQNWLPGEPHPATAEHCVRLGPTGWCNTDLCSAPHSYVCELRPGGPVQDAENLLVGAPSGDLQGPLTPLTPQDGL 568
Cdd:TIGR00864  401 FEAEECEEGLAGEPHPARAEHCVRLDPRGQCNSDLCNAPHAYVCELNPGGPVPDAENFAMGAASFDLHGLLQALAAMDGL 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  569 SAP-HEPVEVMVFPGLSLSHEAFLTTAEFGTQELRRPAQLRLQVYRL---LSTAGTPENGSEPESRSPDNRTQLVPECMP 644
Cdd:TIGR00864  481 PAPpHEGVEVLLFPALRFSRAAFLSSAEFGTQELRRPAHILFQIYRLrcrLPGAGGPACGPEAECRPPDNRSADAPACMK 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  645 GGRWCPAANVCVPLDASCHPQA--NGCTSGPGLPGA----LYALWREFLFSVPAGPPAQYSVTLHGQDVLMLPGDLVGLQ 718
Cdd:TIGR00864  561 GEQWCPFAHICLPLDAPCHPQAcaNGCSQGHGLPGAarmpLYALQREFLFSLPAGPAAHVLLQDHGEDLLMLPGDLIALQ 640
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  719 HDAGPGALLHCSPAPGHPGPQALYLSANASAWLPH------------------------LPAQLEGTR----DCPACALR 770
Cdd:TIGR00864  641 HDAGPAALIHCQPAPGHPGPRAPVFAANASEWFGHnntpvppdnlagdgadplpdpeldLKALLEGTRaswlECAACAIR 720
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  771 LLAATEQLTVLLGLRPNPGLRLPGRYEVRAEVGNGVSRHNLSCSFNVVSPVAGLRVIYPAPHNGHLYVPTNGSALVLQVD 850
Cdd:TIGR00864  721 LLAAGEQETRLLGAELNAGLPLPGLYELLAESAKGSDLHNASCSFDVLPPLAGLRVIHPAPQDGRLFLESNGSALLLQVD 800
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  851 SGANATATARWPGGNVSTRFEAACPALVA-------TLLPGCPWETNDTQFSVVALPWLSEGEHV----VEVVAENSASQ 919
Cdd:TIGR00864  801 SGANAEAKAFWPGGNSSARFENVCPAEFAsrlchpsTFEGGCAEEAEDSLFAVLALNWLKEGEHTgpvqVDLMAENNASE 880
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  920 ANLSLRVTAEEPICGLRATPSPEARVLQGVLVRYSPVVEAGSDVVFRWTINDKQSLTFQNVVFNVIYQSAAVFKLSLTAS 999
Cdd:TIGR00864  881 ANLSLLVQAEEPICGLRAQPHPAARVLMESLVRYSASVEAGSDMTFKWTIDDKPFFTFQNTVFNVIYQHAAVFKLSLTAM 960
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1000 NHVSNVTVNYNVTVERMNRMQGLWVSTVPAVLPPNATLALTAGVLVDSAVEVAFLWTFGDGEQALRQFHPPYNESFPVPD 1079
Cdd:TIGR00864  961 NHVSNLTEDFNVTVDRLNPMQGLQVKGVPAVLPPGATLALTAGVLIDMAVEAAFLWSFGDGEQALFEFKPPYNESFPCPD 1040
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1080 PSVAQVLVEHNVTHTYAAPGEYILTVLTSNAFENLTQQVPVSVRAALPSMAVGVSDSVLVAGRPITFYPHPLPSPGGVLY 1159
Cdd:TIGR00864 1041 PSPAQVLLEHNVMHIYAAPGEYLATVLASNAFENISQQINMSVRAILPRVAIGTEDGLLLAGKPADFEAHPLPSPGGIHY 1120
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1160 TWDFGDSSPVLTQSQPTANHTYASRGTYRVHLEVNNTVSSALAQADVRVFEELRGLSVNMSLAVEQGAPVVVSAAVQTGD 1239
Cdd:TIGR00864 1121 EWDFGDGSALLQGRQPAAAHTFAKRGPFHVCLEVNNTISGAAACADMFAFEEIEGLSADMSLATELGAATTVRAALQSGD 1200
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1240 DITWTFDMGDGTVLSGPEDTVEHVYLRAQNCTVTVGAASPAGRLAQSLHVLVFVLEVLRIEPAACIPTQPDARLTAYVTG 1319
Cdd:TIGR00864 1201 NITWTFDMGDGKSLSGPEATVEHKYAKAGNCTVNIGAANAAGHGARIIHVEVFVFEVAGIEPAACIGEHADANFRARVSG 1280
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1320 NPAHYLFDWTFGDGSSNTTVRGRPTVTHNFTRSGTFPLALVLSSPVNKAHYFTSICVEPEVGNVTLQPERQFVQLGDEVR 1399
Cdd:TIGR00864 1281 NAAHYLFDWSFGDGSPNETHHGCPGISHNFRGNGTFPLALTISSGVNKAHFFTQICVEPELGKISLQAEKQFFALGDEAQ 1360
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1400 LVACVWPPFPYRYAWDFGTEEAAPARAGGPEVTFTYRDPGSYLVTVTASNNVSAANDSALVEVQEPVVVTDIKVNSSL-- 1477
Cdd:TIGR00864 1361 FQACAEPEFNYRYEWDFGGEEAAPLPAAGAEVTFIYNDPGCYLVTVAASNNISAANDSALIEVLEPVGATSFKHNGSHgn 1440
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1478 VLELQQPYLFSAVGRGRPASYLWDLGDGGRLEGPEVTHAYNSIGDFTVRVAGWNDVSRSEAWLNVTVKRRVRGLVVNASR 1557
Cdd:TIGR00864 1441 NLELGQPYLFSAFGRARNASYLWDFGDGGLLEGPEILHAFNSPGDFNIRLAAANEVGKNEATLNVAVKARVRGLTINASL 1520
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1558 TVVPLNGSVSFSTSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFSIIVTAENEVGSAQDSIFVYVLQLIEGLQV 1637
Cdd:TIGR00864 1521 TNVPLNGSVHFEAHLDAGDDVRFSWILCDHCTPIFGGNTIFYTFRSVGTFNIIVTAENDVGAAQASIFLFVLQEIEGLQI 1600
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1638 AG-------------CGSYFPTNHTAQLQAVVRDGTNVSYSWTAWWD---RGPALAGSGKGFSLTALEAGTYHVQLRATN 1701
Cdd:TIGR00864 1601 LGetaegggggvqelDGCYFETNHTVQFHAGFKDGTNLSFSWNAILDnepDGPAFAGSGKGAKLNPLEAGPCDIFLQAAN 1680
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1702 MLGSAWADCTVDFVEPVGWLMVTASPNPAAVNTSVTLSAKLAGGSGVLYTWSLEEGLSWETPEPFTTHSFPTPGLHLVTV 1781
Cdd:TIGR00864 1681 LLGQATADCTIDFLEPAGNLMLAASDNPAAVNALINLSAELAEGSGLQYRWFLEEGDDLETSEPFMSHSFPSAGLHLVTM 1760
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1782 TAGNPLGSASATVEVGVQVPVSGLSIRASESGGS-FVAAGSSVPFWGQLATGTNVSWCWAVPGGSSKRGPHVTMVFPDAG 1860
Cdd:TIGR00864 1761 KAFNELGSANASEEVDVQEPISGLKIRAADAGEQnFFAADSSVCFQGELATGTNVSWCWAIDGGSSKMGKHACMTFPDAG 1840
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1861 TFSVQLNASNAVSWVSATHNLTVEEPIVGLVLWASSKVVAPGQLVHFQILLAAGSAVTFRLQVGGASPAVL-PGPRFSHS 1939
Cdd:TIGR00864 1841 TFAIRLNASNAVSGKSASREFFAEEPIFGLELKASKKIAAIGEKVEFQILLAAGSAVNFRLQIGGAAPEVLqPGPRFSHS 1920
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1940 FPRVGDHVVSVQGENHVSWAQAQVRIVVLEAVSGLQVPNCCEPGIATGTERNFTARVQRGSRVAYAWYFSLQKVQGDSLV 2019
Cdd:TIGR00864 1921 FPRVDDHMVNLRAKNEVSCAQANLHIEVLEAVRGLQIPDCCAAGIATGEEKNFTANVQRGKPVAFAWTFDLHHLHGDSLV 2000
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2020 ILSGRDVTYTPVAAGLLEIQVRAFNALGSENRTLVLEVQDAVQYVALRSGP--CFTNRSAWFEAATSPSPRRVAYHWDFG 2097
Cdd:TIGR00864 2001 IHMGKDVSYTAEAAGLLEIQLGAFNALGAENITLQLEAQDALMDAALQAGPqdCFTNKMAQFEAATSPKPNFMACHWDFG 2080
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2098 DGAPGQDTDEPRAEHCYLRPGDYRVQVNASNLVSFFVAQATVTVQVLACREPEVDVVLPLQVLMRRSQRNYLEAHVDLRD 2177
Cdd:TIGR00864 2081 DGSAGQDTDEPRAEHEYLHPGDYRVQVNASNLVSFFSAHAEINVQVLACEEPEVDVVLALQLAIRRSQPNLLEAHVDLKD 2160
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2178 CVTYQTEYRWEVYRTASCQRPGRPTRVALPG-------------VDVSRPQLVLPRLALPVGHYCFVFVVSFGDTPLARS 2244
Cdd:TIGR00864 2161 CLRYGAEYLWEILRAASCDNDGHFARGALNGatrsfpviplpaeVDVQRLQLSLPKLALAAGHYCFVFSLSFEDTPLKKA 2240
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2245 IQANVTVAPERLVPIIEGGSYRVWSDTQDLVLDGSESYDPNLEDGDQTPLSFHWACVASTQREAGGCALNFGPRG-SSVV 2323
Cdd:TIGR00864 2241 ACANLGVAAARLMPIIEGGSYRVWSDTQDLQLDAEESYDPNLDDDDQSLLHFHWACQASSKGEAGCCALNFGLGGkGPTL 2320
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2324 TIPRERLAAGVEYTFSLTVWKAGRKEEATNQTVLIRRGRVPIVSLECVSCKAQAVYEVSRSSYVYLEGRCLNCSSGSKRG 2403
Cdd:TIGR00864 2321 GIPGEELAAGIEYTFKLSIGKAGMKEEATNQTVLIQSGHIPIVSLECVSCKAQALYEVSQNSYVYLEGRCLNCQSGFHRG 2400
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2404 RWAARTFSNKTLVLDETTTSTGSAGMRLVLRRGVLRDGEGYTFTLTVLGHSGEEEGCASIRLSPNRPPLGGSCRLFPLGN 2483
Cdd:TIGR00864 2401 RWAARTFQNDTLVLDESSTSTGSAGMNLVLRQGVLHDGEGYNFTLHVLDDSGDEEGAASIRLHHNMPPDGGECHLFPGGE 2480
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2484 --------------VHALTTKVHFECTGWHDAEDAGAPLVYALLLRRCRQGHCEEFCVYKGSLSSYGAVLPPGFR-PHFE 2548
Cdd:TIGR00864 2481 tgqehgdkedevwaIEALLDKVHFECSGWHDAEDAEAPLLYALLLNRCRDDHCEEFCVYKGSLPEHGAFLPPGFRsAHFE 2560
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2549 VGLAVVVQDQLGAAVVALNRSLAIALPEPSGGTTGLTVWLHGLTASVLPGLLRQADPQHVIEYSLALVTVLNEYEQALDV 2628
Cdd:TIGR00864 2561 VGLAITVEDHLGAAIRALNKSIAITLPDPNGEASGLPHWLHDLIASKLKGLLDQADFQHVIELSLALITVLNEYEQALDS 2640
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2629 AAEPEHERQRRAQIRKNVTQTLVSLRVHTVDDIQQIAAALAQSMGPSRELVCRSCLKQTLHKLEAMMRILQAETTAGTVT 2708
Cdd:TIGR00864 2641 AAEPKHERGHRAQIRKNITEALTALDLHTVDDIQQIAAALAQCMAPSREFICEECLKQTLHKLEAMLEILQADTKAGIVT 2720
                         2730      2740
                   ....*....|....*....|
gi 1622916307 2709 PTAIGDSILNITGDLIHLAS 2728
Cdd:TIGR00864 2721 PTAIADNILNIMGDLIHLAS 2740
REJ pfam02010
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
2171-2614 9.34e-132

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: 422.68  E-value: 9.34e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2171 AHVDLRDCV-TYQTEYRWEVYRTASCqrpGRPTRVALPgVDVSRPQLVLPRLALPVGHYCFVFVVSFGDTP-LARSIQAN 2248
Cdd:pfam02010    1 ASVELNGCFsAYTIDYLWSVFTVSSN---LNLQTISSP-KDLVLPQLTIPSGTLPYGTYVFTLTVSLSSTPsLAGTDIIT 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2249 VTVAPERLVPIIEGGSYRVWSDTQDLVLDGSESYDPNLEDGDQTPLSFHWACVAST------QREAGGCA-----LNFGP 2317
Cdd:pfam02010   77 VTVQPSPLVAVIDGGSSRVVGYNQDLTLDGSESYDPDVDPGSSSGLTYLWSCRRSSsgdnplLNNDPVCFsdqneGTLLQ 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2318 RGSSVVTIPRERLAAGVEYTFSLTVWKAGRKEEATNQTVLIRRGRVPIVSLECVSCKAQAVYEVSRssYVYLEGRCLNCS 2397
Cdd:pfam02010  157 STSSSLTIPASTLQANVTYTFKLTVSKGSRNSASTTQTILVVDGNPPIIILSCISNCNRKNNPVDR--LVLLASTCLNCS 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2398 SGSKRG--RWAARTFSNKTLVLD--ETTTSTGSAGMRLVLRRGVLRDGEGYTFTLTVLGHSGEEEGCASIRLSPNRPPLG 2473
Cdd:pfam02010  235 SDLSDVtyRWLSLGSENTSLVLDqlNSQTSTGRSGPYLVIKAGVLQSGVSYRFTLIVTVYPGLVSGLASISFITNAPPTG 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 2474 GSCRLFPLGNvHALTTKVHFECTGWHDAEDagaPLVYALLLRRCRQGHCEEFCVYKGSLS-SYGAVLPPGFRPH-FEVGL 2551
Cdd:pfam02010  315 GTCSVTPTEG-TALETKFTVTCQGWTDDDL---PLTYQFGDISFREASEEWFLLYEGSSQiSISTFLPPGLPANdYQVTV 390
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622916307 2552 AVVVQDQLGAAvVALNRSLAIALPEPSGGttglTVWLHGLTASVLPGLLRQADPQHVIEYSLA 2614
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 ...
3115-3234 1.40e-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: 198.65  E-value: 1.40e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 3115 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLDGD--RAFHRNSLDIFQIATPHSLGSVWKIRVWHDNKGLSPAW 3192
Cdd:cd01752      1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPekPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1622916307 3193 FLQHVIVRDLQTARSAFFLVNDWLSVETEanGGLVEKEVLVA 3234
Cdd:cd01752     81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEG--DGTVERTFPVA 120
Polycystin_dom pfam20519
Polycystin domain; This domain represents the polycystin domain from group II of Transient ...
3710-3894 7.02e-56

Polycystin domain; This domain represents the polycystin domain from group II of Transient receptor potential (TRP) channels (TRPP) including PKD1, PKD2, PKD2L and mucolipins. The polycystin domain display a sandwich-like shape with five beta-sheets in the tilted middle layer, three alpha-helices on one side and a large loop with two short antiparallel beta-sheets on the other.


Pssm-ID: 466668  Cd Length: 199  Bit Score: 194.18  E-value: 7.02e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 3710 FLAITRSEELWPWMAHVLLPYVHGNQS------------SPELGPPRLRQVRLQEALC--PDPPGPRVHTCSAAGGFSTS 3775
Cdd:pfam20519    2 LLTVTDLDDIWDWLSSVLLPALHSNKTpsglpgsfiayeSLLLGVPRLRQLRVRNSSClvHDKFVREINECHAGYSPPSE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 3776 DY----DVGWESPHNGSGTW-AYSAPDLL-GAWSWGSCAVYDSGGYVQELGLSLEESRDRLRFLQLHNWLDnsdphplRR 3849
Cdd:pfam20519   82 DRklysALPYKPVHYGSKYWfIYTPPGLLmGYDHWGHLASYPSGGYVVLLPSSREESLKRLAYLQDNNWLD-------RG 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1622916307 3850 SRAVFVELTRYSPAVGLHAAVTLRLEFPAAGRALAALSVRPFALR 3894
Cdd:pfam20519  155 TRAVFVDFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVKLL 199
PKD_channel pfam08016
Polycystin cation channel; This family contains the cation channel region from group II of ...
3895-4116 6.49e-44

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


Pssm-ID: 462341 [Multi-domain]  Cd Length: 225  Bit Score: 160.91  E-value: 6.49e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 3895 RLSAGLSLPLLT-SVCLLLFALHFAVAEARTWHREGCwHVLRpRAW--ARWLLVVLTAATALVRLAQLGAADRQWTrFVR 3971
Cdd:pfam08016    1 RYVTNRSLFILLcEIVFVVFFLYFVVEEILKIRKHRP-SYLR-SVWnlLDLAIVILSVVLIVLNIYRDFLADRLIK-SVE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 3972 GRPRRFTSFDQVAQLSSAARGLAASLLFLLLVKAAQQLRFVRQWSVFGKTLFRALPELLGATLGLVVLGVAYAQLAVLLV 4051
Cdd:pfam08016   78 ASPVTFIDFDRVAQLDNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFGYLLF 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622916307 4052 SSCVDSLWSVAQALLVLCsgtglSTLCPAESWH--------LSPLLCVGLWALRLWGALRLGAVILRWRYHAL 4116
Cdd:pfam08016  158 GTQAPNFSNFVKSILTLF-----RTILGDFGYNeifsgnrvLGPLLFLTFVFLVIFILLNLFLAIINDSYVEV 225
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
3115-3234 5.15e-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: 5.15e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 3115 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLD---GDRAFHRNSLDIFQIATPhSLGSVWKIRVWHDNKGLSPA 3191
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKksnNKNKFERGQTDKFTVEAV-DLGKLKKIRIGHDNSGLGAG 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1622916307 3192 WFLQHVIVRDLQTARSAFFLVNDWLSveTEANGGLVEKEVLVA 3234
Cdd:cd01756     80 WFLDKVEIREPGTGDEYTFPCNRWLD--KDEDDGQIVRELYPS 120
WSC smart00321
present in yeast cell wall integrity and stress response component proteins; Domain present in ...
179-273 1.78e-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: 1.78e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307   179 GEEYIACLPDNSSGTVAAVAFSAAHegLLQPEACSAFCFSTGRGLAALSEQGWCLCGAAQPSSA-----SFACLSFCSGp 253
Cdd:smart00321    1 GATYVGCYSDNSSRTLAAVSSYAYH--NMSVEACSNFCFSAGYALAALENGNECYCGDSLPSTSvsasdSSQCSTTCSG- 77
                            90       100
                    ....*....|....*....|
gi 1622916307   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. ...
3117-3220 4.14e-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: 4.14e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 3117 YEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLDGDR-AFHRNSLDIFQIATPHSLGSVWKIRVWHDNKGLSPAWFLQ 3195
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNpDFERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEWFLK 80
                           90       100
                   ....*....|....*....|....*.
gi 1622916307 3196 HVIV-RDLQTARSAFFLVNDWLSVET 3220
Cdd:pfam01477   81 SITVeVPGETGGKYTFPCNSWVYGSK 106
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
3115-3217 4.65e-19

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 85.00  E-value: 4.65e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  3115 FKYEILVKTGWGRGSGTTAHVGIMLYGVDSRSGHRHLD--GDRAFHRNSLDIFQIATPHSLGSVWKIRVWHDNKglSPAW 3192
Cdd:smart00308    1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDylFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR--HPEW 78
                            90       100
                    ....*....|....*....|....*
gi 1622916307  3193 FLQHVIVRDLQTARSAFFLVNDWLS 3217
Cdd:smart00308   79 FLKSITVKDLPTGGKYHFPCNSWVY 103
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
408-533 7.90e-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: 7.90e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307   408 CPSDTEIFpgNGHCYRLVVEKAAWLQAQEQCRAwAGAALAMVDSPAVQRFL---VSRVTRSLDVWIGFSTVQGPETGLAP 484
Cdd:smart00034    1 CPSGWISY--GGKCYKFSTEKKTWEDAQAFCQS-LGGHLASIHSEAENDFVaslLKNSGSSDYYWIGLSDPDSNGSWQWS 77
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 1622916307   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 4.70e-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: 4.70e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  420 HCYRLVVEKAAWLQAQEQCRAWaGAALAMVDSPAVQRFLVSRVTRSL--DVWIGFSTVQGPETGLAPQGEAFSleSCQNW 497
Cdd:cd00037      1 SCYKFSTEKLTWEEAQEYCRSL-GGHLASIHSEEENDFLASLLKKSSssDVWIGLNDLSSEGTWKWSDGSPLV--DYTNW 77
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1622916307  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. ...
1723-1792 6.57e-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: 6.57e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1723 VTASPNPAAVNTSVTLSAKLAGGSGVLYTWSLEEGLSWETPEPFTTHSFPTPGLHLVTVTAGNPLGSASA 1792
Cdd:pfam00801    1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
3116-3217 8.58e-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: 8.58e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 3116 KYEILVKTGWGRGSGTTAHVGIMLYGVD-SRSGHRHLDGDRAFHRNSLDIFQIATPHSLGSVWKIRVWHDNKGLSPAWFL 3194
Cdd:cd00113      2 RYTVTIKTGDKKGAGTDSNISLALYGENgNSSDIPILDGPGSFERGSTDTFQIDLKLDIGDITKVYLRRDGSGLSDGWYC 81
                           90       100
                   ....*....|....*....|...
gi 1622916307 3195 QHVIVRDLQTARSAFFLVNDWLS 3217
Cdd:cd00113     82 ESITVQALGTKKVYTFPVNRWVL 104
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1131-1209 3.21e-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: 3.21e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916307  1131 VGVSDSVLVAGRPITFYPHPLPSPGGVLYTWDFGDSSpvlTQSQPTANHTYASRGTYRVHLEVNNTVSSALAQADVRVF 1209
Cdd:smart00089    4 VSASPTVGVAGESVTFTATSSDDGSIVSYTWDFGDGT---SSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1553-1622 5.04e-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: 5.04e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1553 VNASRTVVPLNGSVSFSTSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFSIIVTAENEVGSAQD 1622
Cdd:pfam00801    1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1892-1961 6.89e-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: 6.89e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1892 LWASSKVVAPGQLVHFQILLAAGSAVTFRLQVGGASPAVLPGPRFSHSFPRVGDHVVSVQGENHVSWAQA 1961
Cdd:pfam00801    1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1385-1456 8.53e-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: 8.53e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622916307 1385 LQPERQFVQLGDEVRLVACVWPPFPYRYAWDFGteEAAPARAGGPEVTFTYRDPGSYLVTVTASNNVSAAND 1456
Cdd:pfam00801    1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFG--DSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1637-1708 1.22e-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: 1.22e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622916307 1637 VAGCGSYFPTNHTAQLQAVVRDGTNVSYSWTAWwdRGPALAGSGKGFSLTALEAGTYHVQLRATNMLGSAWA 1708
Cdd:pfam00801    1 VSASGTVVAAGQPVTFTATLADGSNVTYTWDFG--DSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1813-1877 4.98e-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: 4.98e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622916307 1813 GGSFVAAGSSVPFWGQLATGTNVSWCWAVPG--GSSKRGPHVTMVFPDAGTFSVQLNASNAVSWVSA 1877
Cdd:pfam00801    4 SGTVVAAGQPVTFTATLADGSNVTYTWDFGDspGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1131-1202 5.13e-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: 5.13e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622916307 1131 VGVSDSVLVAGRPITFYPHpLPSPGGVLYTWDFGDSsPVLTQSQPTANHTYASRGTYRVHLEVNNTVSSALA 1202
Cdd:pfam00801    1 VSASGTVVAAGQPVTFTAT-LADGSNVTYTWDFGDS-PGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
2068-2135 7.96e-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: 7.96e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622916307 2068 SGPCFTNRSAWFEAaTSPSPRRVAYHWDFGDGaPGQDTDEPRAEHCYLRPGDYRVQVNASNLVSFFVA 2135
Cdd:pfam00801    5 GTVVAAGQPVTFTA-TLADGSNVTYTWDFGDS-PGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1220-1285 4.30e-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: 4.30e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916307 1220 SLAVEQGAPVVVSAAVQTGDDITWTFDMGDGTVLSGPEDTVEHVYLRAQNCTVTVGAASPAGRLAQ 1285
Cdd:pfam00801    5 GTVVAAGQPVTFTATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1723-1799 1.19e-13

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 69.02  E-value: 1.19e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622916307  1723 VTASPNPAAVNTSVTLSAKLAG-GSGVLYTWSLEEGLSWEtpEPFTTHSFPTPGLHLVTVTAGNPLGSASATVEVGVQ 1799
Cdd:smart00089    4 VSASPTVGVAGESVTFTATSSDdGSIVSYTWDFGDGTSST--GPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1819-1884 1.36e-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: 1.36e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622916307  1819 AGSSVPFWGQLAT-GTNVSWCWAVPGGSSKRGPHVTMVFPDAGTFSVQLNASNAVSWVSATHNLTVE 1884
Cdd:smart00089   13 AGESVTFTATSSDdGSIVSYTWDFGDGTSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
2060-2142 2.25e-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: 2.25e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  2060 AVQYVALRSGPcfTNRSAWFEAATSPSPRRVAYHWDFGDGapgQDTDEPRAEHCYLRPGDYRVQVNASNLVSFFVAQATV 2139
Cdd:smart00089    2 ADVSASPTVGV--AGESVTFTATSSDDGSIVSYTWDFGDG---TSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTV 76

                    ...
gi 1622916307  2140 TVQ 2142
Cdd:smart00089   77 VVQ 79
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1550-1628 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 1622916307  1550 GLVVNASRTVVPLNGSVSFS-TSLEAGSDVRYSWVLCDRctPIPGGPTISYTFRSVGTFSIIVTAENEVGSAQDSIFVYV 1628
Cdd:smart00089    1 VADVSASPTVGVAGESVTFTaTSSDDGSIVSYTWDFGDG--TSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVV 78
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1468-1545 3.46e-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: 3.46e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  1468 VTDIKVNSSlVLELQQPYLFSAV--GRGRPASYLWDLGDGGRLEGPEVTHAYNSIGDFTVRVAGWNDVSRSEAWLNVTVK 1545
Cdd:smart00089    1 VADVSASPT-VGVAGESVTFTATssDDGSIVSYTWDFGDGTSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1136-1203 8.45e-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: 8.45e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622916307 1136 SVLVAGRPITFYPHPLPSPGGVLYTWDFGDSSpVLTQSQPTANHTYASRGTYRVHLEVNNTVSSALAQ 1203
Cdd:cd00146      9 PVAELGASVTFSASDSSGGSIVSYKWDFGDGE-VSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTK 75
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1473-1538 5.04e-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: 5.04e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916307 1473 VNSSLVLELQQPYLFSA-VGRGRPASYLWDLGD--GGRLEGPEVTHAYNSIGDFTVRVAGWNDVSRSEA 1538
Cdd:pfam00801    2 SASGTVVAAGQPVTFTAtLADGSNVTYTWDFGDspGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
LRR_8 pfam13855
Leucine rich repeat;
72-129 1.30e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 62.54  E-value: 1.30e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622916307   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 1.40e-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: 1.40e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916307  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. ...
1980-2051 2.36e-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: 2.36e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622916307 1980 CEPGIATGTERNFTARVQRGSRVAYAWYFslqkvqGDSLV-ILSGRDVTYTPVAAGLLEIQVRAFNALGSENR 2051
Cdd:pfam00801    4 SGTVVAAGQPVTFTATLADGSNVTYTWDF------GDSPGtSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
WSC pfam01822
WSC domain; This domain is involved in carbohydrate binding.
182-263 2.82e-11

WSC domain; This domain is involved in carbohydrate binding.


Pssm-ID: 460348  Cd Length: 82  Bit Score: 62.09  E-value: 2.82e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  182 YIACLPDNSsGTVAAVAFSAAHEGLLQPEACSAFCFSTGRGLAALSEQGWCLCGAAQPSSASFA----CLSFCSGPPPPP 257
Cdd:pfam01822    1 YLGCYSDGT-GGRRLLLGSSGDYDDMTPEKCIAFCSAAGYTYAGLEYGGECYCGNSLPSGSALAdssdCNTPCPGDSSQT 79

                   ....*.
gi 1622916307  258 aldCGG 263
Cdd:pfam01822   80 ---CGG 82
LRRCT smart00082
Leucine rich repeat C-terminal domain;
127-179 7.36e-11

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 60.14  E-value: 7.36e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1622916307   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 ...
1552-1628 9.88e-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: 9.88e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916307 1552 VVNASRTVVPLNGSVSFS-TSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFSIIVTAENEVGSAQ-DSIFVYV 1628
Cdd:cd00146      3 ASVSAPPVAELGASVTFSaSDSSGGSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSStKTTTVVV 81
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
1487-1804 1.10e-10

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


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 66.62  E-value: 1.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1487 FSAVGRGRPASYLWDLGDGGRLEGPEVTHAYNSIGDFTVRVAGWNDV-SRSEAWLNVTVKRRVRGLVVNASRTVVPLNGS 1565
Cdd:COG3291     16 FTDTSSGNATSYEWDFGDGTTSTEANPSHTYTTPGTYTVTLTVTDAAgCSDTTTKTITVGAPNPGVTTVTTSTTVTTLAN 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1566 VSFSTSLEAGSDVrYSWVLCDRCTPIPGGPTISYTFRSVGTFSIIVTAENEVGSAQDSIFVYVLQLIEGLQVAGCGSYFP 1645
Cdd:COG3291     96 TANGGATTVVAGS-TVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTTSAST 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1646 TNHTAQLQAVVRDGTNVSYSWTAWWDRGPALAGSGKGFSLTALEAGTYHVQLRATNMLGSAWADCTVDFVEPVGWLMVTA 1725
Cdd:COG3291    175 NPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNTVTTS 254
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916307 1726 SPNPAAVNTSVTLSAKLAGGSGVLYTWSLEEGLSWETPEPFTTHSFPTPGLHLVTVTAGNPLGSASATVEVGVQVPVSG 1804
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 1.59e-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: 1.59e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  408 CPSDTEIFpgNGHCYRLVVEKAAWLQAQEQCRAwAGAALAMVDSPAVQRFLVSRVTRSLDVWIGFSTvqgPETglapQGE 487
Cdd:cd03590      1 CPTNWKSF--QSSCYFFSTEKKSWEESRQFCED-MGAHLVIINSQEEQEFISKILSGNRSYWIGLSD---EET----EGE 70
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622916307  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 ...
1380-1463 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 1622916307  1380 VGNVTLQPERqfVQLGDEVRLVACVWP-PFPYRYAWDFGTEEAAParagGPEVTFTYRDPGSYLVTVTASNNVSAANDSA 1458
Cdd:smart00089    1 VADVSASPTV--GVAGESVTFTATSSDdGSIVSYTWDFGDGTSST----GPTVTHTYTKPGTYTVTLTVTNAVGSASATV 74

                    ....*
gi 1622916307  1459 LVEVQ 1463
Cdd:smart00089   75 TVVVQ 79
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1296-1377 2.15e-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: 2.15e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  1296 VLRIEPAACIPTQP-DARLTAYVTGNPAHYLFDWTFGDGssnTTVRGrPTVTHNFTRSGTFPLALVLSSPVNKAHYFTSI 1374
Cdd:smart00089    1 VADVSASPTVGVAGeSVTFTATSSDDGSIVSYTWDFGDG---TSSTG-PTVTHTYTKPGTYTVTLTVTNAVGSASATVTV 76

                    ...
gi 1622916307  1375 CVE 1377
Cdd:smart00089   77 VVQ 79
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
3008-3057 6.64e-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: 6.64e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1622916307  3008 YTSLCQYFSEENMVWRTEGLLPLEETSPHqAVCLTRHLTAFGASLFVPPS 3057
Cdd:smart00303    1 FNPICVFWDESSGEWSTRGCELLETNGTH-TTCSCNHLTTFAVLMDVPPI 49
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
2073-2143 1.88e-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: 1.88e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622916307 2073 TNRSAWFEAATSPSPRRVAYHWDFGDGaPGQDTDEPRAEHCYLRPGDYRVQVNASNLVSfFVAQATVTVQV 2143
Cdd:cd00146     13 LGASVTFSASDSSGGSIVSYKWDFGDG-EVSSSGEPTVTHTYTKPGTYTVTLTVTNAVG-SSSTKTTTVVV 81
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
56-129 2.63e-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: 2.63e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916307   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 ...
1725-1798 4.04e-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: 4.04e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916307 1725 ASPNPAAVNTSVTLSAK-LAGGSGVLYTWSLEEGLSWETPEPFTTHSFPTPGLHLVTVTAGNPLGSASA-TVEVGV 1798
Cdd:cd00146      6 SAPPVAELGASVTFSASdSSGGSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTkTTTVVV 81
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
72-130 5.11e-09

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 61.87  E-value: 5.11e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916307   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 ...
1807-1879 5.36e-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: 5.36e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916307 1807 IRASESGGSFVAAGSSVPFWGQLATG---TNVSWCWAVPGGSSKRGPHVTMVFPDAGTFSVQLNASNAVSWVSATH 1879
Cdd:cd00146      1 PTASVSAPPVAELGASVTFSASDSSGgsiVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKT 76
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1222-1293 5.85e-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: 5.85e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622916307 1222 AVEQGAPVVVSAAVQ-TGDDITWTFDMGDGTVLSGPEDTVEHVYLRAQNCTVTVGAASPAGRlAQSLHVLVFV 1293
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 6.81e-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: 6.81e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  408 CPSDTeiFPGNGHCYRLVVEKAAWLQAQEQCRAW-AGAALAMVDSPAVQRFLVSRV----TRSLDVWIGFSTVQGPETGL 482
Cdd:cd03594      1 CPKGW--LPYKGNCYGYFRQPLSWSDAELFCQKYgPGAHLASIHSPAEAAAIASLIssyqKAYQPVWIGLHDPQQSRGWE 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622916307  483 APQGEAFSLEScqnWLPGEPHPaTAEHCVRL-GPTG---WcNTDLCSAPHSYVCE 533
Cdd:cd03594     79 WSDGSKLDYRS---WDRNPPYA-RGGYCAELsRSTGflkW-NDANCEERNPFICK 128
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
50-130 1.10e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 60.72  E-value: 1.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307   50 RVNCSGRGLRTLGPALripADATAL---DVSHNLLRALDVGLlANLSQLSELDISNNKISTLEEGIfANLFNLSEINLSG 126
Cdd:COG4886    140 ELDLSNNQLTDLPEPL---GNLTNLkslDLSNNQLTDLPEEL-GNLTNLKELDLSNNQITDLPEPL-GNLTNLEELDLSG 214

                   ....
gi 1622916307  127 NPFE 130
Cdd:COG4886    215 NQLT 218
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1226-1292 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: 54.38  E-value: 1.71e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622916307  1226 GAPVVVSAAVQT-GDDITWTFDMGDGTVLSGPedTVEHVYLRAQNCTVTVGAASPAGRLAQSLHVLVF 1292
Cdd:smart00089   14 GESVTFTATSSDdGSIVSYTWDFGDGTSSTGP--TVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
74-130 3.44e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 59.18  E-value: 3.44e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622916307   74 LDVSHNLLRALDVGLlANLSQLSELDISNNKISTLEEGIfANLFNLSEINLSGNPFE 130
Cdd:COG4886    187 LDLSNNQITDLPEPL-GNLTNLEELDLSGNQLTDLPEPL-ANLTNLETLDLSNNQLT 241
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
72-130 3.96e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 59.18  E-value: 3.96e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916307   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 ...
1645-1712 5.63e-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: 5.63e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916307  1645 PTNHTAQLQAVVR-DGTNVSYSWtawwDRGPALAGSGKGFSLTALEAGTYHVQLRATNMLGSAWADCTV 1712
Cdd:smart00089   12 VAGESVTFTATSSdDGSIVSYTW----DFGDGTSSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTV 76
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1387-1462 6.87e-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: 6.87e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622916307 1387 PERQFVQLGDEVRLVACVWP-PFPYRYAWDFGTEEAAPAraGGPEVTFTYRDPGSYLVTVTASNNVSAAN-DSALVEV 1462
Cdd:cd00146      6 SAPPVAELGASVTFSASDSSgGSIVSYKWDFGDGEVSSS--GEPTVTHTYTKPGTYTVTLTVTNAVGSSStKTTTVVV 81
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1024-1122 9.00e-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: 9.00e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  1024 VSTVPAVLPPNATLALTAGVLVDSAVeVAFLWTFGDGeqalrqfhppynesfpvpdpsvaQVLVEHNVTHTYAAPGEYIL 1103
Cdd:smart00089    4 VSASPTVGVAGESVTFTATSSDDGSI-VSYTWDFGDG-----------------------TSSTGPTVTHTYTKPGTYTV 59
                            90
                    ....*....|....*....
gi 1622916307  1104 TVLTSNAFENLTQQVPVSV 1122
Cdd:smart00089   60 TLTVTNAVGSASATVTVVV 78
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1024-1116 1.15e-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: 1.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1024 VSTVPAVLPPNATLALTAGVLvdSAVEVAFLWTFGDgeqalrqfhppynesfpvpdpSVAQVLVEHNVTHTYAAPGEYIL 1103
Cdd:pfam00801    1 VSASGTVVAAGQPVTFTATLA--DGSNVTYTWDFGD---------------------SPGTSGSGPTVTHTYLSPGTYTV 57
                           90
                   ....*....|...
gi 1622916307 1104 TVLTSNAFENLTQ 1116
Cdd:pfam00801   58 TLTASNAVGSANA 70
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
72-130 1.83e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 56.87  E-value: 1.83e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916307   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 ...
1307-1380 3.12e-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: 3.12e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622916307 1307 TQPDARLTAYVTGNPAHYLFDWTFGDGssNTTVRGRPTVTHNFTRSGTFPLALVLSSPVNKAhyfTSICVEPEV 1380
Cdd:cd00146     13 LGASVTFSASDSSGGSIVSYKWDFGDG--EVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSS---STKTTTVVV 81
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
1159-1458 3.17e-07

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


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 55.83  E-value: 3.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1159 YTWDFGDSSpvlTQSQPTANHTYASRGTYRVHLEVNNTV-SSALAQADVRVFEELRGLSVNMSLAVEQGAPVVVSAAVQT 1237
Cdd:COG3291     27 YEWDFGDGT---TSTEANPSHTYTTPGTYTVTLTVTDAAgCSDTTTKTITVGAPNPGVTTVTTSTTVTTLANTANGGATT 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1238 GDDITWTFDMGDGTVLSGPEDTVEHVYLRAQNCTVTVGAASPAGRLAQSLHVLVFVLEVLRIEPAACIPTQPDARLTAYV 1317
Cdd:COG3291    104 VVAGSTVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTTSASTNPSVTTDTV 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1318 TGNPAHYLFDWTFGDGSSNTTVR-GRPTVTHNFTRSGTFPLALVLSSPVNKAHYFTSICVEPEVGNVTLQPERQFVQLGD 1396
Cdd:COG3291    184 TTLTGSYTGTIVGGSGSGTVTSGtAGVTTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNTVTTSGANTAGTST 263
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916307 1397 EVRLVACVWPPF----PYRYAWDFGTEEAAPARAGGPEVTFTYRDPGSYLVTVTASNNVSAANDSA 1458
Cdd:COG3291    264 ITGGTSGVVTTSaatgTSTNGTGGLGTTTAITPGNVSTTADVTGGTATLAVSSTLTTNDTTGSSST 329
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
1408-1728 3.82e-07

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


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 55.45  E-value: 3.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1408 FPYRYAWDFGTeeaaPARAGGPEVTFTYRDPGSYLVTVTASNNV-SAANDSALVEVQEPVVVTDIKVNSSLVlelqqpyl 1486
Cdd:COG3291     23 NATSYEWDFGD----GTTSTEANPSHTYTTPGTYTVTLTVTDAAgCSDTTTKTITVGAPNPGVTTVTTSTTV-------- 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1487 FSAVGRGRPASYLWDLGDGGRLEGPEVTHAYNSIGDFTVRVAGWNDVSRSEAWLNVTVKRRVRGLVVNASRTVVPLNGSV 1566
Cdd:COG3291     91 TTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTT 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1567 SFSTSLEAGSDVRYSWVLCDRCTPIPGGPTISYTFRSVGTFSIIVTAENEVGSAQDSIFVYVLQLIEGLQVAGCGSYFPT 1646
Cdd:COG3291    171 SASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNT 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1647 NHTAQLQAVVRDGTNVSYSWTAWWDRGPALAGSGKGFSLTALEAGTYHVQLRATNMLGSAWADCTVDFVEPVGWLMVTAS 1726
Cdd:COG3291    251 VTTSGANTAGTSTITGGTSGVVTTSAATGTSTNGTGGLGTTTAITPGNVSTTADVTGGTATLAVSSTLTTNDTTGSSSTG 330

                   ..
gi 1622916307 1727 PN 1728
Cdd:COG3291    331 TV 332
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
3117-3224 4.43e-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: 4.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 3117 YEILVKTGWGRGSGTTAHVGIMLYGVDSRS---------GHRHLDGDRAFHRNSLDIFQIATPHSLGSVWKIRVWHDNKG 3187
Cdd:cd01754      3 YTIYVQTGSIWKAGTDSRISLQIYDADGPGlrianleawGGLMGAGHDYFERGNLDRFSGRGPCLPSPPCWMNLTSDGTG 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1622916307 3188 LSPAWFLQHVIVRDL-QTARSA--FFLVNDWLSVETEANG 3224
Cdd:cd01754     83 NHPGWYVNYVEVTQAgQHAPCMqhLFAVEQWLATDESPYM 122
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1478-1544 4.76e-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: 4.76e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622916307 1478 VLELQQPYLFSAV--GRGRPASYLWDLGDGGRL--EGPEVTHAYNSIGDFTVRVAGWNDVSRSEA-WLNVTV 1544
Cdd:cd00146     10 VAELGASVTFSASdsSGGSIVSYKWDFGDGEVSssGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTkTTTVVV 81
PKD_4 pfam18911
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
1152-1208 1.34e-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: 1.34e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1152 PSPGGVL-YTWDFGDSSpvlTQSQPTANHTYASRGTYRVHLEVNNT--VSSALAQADVRV 1208
Cdd:pfam18911   29 DPDGDILsYRWDFGDGT---TATGANVSHTYAAPGTYTVTLTVTDDsgASNSTATDTVTV 85
PKD_4 pfam18911
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
1487-1544 1.34e-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: 1.34e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1487 FSAVGRGRPASYLWDLGDGGRLEGPEVTHAYNSIGDFTVRVAGWND--VSRSEAWLNVTV 1544
Cdd:pfam18911   26 ASDDPDGDILSYRWDFGDGTTATGANVSHTYAAPGTYTVTLTVTDDsgASNSTATDTVTV 85
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
303-355 2.10e-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: 2.10e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1622916307   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 2.39e-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: 2.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  408 CPSDTEIFpgNGHCYRLVVEKAAWLQAQEQCRAwAGAALAMVDSPAVQRFLvSRVTRSLDVWIGFSTVQGPETGLAPQGE 487
Cdd:cd03593      1 CPKDWICY--GNKCYYFSMEKKTWNESKEACSS-KNSSLLKIDDEEELEFL-QSQIGSSSYWIGLSREKSEKPWKWIDGS 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1622916307  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 ...
1426-1903 2.65e-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: 2.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1426 AGGPEVTFTYRDPGSYLVTVTASNNVSAANDSALVEVQEPVVVTDIKVNSSLVLELQQPYLFSAVGRGRPASYLWDLGDG 1505
Cdd:COG5492    144 TAAVAVGSVGVASAGTSVTTTVATATSASLVSTLVVTSVGLTTASGSLNTVVVTSVVGNGATDASTASAVVAAVTAVTSA 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1506 GRLEGPEVTHAYNSIGDFTVRVAGWNDVSrSEAWLNVTVKRRVRGLVVNASRTVVPLNGSVSFSTSLEAGSDVRYSWVLc 1585
Cdd:COG5492    224 GSLTSAASVTTAGDDGTGVVATTVTTTIS-TSSSTTLTVTGATSSASTLGSGSTTSTNTVTAGVGDTGVSVAVASSSAA- 301
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1586 drcTPIPGGPTISYTFRSVGTFSIIVTAENEVGSAQDSIFVYVLQLIEGLQVAGCGSYFPTNHTAQLQAVVR--DGTNVS 1663
Cdd:COG5492    302 ---TTSAVVGTLSSSGGGGGVVTAAATTGVTVVTASSVATTVDVVPVTGVTLNPTSVTLAVGQTLTLTATVTpaNATNKN 378
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1664 YSWTawwDRGPALAG---SGKgfsLTALEAGTYHVQLRATNmlGSAWADCTV---DFVEPVGWLMVTASPNPAAVNTSVT 1737
Cdd:COG5492    379 VTWS---SSDPSVATvdsNGL---VTAVAAGTATITATTKD--GGKTATCTVtvtAAGSTGTVVVVSLAATSAVSASVVL 450
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1738 LSAKLAGGSGVLYTWSLEEGLSWETPEPFTTHSFPTPGLHLVTVTAGNPLGSASATVEVGVQVPVSGLSIRASESGGSFV 1817
Cdd:COG5492    451 TPAGTVNAGASTASLNVNATDGVSTTVGVANVVSAVTVTASVAEVATSVGGGATVTVTVSTAATVTVTVGVKSTGIAVAG 530
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1818 AAGSSVPFWGQLATGTNVSWCWAVPGGSSkrgphVTMVFPDAGTFSVQLNASNAVSWVSATHNLTVEEPIVGLVLWASSK 1897
Cdd:COG5492    531 STGILAGIVLSGSAKGDVAGGATLVDAGT-----ADVGGTTSTTTSVTDASVVSLTGSTSSTGVGVGGTTATGTAVAALV 605

                   ....*.
gi 1622916307 1898 VVAPGQ 1903
Cdd:COG5492    606 TGTGAT 611
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
1304-1366 2.81e-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: 2.81e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622916307 1304 CIPTQPDARLTAYV-TGNPAHYLfdWTFGDgsSNTTVRGRPTVTHNFTRSGTFPLALVLSSPVN 1366
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 2.99e-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: 2.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  431 WLQAQEQCRAwAGAALAMVDSPAVQRFLVSRVT-RSLDVWIGFSTVQGPETGLAPQGEAFSLEscqNWLPGEPHPATAEH 509
Cdd:pfam00059    4 WDEAREACRK-LGGHLVSINSAEELDFLSSTLKkSNKYFWIGLTDRKNEGTWKWVDGSPVNYT---NWAPEPNNNGENED 79
                           90       100
                   ....*....|....*....|....*.
gi 1622916307  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 ...
1888-1967 4.46e-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: 47.45  E-value: 4.46e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  1888 VGLVLWASSKVVApGQLVHFQI-LLAAGSAVTFRLQVGGASpaVLPGPRFSHSFPRVGDHVVSVQGENHVSWAQAQVRIV 1966
Cdd:smart00089    1 VADVSASPTVGVA-GESVTFTAtSSDDGSIVSYTWDFGDGT--SSTGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVV 77

                    .
gi 1622916307  1967 V 1967
Cdd:smart00089   78 V 78
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
282-354 5.49e-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: 5.49e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622916307  282 PHGPLAS-GQLAAFHIAAPLP--VTATRWDFGDGSPEVdAAGPAASHRYVLPGRYHVTAVVALGVSSALLGT-NVQV 354
Cdd:cd00146      6 SAPPVAElGASVTFSASDSSGgsIVSYKWDFGDGEVSS-SGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTtTVVV 81
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
72-130 8.03e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 51.86  E-value: 8.03e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916307   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 ...
1982-2058 3.32e-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: 3.32e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622916307  1982 PGIATGTERNFTARVQR-GSRVAYAWYFslqkvqGDSLViLSGRDVTYTPVAAGLLEIQVRAFNALGSENRTLVLEVQ 2058
Cdd:smart00089    9 TVGVAGESVTFTATSSDdGSIVSYTWDF------GDGTS-STGPTVTHTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
1025-1384 3.68e-05

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


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 49.28  E-value: 3.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1025 STVPAVLPPNATLALTAgvlVDSAVEVAFLWTFGDGEQAlrqfhppynesfpvpdpsvaqvlVEHNVTHTYAAPGEYI-- 1102
Cdd:COG3291      2 TATPTSGCAPLTVQFTD---TSSGNATSYEWDFGDGTTS-----------------------TEANPSHTYTTPGTYTvt 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1103 LTVlTSNAFENLTQQVPVSVRAALPSMAVGVSDSVLVAGRPITFYPHPLPSPGGVLYTWDFGDSSPVLTQSQPTANHTYA 1182
Cdd:COG3291     56 LTV-TDAAGCSDTTTKTITVGAPNPGVTTVTTSTTVTTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTTT 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1183 SRGTYRVHLEVNNTVSSALAQADVRVFEELRGLSVNmslaveqGAPVVVSAAVQTGDDITWTFDMGDGTVLSGPEDTVEH 1262
Cdd:COG3291    135 TTGTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTT-------SASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGT 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1263 VYLRAQNCTVTVGAASPAGRLAQSLHVLVFVLEVLRIEPAACIPTQPDARLTAYVTGNPAHYLFDWTFGDGSSNTTVRGR 1342
Cdd:COG3291    208 AGVTTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNTVTTSGANTAGTSTITGGTSGVVTTSAATGTSTNGTGG 287
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1622916307 1343 PTVTHNFTRSGTFPLALVLSSPVNKAHYFTSICVEPEVGNVT 1384
Cdd:COG3291    288 LGTTTAITPGNVSTTADVTGGTATLAVSSTLTTNDTTGSSST 329
PKD_4 pfam18911
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
302-339 3.87e-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: 3.87e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1622916307  302 VTATRWDFGDGSPevdAAGPAASHRYVLPGRYHVTAVV 339
Cdd:pfam18911   34 ILSYRWDFGDGTT---ATGANVSHTYAAPGTYTVTLTV 68
PKD_4 pfam18911
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
1411-1462 6.19e-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: 6.19e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622916307 1411 RYAWDF--GTEeaaparAGGPEVTFTYRDPGSYLVTVTASNNVSAANDSALVEV 1462
Cdd:pfam18911   36 SYRWDFgdGTT------ATGANVSHTYAAPGTYTVTLTVTDDSGASNSTATDTV 83
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
1554-1895 1.18e-04

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


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 47.74  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1554 NASRTVVPLNGSVSFsTSLEAGSDVRYSWVLCDRCTPipGGPTISYTFRSVGTFSIIVTAENEVG-SAQDSIFVYVLQLI 1632
Cdd:COG3291      2 TATPTSGCAPLTVQF-TDTSSGNATSYEWDFGDGTTS--TEANPSHTYTTPGTYTVTLTVTDAAGcSDTTTKTITVGAPN 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1633 EGLQVAGCGSYFPTNHTAQLQAVVRDGTNVSYSWTAWWDRGPALAGSGKGFSLTALEAGTYHVqlrATNMLGSAWADCTV 1712
Cdd:COG3291     79 PGVTTVTTSTTVTTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTG---LTGSTGTASDTATV 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1713 DFVEPVGWLMVTASPNPAAVNTSVTLSAKLAGGSGVLYTWSLeeGLSWETPEPFTTHSFPTPGLHLVTVTAGNPLGSASA 1792
Cdd:COG3291    156 TTSVSTTDVTSDGTTSASTNPSVTTDTVTTLTGSYTGTIVGG--SGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDV 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1793 TVEVGVQVPVSGLSIRASESGGSFVAAGSSVPFWGqlaTGTNVSWCWAVPGGSSKRGPHVTMVFPDAGTFSVQLNASNAV 1872
Cdd:COG3291    234 TLTGISTGDAGTPGTNTVTTSGANTAGTSTITGGT---SGVVTTSAATGTSTNGTGGLGTTTAITPGNVSTTADVTGGTA 310
                          330       340
                   ....*....|....*....|...
gi 1622916307 1873 SWVSATHNLTVEEPIVGLVLWAS 1895
Cdd:COG3291    311 TLAVSSTLTTNDTTGSSSTGTVF 333
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
934-1014 1.35e-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: 43.21  E-value: 1.35e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307   934 GLRATPSPEARVLQGVLVRYSPVVEAGSDVVFRWTINDKQSLTFQNVVFnvIYQSAAVFKLSLTASNHVSNVTVNYNVTV 1013
Cdd:smart00089    1 VADVSASPTVGVAGESVTFTATSSDDGSIVSYTWDFGDGTSSTGPTVTH--TYTKPGTYTVTLTVTNAVGSASATVTVVV 78

                    .
gi 1622916307  1014 E 1014
Cdd:smart00089   79 Q 79
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
408-534 1.93e-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: 1.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  408 CPSDTEIFpgNGHCYRLVVEKAAWLQAQEQCRAWAG----AALAMVDSPAVQRFL------VSRVTRSLDVWIGF--STV 475
Cdd:cd03589      1 CPTFWTAF--GGYCYRFFGDRLTWEEAELRCRSFSIpgliAHLVSIHSQEENDFVydlfesSRGPDTPYGLWIGLhdRTS 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622916307  476 QGPETGLAPQGEAFSlescqNWLPGEPHPA-TAEHCVRLGPTG-----WcNTDLCSAPHSYVCEL 534
Cdd:cd03589     79 EGPFEWTDGSPVDFT-----KWAGGQPDNYgGNEDCVQMWRRGdagqsW-NDMPCDAVFPYICKM 137
LRR_8 pfam13855
Leucine rich repeat;
93-127 4.28e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.97  E-value: 4.28e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1622916307   93 SQLSELDISNNKISTLEEGIFANLFNLSEINLSGN 127
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNN 35
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1643-1711 5.74e-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: 5.74e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916307 1643 YFPTNHTAQLQAVVR-------DGTNVSYSWTawWDRGPALAGSGKGFSLTALEAGTYHVQLRATNMLGSAWADCT 1711
Cdd:cd00146      4 SVSAPPVAELGASVTfsasdssGGSIVSYKWD--FGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTT 77
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
1227-1476 8.06e-04

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


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 45.05  E-value: 8.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1227 APVVVS-AAVQTGDDITWTFDMGDGTVLSGPedTVEHVYLRAQNCTVTVGAASPAGRLAqSLHVLVFVLEVLRIEPAACI 1305
Cdd:COG3291     10 APLTVQfTDTSSGNATSYEWDFGDGTTSTEA--NPSHTYTTPGTYTVTLTVTDAAGCSD-TTTKTITVGAPNPGVTTVTT 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1306 PTQPDARLTAYVTGNPAHYLFDWTFGDGSSNTTVRGRPTVTHNFTRSGTFPLALVLSSPVNKAHYFTSICVEPEVGNVTL 1385
Cdd:COG3291     87 STTVTTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVTTSVSTTDVTS 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1386 QPERQFVQLGDEVRLVACVWPPFPYRYAWDFGTEEAAPARAGGPEVTFTYRDPGSYLVTVTASNNVSAANDSALVEVQEP 1465
Cdd:COG3291    167 DGTTSASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTP 246
                          250
                   ....*....|.
gi 1622916307 1466 VVVTDIKVNSS 1476
Cdd:COG3291    247 GTNTVTTSGAN 257
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
419-511 8.56e-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: 8.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  419 GHCYRLVVEKAAWLQAQEQCRAwAGAALAMVDSPAVQRFlVSRVTRSLDvWIGFS--TVQGPETGlaPQGEAFSLEscqN 496
Cdd:cd03588     10 GHCYRHFPDRETWEDAERRCRE-QQGHLSSIVTPEEQEF-VNNNAQDYQ-WIGLNdrTIEGDFRW--SDGHPLQFE---N 81
                           90
                   ....*....|....*..
gi 1622916307  497 WLPGEPHP--ATAEHCV 511
Cdd:cd03588     82 WRPNQPDNffATGEDCV 98
LRRNT smart00013
Leucine rich repeat N-terminal domain;
34-73 9.68e-04

Leucine rich repeat N-terminal domain;


Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 39.22  E-value: 9.68e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1622916307    34 PCAPPCLCGPapgaaCRVNCSGRGLRTLgpALRIPADATA 73
Cdd:smart00013    1 ACPAPCNCSG-----TAVDCSGRGLTEV--PLDLPPDTTL 33
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1034-1122 1.27e-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: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307 1034 NATLALTAGVLVDSAVeVAFLWTFGDGEQALRQfhppynesfpvpdpsvaqvlvEHNVTHTYAAPGEYILTV-LTSNAFE 1112
Cdd:cd00146     14 GASVTFSASDSSGGSI-VSYKWDFGDGEVSSSG---------------------EPTVTHTYTKPGTYTVTLtVTNAVGS 71
                           90
                   ....*....|
gi 1622916307 1113 NLTQQVPVSV 1122
Cdd:cd00146     72 SSTKTTTVVV 81
PKD_4 pfam18911
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
2090-2128 1.49e-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: 1.49e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1622916307 2090 VAYHWDFGDGAPGqdtDEPRAEHCYLRPGDYRVQVNASN 2128
Cdd:pfam18911   35 LSYRWDFGDGTTA---TGANVSHTYAAPGTYTVTLTVTD 70
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1891-1967 1.82e-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: 1.82e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622916307 1891 VLWASSKVVAPGQLVHFQI-LLAAGSAVTFRLQVGGASPAVLPGPRFSHSFPRVGDHVVSVQGENHVSWAQAQVRIVV 1967
Cdd:cd00146      3 ASVSAPPVAELGASVTFSAsDSSGGSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTTTVV 80
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
939-1006 1.93e-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: 39.68  E-value: 1.93e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916307  939 PSPEARVL-QGVLVRYSPVVEAGSDVVFRWTINDKQSLTFQNVVFNVIYQSAAVFKLSLTASNHVSNVT 1006
Cdd:pfam00801    1 VSASGTVVaAGQPVTFTATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSAN 69
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
2079-2142 4.07e-03

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


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 42.73  E-value: 4.07e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622916307 2079 FEAATSPSPrrVAYHWDFGDGApgqDTDEPRAEHCYLRPGDYRVQVNASNLV-SFFVAQATVTVQ 2142
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 5.70e-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: 5.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916307  437 QCRAWAGAALAMVDSPAVQRFLVSRVTRSLDVWIGFSTVQGPETG-LAPQGEAFSLEScQNWLPGEP-HPATAEHCVRLg 514
Cdd:cd03601     20 RSRGMRLASLAMRDSEMRDAILAFTLVKGHGYWVGADNLQDGEYDfLWNDGVSLPTDS-DLWAPNEPsNPQSRQLCVQL- 97
                           90       100
                   ....*....|....*....|....
gi 1622916307  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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