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Conserved domains on  [gi|45551542|ref|NP_729566|]
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calcium-independent phospholipase A2 VIA, isoform C [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
563-876 0e+00

Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent phospholipase that catalyzes the hydrolysis of glycerophospholipids at the sn-2 position. PNPLA9 is also known as PLA2G6 (phospholipase A2 group VI) or iPLA2beta. PLA2G6 is stimulated by ATP and inhibited by bromoenol lactone (BEL). In humans, PNPLA9 in expressed ubiquitously and is involved in signal transduction, cell proliferation, and apoptotic cell death. Mutations in human PLA2G6 leads to infantile neuroaxonal dystrophy (INAD) and idiopathic neurodegeneration with brain iron accumulation (NBIA). This family includes PLA2G6 from Homo sapiens and Rattus norvegicus.


:

Pssm-ID: 132851 [Multi-domain]  Cd Length: 312  Bit Score: 550.40  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 563 LLCLDGGGIRGLVLVQMLLEIEKLSRTPIIHMFDWIAGTSTGGILALALGCGKTMRQCMGLYLRMKEQCFVGSRPYNSEF 642
Cdd:cd07212   1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGSRPYNSEP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 643 FESILKDNLGEFNVMTDIKHPKIMVTGVMADRKPVDLHLFRNYTSASDILGIVTpiNNRRIPPPQPSEQLVWRAARATGA 722
Cdd:cd07212  81 LEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEEPEK--NANFLPPTDPAEQLLWRAARSSGA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 723 APSYFRAFGRFLDGGLIANNPTLDAMTEIHEYNMALRSAGRESEAIPVSVVMSLGTGHIPVTELKDIDVFRPESIWDTAK 802
Cdd:cd07212 159 APTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKSKGRKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSNPWELAK 238
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45551542 803 LAYGISTIGNLLVDQATCSDGRVVDRARAWCSTIGIPYFRFNPQLSEDIAMDEKDDQKLINMLWHTKAYMHANR 876
Cdd:cd07212 239 TVFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTHR 312
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
143-418 6.84e-32

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.22  E-value: 6.84e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 143 LVDYISNPKMLQCVDQADAATLMSPFQLAIKQGHMEMVKALLPLSKLEHLDINSNSVFHYAASTTKEIINLIIDKSTVNL 222
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 223 NHLNSDGYTPLHVACLADKPENVKALLLAGANVNlnAKDirkvyktsapttvssflrtnvsklytqdmKYGGTPLHWCSS 302
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN--ARD-----------------------------KDGETPLHLAAY 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 303 R---ETLHALIMEGCDVNATNFDGRTALHVMVARNRFECVVTLLAHDAEIDVLDKDGNAALHIAIEKKLVPIVQCLVVFG 379
Cdd:COG0666 130 NgnlEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 45551542 380 CDINLKNKDGKTPRHMvgndASGNKDDEILYILHSVGAK 418
Cdd:COG0666 210 ADVNAKDNDGKTALDL----AAENGNLEIVKLLLEAGAD 244
 
Name Accession Description Interval E-value
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
563-876 0e+00

Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent phospholipase that catalyzes the hydrolysis of glycerophospholipids at the sn-2 position. PNPLA9 is also known as PLA2G6 (phospholipase A2 group VI) or iPLA2beta. PLA2G6 is stimulated by ATP and inhibited by bromoenol lactone (BEL). In humans, PNPLA9 in expressed ubiquitously and is involved in signal transduction, cell proliferation, and apoptotic cell death. Mutations in human PLA2G6 leads to infantile neuroaxonal dystrophy (INAD) and idiopathic neurodegeneration with brain iron accumulation (NBIA). This family includes PLA2G6 from Homo sapiens and Rattus norvegicus.


Pssm-ID: 132851 [Multi-domain]  Cd Length: 312  Bit Score: 550.40  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 563 LLCLDGGGIRGLVLVQMLLEIEKLSRTPIIHMFDWIAGTSTGGILALALGCGKTMRQCMGLYLRMKEQCFVGSRPYNSEF 642
Cdd:cd07212   1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGSRPYNSEP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 643 FESILKDNLGEFNVMTDIKHPKIMVTGVMADRKPVDLHLFRNYTSASDILGIVTpiNNRRIPPPQPSEQLVWRAARATGA 722
Cdd:cd07212  81 LEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEEPEK--NANFLPPTDPAEQLLWRAARSSGA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 723 APSYFRAFGRFLDGGLIANNPTLDAMTEIHEYNMALRSAGRESEAIPVSVVMSLGTGHIPVTELKDIDVFRPESIWDTAK 802
Cdd:cd07212 159 APTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKSKGRKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSNPWELAK 238
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45551542 803 LAYGISTIGNLLVDQATCSDGRVVDRARAWCSTIGIPYFRFNPQLSEDIAMDEKDDQKLINMLWHTKAYMHANR 876
Cdd:cd07212 239 TVFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTHR 312
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
554-866 1.51e-44

Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function prediction only];


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 162.77  E-value: 1.51e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 554 GDKPYgrgRLLCLDGGGIRGLVLVQMLLEIEKLSRTPIIHMFDWIAGTSTGGILALALGCGKTMRQCMGLYLRMKEQCFV 633
Cdd:COG3621   3 ANKPF---RILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAAGYSAEEILDLYEEEGKEIFP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 634 GSRP-------------YNSEFFESILKDNLGEFnVMTDIKHPkIMVTGVMAD-RKPvdlHLFRNYTSASDIlgivtpin 699
Cdd:COG3621  80 KSRWrkllslrglfgpkYDSEGLEKVLKEYFGDT-TLGDLKTP-VLIPSYDLDnGKP---VFFKSPHAKFDR-------- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 700 NRRIPppqpseqlVWRAARATGAAPSYFRAF---------GRFLDGGLIANNPTLDAMTEiheynmALRSAGRESEAIpv 770
Cdd:COG3621 147 DRDFL--------LVDVARATSAAPTYFPPAqiknltgegYALIDGGVFANNPALCALAE------ALKLLGPDLDDI-- 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 771 sVVMSLGTGHIPvtelkdiDVFRPESIWDTAKLAYGISTIgNLLVDqatcSDGRVVDrarAWCSTI-GIPYFRFNPQLSE 849
Cdd:COG3621 211 -LVLSLGTGTAP-------RSIPYKKVKNWGALGWLLPLI-DILMD----AQSDAVD---YQLRQLlGDRYYRLDPELPE 274
                       330
                ....*....|....*..
gi 45551542 850 DIAMDekDDQKLINMLW 866
Cdd:COG3621 275 EIALD--DNAENIEALL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
143-418 6.84e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.22  E-value: 6.84e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 143 LVDYISNPKMLQCVDQADAATLMSPFQLAIKQGHMEMVKALLPLSKLEHLDINSNSVFHYAASTTKEIINLIIDKSTVNL 222
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 223 NHLNSDGYTPLHVACLADKPENVKALLLAGANVNlnAKDirkvyktsapttvssflrtnvsklytqdmKYGGTPLHWCSS 302
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN--ARD-----------------------------KDGETPLHLAAY 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 303 R---ETLHALIMEGCDVNATNFDGRTALHVMVARNRFECVVTLLAHDAEIDVLDKDGNAALHIAIEKKLVPIVQCLVVFG 379
Cdd:COG0666 130 NgnlEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 45551542 380 CDINLKNKDGKTPRHMvgndASGNKDDEILYILHSVGAK 418
Cdd:COG0666 210 ADVNAKDNDGKTALDL----AAENGNLEIVKLLLEAGAD 244
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
562-781 5.45e-25

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 106.81  E-value: 5.45e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  562 RLLCLDGGGIRGLVLVQMLLEIEKLSRTPIIHMFDWIAGTSTGGILALALGCGKTMRQCMGLYL---------RMKEQCF 632
Cdd:NF041079   2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILALALALEIPARELVELFEehgkdifpkRKWPRRL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  633 VG---SRPYNSEFFESILKDNLGEfNVMTDIKHPkIMVTGVmadrkpvdlhlfrNYTSASdilgivtpinnrrippPQ-- 707
Cdd:NF041079  82 LGllkKPKYSSEPLREVLEEIFGD-KTIGDLKHR-VLIPAV-------------NYTTGK----------------PQvf 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  708 -----PSEQLVWR-----AARATGAAPSYF-RAF---GRFLDGGLIANNPTLDAmteIHEynmALRSAGRESEAIPvsvV 773
Cdd:NF041079 131 ktphhPDFTRDHKlklvdVALATSAAPTYFpLHEfdnEQFVDGGLVANNPGLLG---LHE---ALHFLGVPYDDVR---I 201

                 ....*...
gi 45551542  774 MSLGTGHI 781
Cdd:NF041079 202 LSIGTLSS 209
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
564-748 1.42e-20

Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein but it also has the enzymatic activity of lipid acyl hydrolase, catalysing the cleavage of fatty acids from membrane lipids. Members of this family have been found also in vertebrates.


Pssm-ID: 396341  Cd Length: 190  Bit Score: 90.36  E-value: 1.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542   564 LCLDGGGIRGLVLVQMLLEIEKlsrtpIIHMFDWIAGTSTGGILALALGCGKTMRQCMGLYLRMKEQCFVgSRPYNSEFF 643
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGE-----AGIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFL-SLIRKRALS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542   644 ESILKDNLGEFNVMTDIKHPKIMVTGVMADRKPVDLH----LFRNYTSASDILGIVTPINNRRI---PPPQPSEQLVWRA 716
Cdd:pfam01734  75 LLALLRGLIGEGGLFDGDALRELLRKLLGDLTLEELAarlsLLLVVALRALLTVISTALGTRARillPDDLDDDEDLADA 154
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 45551542   717 ARATGAAPSYFRAF----GRFLDGGLIANNPTLDAM 748
Cdd:pfam01734 155 VLASSALPGVFPPVrldgELYVDGGLVDNVPVEAAL 190
PHA03100 PHA03100
ankyrin repeat protein; Provisional
199-417 1.75e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 85.87  E-value: 1.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  199 VFHYAASTTKEIINLIIDKSTVNLNHLNSDGY----TPLHVACLADKPENVKALLLAGANVNLNAKDIRKVY-------- 266
Cdd:PHA03100   1 LYSYIVLTKSRIIKVKNIKYIIMEDDLNDYSYkkpvLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsniky 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  267 -KTSAPTTVSSFLR--TNVSKLYtqdmKYGGTPLHWCSSRETLHALIME-----GCDVNATNFDGRTALHVMV------- 331
Cdd:PHA03100  81 nLTDVKEIVKLLLEygANVNAPD----NNGITPLLYAISKKSNSYSIVEylldnGANVNIKNSDGENLLHLYLesnkidl 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  332 --------------ARNRFECvvtLLAHDAEIDVLDKDGNAALHIAIEKKLVPIVQCLVVFGCDINLKNKDGKTPRHMvg 397
Cdd:PHA03100 157 kilkllidkgvdinAKNRVNY---LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHI-- 231
                        250       260
                 ....*....|....*....|
gi 45551542  398 ndASGNKDDEILYILHSVGA 417
Cdd:PHA03100 232 --AILNNNKEIFKLLLNNGP 249
Ank_2 pfam12796
Ankyrin repeats (3 copies);
297-386 2.42e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.29  E-value: 2.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542   297 LHWCSSR---ETLHALIMEGCDVNATNFDGRTALHVMVARNRFECVVTLLAHdAEIDVLDkDGNAALHIAIEKKLVPIVQ 373
Cdd:pfam12796   1 LHLAAKNgnlELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 45551542   374 CLVVFGCDINLKN 386
Cdd:pfam12796  79 LLLEKGADINVKD 91
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
102-366 2.74e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 44.69  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542   102 RLPVFVSIVKEYYNVNGLQKACDALADNPSWTLShliayfnlvDYISNPKMLQ--CVDQADAATLmspFQLAIKQGHMEM 179
Cdd:TIGR00870   1 RGPLDIVPAEESPLSDEEKAFLPAAERGDLASVY---------RDLEEPKKLNinCPDRLGRSAL---FVAAIENENLEL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542   180 VKALLPLSKLEHLdinSNSVFHYAASTTKEIINLII------DKSTVNLNHLN-------SDGYTPLHVACLADKPENVK 246
Cdd:TIGR00870  69 TELLLNLSCRGAV---GDTLLHAISLEYVDAVEAILlhllaaFRKSGPLELANdqytsefTPGITALHLAAHRQNYEIVK 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542   247 ALLLAGANVNLNAkdirkvyktsaptTVSSFLRTNvsklYTQDMKYGGTPLHW--CSSRETLHALIME-GCDVNATNFDG 323
Cdd:TIGR00870 146 LLLERGASVPARA-------------CGDFFVKSQ----GVDSFYHGESPLNAaaCLGSPSIVALLSEdPADILTADSLG 208
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 45551542   324 RTALH--VMVARNRFE-------CVVTLLAHDAEID-------VLDKDGNAALHIAIEK 366
Cdd:TIGR00870 209 NTLLHllVMENEFKAEyeelscqMYNFALSLLDKLRdskelevILNHQGLTPLKLAAKE 267
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
166-376 3.08e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 44.62  E-value: 3.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 166 SPFQLAIKQGHMEMVKALLplsKLEHLDINS-----NSVFHYAASTTK-EIINLIIDKSTVNLNH-LNSD---GYTPLHV 235
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLL---KCPSCDLFQrgalgETALHVAALYDNlEAAVVLMEAAPELVNEpMTSDlyqGETALHI 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 236 ACLADKPENVKALLLAGANVNlnakdirkvyktSAPTTVSSFLRTNVSKLYtqdmkYGGTPLHW--C-SSRETLHALIME 312
Cdd:cd22192  96 AVVNQNLNLVRELIARGADVV------------SPRATGTFFRPGPKNLIY-----YGEHPLSFaaCvGNEEIVRLLIEH 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45551542 313 GCDVNATNFDGRTALHVMV--ARNRFECVV--TLLAHDAEID------VLDKDGNAALHIAIEKKLVPIVQCLV 376
Cdd:cd22192 159 GADIRAQDSLGNTVLHILVlqPNKTFACQMydLILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNIVMFQHLV 232
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
228-257 4.14e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 4.14e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 45551542    228 DGYTPLHVACLADKPENVKALLLAGANVNL 257
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
563-876 0e+00

Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent phospholipase that catalyzes the hydrolysis of glycerophospholipids at the sn-2 position. PNPLA9 is also known as PLA2G6 (phospholipase A2 group VI) or iPLA2beta. PLA2G6 is stimulated by ATP and inhibited by bromoenol lactone (BEL). In humans, PNPLA9 in expressed ubiquitously and is involved in signal transduction, cell proliferation, and apoptotic cell death. Mutations in human PLA2G6 leads to infantile neuroaxonal dystrophy (INAD) and idiopathic neurodegeneration with brain iron accumulation (NBIA). This family includes PLA2G6 from Homo sapiens and Rattus norvegicus.


Pssm-ID: 132851 [Multi-domain]  Cd Length: 312  Bit Score: 550.40  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 563 LLCLDGGGIRGLVLVQMLLEIEKLSRTPIIHMFDWIAGTSTGGILALALGCGKTMRQCMGLYLRMKEQCFVGSRPYNSEF 642
Cdd:cd07212   1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGSRPYNSEP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 643 FESILKDNLGEFNVMTDIKHPKIMVTGVMADRKPVDLHLFRNYTSASDILGIVTpiNNRRIPPPQPSEQLVWRAARATGA 722
Cdd:cd07212  81 LEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEEPEK--NANFLPPTDPAEQLLWRAARSSGA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 723 APSYFRAFGRFLDGGLIANNPTLDAMTEIHEYNMALRSAGRESEAIPVSVVMSLGTGHIPVTELKDIDVFRPESIWDTAK 802
Cdd:cd07212 159 APTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKSKGRKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSNPWELAK 238
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45551542 803 LAYGISTIGNLLVDQATCSDGRVVDRARAWCSTIGIPYFRFNPQLSEDIAMDEKDDQKLINMLWHTKAYMHANR 876
Cdd:cd07212 239 TVFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTHR 312
Pat_PNPLA8 cd07211
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ...
555-875 1.11e-49

Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial phospholipase which maintains mitochondrial integrity. PNPLA8 is also known as iPLA2-gamma. In humans, it is predominantly expressed in heart tissue. iPLA2-gamma can catalyze both phospholipase A1 and A2 reactions (PLA1 and PLA2 respectively). This family includes PNPLA8 (iPLA2-gamma) from Homo sapiens and iPLA2-2 from Mus musculus.


Pssm-ID: 132850 [Multi-domain]  Cd Length: 308  Bit Score: 177.83  E-value: 1.11e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 555 DKPYGRG-RLLCLDGGGIRGLVLVQMLLEIEKLSRTPIIHMFDWIAGTSTGGILALALGCGK-TMRQCMGLYLRMKEQCF 632
Cdd:cd07211   1 PPVKGRGiRILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAFLLGLKKmSLDECEELYRKLGKDVF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 633 VGSRP-------------YNSEFFESILKDNLG-----EFNVMTDIkhPKIMVTGVMADRKPVDLHLFRNYTSAsdiLGI 694
Cdd:cd07211  81 SQNTYisgtsrlvlshayYDTETWEKILKEMMGsdeliDTSADPNC--PKVACVSTQVNRTPLKPYVFRNYNHP---PGT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 695 VTPInnrrippPQPSEQLVWRAARATGAAPSYFRAF----GRFLDGGLIANNPTLdamteiheynMALRSAGRESEAIPV 770
Cdd:cd07211 156 RSHY-------LGSCKHKLWEAIRASSAAPGYFEEFklgnNLHQDGGLLANNPTA----------LALHEAKLLWPDTPI 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 771 SVVMSLGTGHIPvtelkdiDVFRPESIWDTaklayGISTIGNLLVDQATCsdgrvVDRARAWCSTIgIP---YFRFNPQL 847
Cdd:cd07211 219 QCLVSVGTGRYP-------SSVRLETGGYT-----SLKTKLLNLIDSATD-----TERVHTALDDL-LPpdvYFRFNPVM 280
                       330       340
                ....*....|....*....|....*...
gi 45551542 848 SEDIAMDEKDDQKLINMLWHTKAYMHAN 875
Cdd:cd07211 281 SECVELDETRPEKLDQLQDDTLEYIKRN 308
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
564-872 4.63e-47

Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes subfamily of PNPLA8 (iPLA2-gamma) and PNPLA9 (iPLA2-beta) like phospholipases from human as well as the Pat17 isozyme from Solanum cardiophyllum.


Pssm-ID: 132838 [Multi-domain]  Cd Length: 258  Bit Score: 168.66  E-value: 4.63e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 564 LCLDGGGIRGLVLVQMLLEIEKL--SRTPIIHMFDWIAGTSTGGILALALGCGK-TMRQCMGLYLRMKEQCFvgsrpyns 640
Cdd:cd07199   2 LSLDGGGIRGIIPAEILAELEKRlgKPSRIADLFDLIAGTSTGGIIALGLALGRySAEELVELYEELGRKIF-------- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 641 effesilkdnlgefnvmtdikhPKIMVTGV-MADRKPvdlHLFRNYTSASdilgivtpinnrripPPQPSEQLVWRAARA 719
Cdd:cd07199  74 ----------------------PRVLVTAYdLSTGKP---VVFSNYDAEE---------------PDDDDDFKLWDVARA 113
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 720 TGAAPSYFRAF--------GRFLDGGLIANNPTLDAMTEiheynmALRSAGRESEAIpvsVVMSLGTGHIPVTELKDIDV 791
Cdd:cd07199 114 TSAAPTYFPPAviesggdeGAFVDGGVAANNPALLALAE------ALRLLAPDKDDI---LVLSLGTGTSPSSSSSKKAS 184
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 792 FRPESIWdtaklaygISTIGNLLVDQATCSDGRVVDRARAWCStIGIPYFRFNPQLSEDI-AMDEKDDQKLINMLWHTKA 870
Cdd:cd07199 185 RWGGLGW--------GRPLLDILMDAQSDGVDQWLDLLFGSLD-SKDNYLRINPPLPGPIpALDDASEANLLALDSAAFE 255

                ..
gi 45551542 871 YM 872
Cdd:cd07199 256 LI 257
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
554-866 1.51e-44

Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function prediction only];


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 162.77  E-value: 1.51e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 554 GDKPYgrgRLLCLDGGGIRGLVLVQMLLEIEKLSRTPIIHMFDWIAGTSTGGILALALGCGKTMRQCMGLYLRMKEQCFV 633
Cdd:COG3621   3 ANKPF---RILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAAGYSAEEILDLYEEEGKEIFP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 634 GSRP-------------YNSEFFESILKDNLGEFnVMTDIKHPkIMVTGVMAD-RKPvdlHLFRNYTSASDIlgivtpin 699
Cdd:COG3621  80 KSRWrkllslrglfgpkYDSEGLEKVLKEYFGDT-TLGDLKTP-VLIPSYDLDnGKP---VFFKSPHAKFDR-------- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 700 NRRIPppqpseqlVWRAARATGAAPSYFRAF---------GRFLDGGLIANNPTLDAMTEiheynmALRSAGRESEAIpv 770
Cdd:COG3621 147 DRDFL--------LVDVARATSAAPTYFPPAqiknltgegYALIDGGVFANNPALCALAE------ALKLLGPDLDDI-- 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 771 sVVMSLGTGHIPvtelkdiDVFRPESIWDTAKLAYGISTIgNLLVDqatcSDGRVVDrarAWCSTI-GIPYFRFNPQLSE 849
Cdd:COG3621 211 -LVLSLGTGTAP-------RSIPYKKVKNWGALGWLLPLI-DILMD----AQSDAVD---YQLRQLlGDRYYRLDPELPE 274
                       330
                ....*....|....*..
gi 45551542 850 DIAMDekDDQKLINMLW 866
Cdd:COG3621 275 EIALD--DNAENIEALL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
143-418 6.84e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.22  E-value: 6.84e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 143 LVDYISNPKMLQCVDQADAATLMSPFQLAIKQGHMEMVKALLPLSKLEHLDINSNSVFHYAASTTKEIINLIIDKSTVNL 222
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 223 NHLNSDGYTPLHVACLADKPENVKALLLAGANVNlnAKDirkvyktsapttvssflrtnvsklytqdmKYGGTPLHWCSS 302
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN--ARD-----------------------------KDGETPLHLAAY 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 303 R---ETLHALIMEGCDVNATNFDGRTALHVMVARNRFECVVTLLAHDAEIDVLDKDGNAALHIAIEKKLVPIVQCLVVFG 379
Cdd:COG0666 130 NgnlEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 45551542 380 CDINLKNKDGKTPRHMvgndASGNKDDEILYILHSVGAK 418
Cdd:COG0666 210 ADVNAKDNDGKTALDL----AAENGNLEIVKLLLEAGAD 244
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
117-423 8.09e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.06  E-value: 8.09e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 117 NGLQKACDALADNPSWTLSHLIAYFNLVDYISNPKMLQCVDQADAATLMSPFQLAIKQGHMEMVKALLPLSK--LEHLDI 194
Cdd:COG0666   6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGadINAKDD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 195 NSNSVFHYAAST-TKEIINLIIDKStVNLNHLNSDGYTPLHVACLADKPENVKALLLAGANVNlnAKDirkvyktsaptt 273
Cdd:COG0666  86 GGNTLLHAAARNgDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVN--AQD------------ 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 274 vssflrtnvsklytqdmKYGGTPLHWCSSR---ETLHALIMEGCDVNATNFDGRTALHVMVARNRFECVVTLLAHDAEID 350
Cdd:COG0666 151 -----------------NDGNTPLHLAAANgnlEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45551542 351 VLDKDGNAALHIAIEKKLVPIVQCLVVFGCDINLKNKDGKTPRHMVGNDASGNKDDEILYILHSVGAKRCKDT 423
Cdd:COG0666 214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
Pat17_PNPLA8_PNPLA9_like3 cd07216
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
562-873 2.19e-27

Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes subfamily of PNPLA8 (iPLA2-gamma) and PNPLA9 (iPLA2-beta) like phospholipases from human as well as the Pat17 isozyme from Solanum cardiophyllum.


Pssm-ID: 132855 [Multi-domain]  Cd Length: 309  Bit Score: 113.55  E-value: 2.19e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 562 RLLCLDGGGIRGLVLVQMLLEI-----EKLSRTPII---HMFDWIAGTSTGGILALALGCGK-TMRQCMGLYLRMKEQCF 632
Cdd:cd07216   2 NLLSLDGGGVRGLSSLLILKEImeridPKEGLDEPPkpcDYFDLIGGTSTGGLIAIMLGRLRmTVDECIDAYTRLAKKIF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 633 -------VGSRPYNSEFF-----ESILKDNLGEFNV-MTDIKHP------KIMVTGVMAD--RKPVdlhLFRNYtsasdi 691
Cdd:cd07216  82 srkrlrlIIGDLRTGARFdskklAEAIKVILKELGNdEDDLLDEgeedgcKVFVCATDKDvtGKAV---RLRSY------ 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 692 lgivtpiNNRRIPPPQPSEQlVWRAARATGAAPSYF--RAFG----RFLDGGLIANNPTLDAMTEIHEYnmaLRSAGREs 765
Cdd:cd07216 153 -------PSKDEPSLYKNAT-IWEAARATSAAPTFFdpVKIGpggrTFVDGGLGANNPIREVWSEAVSL---WEGLARL- 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 766 eaipVSVVMSLGTGhipvteLKDIDVFRPesiwdTAKLAYGISTIGNLLVDqaTCSDGRVVDRARAWCSTIGIpYFRFN- 844
Cdd:cd07216 221 ----VGCLVSIGTG------TPSIKSLGR-----SAEGAGLLKGLKDLVTD--TEAEAKRFSAEHSELDEEGR-YFRFNv 282
                       330       340
                ....*....|....*....|....*....
gi 45551542 845 PQLSEDIAMDEKDDQKLINMLwhTKAYMH 873
Cdd:cd07216 283 PHGLEDVGLDEYEKMEEIVSL--TREYLA 309
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
562-781 5.45e-25

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 106.81  E-value: 5.45e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  562 RLLCLDGGGIRGLVLVQMLLEIEKLSRTPIIHMFDWIAGTSTGGILALALGCGKTMRQCMGLYL---------RMKEQCF 632
Cdd:NF041079   2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILALALALEIPARELVELFEehgkdifpkRKWPRRL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  633 VG---SRPYNSEFFESILKDNLGEfNVMTDIKHPkIMVTGVmadrkpvdlhlfrNYTSASdilgivtpinnrrippPQ-- 707
Cdd:NF041079  82 LGllkKPKYSSEPLREVLEEIFGD-KTIGDLKHR-VLIPAV-------------NYTTGK----------------PQvf 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  708 -----PSEQLVWR-----AARATGAAPSYF-RAF---GRFLDGGLIANNPTLDAmteIHEynmALRSAGRESEAIPvsvV 773
Cdd:NF041079 131 ktphhPDFTRDHKlklvdVALATSAAPTYFpLHEfdnEQFVDGGLVANNPGLLG---LHE---ALHFLGVPYDDVR---I 201

                 ....*...
gi 45551542  774 MSLGTGHI 781
Cdd:NF041079 202 LSIGTLSS 209
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
119-391 1.15e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 105.04  E-value: 1.15e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 119 LQKACDALADNPSWTLSHLIAYFNLVDYISNPKMLQCVDQADAATLMSPFQLAIKQGHMEMVKALLPL-SKLEHLDINSN 197
Cdd:COG0666  42 LALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAgADVNARDKDGE 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 198 SVFHYAAST-TKEIINLIIDKStVNLNHLNSDGYTPLHVACLADKPENVKALLLAGANVNlnAKDirkvyktsapttvss 276
Cdd:COG0666 122 TPLHLAAYNgNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN--ARD--------------- 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 277 flrtnvsklytqdmKYGGTPLHWCSSR---ETLHALIMEGCDVNATNFDGRTALHVMVARNRFECVVTLLAHDAEIDVLD 353
Cdd:COG0666 184 --------------NDGETPLHLAAENghlEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 45551542 354 KDGNAALHIAIEKKLVPIVQCLVVFGCDINLKNKDGKT 391
Cdd:COG0666 250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
562-858 1.17e-23

Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes subfamily of PNPLA8 (iPLA2-gamma) and PNPLA9 (iPLA2-beta) like phospholipases from human as well as the Pat17 isozyme from Solanum cardiophyllum.


Pssm-ID: 132852 [Multi-domain]  Cd Length: 288  Bit Score: 101.98  E-value: 1.17e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 562 RLLCLDGGGIRGLVLVQMLLEIEK-----LSRtpiIHMFdwiAGTSTGGILALALGCGKTMRQCMGLYLRMKEQCFVGSR 636
Cdd:cd07213   3 RILSLDGGGVKGIVQLVLLKRLAEefpsfLDQ---IDLF---AGTSAGSLIALGLALGYSPRQVLKLYEEVGLKVFSKSS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 637 P--------YNSEFFESILKDNLGEFNVMTDIKHpKIMVTGVMADRKPVDlhlfRNYTSASDILgivtpiNNrrIPPPQP 708
Cdd:cd07213  77 AgggagnnqYFAAGFLKAFAEVFFGDLTLGDLKR-KVLVPSFQLDSGKDD----PNRRWKPKLF------HN--FPGEPD 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 709 SEQLVWRAARATGAAPSYFRAFGRFLDGGLIANNPTLDAMTEIheynmalrsAGRESEAIPV--SVVMSLGTG-----HI 781
Cdd:cd07213 144 LDELLVDVCLRSSAAPTYFPSYQGYVDGGVFANNPSLCAIAQA---------IGEEGLNIDLkdIVVLSLGTGrppsyLD 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 782 PVTELKDidvfrpesiWDTAKLAygiSTIGNLLVD---QATCSDGRVVDRARawcstigipYFRFNPQLSEDIAMDEKDD 858
Cdd:cd07213 215 GANGYGD---------WGLLQWL---PDLLDLFMDagvDAADFQCRQLLGER---------YFRLDPVLPANIDLDDNKQ 273
Pat17_PNPLA8_PNPLA9_like2 cd07215
Patatin-like phospholipase of bacteria; Patatin is a storage protein of the potato tuber that ...
562-779 4.50e-21

Patatin-like phospholipase of bacteria; Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes subfamily of PNPLA8 (iPLA2-gamma) and PNPLA9 (iPLA2-beta) like phospholipases from human as well as the Pat17 isozyme from Solanum cardiophyllum.


Pssm-ID: 132854 [Multi-domain]  Cd Length: 329  Bit Score: 95.17  E-value: 4.50e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 562 RLLCLDGGGIRGL----VLVQMLLEIEKLSRTP---IIHMFDWIAGTSTGGILALALGC----GK---TMRQCMGLYLR- 626
Cdd:cd07215   1 RILSIDGGGIRGIipatILVSVEEKLQKKTGNPearLADYFDLVAGTSTGGILTCLYLCpnesGRpkfSAKEALNFYLEr 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 627 ----MKEQCF--VGSRP------YNSEFFESILKDNLGEFNvMTDIKHPKIMVTGVMADRKPvdlHLFRNYTsasdilGI 694
Cdd:cd07215  81 gnyiFKKKIWnkIKSRGgflnekYSHKPLEEVLLEYFGDTK-LSELLKPCLITSYDIERRSP---HFFKSHT------AI 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 695 VTPINNRripppqpseqLVWRAARATGAAPSYF-----RAFGR----FLDGGLIANNPTLDAMTEIheynMALRSAGRES 765
Cdd:cd07215 151 KNEQRDF----------YVRDVARATSAAPTYFepariHSLTGekytLIDGGVFANNPTLCAYAEA----RKLKFEQPGK 216
                       250
                ....*....|....
gi 45551542 766 EAIPVSVVMSLGTG 779
Cdd:cd07215 217 PTAKDMIILSLGTG 230
Pat17_PNPLA8_PNPLA9_like4 cd07217
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
562-850 9.88e-21

Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes subfamily of PNPLA8 (iPLA2-gamma) and PNPLA9 (iPLA2-beta) like phospholipases from human as well as the Pat17 isozyme from Solanum cardiophyllum.


Pssm-ID: 132856 [Multi-domain]  Cd Length: 344  Bit Score: 94.48  E-value: 9.88e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 562 RLLCLDGGGIRGLVLVQMLLEIEKLSRT----PIIHM---FDWIAGTSTGGILALALGCGKTMRQCMGLYLRMKEQCF-- 632
Cdd:cd07217   2 KILALDGGGIRGLLSVEILGRIEKDLRThlddPEFRLgdyFDFVGGTSTGSIIAACIALGMSVTDLLSFYTLNGVNMFdk 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 633 ------VGSRPYNSEFFESILKDNLGEFNVMTDIKHPKIMvTGVMAdrkpvdlhLFRNYTSASDilgivTPI-NNRR--- 702
Cdd:cd07217  82 awlaqrLFLNKLYNQYDPTNLGKKLNTVFPETTLGDDTLR-TLLMI--------VTRNATTGSP-----WPVcNNPEaky 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 703 --IPPPQPSEQL-VWRAARATGAAPSYF---------RAFGRFLDGGL-IANNPTLDA--MTEIHEYNMALRSaGRESea 767
Cdd:cd07217 148 ndSDRSDCNLDLpLWQLVRASTAAPTFFppevvsiapGTAFVFVDGGVtTYNNPAFQAflMATAKPYKLNWEV-GADN-- 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 768 ipvSVVMSLGTGHIPvtelKDIDVFRPESIWDTAKLAYGISTI---GNLLVDQ-----ATCSDGRVVDR-------ARAW 832
Cdd:cd07217 225 ---LLLVSVGTGFAP----EARPDLKAADMWALDHAKYIPSALmnaANAGQDMvcrvlGECRKGGLVDReigtmhvDPNW 297
                       330
                ....*....|....*...
gi 45551542 833 CSTIGIPYFRFNPQLSED 850
Cdd:cd07217 298 LGPKLFTYVRYDVSLSRS 315
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
564-748 1.42e-20

Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein but it also has the enzymatic activity of lipid acyl hydrolase, catalysing the cleavage of fatty acids from membrane lipids. Members of this family have been found also in vertebrates.


Pssm-ID: 396341  Cd Length: 190  Bit Score: 90.36  E-value: 1.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542   564 LCLDGGGIRGLVLVQMLLEIEKlsrtpIIHMFDWIAGTSTGGILALALGCGKTMRQCMGLYLRMKEQCFVgSRPYNSEFF 643
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGE-----AGIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFL-SLIRKRALS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542   644 ESILKDNLGEFNVMTDIKHPKIMVTGVMADRKPVDLH----LFRNYTSASDILGIVTPINNRRI---PPPQPSEQLVWRA 716
Cdd:pfam01734  75 LLALLRGLIGEGGLFDGDALRELLRKLLGDLTLEELAarlsLLLVVALRALLTVISTALGTRARillPDDLDDDEDLADA 154
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 45551542   717 ARATGAAPSYFRAF----GRFLDGGLIANNPTLDAM 748
Cdd:pfam01734 155 VLASSALPGVFPPVrldgELYVDGGLVDNVPVEAAL 190
PHA03100 PHA03100
ankyrin repeat protein; Provisional
199-417 1.75e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 85.87  E-value: 1.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  199 VFHYAASTTKEIINLIIDKSTVNLNHLNSDGY----TPLHVACLADKPENVKALLLAGANVNLNAKDIRKVY-------- 266
Cdd:PHA03100   1 LYSYIVLTKSRIIKVKNIKYIIMEDDLNDYSYkkpvLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsniky 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  267 -KTSAPTTVSSFLR--TNVSKLYtqdmKYGGTPLHWCSSRETLHALIME-----GCDVNATNFDGRTALHVMV------- 331
Cdd:PHA03100  81 nLTDVKEIVKLLLEygANVNAPD----NNGITPLLYAISKKSNSYSIVEylldnGANVNIKNSDGENLLHLYLesnkidl 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  332 --------------ARNRFECvvtLLAHDAEIDVLDKDGNAALHIAIEKKLVPIVQCLVVFGCDINLKNKDGKTPRHMvg 397
Cdd:PHA03100 157 kilkllidkgvdinAKNRVNY---LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHI-- 231
                        250       260
                 ....*....|....*....|
gi 45551542  398 ndASGNKDDEILYILHSVGA 417
Cdd:PHA03100 232 --AILNNNKEIFKLLLNNGP 249
PHA03095 PHA03095
ankyrin-like protein; Provisional
201-395 5.01e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.45  E-value: 5.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  201 HYAASTTKEIINLIIDKStVNLNHLNSDGYTPLHV-ACLADKPENVKALLLAGANVN---LNAKDIRKVYKTSA---PTT 273
Cdd:PHA03095  56 HYSSEKVKDIVRLLLEAG-ADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNakdKVGRTPLHVYLSGFninPKV 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  274 VSSFLRTNVSklyTQDMK-YGGTPLH-WCSSR----ETLHALIMEGCDVNATNFDGRTALHVM--VARNRFECVVTLLAH 345
Cdd:PHA03095 135 IRLLLRKGAD---VNALDlYGMTPLAvLLKSRnanvELLRLLIDAGADVYAVDDRFRSLLHHHlqSFKPRARIVRELIRA 211
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 45551542  346 DAEIDVLDKDGNAALHIA--IEKKLVPIVQCLVVFGCDINLKNKDGKTPRHM 395
Cdd:PHA03095 212 GCDPAATDMLGNTPLHSMatGSSCKRSLVLPLLIAGISINARNRYGQTPLHY 263
Ank_2 pfam12796
Ankyrin repeats (3 copies);
297-386 2.42e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.29  E-value: 2.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542   297 LHWCSSR---ETLHALIMEGCDVNATNFDGRTALHVMVARNRFECVVTLLAHdAEIDVLDkDGNAALHIAIEKKLVPIVQ 373
Cdd:pfam12796   1 LHLAAKNgnlELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 45551542   374 CLVVFGCDINLKN 386
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
193-395 2.61e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.14  E-value: 2.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  193 DINSNSVFHY---AASTTKEIINLIIDKSTvNLNHLNSDGYTPLHVaCLA----DKPENVKALLLAGANVnlNAKDIRKV 265
Cdd:PHA03095   9 IIMEAALYDYllnASNVTVEEVRRLLAAGA-DVNFRGEYGKTPLHL-YLHysseKVKDIVRLLLEAGADV--NAPERCGF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  266 -----YKTSAPT-TVSSFL-----RTNVSKlytqdmKYGGTPLHWCSSRETLH-----ALIMEGCDVNATNFDGRTALHV 329
Cdd:PHA03095  85 tplhlYLYNATTlDVIKLLikagaDVNAKD------KVGRTPLHVYLSGFNINpkvirLLLRKGADVNALDLYGMTPLAV 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  330 MVARNR--FECVVTLLAHDAEIDVLDKDGNAALHIAIE--KKLVPIVQCLVVFGCDINLKNKDGKTPRHM 395
Cdd:PHA03095 159 LLKSRNanVELLRLLIDAGADVYAVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHS 228
Ank_2 pfam12796
Ankyrin repeats (3 copies);
168-258 6.84e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.44  E-value: 6.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542   168 FQLAIKQGHMEMVKALLPL-SKLEHLDINSNSVFHYAAST-TKEIINLIIDKSTVNLNhlnSDGYTPLHVACLADKPENV 245
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENgADANLQDKNGRTALHLAAKNgHLEIVKLLLEHADVNLK---DNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|...
gi 45551542   246 KALLLAGANVNLN 258
Cdd:pfam12796  78 KLLLEKGADINVK 90
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
564-747 7.03e-12

Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes PNPLA (1-9), TGL (3-5), ExoU-like, and SDP1-like subfamilies. There are some additional hypothetical proteins included in this family.


Pssm-ID: 132837 [Multi-domain]  Cd Length: 172  Bit Score: 64.67  E-value: 7.03e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 564 LCLDGGGIRGLVLVQMLLEIEKlsRTPIIHMfdwIAGTSTGGILALALGCGKTMRQCMGLYLRMKEqcfvGSRPYNSEFF 643
Cdd:cd07198   1 LVLSGGGALGIYHVGVAKALRE--RGPLIDI---IAGTSAGAIVAALLASGRDLEEALLLLLRLSR----EVRLRFDGAF 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 644 EsilkdnlGEFNVMTDIKHPkiMVTGVMADRKPVDLH-LFRNYTSASDIlgivtpinnRRIPPPQPSEQLVWRAARATGA 722
Cdd:cd07198  72 P-------PTGRLLGILRQP--LLSALPDDAHEDASGkLFISLTRLTDG---------ENVLVSDTSKGELWSAVRASSS 133
                       170       180       190
                ....*....|....*....|....*....|.
gi 45551542 723 APSYFRAF-----G-RFLDGGLIANNPTLDA 747
Cdd:cd07198 134 IPGYFGPVplsfrGrRYGDGGLSNNLPVAEL 164
PHA03095 PHA03095
ankyrin-like protein; Provisional
193-392 1.06e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.13  E-value: 1.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  193 DINSNSV-----FHYAA--STTKEIINLIIDKStVNLNHLNSDGYTPLHVaCLADK---PENVKALLLAGANVNlnAKDi 262
Cdd:PHA03095  75 DVNAPERcgftpLHLYLynATTLDVIKLLIKAG-ADVNAKDKVGRTPLHV-YLSGFninPKVIRLLLRKGADVN--ALD- 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  263 rkvykTSAPTTVSSFLR-TNVS------------KLYTQDMkYGGTPLH----WCSSRET-LHALIMEGCDVNATNFDGR 324
Cdd:PHA03095 150 -----LYGMTPLAVLLKsRNANvellrllidagaDVYAVDD-RFRSLLHhhlqSFKPRARiVRELIRAGCDPAATDMLGN 223
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  325 TALHVMVA--RNRFECVVTLLAHDAEIDVLDKDGNAALHIAIEKKLVPIVQCLVVFGCDINLKNKDGKTP 392
Cdd:PHA03095 224 TPLHSMATgsSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293
PHA02876 PHA02876
ankyrin repeat protein; Provisional
165-394 2.05e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.78  E-value: 2.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  165 MSPFQLAIKQGHMEMVKALLPL-SKLEHLDINSNSVFHYAA-STTKEIINLIID-KSTVNLNHL-------NSD------ 228
Cdd:PHA02876 179 ITPIHYAAERGNAKMVNLLLSYgADVNIIALDDLSVLECAVdSKNIDTIKAIIDnRSNINKNDLsllkairNEDletsll 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  229 ----GY----------TPLHVACLADKPEN-VKALLLAGANVNlnAKDIR---KVYKTSAPTTVSSFLRTNVSK---LYT 287
Cdd:PHA02876 259 lydaGFsvnsiddcknTPLHHASQAPSLSRlVPKLLERGADVN--AKNIKgetPLYLMAKNGYDTENIRTLIMLgadVNA 336
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  288 QDMKYGgTPLHWCSS----RETLHALIMEGCDVNATNFDGRTALHVMVARNRFECVVTLLAHDAEIDVLDKDGNAALHIA 363
Cdd:PHA02876 337 ADRLYI-TPLHQASTldrnKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA 415
                        250       260       270
                 ....*....|....*....|....*....|..
gi 45551542  364 I-EKKLVPIVQCLVVFGCDINLKNKDGKTPRH 394
Cdd:PHA02876 416 LcGTNPYMSVKTLIDRGANVNSKNKDLSTPLH 447
PHA02878 PHA02878
ankyrin repeat protein; Provisional
209-417 2.16e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.21  E-value: 2.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  209 EIINLIIDKStVNLNHLNSDGYTPLHVACLADKPENVKALL--LAGANVNLNAKDIRKVYKTSAPTTVSSFLRTNVSKLY 286
Cdd:PHA02878  51 DVVKSLLTRG-HNVNQPDHRDLTPLHIICKEPNKLGMKEMIrsINKCSVFYTLVAIKDAFNNRNVEIFKIILTNRYKNIQ 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  287 TQDMKYGGTPLHWCSSRETLHALIME-GCDVNATNFD-GRTALHVMVARNRFECVVTLLAHDAEIDVLDKDGNAALHIAI 364
Cdd:PHA02878 130 TIDLVYIDKKSKDDIIEAEITKLLLSyGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAV 209
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 45551542  365 EKKLVPIVQCLVVFGCDINLKNKDGKTPRHMvgndASGN-KDDEILYILHSVGA 417
Cdd:PHA02878 210 KHYNKPIVHILLENGASTDARDKCGNTPLHI----SVGYcKDYDILKLLLEHGV 259
PHA02874 PHA02874
ankyrin repeat protein; Provisional
167-392 2.75e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.53  E-value: 2.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  167 PFQLAIKQGHMEMVKALL----PLSKLEHLDINsnsvfhyaasttKEIINLIIDkSTVNLNHLNSDGYTPLHVACLADKP 242
Cdd:PHA02874  71 PLLTAIKIGAHDIIKLLIdngvDTSILPIPCIE------------KDMIKTILD-CGIDVNIKDAELKTFLHYAIKKGDL 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  243 ENVKALLLAGANVNLnaKDIRKVYKTSAPTTVSSF-----LRTNVSKLYTQDmKYGGTPLHWCSSR---ETLHALIMEGC 314
Cdd:PHA02874 138 ESIKMLFEYGADVNI--EDDNGCYPIHIAIKHNFFdiiklLLEKGAYANVKD-NNGESPLHNAAEYgdyACIKLLIDHGN 214
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45551542  315 DVNATNFDGRTALHVMVARNRfeCVVTLLAHDAEIDVLDKDGNAALHIAIEKKL-VPIVQCLVVFGCDINLKNKDGKTP 392
Cdd:PHA02874 215 HIMNKCKNGFTPLHNAIIHNR--SAIELLINNASINDQDIDGSTPLHHAINPPCdIDIIDILLYHKADISIKDNKGENP 291
Pat17_isozyme_like cd07214
Patatin-like phospholipase of plants; Pat17 is an isozyme of patatin cloned from Solanum ...
563-779 7.31e-11

Patatin-like phospholipase of plants; Pat17 is an isozyme of patatin cloned from Solanum cardiophyllum. Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue, and Nu = nucleophile). Patatin-like phospholipase are included in this group. Members of this family have also been found in vertebrates.


Pssm-ID: 132853 [Multi-domain]  Cd Length: 349  Bit Score: 64.77  E-value: 7.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 563 LLCLDGGGIRGLVLVQMLLEIE-KL-----SRTPIIHMFDWIAGTSTGGILALALG----------------------CG 614
Cdd:cd07214   6 VLSIDGGGIRGIIPATILEFLEgKLqeldgPDARIADYFDVIAGTSTGGLITAMLTapnenkrplfaakdivqfylenGP 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 615 KTMRQCMGLY--LRMKEQCFVGSRpYNSEFFESILKDNLGEFNVmTDIKHPKIMVTGVMADRKPVdlhLFRNYTSASDil 692
Cdd:cd07214  86 KIFPQSTGQFedDRKKLRSLLGPK-YDGVYLHDLLNELLGDTRL-SDTLTNVVIPTFDIKLLQPV---IFSSSKAKND-- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 693 givtPINNRRIpppqpseqlvWRAARATGAAPSYFRAFgRF--------------LDGGLIANNPTLDAMTEIheYNMAL 758
Cdd:cd07214 159 ----KLTNARL----------ADVCISTSAAPTYFPAH-YFttedsngdirefnlVDGGVAANNPTLLAISEV--TKEII 221
                       250       260
                ....*....|....*....|....*
gi 45551542 759 RSAGRESEAIPVS----VVMSLGTG 779
Cdd:cd07214 222 KDNPFFASIKPLDykklLVLSLGTG 246
PHA02874 PHA02874
ankyrin repeat protein; Provisional
300-394 2.10e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.83  E-value: 2.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  300 CSSRETLHALIMEGCDVNATNFDGRTALHVMVARNRFECVVTLLAHDAEIDVLDKDGNAALHIAIEKKLVPIVQCLVVFG 379
Cdd:PHA02874 101 CIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG 180
                         90
                 ....*....|....*
gi 45551542  380 CDINLKNKDGKTPRH 394
Cdd:PHA02874 181 AYANVKDNNGESPLH 195
PHA02876 PHA02876
ankyrin repeat protein; Provisional
165-394 4.50e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.54  E-value: 4.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  165 MSPFQLAIKQGHMEMVKALLPlsklEHLDINSNSVF-----HYAAST-TKEIINLIIDKSTvNLNHLNSDGYTPLHVACL 238
Cdd:PHA02876 146 MKLIKERIQQDELLIAEMLLE----GGADVNAKDIYcitpiHYAAERgNAKMVNLLLSYGA-DVNIIALDDLSVLECAVD 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  239 ADKPENVKALLLAGANVNLNakDIRKVYKTSAPTTVSSFLRTNVSKLYTQDMKYGGTPLHWCSSRETLHALIME----GC 314
Cdd:PHA02876 221 SKNIDTIKAIIDNRSNINKN--DLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKllerGA 298
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  315 DVNATNFDGRTALHVMvARNRF--ECVVTLLAHDAEIDVLDKDGNAALHIAIE-KKLVPIVQCLVVFGCDINLKNKDGKT 391
Cdd:PHA02876 299 DVNAKNIKGETPLYLM-AKNGYdtENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKT 377

                 ...
gi 45551542  392 PRH 394
Cdd:PHA02876 378 PIH 380
PHA03100 PHA03100
ankyrin repeat protein; Provisional
165-383 2.10e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.45  E-value: 2.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  165 MSPFQLAIKQGHMEMVKALLPLSKLEHLDINSNSVF-HYAASTT------KEIINLIIdKSTVNLNHLNSDGYTPLHVAC 237
Cdd:PHA03100  36 VLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPlHYLSNIKynltdvKEIVKLLL-EYGANVNAPDNNGITPLLYAI 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  238 LADK--PENVKALLLAGANVNLNAKD---IRKVYkTSAPTTVSSFLRTNVSKLYTQDMKyggtplhwcssrETLHALIME 312
Cdd:PHA03100 115 SKKSnsYSIVEYLLDNGANVNIKNSDgenLLHLY-LESNKIDLKILKLLIDKGVDINAK------------NRVNYLLSY 181
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45551542  313 GCDVNATNFDGRTALHVMVARNRFECVVTLLAHDAEIDVLDKDGNAALHIAIEKKLVPIVQCLVVFGCDIN 383
Cdd:PHA03100 182 GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02874 PHA02874
ankyrin repeat protein; Provisional
209-394 8.76e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.82  E-value: 8.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  209 EIINLIIdKSTVNLNHLNSDGYTPLHVACLADKPENVKALLLAGANVN-LNAKDIRKvyktsapTTVSSFLRTNVsKLYT 287
Cdd:PHA02874  49 KIVELFI-KHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSiLPIPCIEK-------DMIKTILDCGI-DVNI 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  288 QDMKYGgTPLHWCSSR---ETLHALIMEGCDVNATNFDGRTALHVMVARNRFECVVTLLAHDAEIDVLDKDGNAALHIAI 364
Cdd:PHA02874 120 KDAELK-TFLHYAIKKgdlESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAA 198
                        170       180       190
                 ....*....|....*....|....*....|
gi 45551542  365 EKKLVPIVQCLVVFGCDINLKNKDGKTPRH 394
Cdd:PHA02874 199 EYGDYACIKLLIDHGNHIMNKCKNGFTPLH 228
Ank_2 pfam12796
Ankyrin repeats (3 copies);
327-412 2.33e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.04  E-value: 2.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542   327 LHVMVARNRFECVVTLLAHDAEIDVLDKDGNAALHIAIEKKLVPIVQCLVVFgCDINLKNkDGKTPRHMvgndASGNKDD 406
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHY----AARSGHL 74

                  ....*.
gi 45551542   407 EILYIL 412
Cdd:pfam12796  75 EIVKLL 80
Ank_2 pfam12796
Ankyrin repeats (3 copies);
200-320 6.56e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.88  E-value: 6.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542   200 FHYAASTTK-EIINLIIDKStVNLNHLNSDGYTPLHVACLADKPENVKALLlagANVNLNAKDirkvyktsapttvssfl 278
Cdd:pfam12796   1 LHLAAKNGNlELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLL---EHADVNLKD----------------- 59
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 45551542   279 rtnvsklytqdmkYGGTPLHWCS---SRETLHALIMEGCDVNATN 320
Cdd:pfam12796  60 -------------NGRTALHYAArsgHLEIVKLLLEKGADINVKD 91
Ank_5 pfam13857
Ankyrin repeats (many copies);
314-363 6.81e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.65  E-value: 6.81e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 45551542   314 CDVNATNFDGRTALHVMVARNRFECVVTLLAHDAEIDVLDKDGNAALHIA 363
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
564-744 1.02e-07

ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is a potent virulence factor of Pseudomonas aeruginosa. One of the pathogenic mechanisms of P. aeruginosa is to induce cytotoxicity by the injection of effector proteins (e.g. ExoU) using the type III secretion (T3S) system. ExoU is homologus to patatin and also has the conserved catalytic residues of mammalian calcium-independent (iPLA2) and cytosolic (cPLA2) PLA2. In vitro, ExoU cytotoxity is blocked by the inhibitor of cytosolic and Ca2-independent phospholipase A2 (cPLA2 and iPLA2) enzymes, suggesting that phospholipase A2 inhibitors may represent a novel mode of treatment for acute P. aeruginosa infections. ExoU requires eukaryotic superoxide dismutase as a cofactor and cleaves phosphatidylcholine and phosphatidylethanolamine in vitro. VipD, a 69-kDa cytosolic protein, belongs to the members of Legionella pneumophila family and is homologus to ExoU from Pseudomonas. Even though VipD shows high sequence similarity with several functional regions of ExoU (e.g. oxyanion hole, active site serine, active site aspartate), it has been shown to have no phospholipase activity. This family includes ExoU from Pseudomonas aeruginosa and VipD of Legionella pneumophila.


Pssm-ID: 132846  Cd Length: 194  Bit Score: 53.05  E-value: 1.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 564 LCLDGGGIRGLVLVQMLleiEKLSRTPIihMFDWIAGTSTGGILA--LALGC-GKTMRQcmgLYLRMKEQCFVGSRP--- 637
Cdd:cd07207   2 LVFEGGGAKGIAYIGAL---KALEEAGI--LKKRVAGTSAGAITAalLALGYsAADIKD---ILKETDFAKLLDSPVgll 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 638 ------------YNSEFFESILKDNLGEFNVMTDIKHpkimVTGVMADRKPVDLHLfrnytsasdilgIVTPINNRRI-- 703
Cdd:cd07207  74 fllpslfkegglYKGDALEEWLRELLKEKTGNSFATS----LLRDLDDDLGKDLKV------------VATDLTTGALvv 137
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 45551542 704 -PPPQPSEQLVWRAARATGAAPSYFRA--FGR---FLDGGLIANNPT 744
Cdd:cd07207 138 fSAETTPDMPVAKAVRASMSIPFVFKPvrLAKgdvYVDGGVLDNYPV 184
PHA02875 PHA02875
ankyrin repeat protein; Provisional
218-389 1.16e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.00  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  218 STVNLNHLNSDGYTPLHVACLADKPENVKALLLAGANVNLNAKDIR-KVYKTSAPTTVSSFLRTNVSKLYTQDMKY--GG 294
Cdd:PHA02875  24 IGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIEsELHDAVEEGDVKAVEELLDLGKFADDVFYkdGM 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  295 TPLHWCS---SRETLHALIMEGCDVNATNFDGRTALHVMVARNRFECVVTLLAHDAEIDVLDKDGNAALHIAIEKKLVPI 371
Cdd:PHA02875 104 TPLHLATilkKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183
                        170
                 ....*....|....*...
gi 45551542  372 VQCLVVFGCDINLKNKDG 389
Cdd:PHA02875 184 CKMLLDSGANIDYFGKNG 201
Ank_4 pfam13637
Ankyrin repeats (many copies);
323-376 1.17e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 1.17e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 45551542   323 GRTALHVMVARNRFECVVTLLAHDAEIDVLDKDGNAALHIAIEKKLVPIVQCLV 376
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
342-396 1.47e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 1.47e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 45551542   342 LLAHD-AEIDVLDKDGNAALHIAIEKKLVPIVQCLVVFGCDINLKNKDGKTPRHMV 396
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
205-363 1.60e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.56  E-value: 1.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  205 STTKEIINLIIDKStVNLNHLNSDGYTPLHV------ACladkPENVKALLLAGANVnLNAKDIRKV--------YKTSA 270
Cdd:PHA03095 129 NINPKVIRLLLRKG-ADVNALDLYGMTPLAVllksrnAN----VELLRLLIDAGADV-YAVDDRFRSllhhhlqsFKPRA 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  271 ------------PTTVSSFLRTNVSKLYTQDM--------------------KYGGTPLHWCSSRETLHA---LIMEGCD 315
Cdd:PHA03095 203 rivreliragcdPAATDMLGNTPLHSMATGSSckrslvlplliagisinarnRYGQTPLHYAAVFNNPRAcrrLIALGAD 282
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 45551542  316 VNATNFDGRTALHVMVARNRFECVVTLLAHDAEIDVLDkdgnAALHIA 363
Cdd:PHA03095 283 INAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA----ATLNTA 326
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
309-375 2.54e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 2.54e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45551542  309 LIMEGCDVNATNFDGRTALHVMVARNRFECVVTLLAHDAEIDVLDKDGNAALHIAIEKKLVPIVQCL 375
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
564-743 2.55e-06

Predicted acylesterase/phospholipase RssA, containd patatin domain [General function prediction only];


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 49.90  E-value: 2.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 564 LCLDGGGIRGLVLVQMLLEIEKLSrtpiIHmFDWIAGTSTGGILALALGCGKTMRQcmglyLRmkeqcfvgsrpynsEFF 643
Cdd:COG1752   9 LVLSGGGARGAAHIGVLKALEEAG----IP-PDVIAGTSAGAIVGALYAAGYSADE-----LE--------------ELW 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 644 ESILKDNLGEFNVMTDIKHPKIMVTGV-MADRKPVdLHLFRNYTSASDIlgivtpinnRRIPPP-----------QP--- 708
Cdd:COG1752  65 RSLDRRDLFDLSLPRRLLRLDLGLSPGgLLDGDPL-RRLLERLLGDRDF---------EDLPIPlavvatdletgREvvf 134
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 45551542 709 SEQLVWRAARATGAAPSYFRAF---GRFL-DGGLIANNP 743
Cdd:COG1752 135 DSGPLADAVRASAAIPGVFPPVeidGRLYvDGGVVNNLP 173
Ank_4 pfam13637
Ankyrin repeats (many copies);
293-343 8.32e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 8.32e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 45551542   293 GGTPLHWCSSR---ETLHALIMEGCDVNATNFDGRTALHVMVARNRFECVVTLL 343
Cdd:pfam13637   1 ELTALHAAAASghlELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
214-257 4.13e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 4.13e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 45551542   214 IIDKSTVNLNHLNSDGYTPLHVACLADKPENVKALLLAGANVNL 257
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNL 44
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
306-367 6.40e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.78  E-value: 6.40e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45551542  306 LHALIMEGCDVNATNFDGRTALHVMVARNRFECVVTLLAHDAEIDVLDKDGNAALHIAIEKK 367
Cdd:PLN03192 541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAK 602
PHA02878 PHA02878
ankyrin repeat protein; Provisional
245-396 7.34e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.41  E-value: 7.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  245 VKALLLAGANVNLNAKDIRKV---YKTSAPTT-VSSFLRTNVSKLYTQDmKYGGTPLHWC---SSRETLHALIMEGCDVN 317
Cdd:PHA02878 150 TKLLLSYGADINMKDRHKGNTalhYATENKDQrLTELLLSYGANVNIPD-KTNNSPLHHAvkhYNKPIVHILLENGASTD 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  318 ATNFDGRTALHVMVAR-NRFECVVTLLAHDAEIDVLDK-DGNAALHIAI--EKKLvpivQCLVVFGCDINLKNKDGKTPR 393
Cdd:PHA02878 229 ARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIksERKL----KLLLEYGADINSLNSYKLTPL 304

                 ...
gi 45551542  394 HMV 396
Cdd:PHA02878 305 SSA 307
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
102-366 2.74e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 44.69  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542   102 RLPVFVSIVKEYYNVNGLQKACDALADNPSWTLShliayfnlvDYISNPKMLQ--CVDQADAATLmspFQLAIKQGHMEM 179
Cdd:TIGR00870   1 RGPLDIVPAEESPLSDEEKAFLPAAERGDLASVY---------RDLEEPKKLNinCPDRLGRSAL---FVAAIENENLEL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542   180 VKALLPLSKLEHLdinSNSVFHYAASTTKEIINLII------DKSTVNLNHLN-------SDGYTPLHVACLADKPENVK 246
Cdd:TIGR00870  69 TELLLNLSCRGAV---GDTLLHAISLEYVDAVEAILlhllaaFRKSGPLELANdqytsefTPGITALHLAAHRQNYEIVK 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542   247 ALLLAGANVNLNAkdirkvyktsaptTVSSFLRTNvsklYTQDMKYGGTPLHW--CSSRETLHALIME-GCDVNATNFDG 323
Cdd:TIGR00870 146 LLLERGASVPARA-------------CGDFFVKSQ----GVDSFYHGESPLNAaaCLGSPSIVALLSEdPADILTADSLG 208
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 45551542   324 RTALH--VMVARNRFE-------CVVTLLAHDAEID-------VLDKDGNAALHIAIEK 366
Cdd:TIGR00870 209 NTLLHllVMENEFKAEyeelscqMYNFALSLLDKLRdskelevILNHQGLTPLKLAAKE 267
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
166-376 3.08e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 44.62  E-value: 3.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 166 SPFQLAIKQGHMEMVKALLplsKLEHLDINS-----NSVFHYAASTTK-EIINLIIDKSTVNLNH-LNSD---GYTPLHV 235
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLL---KCPSCDLFQrgalgETALHVAALYDNlEAAVVLMEAAPELVNEpMTSDlyqGETALHI 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 236 ACLADKPENVKALLLAGANVNlnakdirkvyktSAPTTVSSFLRTNVSKLYtqdmkYGGTPLHW--C-SSRETLHALIME 312
Cdd:cd22192  96 AVVNQNLNLVRELIARGADVV------------SPRATGTFFRPGPKNLIY-----YGEHPLSFaaCvGNEEIVRLLIEH 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45551542 313 GCDVNATNFDGRTALHVMV--ARNRFECVV--TLLAHDAEID------VLDKDGNAALHIAIEKKLVPIVQCLV 376
Cdd:cd22192 159 GADIRAQDSLGNTVLHILVlqPNKTFACQMydLILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNIVMFQHLV 232
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
342-403 3.46e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.50  E-value: 3.46e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45551542  342 LLAHDAEIDVLDKDGNAALHIAIEKKLVPIVQCLVVFGCDINLKNKDGKTPRHMVGNDASGN 403
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFRE 162
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
228-257 4.14e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 4.14e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 45551542    228 DGYTPLHVACLADKPENVKALLLAGANVNL 257
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
228-256 4.18e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.39  E-value: 4.18e-04
                          10        20
                  ....*....|....*....|....*....
gi 45551542   228 DGYTPLHVACLADKPENVKALLLAGANVN 256
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
228-257 4.49e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 4.49e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 45551542   228 DGYTPLHVACL-ADKPENVKALLLAGANVNL 257
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNA 31
PHA02875 PHA02875
ankyrin repeat protein; Provisional
322-395 5.53e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.44  E-value: 5.53e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45551542  322 DGRTALHVMVARNRFECVVTLLAHDAEI-DVLDKDGNAALHIAIEKKLVPIVQCLVVFGCDINLKNKDGKTPRHM 395
Cdd:PHA02875  67 DIESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHL 141
PHA02876 PHA02876
ankyrin repeat protein; Provisional
207-382 9.68e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.74  E-value: 9.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  207 TKEIINLIIDKSTVNLNhlNSDGYTPLHVACLADKPEN-VKALLLAGANVNlnAKDirkvYKTSAPTTVSSfLRTNVSKL 285
Cdd:PHA02876 321 TENIRTLIMLGADVNAA--DRLYITPLHQASTLDRNKDiVITLLELGANVN--ARD----YCDKTPIHYAA-VRNNVVII 391
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  286 YTQdMKYG----------GTPLHWC----SSRETLHALIMEGCDVNATNFDGRTALHVMVARN-RFECVVTLLAHDAEID 350
Cdd:PHA02876 392 NTL-LDYGadiealsqkiGTALHFAlcgtNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVN 470
                        170       180       190
                 ....*....|....*....|....*....|..
gi 45551542  351 VLDKDGNAALHIAIEKKlvPIVQCLVVFGCDI 382
Cdd:PHA02876 471 AINIQNQYPLLIALEYH--GIVNILLHYGAEL 500
PHA02876 PHA02876
ankyrin repeat protein; Provisional
166-266 1.12e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.74  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  166 SPFQLAIKQGHMEMVKALLPL-SKLEHLDINSNSVFHYAASTTKEIINL--IIDKSTvNLNHLNSDGYTPLHVACLAD-K 241
Cdd:PHA02876 377 TPIHYAAVRNNVVIINTLLDYgADIEALSQKIGTALHFALCGTNPYMSVktLIDRGA-NVNSKNKDLSTPLHYACKKNcK 455
                         90       100
                 ....*....|....*....|....*
gi 45551542  242 PENVKALLLAGANVnlNAKDIRKVY 266
Cdd:PHA02876 456 LDVIEMLLDNGADV--NAINIQNQY 478
PHA02798 PHA02798
ankyrin-like protein; Provisional
309-386 1.66e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.13  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  309 LIMEGCDVNATNFDGRTALHVMVAR---NRFECVVTLLAHDAEIDVLDKDGNAALHIAIEKKL---VPIVQCLVVFGCDI 382
Cdd:PHA02798  95 LIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDI 174

                 ....
gi 45551542  383 NLKN 386
Cdd:PHA02798 175 NTHN 178
PHA02878 PHA02878
ankyrin repeat protein; Provisional
156-331 1.79e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.79  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  156 VDQADAATLMSPFQLAIKQGHMEMVKALLPL-SKLEHLDINSNSVFHYAASTTKEIINLIIDKSTVNLNHLNSDGYTPLH 234
Cdd:PHA02878 160 INMKDRHKGNTALHYATENKDQRLTELLLSYgANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  235 VACLADKPENV-KALLLAGANVNlnakdirkvyktsapttVSSFLRtnvsklytqdmkyGGTPLHWCSSRETLHALIME- 312
Cdd:PHA02878 240 ISVGYCKDYDIlKLLLEHGVDVN-----------------AKSYIL-------------GLTALHSSIKSERKLKLLLEy 289
                        170
                 ....*....|....*....
gi 45551542  313 GCDVNATNFDGRTALHVMV 331
Cdd:PHA02878 290 GADINSLNSYKLTPLSSAV 308
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
158-350 2.51e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 2.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  158 QADAATLMSPFQlaikQGHMEM----VKALLPLSKLEHLDINSNSVFHYAASTTKEIINLIIDKSTVNLNHLNSDGYTPL 233
Cdd:PLN03192 487 QEDNVVILKNFL----QHHKELhdlnVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPL 562
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542  234 HVACLADKPENVKALLLAGANVNLnaKDIRKvyKTSAPTTVSSFLRTNVSKLY----TQDMKYGGTPLHWCSSR---ETL 306
Cdd:PLN03192 563 HIAASKGYEDCVLVLLKHACNVHI--RDANG--NTALWNAISAKHHKIFRILYhfasISDPHAAGDLLCTAAKRndlTAM 638
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 45551542  307 HALIMEGCDVNATNFDGRTALHVMVARNRFECVVTLLAHDAEID 350
Cdd:PLN03192 639 KELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVD 682
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
322-354 3.51e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 3.51e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 45551542   322 DGRTALHVMVAR-NRFECVVTLLAHDAEIDVLDK 354
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
197-249 4.93e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 4.93e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 45551542   197 NSVFHYAASTTK-EIINLIIDKStVNLNHLNSDGYTPLHVACLADKPENVKALL 249
Cdd:pfam13637   2 LTALHAAAASGHlELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
564-743 5.91e-03

Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase similar to Z1214 protein of Escherichia coli. This family predominantly consists of bacterial patatin glycoproteins and some representatives from eukaryotes and archaea. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates.


Pssm-ID: 132848 [Multi-domain]  Cd Length: 215  Bit Score: 39.20  E-value: 5.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 564 LCLDGGGIRG-------LVLVQMLLEieklsrtpiihmFDWIAGTSTGGILALALGCGKTMR--QCMGLYLRMKeqcfvg 634
Cdd:cd07209   1 LVLSGGGALGayqagvlKALAEAGIE------------PDIISGTSIGAINGALIAGGDPEAveRLEKLWRELS------ 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551542 635 srpYNSEFFESILKDNLGeFNVMTDIKHPKIMVTGVMADRKPVDLHLFRNytsasdilgivtpINNRRIPPpqpseqlvw 714
Cdd:cd07209  63 ---REDVFLRGLLDRALD-FDTLRLLAILFAGLVIVAVNVLTGEPVYFDD-------------IPDGILPE--------- 116
                       170       180       190
                ....*....|....*....|....*....|...
gi 45551542 715 rAARATGAAPSYFRAF---GR-FLDGGLIANNP 743
Cdd:cd07209 117 -HLLASAALPPFFPPVeidGRyYWDGGVVDNTP 148
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
355-387 7.72e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 7.72e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 45551542   355 DGNAALHIAIEK-KLVPIVQCLVVFGCDINLKNK 387
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
322-351 8.71e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.49  E-value: 8.71e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 45551542    322 DGRTALHVMVARNRFECVVTLLAHDAEIDV 351
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
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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