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Conserved domains on  [gi|1622838064|ref|XP_028683552|]
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85/88 kDa calcium-independent phospholipase A2 isoform X5 [Macaca mulatta]

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 ...
 254-566 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: 551.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 254 LLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHGKSMAYMRGVYFRMKDEVFRGSRPYESGP 333
Cdd:cd07212     1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGSRPYNSEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 334 LEEFLKREFGEHTKMTDVKKPKVMLTGTLSDRQPAELHLFRNYDAPETVREPRFNqnVNLRPPAQPSDQLVWRAARSSGA 413
Cdd:cd07212    81 LEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEEPEKN--ANFLPPTDPAEQLLWRAARSSGA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 414 APTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAK 493
Cdd:cd07212   159 APTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKSKGRKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSNPWELAK 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622838064 494 TVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVNALWETEVYIYEH 566
Cdd:cd07212   239 TVFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTH 311
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-177 1.43e-29

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.13  E-value: 1.43e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  53 IHSKDpRYGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADAHGEHGNTPLH 129
Cdd:COG0666   113 VNARD-KDGETPLHLAaynGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLH 191

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622838064 130 LAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKISRLDTRKAIL 177
Cdd:COG0666   192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
 
Name Accession Description Interval E-value
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
 254-566 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: 551.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 254 LLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHGKSMAYMRGVYFRMKDEVFRGSRPYESGP 333
Cdd:cd07212     1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGSRPYNSEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 334 LEEFLKREFGEHTKMTDVKKPKVMLTGTLSDRQPAELHLFRNYDAPETVREPRFNqnVNLRPPAQPSDQLVWRAARSSGA 413
Cdd:cd07212    81 LEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEEPEKN--ANFLPPTDPAEQLLWRAARSSGA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 414 APTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAK 493
Cdd:cd07212   159 APTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKSKGRKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSNPWELAK 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622838064 494 TVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVNALWETEVYIYEH 566
Cdd:cd07212   239 TVFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTH 311
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 244-545 2.08e-41

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 151.21  E-value: 2.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 244 MRDEKRTHdhLLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHGKSMAYMRGVYFRMKDEVF 323
Cdd:COG3621     1 MSANKPFR--ILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAAGYSAEEILDLYEEEGKEIF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 324 RGSRP-------------YESGPLEEFLKREFGEhTKMTDVKKPkVMLTGT-LSDRQPaelHLFRNYDAPetvreprFNQ 389
Cdd:COG3621    79 PKSRWrkllslrglfgpkYDSEGLEKVLKEYFGD-TTLGDLKTP-VLIPSYdLDNGKP---VFFKSPHAK-------FDR 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 390 NVNLrppaqpsdqLVWRAARSSGAAPTYFRP---------NGRFLDGGLLANNPTLDAMTE-IHEYNQDL--IRkgqank 457
Cdd:COG3621   147 DRDF---------LLVDVARATSAAPTYFPPaqiknltgeGYALIDGGVFANNPALCALAEaLKLLGPDLddIL------ 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 458 vkklsiVVSLGTGRSPQvpvtcvdvfrpSNPWELAKTvFGAKELGKMVVDCCTDPDGRAVDrarAWCEMV-GIQYFRLNP 536
Cdd:COG3621   212 ------VLSLGTGTAPR-----------SIPYKKVKN-WGALGWLLPLIDILMDAQSDAVD---YQLRQLlGDRYYRLDP 270


                  ....*....
gi 1622838064 537 QLGTDIMLD 545
Cdd:COG3621   271 ELPEEIALD 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-177 1.43e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.13  E-value: 1.43e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  53 IHSKDpRYGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADAHGEHGNTPLH 129
Cdd:COG0666   113 VNARD-KDGETPLHLAaynGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLH 191

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622838064 130 LAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKISRLDTRKAIL 177
Cdd:COG0666   192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 255-439 1.28e-19

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: 86.89  E-value: 1.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 255 LCLDGGGVKGLIiiqlliaiekASGVA-----TKDLFDWVAGTSTGGILALAILHGKSMAYMRGVYFRMKDEVFRGSRP- 328
Cdd:pfam01734   1 LVLSGGGARGAY----------HLGVLkalgeAGIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRk 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 329 ------------------YESGPLEEFLKREFGEHTKMTDVKKPKVMLTGTLSDRqpaelhlfrnydaPETVREPRFNQN 390
Cdd:pfam01734  71 ralsllallrgligegglFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRAL-------------LTVISTALGTRA 137

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622838064 391 VNLRPPAQPSDQLVWRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAM 439
Cdd:pfam01734 138 RILLPDDLDDDEDLADAVLASSALPGVFPPvrldGELYVDGGLVDNVPVEAAL 190
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
253-463 1.30e-18

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 86.78  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 253 HLLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHGKSMAYMRGVYFRMKDEVFRGSR----- 327
Cdd:NF041079    2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILALALALEIPARELVELFEEHGKDIFPKRKwprrl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 328 -------PYESGPLEEFLKREFGEhTKMTDVKKPKVMLTGTLSDRQPaelHLFRnydapeTVREPRFNQNVNLRppaqps 400
Cdd:NF041079   82 lgllkkpKYSSEPLREVLEEIFGD-KTIGDLKHRVLIPAVNYTTGKP---QVFK------TPHHPDFTRDHKLK------ 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622838064 401 dqLVwRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAMTEIHEY-NQdlirkgQANKVKKLSI 463
Cdd:NF041079  146 --LV-DVALATSAAPTYFPLhefdNEQFVDGGLVANNPGLLGLHEALHFlGV------PYDDVRILSI 204
Ank_2 pfam12796
Ankyrin repeats (3 copies);
65-154 1.17e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 1.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  65 LHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHgANADAhGEHGNTPLHLAMSKDNVEMIK 141
Cdd:pfam12796   1 LHLAaknGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNL-KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1622838064 142 ALIVFGAEVDTPN 154
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 59-177 7.56e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 79.71  E-value: 7.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  59 RYGASPLHWA-----KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIV------------------LLTHGA 115
Cdd:PHA03100  104 NNGITPLLYAiskksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILkllidkgvdinaknrvnyLLSYGV 183

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622838064 116 NADAHGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKISRLDTRKAIL 177
Cdd:PHA03100  184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 73-153 3.88e-09

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: 59.26  E-value: 3.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  73 MARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHG---ANADAHGE--HGNTPLHLAMSKDNVEMIKALIVFG 147
Cdd:cd22192    33 IKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelVNEPMTSDlyQGETALHIAVVNQNLNLVRELIARG 112


                  ....*.
gi 1622838064 148 AEVDTP 153
Cdd:cd22192   113 ADVVSP 118
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 123-151 2.50e-05

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: 41.42  E-value: 2.50e-05
                           10        20
                   ....*....|....*....|....*....
gi 1622838064  123 HGNTPLHLAMSKDNVEMIKALIVFGAEVD 151
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 50-150 8.09e-05

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: 45.46  E-value: 8.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  50 SSQIHSKDPrYGASPLHWA----KNAEMARMLLKRGCNVnstsSAGNTALHVAVMR---NRFDCAIVLLTHG-------- 114
Cdd:TIGR00870  42 KLNINCPDR-LGRSALFVAaienENLELTELLLNLSCRG----AVGDTLLHAISLEyvdAVEAILLHLLAAFrksgplel 116

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1622838064 115 ANADAHGE--HGNTPLHLAMSKDNVEMIKALIVFGAEV 150
Cdd:TIGR00870 117 ANDQYTSEftPGITALHLAAHRQNYEIVKLLLERGASV 154
 
Name Accession Description Interval E-value
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
 254-566 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: 551.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 254 LLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHGKSMAYMRGVYFRMKDEVFRGSRPYESGP 333
Cdd:cd07212     1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGSRPYNSEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 334 LEEFLKREFGEHTKMTDVKKPKVMLTGTLSDRQPAELHLFRNYDAPETVREPRFNqnVNLRPPAQPSDQLVWRAARSSGA 413
Cdd:cd07212    81 LEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEEPEKN--ANFLPPTDPAEQLLWRAARSSGA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 414 APTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAK 493
Cdd:cd07212   159 APTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKSKGRKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSNPWELAK 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622838064 494 TVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVNALWETEVYIYEH 566
Cdd:cd07212   239 TVFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTH 311
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
 255-563 8.56e-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: 164.81  E-value: 8.56e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 255 LCLDGGGVKGLIIIQLLIAIEKASGVATK--DLFDWVAGTSTGGILALAILHGK-SMAYMRGVYFRMKDEVFrgsrpyes 331
Cdd:cd07199     2 LSLDGGGIRGIIPAEILAELEKRLGKPSRiaDLFDLIAGTSTGGIIALGLALGRySAEELVELYEELGRKIF-------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 332 gpleeflkrefgehtkmtdvkkPKVMLTGTlsDRQPAELHLFRNYDAPETVREPRFnqnvnlrppaqpsdqLVWRAARSS 411
Cdd:cd07199    74 ----------------------PRVLVTAY--DLSTGKPVVFSNYDAEEPDDDDDF---------------KLWDVARAT 114

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 412 GAAPTYFRP--------NGRFLDGGLLANNPTLDAMTEiheynqdlIRKGQANKVKKLsIVVSLGTGRSPQVPVTCVDVF 483
Cdd:cd07199   115 SAAPTYFPPaviesggdEGAFVDGGVAANNPALLALAE--------ALRLLAPDKDDI-LVLSLGTGTSPSSSSSKKASR 185

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 484 RPSNPWelaktvfgAKELGKMVVDCCTDPDGRAVDRARAwCEMVGIQYFRLNPQLGTDIM-LDEVSDTVLVNALWETEVY 562
Cdd:cd07199   186 WGGLGW--------GRPLLDILMDAQSDGVDQWLDLLFG-SLDSKDNYLRINPPLPGPIPaLDDASEANLLALDSAAFEL 256


                  .
gi 1622838064 563 I 563
Cdd:cd07199   257 I 257
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 244-545 2.08e-41

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 151.21  E-value: 2.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 244 MRDEKRTHdhLLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHGKSMAYMRGVYFRMKDEVF 323
Cdd:COG3621     1 MSANKPFR--ILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAAGYSAEEILDLYEEEGKEIF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 324 RGSRP-------------YESGPLEEFLKREFGEhTKMTDVKKPkVMLTGT-LSDRQPaelHLFRNYDAPetvreprFNQ 389
Cdd:COG3621    79 PKSRWrkllslrglfgpkYDSEGLEKVLKEYFGD-TTLGDLKTP-VLIPSYdLDNGKP---VFFKSPHAK-------FDR 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 390 NVNLrppaqpsdqLVWRAARSSGAAPTYFRP---------NGRFLDGGLLANNPTLDAMTE-IHEYNQDL--IRkgqank 457
Cdd:COG3621   147 DRDF---------LLVDVARATSAAPTYFPPaqiknltgeGYALIDGGVFANNPALCALAEaLKLLGPDLddIL------ 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 458 vkklsiVVSLGTGRSPQvpvtcvdvfrpSNPWELAKTvFGAKELGKMVVDCCTDPDGRAVDrarAWCEMV-GIQYFRLNP 536
Cdd:COG3621   212 ------VLSLGTGTAPR-----------SIPYKKVKN-WGALGWLLPLIDILMDAQSDAVD---YQLRQLlGDRYYRLDP 270


                  ....*....
gi 1622838064 537 QLGTDIMLD 545
Cdd:COG3621   271 ELPEEIALD 279
Pat_PNPLA8 cd07211
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ...
 253-563 9.71e-34

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: 130.45  E-value: 9.71e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 253 HLLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAI-LHGKSMAYMRGVYFRMKDEVF-RGSRP-- 328
Cdd:cd07211     9 RILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAFLLgLKKMSLDECEELYRKLGKDVFsQNTYIsg 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 329 ----------YESGPLEEFLKREFGEHTKMTDVKK---PKVMLTGTLSDRQPAELHLFRNYDAPETVREPRFNQnvnlrp 395
Cdd:cd07211    89 tsrlvlshayYDTETWEKILKEMMGSDELIDTSADpncPKVACVSTQVNRTPLKPYVFRNYNHPPGTRSHYLGS------ 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 396 paqpSDQLVWRAARSSGAAPTYF----RPNGRFLDGGLLANNPTLDAMTEIHEYNQDlirkgqankvKKLSIVVSLGTGR 471
Cdd:cd07211   163 ----CKHKLWEAIRASSAAPGYFeefkLGNNLHQDGGLLANNPTALALHEAKLLWPD----------TPIQCLVSVGTGR 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 472 SpqvpvtcvdvfrPSNPWELAKTVFGAKELGKMVVDCCTDPDgrAVDrarawcEMV-----GIQYFRLNPQLGTDIMLDE 546
Cdd:cd07211   229 Y------------PSSVRLETGGYTSLKTKLLNLIDSATDTE--RVH------TALddllpPDVYFRFNPVMSECVELDE 288

                         330
                  ....*....|....*..
gi 1622838064 547 VSDTVLVNALWETEVYI 563
Cdd:cd07211   289 TRPEKLDQLQDDTLEYI 305
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-177 1.43e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.13  E-value: 1.43e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  53 IHSKDpRYGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADAHGEHGNTPLH 129
Cdd:COG0666   113 VNARD-KDGETPLHLAaynGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLH 191

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622838064 130 LAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKISRLDTRKAIL 177
Cdd:COG0666   192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
60-185 2.84e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 114.67  E-value: 2.84e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  60 YGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADAHGEHGNTPLHLAMSKDN 136
Cdd:COG0666    86 GGNTLLHAAarnGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1622838064 137 VEMIKALIVFGAEVDTPNDFGETPTFLASKISRLDtrkaILTLLRTVGA 185
Cdd:COG0666   166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE----IVKLLLEAGA 210
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-181 6.37e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 105.04  E-value: 6.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  53 IHSKDpRYGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADAHGEHGNTPLH 129
Cdd:COG0666   146 VNAQD-NDGNTPLHLAaanGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALD 224

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622838064 130 LAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKISRLDTRKAILTLLR 181
Cdd:COG0666   225 LAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
Pat17_PNPLA8_PNPLA9_like2 cd07215
Patatin-like phospholipase of bacteria; Patatin is a storage protein of the potato tuber that ...
 254-577 2.70e-24

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: 104.02  E-value: 2.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 254 LLCLDGGGVKGLIIIQLLIAIE----KASG---VATKDLFDWVAGTSTGGILALAIL-------HGKSMAYMRGVYFRMK 319
Cdd:cd07215     2 ILSIDGGGIRGIIPATILVSVEeklqKKTGnpeARLADYFDLVAGTSTGGILTCLYLcpnesgrPKFSAKEALNFYLERG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 320 DEVFRGSR-------------PYESGPLEEFLKREFGEhTKMTDVKKPKVMLTGTLSDRQPaelHLFRNYDApeTVREPR 386
Cdd:cd07215    82 NYIFKKKIwnkiksrggflneKYSHKPLEEVLLEYFGD-TKLSELLKPCLITSYDIERRSP---HFFKSHTA--IKNEQR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 387 fnqnvnlrppaqpsDQLVWRAARSSGAAPTYFRPNgRF----------LDGGLLANNPTLDAMTEiheynqdlIRKGQAN 456
Cdd:cd07215   156 --------------DFYVRDVARATSAAPTYFEPA-RIhsltgekytlIDGGVFANNPTLCAYAE--------ARKLKFE 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 457 KVKKLS----IVVSLGTGRSpqvpvtcvdvfRPSNPWELAKTvFGAKELGKMVVDCCTDPDGRAVDRARAW---CEMVGI 529
Cdd:cd07215   213 QPGKPTakdmIILSLGTGKN-----------KKSYTYEKVKD-WGLLGWAKPLIDIMMDGASQTVDYQLKQifdAEGDQQ 280

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1622838064 530 QYFRLNPQL-GTDIMLDEVSDTVLVNALWETEVYIYEHHEEFQKLIQLL 577
Cdd:cd07215   281 QYLRIQPELeDADPEMDDASPENLEKLREVGQALAEDHKDQLDEIVDRL 329
Pat17_PNPLA8_PNPLA9_like3 cd07216
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 254-546 6.13e-22

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: 96.60  E-value: 6.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 254 LLCLDGGGVKGLII--------IQLLIAIEKASGVATKDLFDWVAGTSTGGILALailhgksmayMRG-----------V 314
Cdd:cd07216     3 LLSLDGGGVRGLSSllilkeimERIDPKEGLDEPPKPCDYFDLIGGTSTGGLIAI----------MLGrlrmtvdecidA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 315 YFRMKDEVFRGSRPYESGPLEEFLKREFG----------------EHTKMTDVKKP---KVMLTGTLSDrQPAELHLFRN 375
Cdd:cd07216    73 YTRLAKKIFSRKRLRLIIGDLRTGARFDSkklaeaikvilkelgnDEDDLLDEGEEdgcKVFVCATDKD-VTGKAVRLRS 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 376 YDAPetvREPRFNQNVNlrppaqpsdqlVWRAARSSGAAPTYFRP------NGRFLDGGLLANNPTLDAMTEIHEYNQDL 449
Cdd:cd07216   152 YPSK---DEPSLYKNAT-----------IWEAARATSAAPTFFDPvkigpgGRTFVDGGLGANNPIREVWSEAVSLWEGL 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 450 IRkgqankvkKLSIVVSLGTGRSPQVpvtcvdVFRPSnpwelAKTVFGAKELGKMVvdccTDPDGRAVDRARAWCEMVGI 529
Cdd:cd07216   218 AR--------LVGCLVSIGTGTPSIK------SLGRS-----AEGAGLLKGLKDLV----TDTEAEAKRFSAEHSELDEE 274

                         330
                  ....*....|....*....
gi 1622838064 530 -QYFRLN-PQLGTDIMLDE 546
Cdd:cd07216   275 gRYFRFNvPHGLEDVGLDE 293
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 255-549 3.93e-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: 132852 [Multi-domain]  Cd Length: 288  Bit Score: 93.89  E-value: 3.93e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 255 LCLDGGGVKGLIIIQLLIAIEKA--SGVATKDLFdwvAGTSTGGILALAILHGKSMAYMRGVYFRMKDEVFRGSRPYE-- 330
Cdd:cd07213     5 LSLDGGGVKGIVQLVLLKRLAEEfpSFLDQIDLF---AGTSAGSLIALGLALGYSPRQVLKLYEEVGLKVFSKSSAGGga 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 331 -------SGPLEEFLKREFGEhTKMTDVKKpKVMLTGTLSDRQPaelhlfrnydaPETVR--EPRFNQNVnlrPPAQPSD 401
Cdd:cd07213    82 gnnqyfaAGFLKAFAEVFFGD-LTLGDLKR-KVLVPSFQLDSGK-----------DDPNRrwKPKLFHNF---PGEPDLD 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 402 QLVWRAARSSGAAPTYFRPNGRFLDGGLLANNPTLDAMTEIheynqdLIRKGQANKVKKLSiVVSLGTGRSPQvPVTcvD 481
Cdd:cd07213   146 ELLVDVCLRSSAAPTYFPSYQGYVDGGVFANNPSLCAIAQA------IGEEGLNIDLKDIV-VLSLGTGRPPS-YLD--G 215

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622838064 482 VFRPSNpWELAKTvfgAKELGKMVVdcctdpDGRaVDRARAWCEMV-GIQYFRLNPQLGTDIMLDEVSD 549
Cdd:cd07213   216 ANGYGD-WGLLQW---LPDLLDLFM------DAG-VDAADFQCRQLlGERYFRLDPVLPANIDLDDNKQ 273
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 255-439 1.28e-19

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: 86.89  E-value: 1.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 255 LCLDGGGVKGLIiiqlliaiekASGVA-----TKDLFDWVAGTSTGGILALAILHGKSMAYMRGVYFRMKDEVFRGSRP- 328
Cdd:pfam01734   1 LVLSGGGARGAY----------HLGVLkalgeAGIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRk 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 329 ------------------YESGPLEEFLKREFGEHTKMTDVKKPKVMLTGTLSDRqpaelhlfrnydaPETVREPRFNQN 390
Cdd:pfam01734  71 ralsllallrgligegglFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRAL-------------LTVISTALGTRA 137

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622838064 391 VNLRPPAQPSDQLVWRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAM 439
Cdd:pfam01734 138 RILLPDDLDDDEDLADAVLASSALPGVFPPvrldGELYVDGGLVDNVPVEAAL 190
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
68-177 1.54e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 89.24  E-value: 1.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  68 AKNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADAHGEHGNTPLHLAMSKDNVEMIKALIVFG 147
Cdd:COG0666    64 AGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG 143

                          90       100       110
                  ....*....|....*....|....*....|
gi 1622838064 148 AEVDTPNDFGETPTFLASKISRLDTRKAIL 177
Cdd:COG0666   144 ADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
253-463 1.30e-18

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 86.78  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 253 HLLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHGKSMAYMRGVYFRMKDEVFRGSR----- 327
Cdd:NF041079    2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILALALALEIPARELVELFEEHGKDIFPKRKwprrl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 328 -------PYESGPLEEFLKREFGEhTKMTDVKKPKVMLTGTLSDRQPaelHLFRnydapeTVREPRFNQNVNLRppaqps 400
Cdd:NF041079   82 lgllkkpKYSSEPLREVLEEIFGD-KTIGDLKHRVLIPAVNYTTGKP---QVFK------TPHHPDFTRDHKLK------ 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622838064 401 dqLVwRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAMTEIHEY-NQdlirkgQANKVKKLSI 463
Cdd:NF041079  146 --LV-DVALATSAAPTYFPLhefdNEQFVDGGLVANNPGLLGLHEALHFlGV------PYDDVRILSI 204
Ank_2 pfam12796
Ankyrin repeats (3 copies);
65-154 1.17e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 1.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  65 LHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHgANADAhGEHGNTPLHLAMSKDNVEMIK 141
Cdd:pfam12796   1 LHLAaknGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNL-KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1622838064 142 ALIVFGAEVDTPN 154
Cdd:pfam12796  79 LLLEKGADINVKD 91
Pat17_PNPLA8_PNPLA9_like4 cd07217
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 254-538 3.36e-16

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: 80.23  E-value: 3.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 254 LLCLDGGGVKGLIIIQLLIAIEKASGVATK-------DLFDWVAGTSTGGILALAILHGKSMAYMRGVYFRMKDEVF--- 323
Cdd:cd07217     3 ILALDGGGIRGLLSVEILGRIEKDLRTHLDdpefrlgDYFDFVGGTSTGSIIAACIALGMSVTDLLSFYTLNGVNMFdka 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 324 ------RGSRPYESGPLEEFLKR--EFGEHTKMTD--VKKPKVMLTGTLSDRQPAELHlfRNYDApetvrepRFNQNVnl 393
Cdd:cd07217    83 wlaqrlFLNKLYNQYDPTNLGKKlnTVFPETTLGDdtLRTLLMIVTRNATTGSPWPVC--NNPEA-------KYNDSD-- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 394 rPPAQPSDQLVWRAARSSGAAPTYFRPN---------GRFLDGGL-LANNPTLDAMTEIHEYNQDLIRKGQANKVkklsI 463
Cdd:cd07217   152 -RSDCNLDLPLWQLVRASTAAPTFFPPEvvsiapgtaFVFVDGGVtTYNNPAFQAFLMATAKPYKLNWEVGADNL----L 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 464 VVSLGTGRSPQVpvtcVDVFRPSNPWEL--AKTV-----FGAKELGKMVV----DCctdPDGRAVDR-------ARAWCE 525
Cdd:cd07217   227 LVSVGTGFAPEA----RPDLKAADMWALdhAKYIpsalmNAANAGQDMVCrvlgEC---RKGGLVDReigtmhvDPNWLG 299

                         330
                  ....*....|...
gi 1622838064 526 MVGIQYFRLNPQL 538
Cdd:cd07217   300 PKLFTYVRYDVSL 312
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 59-177 7.56e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 79.71  E-value: 7.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  59 RYGASPLHWA-----KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIV------------------LLTHGA 115
Cdd:PHA03100  104 NNGITPLLYAiskksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILkllidkgvdinaknrvnyLLSYGV 183

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622838064 116 NADAHGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKISRLDTRKAIL 177
Cdd:PHA03100  184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
59-159 3.55e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.45  E-value: 3.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  59 RYGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADAHGEHGNTPLHLAMSKD 135
Cdd:COG0666   184 NDGETPLHLAaenGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263

                          90       100
                  ....*....|....*....|....
gi 1622838064 136 NVEMIKALIVFGAEVDTPNDFGET 159
Cdd:COG0666   264 AALIVKLLLLALLLLAAALLDLLT 287
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 51-151 7.70e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 70.68  E-value: 7.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  51 SQIHSKDPRYGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADAHGEHGNTP 127
Cdd:PHA02878  158 ADINMKDRHKGNTALHYAtenKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTP 237

                          90       100
                  ....*....|....*....|....*
gi 1622838064 128 LHLAMSK-DNVEMIKALIVFGAEVD 151
Cdd:PHA02878  238 LHISVGYcKDYDILKLLLEHGVDVN 262
PHA03095 PHA03095
ankyrin-like protein; Provisional
 59-190 2.69e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 69.28  E-value: 2.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  59 RYGASPLHW----AKNAEMARMLLKRGCNVNSTSSAGNTALHV--AVMRNRFDCAIVLLTHGANADAHGEHGNTPLHLAM 132
Cdd:PHA03095   81 RCGFTPLHLylynATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLL 160

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622838064 133 -SKD-NVEMIKALIVFGAEVDTPNDFGETP--TFLASkisrLDTRKAIltlLRTVGAEYCSP 190
Cdd:PHA03095  161 kSRNaNVELLRLLIDAGADVYAVDDRFRSLlhHHLQS----FKPRARI---VRELIRAGCDP 215
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-177 5.97e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 66.52  E-value: 5.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  42 AEMIISMDSSQIHSKDPRYGASPLHWAKNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADAHG 121
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622838064 122 EHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKISRLDTRKAIL 177
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL 140
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 61-186 6.84e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 67.71  E-value: 6.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  61 GASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADAHGEHGNTPLHLAMSKDNV 137
Cdd:PHA02875  102 GMTPLHLAtilKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDI 181

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1622838064 138 EMIKALIVFGAevdTPNDFGETPTFLASKISRLDTRKAILTLLRTVGAE 186
Cdd:PHA02875  182 AICKMLLDSGA---NIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
PHA03095 PHA03095
ankyrin-like protein; Provisional
 44-186 2.46e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.20  E-value: 2.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  44 MIISMDSSqIHSKDPrYGASPLH------WAKNAEMARMLLKRGCNVNSTSSAGNTALHVAVM-RNRFDCAIVLLTHGAN 116
Cdd:PHA03095   32 RLLAAGAD-VNFRGE-YGKTPLHlylhysSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYnATTLDVIKLLIKAGAD 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622838064 117 ADAHGEHGNTPLHLAMSKDNV--EMIKALIVFGAEVDTPNDFGETPtfLASKISRLDTRKAILTLLRTVGAE 186
Cdd:PHA03095  110 VNAKDKVGRTPLHVYLSGFNInpKVIRLLLRKGADVNALDLYGMTP--LAVLLKSRNANVELLRLLIDAGAD 179
Ank_2 pfam12796
Ankyrin repeats (3 copies);
95-177 3.58e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 3.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  95 LHVAVMRNRFDCAIVLLTHGANADAHGEHGNTPLHLAMSKDNVEMIKALIVFgAEVDtPNDFGETPTFLASKISRLDTRK 174
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78


                  ...
gi 1622838064 175 AIL 177
Cdd:pfam12796  79 LLL 81
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 69-193 1.23e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.53  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  69 KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIV--LLTHGANADAHGEHGNTPLHLAMS--KDNVEMIKALI 144
Cdd:PHA03100   84 DVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIVeyLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLI 163

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622838064 145 VFGAEV----------------DTPNDFGETPTFLASKISRLDTRKAILTLlrtvGA------EYCSPPIH 193
Cdd:PHA03100  164 DKGVDInaknrvnyllsygvpiNIKDVYGFTPLHYAVYNNNPEFVKYLLDL----GAnpnlvnKYGDTPLH 230
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 61-151 1.50e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.93  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  61 GASPLH-WAKNA---EMARMLLKRGCNVNSTSSAGNTALHVAVMRNRF-DCAIVLLTHGANADAHGEHGNTPLHLAMSKD 135
Cdd:PHA02876  307 GETPLYlMAKNGydtENIRTLIMLGADVNAADRLYITPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRN 386

                          90
                  ....*....|....*.
gi 1622838064 136 NVEMIKALIVFGAEVD 151
Cdd:PHA02876  387 NVVIINTLLDYGADIE 402
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 70-178 5.20e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.90  E-value: 5.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  70 NAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADAHGEHGNTPLHLAMSKDNVEMIKALIVFGAE 149
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                          90       100
                  ....*....|....*....|....*....
gi 1622838064 150 VDTPNDFGETPTFLASKISRLDTRKAILT 178
Cdd:PHA02874  183 ANVKDNNGESPLHNAAEYGDYACIKLLID 211
Ank_5 pfam13857
Ankyrin repeats (many copies);
77-131 1.34e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.89  E-value: 1.34e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622838064  77 LLKRG-CNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADAHGEHGNTPLHLA 131
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 61-164 1.72e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.00  E-value: 1.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  61 GASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANA-DAHGEHGNTPLHLAMSKDN 136
Cdd:PHA02875   35 GISPIKLAmkfRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKK 114

                          90       100
                  ....*....|....*....|....*...
gi 1622838064 137 VEMIKALIVFGAEVDTPNDFGETPTFLA 164
Cdd:PHA02875  115 LDIMKLLIARGADPDIPNTDKFSPLHLA 142
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 71-165 2.01e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.89  E-value: 2.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  71 AEMARMLLKRGCNVN-STSSAGNTALHVAVMRNRFDCAIVLLTHGANADAHGEHGNTPLHLAMSKDNVEMIKALIVFGAE 149
Cdd:PHA02878  147 AEITKLLLSYGADINmKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                          90
                  ....*....|....*.
gi 1622838064 150 VDTPNDFGETPTFLAS 165
Cdd:PHA02878  227 TDARDKCGNTPLHISV 242
Pat17_isozyme_like cd07214
Patatin-like phospholipase of plants; Pat17 is an isozyme of patatin cloned from Solanum ...
 254-474 2.94e-09

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: 58.99  E-value: 2.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 254 LLCLDGGGVKGLIIIQLLIAIEK------ASGVATKDLFDWVAGTSTGGILAlAIL-----HGKSMAYMRGV---YFRMK 319
Cdd:cd07214     6 VLSIDGGGIRGIIPATILEFLEGklqeldGPDARIADYFDVIAGTSTGGLIT-AMLtapneNKRPLFAAKDIvqfYLENG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 320 DEVFRGSR-PYES---------GP------LEEFLKREFGEhTKMTDVKKPKVMLTGTLSDRQPAelhLFRNYDApetVR 383
Cdd:cd07214    85 PKIFPQSTgQFEDdrkklrsllGPkydgvyLHDLLNELLGD-TRLSDTLTNVVIPTFDIKLLQPV---IFSSSKA---KN 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 384 EPRFNqnvnlrppAQPSDqlvwrAARSSGAAPTYFrPNGRF--------------LDGGLLANNPTLDAMT----EIHEY 445
Cdd:cd07214   158 DKLTN--------ARLAD-----VCISTSAAPTYF-PAHYFttedsngdirefnlVDGGVAANNPTLLAISevtkEIIKD 223

                         250       260
                  ....*....|....*....|....*....
gi 1622838064 446 NQDLIRKGQANKVKKLsiVVSLGTGRSPQ 474
Cdd:cd07214   224 NPFFASIKPLDYKKLL--VLSLGTGSAEE 250
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 73-153 3.88e-09

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: 59.26  E-value: 3.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  73 MARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHG---ANADAHGE--HGNTPLHLAMSKDNVEMIKALIVFG 147
Cdd:cd22192    33 IKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelVNEPMTSDlyQGETALHIAVVNQNLNLVRELIARG 112


                  ....*.
gi 1622838064 148 AEVDTP 153
Cdd:cd22192   113 ADVVSP 118
PHA03095 PHA03095
ankyrin-like protein; Provisional
 75-181 7.84e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.11  E-value: 7.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  75 RMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCA-IV--LLTHGANADAHGEHGNTPLHLAMSKDNVE-MIKALIVFGAEV 150
Cdd:PHA03095   31 RRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdIVrlLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADV 110

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622838064 151 DTPNDFGETP--TFLASKISRLDTrkaILTLLR 181
Cdd:PHA03095  111 NAKDKVGRTPlhVYLSGFNINPKV---IRLLLR 140
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 61-163 1.04e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.34  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  61 GASPLHWAKN---AEMARMLLKRGCNVNSTSSAGNTALHVAVM-------------------------------RNRFDC 106
Cdd:PLN03192  558 GRTPLHIAASkgyEDCVLVLLKHACNVHIRDANGNTALWNAISakhhkifrilyhfasisdphaagdllctaakRNDLTA 637

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622838064 107 AIVLLTHGANADAHGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGE-TPTFL 163
Cdd:PLN03192  638 MKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDfSPTEL 695
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 65-160 1.19e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  65 LHWA-KNA--EMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADAHGEHGNTPLHLAMSKDNVEMIK 141
Cdd:PHA02874  128 LHYAiKKGdlESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207

                          90
                  ....*....|....*....
gi 1622838064 142 ALIVFGAEVDTPNDFGETP 160
Cdd:PHA02874  208 LLIDHGNHIMNKCKNGFTP 226
Ank_4 pfam13637
Ankyrin repeats (many copies);
91-144 3.78e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 3.78e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622838064  91 GNTALHVAVMRNRFDCAIVLLTHGANADAHGEHGNTPLHLAMSKDNVEMIKALI 144
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 48-166 4.52e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 56.23  E-value: 4.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  48 MDSSQIHSKDPRYgASPLHWA----KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADAHGEH 123
Cdd:PHA02876  329 MLGADVNAADRLY-ITPLHQAstldRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQK 407

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622838064 124 GNTPLHLAMSKDNVEM-IKALIVFGAEVDTPNDFGETPTFLASK 166
Cdd:PHA02876  408 IGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACK 451
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 64-180 9.91e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.67  E-value: 9.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  64 PLHWAK---NAEMARMLLKRGCNVNSTSSAGNTALH-----VAVMRNRFDCAIVLLTHGANADAHGEHGNTPLHLAMSK- 134
Cdd:PHA03100   38 PLYLAKearNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKk 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1622838064 135 -DNVEMIKALIVFGAEVDTPNDFGETPTFLASKISRLDTRkaILTLL 180
Cdd:PHA03100  118 sNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLK--ILKLL 162
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 72-193 1.20e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 54.68  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  72 EMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAI-VLLTHGANADAHGEHGNTPLHLaMSKD--NVEMIKALIVFGA 148
Cdd:PHA02876  254 ETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVpKLLERGADVNAKNIKGETPLYL-MAKNgyDTENIRTLIMLGA 332

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622838064 149 EVDTPNDFGETPTFLASKISRL-DTRKAILTLLRTVGA-EYCSP-PIH 193
Cdd:PHA02876  333 DVNAADRLYITPLHQASTLDRNkDIVITLLELGANVNArDYCDKtPIH 380
Ank_4 pfam13637
Ankyrin repeats (many copies);
63-111 1.82e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 1.82e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622838064  63 SPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLL 111
Cdd:pfam13637   3 TALHAAaasGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 77-155 1.94e-07

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 53.52  E-value: 1.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  77 LLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADAHGEHGNTPLHLAMSKDN--VEMIKALIVFGAEVDTPN 154
Cdd:PHA02946   58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNSV 137


                  .
gi 1622838064 155 D 155
Cdd:PHA02946  138 D 138
PHA03095 PHA03095
ankyrin-like protein; Provisional
 51-182 3.39e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.10  E-value: 3.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  51 SQIHSKDPRyGASPLH-----WAKNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIV--LLTHGANADAHGEH 123
Cdd:PHA03095  178 ADVYAVDDR-FRSLLHhhlqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRY 256

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622838064 124 GNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPtfLASKISRLDTRkAILTLLRT 182
Cdd:PHA03095  257 GQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP--LSLMVRNNNGR-AVRAALAK 312
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 76-152 6.62e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.97  E-value: 6.62e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622838064  76 MLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADAHGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDT 152
Cdd:PHA03100  177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 74-168 8.12e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 8.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  74 ARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADAHGEHGNTPLHLAMSKDNVEMIKALI-----VFGA 148
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSrhsqcHFEL 177

                          90       100
                  ....*....|....*....|..
gi 1622838064 149 EVDTPND--FGETPTFLASKIS 168
Cdd:PTZ00322  178 GANAKPDsfTGKPPSLEDSPIS 199
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 70-186 1.07e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.79  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  70 NAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADAHGEHGNTPLHLAMSKDNVEMIKALIVFgAE 149
Cdd:PLN03192  537 NAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-AS 615

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622838064 150 VDTPNDFGETPTFlASKISRLDTRKAILTLLRTVGAE 186
Cdd:PLN03192  616 ISDPHAAGDLLCT-AAKRNDLTAMKELLKQGLNVDSE 651
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 109-218 1.92e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 109 VLLTHGANADAHGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLAskiSRLDTRKAILTLLRTVG---- 184
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA---EENGFREVVQLLSRHSQchfe 176

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1622838064 185 AEYCSPP--IHGVPA--EQGFAAPHHP-FSlerAQPPPI 218
Cdd:PTZ00322  177 LGANAKPdsFTGKPPslEDSPISSHHPdFS---AVPQPM 212
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 40-166 3.57e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.06  E-value: 3.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  40 RCAEMIISmDSSQIHSKDPrYGASPLHWAK---NAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFD----------- 105
Cdd:PHA02876  159 LIAEMLLE-GGADVNAKDI-YCITPIHYAAergNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDtikaiidnrsn 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 106 ------------------CAIVLLTHGANADAHGEHGNTPLHLAMSKDNV-EMIKALIVFGAEVDTPNDFGETPTFLASK 166
Cdd:PHA02876  237 inkndlsllkairnedleTSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAK 316
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 60-177 4.25e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.19  E-value: 4.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  60 YGASPLHWAK---NAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRfdCAIVLLTHGANADAHGEHGNTPLHLAMSKD- 135
Cdd:PHA02874  189 NGESPLHNAAeygDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR--SAIELLINNASINDQDIDGSTPLHHAINPPc 266

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622838064 136 NVEMIKALIVFGAEVDTPNDFGETPTFLASK-ISRLDTRKAIL 177
Cdd:PHA02874  267 DIDIIDILLYHKADISIKDNKGENPIDTAFKyINKDPVIKDII 309
Ank_5 pfam13857
Ankyrin repeats (many copies);
59-98 1.53e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 1.53e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1622838064  59 RYGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVA 98
Cdd:pfam13857  14 GEGYTPLHVAakyGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 285-438 1.55e-05

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: 45.41  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 285 LFDWVAGTSTGGILALAILHGKSMAYMRGVYFRMKdevfRGSRPYESGPLEeflkREFgehtKMTDVkkpkvmltgtlsD 364
Cdd:cd07198    26 LIDIIAGTSAGAIVAALLASGRDLEEALLLLLRLS----REVRLRFDGAFP----PTG----RLLGI------------L 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 365 RQPAELHLFRNYDAPETVREPRFNQNV---NLRPPAQPSDQLVWRAARSSGAAPTYFRP------NGRFLDGGLLANNPT 435
Cdd:cd07198    82 RQPLLSALPDDAHEDASGKLFISLTRLtdgENVLVSDTSKGELWSAVRASSSIPGYFGPvplsfrGRRYGDGGLSNNLPV 161


                  ...
gi 1622838064 436 LDA 438
Cdd:cd07198   162 AEL 164
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 64-177 2.05e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.18  E-value: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  64 PLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMR--------------------------------------- 101
Cdd:PHA02878   40 PLHQAveaRNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklgmkemirsinkcsvfytlvaikdafnnrnveifki 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 102 ---NRFD----------CAI------------VLLTHGANADAHGEH-GNTPLHLAMSKDNVEMIKALIVFGAEVDTPND 155
Cdd:PHA02878  120 iltNRYKniqtidlvyiDKKskddiieaeitkLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDK 199

                         170       180
                  ....*....|....*....|..
gi 1622838064 156 FGETPTFLASKISRLDTRKAIL 177
Cdd:PHA02878  200 TNNSPLHHAVKHYNKPIVHILL 221
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 123-151 2.50e-05

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: 41.42  E-value: 2.50e-05
                           10        20
                   ....*....|....*....|....*....
gi 1622838064  123 HGNTPLHLAMSKDNVEMIKALIVFGAEVD 151
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_4 pfam13637
Ankyrin repeats (many copies);
124-171 2.60e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 2.60e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622838064 124 GNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKISRLD 171
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE 48
Ank_5 pfam13857
Ankyrin repeats (many copies);
110-160 2.73e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 2.73e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622838064 110 LLTHG-ANADAHGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETP 160
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 123-155 5.83e-05

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: 40.35  E-value: 5.83e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1622838064 123 HGNTPLHLA-MSKDNVEMIKALIVFGAEVDTPND 155
Cdd:pfam00023   1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 123-152 6.25e-05

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: 40.32  E-value: 6.25e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1622838064 123 HGNTPLHLAMSKDNVEMIKALIVFGAEVDT 152
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 50-150 8.09e-05

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: 45.46  E-value: 8.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  50 SSQIHSKDPrYGASPLHWA----KNAEMARMLLKRGCNVnstsSAGNTALHVAVMR---NRFDCAIVLLTHG-------- 114
Cdd:TIGR00870  42 KLNINCPDR-LGRSALFVAaienENLELTELLLNLSCRG----AVGDTLLHAISLEyvdAVEAILLHLLAAFrksgplel 116

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1622838064 115 ANADAHGE--HGNTPLHLAMSKDNVEMIKALIVFGAEV 150
Cdd:TIGR00870 117 ANDQYTSEftPGITALHLAAHRQNYEIVKLLLERGASV 154
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 45-160 1.04e-04

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 45.29  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  45 IISMDSSQIhSKDPRYGASPLHWAKNAEMARM--LLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIV--LLTHGANADAH 120
Cdd:PHA02716  270 IESLDGNKV-KNIPMILHSYITLARNIDISVVysFLQPGVKLHYKDSAGRTCLHQYILRHNISTDIIklLHEYGNDLNEP 348

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622838064 121 GEHGNTPLHLAMSK-----------DN---VEMIKALIVFGAEVDTPNDFGETP 160
Cdd:PHA02716  349 DNIGNTVLHTYLSMlsvvnildpetDNdirLDVIQCLISLGADITAVNCLGYTP 402
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 61-132 1.17e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.95  E-value: 1.17e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622838064  61 GASPLHWAKNA---EMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADAHGEHGNTPLHLAM 132
Cdd:PHA02874  157 GCYPIHIAIKHnffDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 43-151 1.33e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 44.66  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  43 EMIISMDSSqIHSKDpRYGASPLH---WAKNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADA 119
Cdd:PHA03100  176 NYLLSYGVP-INIKD-VYGFTPLHyavYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1622838064 120 HGEH----GNTPLHlamSKDNVEMIKALIVFGAEVD 151
Cdd:PHA03100  254 IIETllyfKDKDLN---TITKIKMLKKSIMYMFLLD 286
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 255-435 1.66e-04

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: 43.04  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 255 LCLDGGGVKGLIIIQLLIAIEKAsGVatkdLFDWVAGTSTGGILALAILHGKSMAYMRGV-----YFRMKDE----VFRG 325
Cdd:cd07207     2 LVFEGGGAKGIAYIGALKALEEA-GI----LKKRVAGTSAGAITAALLALGYSAADIKDIlketdFAKLLDSpvglLFLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064 326 SRPYESG------PLEEFLKREFGEHTKMTDVKKpkvmLTGTLSDRQPAELHLF-RNYDapeTVREPRFNQNvnlrppaQ 398
Cdd:cd07207    77 PSLFKEGglykgdALEEWLRELLKEKTGNSFATS----LLRDLDDDLGKDLKVVaTDLT---TGALVVFSAE-------T 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622838064 399 PSDQLVWRAARSSGAAPTYFRP-----NGRFLDGGLLANNPT 435
Cdd:cd07207   143 TPDMPVAKAVRASMSIPFVFKPvrlakGDVYVDGGVLDNYPV 184
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 60-134 2.18e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  60 YGASPLHWA----KNAEMARMLLKRGCNVNSTSSA-GNTALHVAVMRNRfdCAIVLLTHGANADAHGEHGNTPLHLAMSK 134
Cdd:PHA02878  233 CGNTPLHISvgycKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 60-144 2.21e-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: 44.23  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  60 YGASPLHWAK---NAEMARMLLKRGCNVNSTSSAGNTALHVAVMRN--RFDCAI--VLLTHGANADAHG-EH-----GNT 126
Cdd:cd22192   135 YGEHPLSFAAcvgNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPnkTFACQMydLILSYDKEDDLQPlDLvpnnqGLT 214

                          90
                  ....*....|....*...
gi 1622838064 127 PLHLAMSKDNVEMIKALI 144
Cdd:cd22192   215 PFKLAAKEGNIVMFQHLV 232
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 91-119 2.26e-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: 38.72  E-value: 2.26e-04
                           10        20
                   ....*....|....*....|....*....
gi 1622838064   91 GNTALHVAVMRNRFDCAIVLLTHGANADA 119
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 45-162 4.54e-04

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 41.34  E-value: 4.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  45 IISMDSSQIHSKDpRYGASPLHWA-----KNAEMA-RMLLKRGCNVNSTSS-AGNTALHVAVMRNRFDCAIVLLTH-GAN 116
Cdd:PHA02743   42 FISGDGHLLHRYD-HHGRQCTHMVawydrANAVMKiELLVNMGADINARELgTGNTLLHIAASTKNYELAEWLCRQlGVN 120

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1622838064 117 ADAHGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTF 162
Cdd:PHA02743  121 LGAINYQHETAYHIAYKMRDRRMMEILRANGAVCDDPLSIGLSDET 166
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 73-177 6.38e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.74  E-value: 6.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  73 MARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADAHGEHGNTPLHLAMSKDNVEMIKALIvfgaevDT 152
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII------DN 233

                          90       100
                  ....*....|....*....|....*
gi 1622838064 153 PNDFGETPTFLASKISRLDTRKAIL 177
Cdd:PHA02876  234 RSNINKNDLSLLKAIRNEDLETSLL 258
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 70-177 7.55e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.29  E-value: 7.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  70 NAEMARMLLKRGCNVNSTSSAGNTALHVAvMRNRFDCAI-VLLTHGANADAHGEHGNTPLHLAMSKDNVEMIKALIVFGA 148
Cdd:PHA02875   14 ELDIARRLLDIGINPNFEIYDGISPIKLA-MKFRDSEAIkLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                          90       100       110
                  ....*....|....*....|....*....|
gi 1622838064 149 EV-DTPNDFGETPTFLASKISRLDTRKAIL 177
Cdd:PHA02875   93 FAdDVFYKDGMTPLHLATILKKLDIMKLLI 122
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 60-87 9.68e-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: 36.88  E-value: 9.68e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1622838064  60 YGASPLHWA----KNAEMARMLLKRGCNVNST 87
Cdd:pfam00023   1 DGNTPLHLAagrrGNLEIVKLLLSKGADVNAR 32
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 91-119 1.05e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.85  E-value: 1.05e-03
                          10        20
                  ....*....|....*....|....*....
gi 1622838064  91 GNTALHVAVMRNRFDCAIVLLTHGANADA 119
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 91-119 1.21e-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: 36.50  E-value: 1.21e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1622838064  91 GNTALHVAVMR-NRFDCAIVLLTHGANADA 119
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNA 31
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 51-160 1.65e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.19  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  51 SQIHSKDPRYGASPLH----WAKNA--EMARMLLKRGCNVNSTSSAGNTALHVaVMRN---RFDCAIVLLTHGANADAHG 121
Cdd:PHA02859   77 ADVNFKTRDNNLSALHhylsFNKNVepEILKILIDSGSSITEEDEDGKNLLHM-YMCNfnvRINVIKLLIDSGVSFLNKD 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1622838064 122 EHGNTPLH-LAMSKDNVEMIKALIVFGAEVDTPNDFGETP 160
Cdd:PHA02859  156 FDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNC 195
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 75-151 2.26e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.09  E-value: 2.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622838064  75 RMLLKRGCNVNSTSSA-GNTALHVAVMRNRFDCAIVLLTH-GANADAHGEHGNTPLHLAMSKDNVEMIKALIVFGAEVD 151
Cdd:PHA02736   75 KLLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQCK 153
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 54-173 2.28e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.01  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  54 HSKDPRYGASPLHWAK---NAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADAHGEHGN-TPLH 129
Cdd:PLN03192  615 SISDPHAAGDLLCTAAkrnDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDfSPTE 694

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622838064 130 LAMSKDNVEMIKALIVFGA----EVDTPNDFGETPTFLASKISRLDTR 173
Cdd:PLN03192  695 LRELLQKRELGHSITIVDSvpadEPDLGRDGGSRPGRLQGTSSDNQCR 742
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 61-160 2.30e-03

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: 40.77  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  61 GASPLHWA---KNAEMARMLLK---RGCNVNSTSS--AGNTALHVAVMRNRFDCAIVLLTHGA---NADA---------- 119
Cdd:cd22192    51 GETALHVAalyDNLEAAVVLMEaapELVNEPMTSDlyQGETALHIAVVNQNLNLVRELIARGAdvvSPRAtgtffrpgpk 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1622838064 120 ----HGEHgntPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETP 160
Cdd:cd22192   131 nliyYGEH---PLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 60-118 2.38e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 40.74  E-value: 2.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622838064  60 YGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGN-TALHVAVMRNRFDCAIVLLTHGANAD 118
Cdd:PHA02875  167 CGCTPLIIAmakGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCN 229
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 60-85 4.06e-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: 34.87  E-value: 4.06e-03
                           10        20
                   ....*....|....*....|....*....
gi 1622838064   60 YGASPLHWA---KNAEMARMLLKRGCNVN 85
Cdd:smart00248   1 DGRTPLHLAaenGNLEVVKLLLDKGADIN 29
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 65-150 8.31e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.28  E-value: 8.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838064  65 LHWA---KNAEMA-RMLLKRGCNVNSTSSAGNTALHVAVMRN-RFDCAIVLLTHGANADAHGEHGNTPLHLAMSKDNVem 139
Cdd:PHA02876  412 LHFAlcgTNPYMSvKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGI-- 489

                          90
                  ....*....|.
gi 1622838064 140 IKALIVFGAEV 150
Cdd:PHA02876  490 VNILLHYGAEL 500
 
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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