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Conserved domains on  [gi|1907113554|ref|XP_036015406|]
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85/88 kDa calcium-independent phospholipase A2 isoform X2 [Mus musculus]

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 ...
 426-885 1.82e-178

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: 517.65  E-value: 1.82e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 426 LLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRPYESGP 505
Cdd:cd07212     1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGSRPYNSEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 506 LEEFLKREFGEHTKMTDVKKPKVMLTGTLSDRQPAELHLFRNYDAPEAVREprCNQNINLKPPTQPADQLVWRAARSSGA 585
Cdd:cd07212    81 LEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEE--PEKNANFLPPTDPAEQLLWRAARSSGA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 586 APTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDMIRklpqgaaagpgqdgtwvcsccsccsccsccsccscscccccs 665
Cdd:cd07212   159 APTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKS------------------------------------------ 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 666 ccsccscccccsccsccsccsccscccccsccscccccsccsccsccscccsccscscscsyslsysrsrvlsvphsplp 745
Cdd:cd07212       --------------------------------------------------------------------------------

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 746 slgpvltpiptcgksslttlscssQGQGNKVKKLSIVVSLGTGKSPQVPVTCVDVFRPSNPWELAKTVFGAKELGKMVVD 825
Cdd:cd07212   197 ------------------------KGRKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSNPWELAKTVFGAKNLGKMVVD 252

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 826 CCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGSDIMLDEVSDAVLVNALWETEVYIYEHR 885
Cdd:cd07212   253 QCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTHR 312
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
102-392 3.50e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.33  E-value: 3.50e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 102 LHVEVLQHLTDLIRNHPSWTVTHLAVELGIRECFHHSRIISCANSTENEEGCTPLHLACRKGDSEILVELVQYCHAQMDV 181
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 182 TDNKGETAFHYAVQGDNPQVLQLLgKNASAGLNQVNNQGLTPLHLACKMGKQEMVRVLLLCNArcnimgpggfpihtamk 261
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLL-LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA----------------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 262 fsqkgcaemiismdsnQIHSKDpRYGASPLHWA---KNAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLT 338
Cdd:COG0666   145 ----------------DVNAQD-NDGNTPLHLAaanGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907113554 339 YGANAGARGEHGNTPLHLAMSKDNMEMVKALIVFGAEVDTPNDFGETPALIASK 392
Cdd:COG0666   208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261
 
Name Accession Description Interval E-value
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
 426-885 1.82e-178

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: 517.65  E-value: 1.82e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 426 LLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRPYESGP 505
Cdd:cd07212     1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGSRPYNSEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 506 LEEFLKREFGEHTKMTDVKKPKVMLTGTLSDRQPAELHLFRNYDAPEAVREprCNQNINLKPPTQPADQLVWRAARSSGA 585
Cdd:cd07212    81 LEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEE--PEKNANFLPPTDPAEQLLWRAARSSGA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 586 APTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDMIRklpqgaaagpgqdgtwvcsccsccsccsccsccscscccccs 665
Cdd:cd07212   159 APTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKS------------------------------------------ 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 666 ccsccscccccsccsccsccsccscccccsccscccccsccsccsccscccsccscscscsyslsysrsrvlsvphsplp 745
Cdd:cd07212       --------------------------------------------------------------------------------

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 746 slgpvltpiptcgksslttlscssQGQGNKVKKLSIVVSLGTGKSPQVPVTCVDVFRPSNPWELAKTVFGAKELGKMVVD 825
Cdd:cd07212   197 ------------------------KGRKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSNPWELAKTVFGAKNLGKMVVD 252

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 826 CCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGSDIMLDEVSDAVLVNALWETEVYIYEHR 885
Cdd:cd07212   253 QCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTHR 312
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 416-617 1.59e-39

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 148.51  E-value: 1.59e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 416 MRDEKRSHdhLLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVF 495
Cdd:COG3621     1 MSANKPFR--ILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAAGYSAEEILDLYEEEGKEIF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 496 RGSRP-------------YESGPLEEFLKREFGEhTKMTDVKKPkVMLTGT-LSDRQPaelHLFRNYDAPeavrePRCNQ 561
Cdd:COG3621    79 PKSRWrkllslrglfgpkYDSEGLEKVLKEYFGD-TTLGDLKTP-VLIPSYdLDNGKP---VFFKSPHAK-----FDRDR 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907113554 562 NInlkpptqpadqLVWRAARSSGAAPTYFRP---------NGRFLDGGLLANNPTLDAMTEIHEY 617
Cdd:COG3621   149 DF-----------LLVDVARATSAAPTYFPPaqiknltgeGYALIDGGVFANNPALCALAEALKL 202
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
102-392 3.50e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.33  E-value: 3.50e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 102 LHVEVLQHLTDLIRNHPSWTVTHLAVELGIRECFHHSRIISCANSTENEEGCTPLHLACRKGDSEILVELVQYCHAQMDV 181
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 182 TDNKGETAFHYAVQGDNPQVLQLLgKNASAGLNQVNNQGLTPLHLACKMGKQEMVRVLLLCNArcnimgpggfpihtamk 261
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLL-LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA----------------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 262 fsqkgcaemiismdsnQIHSKDpRYGASPLHWA---KNAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLT 338
Cdd:COG0666   145 ----------------DVNAQD-NDGNTPLHLAaanGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907113554 339 YGANAGARGEHGNTPLHLAMSKDNMEMVKALIVFGAEVDTPNDFGETPALIASK 392
Cdd:COG0666   208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 427-611 2.68e-21

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: 92.29  E-value: 2.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 427 LCLDGGGVKGLVIIQLLIAIEKAsgvatKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRP------ 500
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEA-----GIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRkralsl 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 501 -------------YESGPLEEFLKREFGEHTKMTDVKKPKVMLTGTLSdrqpAELHLFRNYDAPEAvreprcnqnINLKP 567
Cdd:pfam01734  76 lallrgligegglFDGDALRELLRKLLGDLTLEELAARLSLLLVVALR----ALLTVISTALGTRA---------RILLP 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907113554 568 PTQPADQLVWRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAM 611
Cdd:pfam01734 143 DDLDDDEDLADAVLASSALPGVFPPvrldGELYVDGGLVDNVPVEAAL 190
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
425-613 1.81e-20

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 93.33  E-value: 1.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 425 HLLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSR----- 499
Cdd:NF041079    2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILALALALEIPARELVELFEEHGKDIFPKRKwprrl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 500 -------PYESGPLEEFLKREFGEhTKMTDVKKPKVMLTGTLSDRQPaelHLFRNYDAPEAVREPRCnqninlkpptqpa 572
Cdd:NF041079   82 lgllkkpKYSSEPLREVLEEIFGD-KTIGDLKHRVLIPAVNYTTGKP---QVFKTPHHPDFTRDHKL------------- 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907113554 573 dQLVwRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAMTE 613
Cdd:NF041079  145 -KLV-DVALATSAAPTYFPLhefdNEQFVDGGLVANNPGLLGLHE 187
Ank_2 pfam12796
Ankyrin repeats (3 copies);
156-249 2.16e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 2.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 156 LHLACRKGDSEILVELVQyCHAQMDVTDNKGETAFHYAVQGDNPQVLQLLGKNASAglnQVNNQGLTPLHLACKMGKQEM 235
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEI 76

                          90
                  ....*....|....
gi 1907113554 236 VRVLLLCNARCNIM 249
Cdd:pfam12796  77 VKLLLEKGADINVK 90
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 220-390 3.96e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 84.66  E-value: 3.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 220 GLTPLHLACKMGKQEMVRVLLLCNARCNIMGPG-GFPIHTAMKFSQKGCAEMIISMDS--NQIHSKDpryGASPLHWA-- 294
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDiESELHDAVEEGDVKAVEELLDLGKfaDDVFYKD---GMTPLHLAti 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 295 -KNAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLTYGANAGARGEHGNTPLHLAMSKDNMEMVKALIVFG 373
Cdd:PHA02875  112 lKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191

                         170
                  ....*....|....*..
gi 1907113554 374 AevdTPNDFGETPALIA 390
Cdd:PHA02875  192 A---NIDYFGKNGCVAA 205
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 154-370 2.69e-13

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: 73.51  E-value: 2.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 154 TPLHLACRKGDSEILVELVQYCHAQMDVTDNKGETAFHYAVQGDNPQVLQLLGKNASAGLNQVNN----QGLTPLHLACK 229
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 230 MGKQEMVRVLL-----LCNARCnimgpggfpihTAMKFSQKGCaemiismdsNQIHskdprYGASPLHWAK---NAEMAR 301
Cdd:cd22192    99 NQNLNLVRELIargadVVSPRA-----------TGTFFRPGPK---------NLIY-----YGEHPLSFAAcvgNEEIVR 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907113554 302 MLLKRGCDVDSTSSSGNTALHVAVMRN--RFDCVM--VLLTYGANAGA------RGEHGNTPLHLAMSKDNMEMVKALI 370
Cdd:cd22192   154 LLIEHGADIRAQDSLGNTVLHILVLQPnkTFACQMydLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLV 232
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 349-377 3.33e-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: 3.33e-05
                           10        20
                   ....*....|....*....|....*....
gi 1907113554  349 HGNTPLHLAMSKDNMEMVKALIVFGAEVD 377
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 152-365 3.88e-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: 47.38  E-value: 3.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 152 GCTPLHLACRKGDSEILVELVQYCHAQMDVtdnkGETAFHYAVQGDNPQV---LQLLGKNASAGLNQ--VNNQ------- 219
Cdd:TIGR00870  52 GRSALFVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLEYVDAVeaiLLHLLAAFRKSGPLelANDQytseftp 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 220 GLTPLHLACKMGKQEMVRVLLL----CNARCNimgpggfpihtamkfsqkgCAEMIISMDSNQIhskdpRYGASPLHWAK 295
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLErgasVPARAC-------------------GDFFVKSQGVDSF-----YHGESPLNAAA 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 296 ---NAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFD-------CVMVLLTYGANAGARG----EH-----GNTPLHL 356
Cdd:TIGR00870 184 clgSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKaeyeelsCQMYNFALSLLDKLRDskelEVilnhqGLTPLKL 263


                  ....*....
gi 1907113554 357 AMSKDNMEM 365
Cdd:TIGR00870 264 AAKEGRIVL 272
 
Name Accession Description Interval E-value
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
 426-885 1.82e-178

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: 517.65  E-value: 1.82e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 426 LLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRPYESGP 505
Cdd:cd07212     1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGSRPYNSEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 506 LEEFLKREFGEHTKMTDVKKPKVMLTGTLSDRQPAELHLFRNYDAPEAVREprCNQNINLKPPTQPADQLVWRAARSSGA 585
Cdd:cd07212    81 LEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEE--PEKNANFLPPTDPAEQLLWRAARSSGA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 586 APTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDMIRklpqgaaagpgqdgtwvcsccsccsccsccsccscscccccs 665
Cdd:cd07212   159 APTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKS------------------------------------------ 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 666 ccsccscccccsccsccsccsccscccccsccscccccsccsccsccscccsccscscscsyslsysrsrvlsvphsplp 745
Cdd:cd07212       --------------------------------------------------------------------------------

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 746 slgpvltpiptcgksslttlscssQGQGNKVKKLSIVVSLGTGKSPQVPVTCVDVFRPSNPWELAKTVFGAKELGKMVVD 825
Cdd:cd07212   197 ------------------------KGRKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSNPWELAKTVFGAKNLGKMVVD 252

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 826 CCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGSDIMLDEVSDAVLVNALWETEVYIYEHR 885
Cdd:cd07212   253 QCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTHR 312
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 416-617 1.59e-39

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 148.51  E-value: 1.59e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 416 MRDEKRSHdhLLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVF 495
Cdd:COG3621     1 MSANKPFR--ILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAAGYSAEEILDLYEEEGKEIF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 496 RGSRP-------------YESGPLEEFLKREFGEhTKMTDVKKPkVMLTGT-LSDRQPaelHLFRNYDAPeavrePRCNQ 561
Cdd:COG3621    79 PKSRWrkllslrglfgpkYDSEGLEKVLKEYFGD-TTLGDLKTP-VLIPSYdLDNGKP---VFFKSPHAK-----FDRDR 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907113554 562 NInlkpptqpadqLVWRAARSSGAAPTYFRP---------NGRFLDGGLLANNPTLDAMTEIHEY 617
Cdd:COG3621   149 DF-----------LLVDVARATSAAPTYFPPaqiknltgeGYALIDGGVFANNPALCALAEALKL 202
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
102-392 3.50e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.33  E-value: 3.50e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 102 LHVEVLQHLTDLIRNHPSWTVTHLAVELGIRECFHHSRIISCANSTENEEGCTPLHLACRKGDSEILVELVQYCHAQMDV 181
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 182 TDNKGETAFHYAVQGDNPQVLQLLgKNASAGLNQVNNQGLTPLHLACKMGKQEMVRVLLLCNArcnimgpggfpihtamk 261
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLL-LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA----------------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 262 fsqkgcaemiismdsnQIHSKDpRYGASPLHWA---KNAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLT 338
Cdd:COG0666   145 ----------------DVNAQD-NDGNTPLHLAaanGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907113554 339 YGANAGARGEHGNTPLHLAMSKDNMEMVKALIVFGAEVDTPNDFGETPALIASK 392
Cdd:COG0666   208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
 427-618 3.70e-38

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: 143.24  E-value: 3.70e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 427 LCLDGGGVKGLVIIQLLIAIEKASGVATK--DLFDWVAGTSTGGILALAILHSK-SMAYMRGVYFRMKDEVFrgsrpyes 503
Cdd:cd07199     2 LSLDGGGIRGIIPAEILAELEKRLGKPSRiaDLFDLIAGTSTGGIIALGLALGRySAEELVELYEELGRKIF-------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 504 gpleeflkrefgehtkmtdvkkPKVMLTGTlsDRQPAELHLFRNYDAPEavreprcnqninlkpPTQPADQLVWRAARSS 583
Cdd:cd07199    74 ----------------------PRVLVTAY--DLSTGKPVVFSNYDAEE---------------PDDDDDFKLWDVARAT 114

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1907113554 584 GAAPTYFRP--------NGRFLDGGLLANNPTLDAMTEIHEYN 618
Cdd:cd07199   115 SAAPTYFPPaviesggdEGAFVDGGVAANNPALLALAEALRLL 157
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
101-387 6.43e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.08  E-value: 6.43e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 101 VLHVEVLQHLTDLIRNHPSWTVTHLAVELGIRECFHHSRIISCANSTENEEGCTPLHLACRKGDSEILVELVQYcHAQMD 180
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVN 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 181 VTDNKGETAFHYAVQGDNPQVLQLLgKNASAGLNQVNNQGLTPLHLACKMGKQEMVRVLLLCNARCNImgpggfpihtam 260
Cdd:COG0666   115 ARDKDGETPLHLAAYNGNLEIVKLL-LEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA------------ 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 261 kfsqkgcaemiismdsnqihsKDpRYGASPLHWA---KNAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLL 337
Cdd:COG0666   182 ---------------------RD-NDGETPLHLAaenGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907113554 338 TYGANAGARGEHGNTPLHLAMSKDNMEMVKALIVFGAEVDTPNDFGETPA 387
Cdd:COG0666   240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Pat_PNPLA8 cd07211
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ...
 425-613 5.79e-31

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: 123.90  E-value: 5.79e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 425 HLLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILA--LAILHSkSMAYMRGVYFRMKDEVF-RGSRP- 500
Cdd:cd07211     9 RILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAflLGLKKM-SLDECEELYRKLGKDVFsQNTYIs 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 501 -----------YESGPLEEFLKREFGEHTKMTDVKK---PKVMLTGTLSDRQPAELHLFRNYDAPEAVREP---RCNqni 563
Cdd:cd07211    88 gtsrlvlshayYDTETWEKILKEMMGSDELIDTSADpncPKVACVSTQVNRTPLKPYVFRNYNHPPGTRSHylgSCK--- 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907113554 564 nlkpptqpadQLVWRAARSSGAAPTYF----RPNGRFLDGGLLANNPTLDAMTE 613
Cdd:cd07211   165 ----------HKLWEAIRASSAAPGYFeefkLGNNLHQDGGLLANNPTALALHE 208
Pat17_PNPLA8_PNPLA9_like2 cd07215
Patatin-like phospholipase of bacteria; Patatin is a storage protein of the potato tuber that ...
 426-613 1.79e-23

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: 102.48  E-value: 1.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 426 LLCLDGGGVKGLVIIQLLIAIE----KASG---VATKDLFDWVAGTSTGGILALAIL-------HSKSMAYMRGVYFRMK 491
Cdd:cd07215     2 ILSIDGGGIRGIIPATILVSVEeklqKKTGnpeARLADYFDLVAGTSTGGILTCLYLcpnesgrPKFSAKEALNFYLERG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 492 DEVFRGSR-------------PYESGPLEEFLKREFGEhTKMTDVKKPKVMLTGTLSDRQPaelHLFRNYDApeAVREPR 558
Cdd:cd07215    82 NYIFKKKIwnkiksrggflneKYSHKPLEEVLLEYFGD-TKLSELLKPCLITSYDIERRSP---HFFKSHTA--IKNEQR 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907113554 559 cnqninlkpptqpaDQLVWRAARSSGAAPTYFRPNgRF----------LDGGLLANNPTLDAMTE 613
Cdd:cd07215   156 --------------DFYVRDVARATSAAPTYFEPA-RIhsltgekytlIDGGVFANNPTLCAYAE 205
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 427-611 2.68e-21

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: 92.29  E-value: 2.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 427 LCLDGGGVKGLVIIQLLIAIEKAsgvatKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRP------ 500
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEA-----GIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRkralsl 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 501 -------------YESGPLEEFLKREFGEHTKMTDVKKPKVMLTGTLSdrqpAELHLFRNYDAPEAvreprcnqnINLKP 567
Cdd:pfam01734  76 lallrgligegglFDGDALRELLRKLLGDLTLEELAARLSLLLVVALR----ALLTVISTALGTRA---------RILLP 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907113554 568 PTQPADQLVWRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAM 611
Cdd:pfam01734 143 DDLDDDEDLADAVLASSALPGVFPPvrldGELYVDGGLVDNVPVEAAL 190
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
425-613 1.81e-20

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 93.33  E-value: 1.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 425 HLLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSR----- 499
Cdd:NF041079    2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILALALALEIPARELVELFEEHGKDIFPKRKwprrl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 500 -------PYESGPLEEFLKREFGEhTKMTDVKKPKVMLTGTLSDRQPaelHLFRNYDAPEAVREPRCnqninlkpptqpa 572
Cdd:NF041079   82 lgllkkpKYSSEPLREVLEEIFGD-KTIGDLKHRVLIPAVNYTTGKP---QVFKTPHHPDFTRDHKL------------- 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907113554 573 dQLVwRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAMTE 613
Cdd:NF041079  145 -KLV-DVALATSAAPTYFPLhefdNEQFVDGGLVANNPGLLGLHE 187
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 427-614 2.06e-18

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: 86.57  E-value: 2.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 427 LCLDGGGVKGLVIIQLLIAIEKA--SGVATKDLFdwvAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRPYE-- 502
Cdd:cd07213     5 LSLDGGGVKGIVQLVLLKRLAEEfpSFLDQIDLF---AGTSAGSLIALGLALGYSPRQVLKLYEEVGLKVFSKSSAGGga 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 503 -------SGPLEEFLKREFGEhTKMTDVKKpKVMLTGTLSDRQPaelhlfrnydaPEAVR--EPRCNQNInlkPPTQPAD 573
Cdd:cd07213    82 gnnqyfaAGFLKAFAEVFFGD-LTLGDLKR-KVLVPSFQLDSGK-----------DDPNRrwKPKLFHNF---PGEPDLD 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1907113554 574 QLVWRAARSSGAAPTYFRPNGRFLDGGLLANNPTLDAMTEI 614
Cdd:cd07213   146 ELLVDVCLRSSAAPTYFPSYQGYVDGGVFANNPSLCAIAQA 186
Ank_2 pfam12796
Ankyrin repeats (3 copies);
156-249 2.16e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 2.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 156 LHLACRKGDSEILVELVQyCHAQMDVTDNKGETAFHYAVQGDNPQVLQLLGKNASAglnQVNNQGLTPLHLACKMGKQEM 235
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEI 76

                          90
                  ....*....|....
gi 1907113554 236 VRVLLLCNARCNIM 249
Cdd:pfam12796  77 VKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
291-380 4.36e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 4.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 291 LHWA---KNAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLTYgaNAGARGEHGNTPLHLAMSKDNMEMVK 367
Cdd:pfam12796   1 LHLAaknGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1907113554 368 ALIVFGAEVDTPN 380
Cdd:pfam12796  79 LLLEKGADINVKD 91
Pat17_PNPLA8_PNPLA9_like3 cd07216
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 426-613 1.54e-17

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: 84.28  E-value: 1.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 426 LLCLDGGGVKG---LVIIQ-LLIAIEKASGVA----TKDLFDWVAGTSTGGILALailhsksmayMRG-----------V 486
Cdd:cd07216     3 LLSLDGGGVRGlssLLILKeIMERIDPKEGLDeppkPCDYFDLIGGTSTGGLIAI----------MLGrlrmtvdecidA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 487 YFRMKDEVFRGSRPYESGPLEEFLKREFG----------------EHTKMTDVKKP---KVMLTGTLSDrQPAELHLFRN 547
Cdd:cd07216    73 YTRLAKKIFSRKRLRLIIGDLRTGARFDSkklaeaikvilkelgnDEDDLLDEGEEdgcKVFVCATDKD-VTGKAVRLRS 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907113554 548 YDAPeavREPrcNQNINLKpptqpadqlVWRAARSSGAAPTYFRP------NGRFLDGGLLANNPTLDAMTE 613
Cdd:cd07216   152 YPSK---DEP--SLYKNAT---------IWEAARATSAAPTFFDPvkigpgGRTFVDGGLGANNPIREVWSE 209
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 220-390 3.96e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 84.66  E-value: 3.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 220 GLTPLHLACKMGKQEMVRVLLLCNARCNIMGPG-GFPIHTAMKFSQKGCAEMIISMDS--NQIHSKDpryGASPLHWA-- 294
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDiESELHDAVEEGDVKAVEELLDLGKfaDDVFYKD---GMTPLHLAti 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 295 -KNAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLTYGANAGARGEHGNTPLHLAMSKDNMEMVKALIVFG 373
Cdd:PHA02875  112 lKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191

                         170
                  ....*....|....*..
gi 1907113554 374 AevdTPNDFGETPALIA 390
Cdd:PHA02875  192 A---NIDYFGKNGCVAA 205
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 153-390 3.12e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 82.02  E-value: 3.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 153 CTPLHLAcRKGDSEILVELVQYCHAQMDVTDNKGETAFHY-----AVQGDNPQVLQLLGKNAsAGLNQVNNQGLTPLHLA 227
Cdd:PHA03100   36 VLPLYLA-KEARNIDVVKILLDNGADINSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYG-ANVNAPDNNGITPLLYA 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 228 --CKMGKQEMVRVLLLCNARCNIMGPGGF-PIHTAMKfsqkgcaemiismdSNQIhskdprygasplhwakNAEMARMLL 304
Cdd:PHA03100  114 isKKSNSYSIVEYLLDNGANVNIKNSDGEnLLHLYLE--------------SNKI----------------DLKILKLLI 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 305 KRGCDVDSTsssgntalhvavmrNRFDCvmvLLTYGANAGARGEHGNTPLHLAMSKDNMEMVKALIVFGAEVDTPNDFGE 384
Cdd:PHA03100  164 DKGVDINAK--------------NRVNY---LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226


                  ....*.
gi 1907113554 385 TPALIA 390
Cdd:PHA03100  227 TPLHIA 232
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 190-391 5.33e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 81.85  E-value: 5.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 190 FHYAVQGDNPQVLQLL---GKNasagLNQVNNQGLTPLHLAC----KMGKQEMVRVLLLCNarcniMGPGGFPIHTAMKF 262
Cdd:PHA02878   41 LHQAVEARNLDVVKSLltrGHN----VNQPDHRDLTPLHIICkepnKLGMKEMIRSINKCS-----VFYTLVAIKDAFNN 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 263 SQKGCAEMIISMDSNQIHSKDPRY-GASPLHWAKNAEMARMLLKRGCDVD-STSSSGNTALHVAVMRNRFDCVMVLLTYG 340
Cdd:PHA02878  112 RNVEIFKIILTNRYKNIQTIDLVYiDKKSKDDIIEAEITKLLLSYGADINmKDRHKGNTALHYATENKDQRLTELLLSYG 191

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907113554 341 ANAGARGEHGNTPLHLAMSKDNMEMVKALIVFGAEVDTPNDFGETPALIAS 391
Cdd:PHA02878  192 ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV 242
Pat17_PNPLA8_PNPLA9_like4 cd07217
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 426-610 4.82e-15

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: 77.53  E-value: 4.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 426 LLCLDGGGVKGLVIIQLLIAIEKASGVATK-------DLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVF--- 495
Cdd:cd07217     3 ILALDGGGIRGLLSVEILGRIEKDLRTHLDdpefrlgDYFDFVGGTSTGSIIAACIALGMSVTDLLSFYTLNGVNMFdka 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 496 ------RGSRPYESGPLEEFLKR--EFGEHTKMTD--VKKPKVMLTGTLSDRQPAELHlfrnyDAPEAVREPRCNQNINL 565
Cdd:cd07217    83 wlaqrlFLNKLYNQYDPTNLGKKlnTVFPETTLGDdtLRTLLMIVTRNATTGSPWPVC-----NNPEAKYNDSDRSDCNL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907113554 566 kpptqpaDQLVWRAARSSGAAPTYFRPN---------GRFLDGGL-LANNPTLDA 610
Cdd:cd07217   158 -------DLPLWQLVRASTAAPTFFPPEvvsiapgtaFVFVDGGVtTYNNPAFQA 205
PHA03095 PHA03095
ankyrin-like protein; Provisional
 152-390 1.41e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 77.37  E-value: 1.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 152 GCTPLHLACRKG---DSEILVELVQYcHAQMDVTDNKGETAFHYAVQGDN-PQVLQLLGKnASAGLNQVNNQGLTPLH-- 225
Cdd:PHA03095   47 GKTPLHLYLHYSsekVKDIVRLLLEA-GADVNAPERCGFTPLHLYLYNATtLDVIKLLIK-AGADVNAKDKVGRTPLHvy 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 226 LACKMGKQEMVRVLLLCNARCNIMGPGGF-PIHTAMKFsqKGCA----EMIISMDSNqIHSKDPRyGASPLH-----WAK 295
Cdd:PHA03095  125 LSGFNINPKVIRLLLRKGADVNALDLYGMtPLAVLLKS--RNANvellRLLIDAGAD-VYAVDDR-FRSLLHhhlqsFKP 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 296 NAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMV--LLTYGANAGARGEHGNTPLHLAMSKDNMEMVKALIVFG 373
Cdd:PHA03095  201 RARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280

                         250
                  ....*....|....*..
gi 1907113554 374 AEVDTPNDFGETPALIA 390
Cdd:PHA03095  281 ADINAVSSDGNTPLSLM 297
PHA03095 PHA03095
ankyrin-like protein; Provisional
 182-392 2.98e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.22  E-value: 2.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 182 TDNKGETAFHYAVQ---GDNPQVLQLLgKNASAGLNQVNNQGLTPLHL-ACKMGKQEMVRVLLLCNARCNIMGPGGF-PI 256
Cdd:PHA03095   43 RGEYGKTPLHLYLHyssEKVKDIVRLL-LEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRtPL 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 257 HTAM--KFSQKGCAEMIISMDSNqIHSKDpRYGASPLHW-----AKNAEMARMLLKRGCDVDSTSSSGNTALHV--AVMR 327
Cdd:PHA03095  122 HVYLsgFNINPKVIRLLLRKGAD-VNALD-LYGMTPLAVllksrNANVELLRLLIDAGADVYAVDDRFRSLLHHhlQSFK 199

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907113554 328 NRFDCVMVLLTYGANAGARGEHGNTPLH-LAM-SKDNMEMVKALIVFGAEVDTPNDFGETPALIASK 392
Cdd:PHA03095  200 PRARIVRELIRAGCDPAATDMLGNTPLHsMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAV 266
PHA03095 PHA03095
ankyrin-like protein; Provisional
 234-386 7.92e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.06  E-value: 7.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 234 EMVRVLLLCNARCNIMGP-GGFPIHTAMKFSQKGCAEMIISMDSNQIHSKDP-RYGASPLHW----AKNAEMARMLLKRG 307
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEyGKTPLHLYLHYSSEKVKDIVRLLLEAGADVNAPeRCGFTPLHLylynATTLDVIKLLIKAG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 308 CDVDSTSSSGNTALHV--AVMRNRFDCVMVLLTYGANAGARGEHGNTPLHLAM-SKD-NMEMVKALIVFGAEVDTPNDFG 383
Cdd:PHA03095  108 ADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLkSRNaNVELLRLLIDAGADVYAVDDRF 187


                  ...
gi 1907113554 384 ETP 386
Cdd:PHA03095  188 RSL 190
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 183-390 9.10e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 75.49  E-value: 9.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 183 DNKGETAFHYAVQGdnPQVLQLLGKNASAG--LNQVNNQGLTPLHLACKMG-KQEMVRVLLLCNARCNIMGP-GGFPIHT 258
Cdd:PHA02876  270 DDCKNTPLHHASQA--PSLSRLVPKLLERGadVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRlYITPLHQ 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 259 AMKFSQ-KGCAEMIISMDSNqIHSKDpRYGASPLHWA---KNAEMARMLLKRGCDVDSTSSSGNTALHVAVM-RNRFDCV 333
Cdd:PHA02876  348 ASTLDRnKDIVITLLELGAN-VNARD-YCDKTPIHYAavrNNVVIINTLLDYGADIEALSQKIGTALHFALCgTNPYMSV 425

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907113554 334 MVLLTYGANAGARGEHGNTPLHLAMSKD-NMEMVKALIVFGAEVDTPNDFGETPALIA 390
Cdd:PHA02876  426 KTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA 483
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 151-343 2.51e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 73.10  E-value: 2.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 151 EGCTPLHLACRKGDSEILVELVQYcHAQMDVTDNKGETAFHYAV-QGDNPQVLQLLGKNASAGlNQVNNQGLTPLHLACK 229
Cdd:PHA02875   34 DGISPIKLAMKFRDSEAIKLLMKH-GAIPDVKYPDIESELHDAVeEGDVKAVEELLDLGKFAD-DVFYKDGMTPLHLATI 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 230 MGKQEMVRVLLLCNARCNIMGPGGF-PIHTAMKFSQKGCAEMIIsmDSNQIHSKDPRYGASPLHWA---KNAEMARMLLK 305
Cdd:PHA02875  112 LKKLDIMKLLIARGADPDIPNTDKFsPLHLAVMMGDIKGIELLI--DHKACLDIEDCCGCTPLIIAmakGDIAICKMLLD 189

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907113554 306 RGCDVDSTSSSGN-TALHVAVMRNRFDCVMVLLTYGANA 343
Cdd:PHA02875  190 SGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADC 228
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 154-370 2.69e-13

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: 73.51  E-value: 2.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 154 TPLHLACRKGDSEILVELVQYCHAQMDVTDNKGETAFHYAVQGDNPQVLQLLGKNASAGLNQVNN----QGLTPLHLACK 229
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 230 MGKQEMVRVLL-----LCNARCnimgpggfpihTAMKFSQKGCaemiismdsNQIHskdprYGASPLHWAK---NAEMAR 301
Cdd:cd22192    99 NQNLNLVRELIargadVVSPRA-----------TGTFFRPGPK---------NLIY-----YGEHPLSFAAcvgNEEIVR 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907113554 302 MLLKRGCDVDSTSSSGNTALHVAVMRN--RFDCVM--VLLTYGANAGA------RGEHGNTPLHLAMSKDNMEMVKALI 370
Cdd:cd22192   154 LLIEHGADIRAQDSLGNTVLHILVLQPnkTFACQMydLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLV 232
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 193-386 2.85e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.07  E-value: 2.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 193 AVQGDNPQVLQLLgKNASAGLNQVNNQGLTPLHLACKMGKQEMVRVLLLCNARCNIMgpggfPIHTAMKFSQKGCAEMII 272
Cdd:PHA02874   42 AIRSGDAKIVELF-IKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIL-----PIPCIEKDMIKTILDCGI 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 273 SMDSNQIHSKdprygaSPLHWA-KNA--EMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLTYGANAGARGEH 349
Cdd:PHA02874  116 DVNIKDAELK------TFLHYAiKKGdlESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907113554 350 GNTPLHLAMSKDNMEMVKALIVFGAEVDTPNDFGETP 386
Cdd:PHA02874  190 GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 154-377 4.91e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 73.17  E-value: 4.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 154 TPLHLACRKGDSEILVELVQYcHAQMDVTDNKGETAFHYAVQGDNPQVLQLLGKNASaglnQVNNQGLTPLHlacKMGKQ 233
Cdd:PHA02876  180 TPIHYAAERGNAKMVNLLLSY-GADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS----NINKNDLSLLK---AIRNE 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 234 EMVRVLLLCNARCNIMGPGGF---PIHTAM----------KFSQKGcaemiisMDSNQIHSKdpryGASPLH-WAKNA-- 297
Cdd:PHA02876  252 DLETSLLLYDAGFSVNSIDDCkntPLHHASqapslsrlvpKLLERG-------ADVNAKNIK----GETPLYlMAKNGyd 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 298 -EMARMLLKRGCDVDSTSSSGNTALHVAVMRNRF-DCVMVLLTYGANAGARGEHGNTPLHLAMSKDNMEMVKALIVFGAE 375
Cdd:PHA02876  321 tENIRTLIMLGADVNAADRLYITPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400


                  ..
gi 1907113554 376 VD 377
Cdd:PHA02876  401 IE 402
PHA03095 PHA03095
ankyrin-like protein; Provisional
 152-336 1.70e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.82  E-value: 1.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 152 GCTPLHLACRKGDSEILVELVQYCHAQMDVTDNKGETAFHYAVQGDN--PQVLQLLgKNASAGLNQVNNQGLTPLHL--- 226
Cdd:PHA03095   83 GFTPLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNinPKVIRLL-LRKGADVNALDLYGMTPLAVllk 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 227 --ACKMgkqEMVRVLL---------------------------------LCNARCNIMGP---GGFPIHTAMKFSQkgCA 268
Cdd:PHA03095  162 srNANV---ELLRLLIdagadvyavddrfrsllhhhlqsfkprarivreLIRAGCDPAATdmlGNTPLHSMATGSS--CK 236

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907113554 269 EMIIS--MDSN-QIHSKDpRYGASPLHWA---KNAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCV-MVL 336
Cdd:PHA03095  237 RSLVLplLIAGiSINARN-RYGQTPLHYAavfNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVrAAL 310
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 218-360 1.26e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.98  E-value: 1.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 218 NQGLTPLHLACKMGKQEMVRVLLLCNARCNIMGPGG-FPIHTAMKFSQKGCAEMIISMDSNqIHSKDpRYGASPLHWA-- 294
Cdd:PHA02878  166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNnSPLHHAVKHYNKPIVHILLENGAS-TDARD-KCGNTPLHISvg 243

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907113554 295 --KNAEMARMLLKRGCDVDSTSS-SGNTALHVAVMRNRfdCVMVLLTYGANAGARGEHGNTPLHLAMSK 360
Cdd:PHA02878  244 ycKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
Ank_2 pfam12796
Ankyrin repeats (3 copies);
124-205 1.60e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 1.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 124 HLAVELGIRECFHHSRIISCANSTENEEGCTPLHLACRKGDSEILVELVQYCHAQMdvtDNKGETAFHYAVQGDNPQVLQ 203
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIVK 78


                  ..
gi 1907113554 204 LL 205
Cdd:pfam12796  79 LL 80
Ank_2 pfam12796
Ankyrin repeats (3 copies);
224-313 5.11e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 5.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 224 LHLACKMGKQEMVRVLLLCNARCNIMGPGGF-PIHTAMKFSQKGCAEMIIsmdsNQIHSKDPRYGASPLHWA---KNAEM 299
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRtALHLAAKNGHLEIVKLLL----EHADVNLKDNGRTALHYAarsGHLEI 76

                          90
                  ....*....|....
gi 1907113554 300 ARMLLKRGCDVDST 313
Cdd:pfam12796  77 VKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
321-392 1.09e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 1.09e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907113554 321 LHVAVMRNRFDCVMVLLTYGANAGARGEHGNTPLHLAMSKDNMEMVKALIVFgAEVDtPNDFGETPALIASK 392
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAAR 70
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 146-353 1.15e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.60  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 146 STENEEGCTPLHLACRKGDSEILVELVQYcHAQMDVTDNKGETAFHYAVQGDNPQVLQLLGKNAsAGLNQVNNQGLTPLH 225
Cdd:PHA02874  118 NIKDAELKTFLHYAIKKGDLESIKMLFEY-GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLH 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 226 LACKMGKQEMVRVLLLCNARCNIMGPGGF-PIHTAMKFSqKGCAEMIISMDSNQIHSKDpryGASPLHWAKN----AEMA 300
Cdd:PHA02874  196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFtPLHNAIIHN-RSAIELLINNASINDQDID---GSTPLHHAINppcdIDII 271

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907113554 301 RMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLTygANAGARGEHGNTP 353
Cdd:PHA02874  272 DILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDII--ANAVLIKEADKLK 322
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 175-377 1.87e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.21  E-value: 1.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 175 CHAQMDVTDNKGETAFHYAVQGDNPQVLQLLGKnASAGLNQVNNQGLTPLHLACKMGKQEMVRVLLLCNARCNIMG-PGG 253
Cdd:PHA02874  113 CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFE-YGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDnNGE 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 254 FPIHTAMKFSQKGCAEMIISmDSNQIHSKDPRyGASPLHWA--KNAEMARMLLKRGcDVDSTSSSGNTALHVAVMRN-RF 330
Cdd:PHA02874  192 SPLHNAAEYGDYACIKLLID-HGNHIMNKCKN-GFTPLHNAiiHNRSAIELLINNA-SINDQDIDGSTPLHHAINPPcDI 268

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907113554 331 DCVMVLLTYGANAGARGEHGNTPLHLAMSKDN-MEMVKALI---VFGAEVD 377
Cdd:PHA02874  269 DIIDILLYHKADISIKDNKGENPIDTAFKYINkDPVIKDIIanaVLIKEAD 319
Pat17_isozyme_like cd07214
Patatin-like phospholipase of plants; Pat17 is an isozyme of patatin cloned from Solanum ...
 426-614 2.22e-10

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: 63.22  E-value: 2.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 426 LLCLDGGGVKGLVIIQLLIAIEK------ASGVATKDLFDWVAGTSTGGILAlAIL-----HSKSMAYMRGV---YFRMK 491
Cdd:cd07214     6 VLSIDGGGIRGIIPATILEFLEGklqeldGPDARIADYFDVIAGTSTGGLIT-AMLtapneNKRPLFAAKDIvqfYLENG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 492 DEVFRGSR-PYES---------GP------LEEFLKREFGEhTKMTDVKKPKVMLTGTLSDRQPAelhLFRNYDApeavr 555
Cdd:cd07214    85 PKIFPQSTgQFEDdrkklrsllGPkydgvyLHDLLNELLGD-TRLSDTLTNVVIPTFDIKLLQPV---IFSSSKA----- 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907113554 556 epRCNQNINLKpptqPADqlvwrAARSSGAAPTYFrPNGRF--------------LDGGLLANNPTLDAMTEI 614
Cdd:cd07214   156 --KNDKLTNAR----LAD-----VCISTSAAPTYF-PAHYFttedsngdirefnlVDGGVAANNPTLLAISEV 216
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 299-379 2.94e-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: 60.80  E-value: 2.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 299 MARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLTYG---ANAGARGE--HGNTPLHLAMSKDNMEMVKALIVFG 373
Cdd:cd22192    33 IKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelVNEPMTSDlyQGETALHIAVVNQNLNLVRELIARG 112


                  ....*.
gi 1907113554 374 AEVDTP 379
Cdd:cd22192   113 ADVVSP 118
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 300-405 5.20e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.91  E-value: 5.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 300 ARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLTYGANAGARGEHGNTPLHLAMSKDNMEMVKALI-----VFGA 374
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSrhsqcHFEL 177

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907113554 375 EVDTPND--FGETPALIASKISKQLQDLMPISR 405
Cdd:PTZ00322  178 GANAKPDsfTGKPPSLEDSPISSHHPDFSAVPQ 210
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 427-607 5.48e-09

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: 56.90  E-value: 5.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 427 LCLDGGGVKGLVIIQLLIAIEKAsGVatkdLFDWVAGTSTGGILA--LAI-LHSKSMAY--MRGVYFRMKDE----VFRG 497
Cdd:cd07207     2 LVFEGGGAKGIAYIGALKALEEA-GI----LKKRVAGTSAGAITAalLALgYSAADIKDilKETDFAKLLDSpvglLFLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 498 SRPYESG------PLEEFLKREFGEHTKMTDVKKpkvmLTGTLSDRQPAELHLFrnydapeAVREPRCnQNINLKPPTQP 571
Cdd:cd07207    77 PSLFKEGglykgdALEEWLRELLKEKTGNSFATS----LLRDLDDDLGKDLKVV-------ATDLTTG-ALVVFSAETTP 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1907113554 572 aDQLVWRAARSSGAAPTYFRP-----NGRFLDGGLLANNPT 607
Cdd:cd07207   145 -DMPVAKAVRASMSIPFVFKPvrlakGDVYVDGGVLDNYPV 184
Ank_4 pfam13637
Ankyrin repeats (many copies);
317-370 6.31e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 6.31e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907113554 317 GNTALHVAVMRNRFDCVMVLLTYGANAGARGEHGNTPLHLAMSKDNMEMVKALI 370
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
303-357 6.51e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.73  E-value: 6.51e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907113554 303 LLKRG-CDVDSTSSSGNTALHVAVMRNRFDCVMVLLTYGANAGARGEHGNTPLHLA 357
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 114-262 7.88e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.82  E-value: 7.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 114 IRNHPSWTVTHLAVELGIRECFHHSRIISCANSTENEEGCTPLHLACRKGDSEILVELVQYcHAQMDVTDNKGETAFHYA 193
Cdd:PHA02874  119 IKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK-GAYANVKDNNGESPLHNA 197

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 194 VQGDNPQVLQLLGKNASAGLNQVNNqGLTPLHLACKMGKQemVRVLLLCNARCNIMGPGGF-PIHTAMKF 262
Cdd:PHA02874  198 AEYGDYACIKLLIDHGNHIMNKCKN-GFTPLHNAIIHNRS--AIELLINNASINDQDIDGStPLHHAINP 264
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 296-390 8.80e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 59.50  E-value: 8.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 296 NAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLTYGANAGARGEHGNTPL-------H------------- 355
Cdd:PLN03192  537 NAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHhkifrilyhfasi 616

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907113554 356 -----------LAMSKDNMEMVKALIVFGAEVDTPNDFGETPALIA 390
Cdd:PLN03192  617 sdphaagdllcTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVA 662
Ank_4 pfam13637
Ankyrin repeats (many copies);
154-205 8.72e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 8.72e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907113554 154 TPLHLACRKGDSEILVELVQYcHAQMDVTDNKGETAFHYAVQGDNPQVLQLL 205
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
289-337 4.10e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 4.10e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907113554 289 SPLHWA---KNAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLL 337
Cdd:pfam13637   3 TALHAAaasGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 201-386 7.25e-07

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 52.99  E-value: 7.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 201 VLQLLGKNAsAGLNQVNNQGLTPLHLACKMGK------QEMVRVLLLCNARC-NIMGPGGFPIHTAMKFSQKGCAEMIIS 273
Cdd:PHA02716  194 ILEWLCNNG-VNVNLQNNHLITPLHTYLITGNvcasviKKIIELGGDMDMKCvNGMSPIMTYIINIDNINPEITNIYIES 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 274 MDSNQIhSKDPRYGASPLHWAKNAEMARM--LLKRGCDVDSTSSSGNTALHVAVMRNRF--DCVMVLLTYGANAGARGEH 349
Cdd:PHA02716  273 LDGNKV-KNIPMILHSYITLARNIDISVVysFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNI 351

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907113554 350 GNTPLHLAMSK-----------DN---MEMVKALIVFGAEVDTPNDFGETP 386
Cdd:PHA02716  352 GNTVLHTYLSMlsvvnildpetDNdirLDVIQCLISLGADITAVNCLGYTP 402
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 144-309 9.80e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.30  E-value: 9.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 144 ANSTENEEGCTPLHLACRKGDSEILVELVQYcHAQMDVTDNKGETAFHYAVQGDNPQVLQLLGKNaSAGLNQVNNQGLTP 223
Cdd:PHA02875   94 ADDVFYKDGMTPLHLATILKKLDIMKLLIAR-GADPDIPNTDKFSPLHLAVMMGDIKGIELLIDH-KACLDIEDCCGCTP 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 224 LHLACKMGKQEMVRVLLLCNARCNImgpggfpihtamkFSQKGC-AEMIISMDSNQIhskdprygasplhwaknaEMARM 302
Cdd:PHA02875  172 LIIAMAKGDIAICKMLLDSGANIDY-------------FGKNGCvAALCYAIENNKI------------------DIVRL 220


                  ....*..
gi 1907113554 303 LLKRGCD 309
Cdd:PHA02875  221 FIKRGAD 227
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 287-385 1.19e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.56  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 287 GASPLHWAKN---AEMARMLLKRGCDVDSTSSSGNTALHVAVM-------------------------------RNRFDC 332
Cdd:PLN03192  558 GRTPLHIAASkgyEDCVLVLLKHACNVHIRDANGNTALWNAISakhhkifrilyhfasisdphaagdllctaakRNDLTA 637

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907113554 333 VMVLLTYGANAGARGEHGNTPLHLAMSKDNMEMVKALIVFGAEVD---TPNDFGET 385
Cdd:PLN03192  638 MKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDkanTDDDFSPT 693
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 206-342 1.54e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.18  E-value: 1.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 206 GKNASAGlnqvNNQGLTPLHLACKMGKQEMVRVLLLCNARCNIMGPGGfpiHTAMKFSQKGCAEMIISMDSNQIHSKDPR 285
Cdd:PLN03192  548 KLDPDIG----DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANG---NTALWNAISAKHHKIFRILYHFASISDPH 620

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 286 YGASPLHWA---KNAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLTYGAN 342
Cdd:PLN03192  621 AAGDLLCTAakrNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 180-249 2.26e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.20  E-value: 2.26e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 180 DVTDNKGETAFHYAVQGDNPQVLQLLgKNASAGLNQVNNQGLTPLHLACKMGKQEMVRVLLLCNARCNIM 249
Cdd:PHA03100  186 NIKDVYGFTPLHYAVYNNNPEFVKYL-LDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 222-430 2.39e-06

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: 51.17  E-value: 2.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 222 TPLHLACKMGKQEMVRVLLLCNaRCNIMGPGGF---PIHTAMKFSQKGCAEMIISMDS---NQIHSKDPRYGASPLHWA- 294
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCP-SCDLFQRGALgetALHVAALYDNLEAAVVLMEAAPelvNEPMTSDLYQGETALHIAv 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 295 --KNAEMARMLLKRGCDVDSTSSSGntalhvAVMRNRFDCvmvLLTYganagarGEHgntPLHLAMSKDNMEMVKALIVF 372
Cdd:cd22192    98 vnQNLNLVRELIARGADVVSPRATG------TFFRPGPKN---LIYY-------GEH---PLSFAACVGNEEIVRLLIEH 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907113554 373 GAEVDTPNDFGETP----ALIASK-ISKQLQDlmpisrarkpaFILSSMRdekrsHDHLLCLD 430
Cdd:cd22192   159 GADIRAQDSLGNTVlhilVLQPNKtFACQMYD-----------LILSYDK-----EDDLQPLD 205
Ank_5 pfam13857
Ankyrin repeats (many copies);
336-390 7.64e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 7.64e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907113554 336 LLTYG-ANAGARGEHGNTPLHLAMSKDNMEMVKALIVFGAEVDTPNDFGETPALIA 390
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02946 PHA02946
ankyin-like protein; Provisional
 303-381 8.24e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 49.28  E-value: 8.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 303 LLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLTYGANAGARGEHGNTPLHLAMSKDN--MEMVKALIVFGAEVDTPN 380
Cdd:PHA02946   58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNSV 137


                  .
gi 1907113554 381 D 381
Cdd:PHA02946  138 D 138
Ank_2 pfam12796
Ankyrin repeats (3 copies);
103-183 9.84e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.72  E-value: 9.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 103 HVEVLQHLTDL-----IRNHPSWTVTHLAVELGIRECFhhSRIISCANSTENEEGCTPLHLACRKGDSEILVELVQYcHA 177
Cdd:pfam12796   9 NLELVKLLLENgadanLQDKNGRTALHLAAKNGHLEIV--KLLLEHADVNLKDNGRTALHYAARSGHLEIVKLLLEK-GA 85


                  ....*.
gi 1907113554 178 QMDVTD 183
Cdd:pfam12796  86 DINVKD 91
Ank_5 pfam13857
Ankyrin repeats (many copies);
285-324 1.25e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.25e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1907113554 285 RYGASPLHWA---KNAEMARMLLKRGCDVDSTSSSGNTALHVA 324
Cdd:pfam13857  14 GEGYTPLHVAakyGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
350-393 1.63e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 1.63e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1907113554 350 GNTPLHLAMSKDNMEMVKALIVFGAEVDTPNDFGETPALIASKI 393
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASN 44
Ank_5 pfam13857
Ankyrin repeats (many copies);
147-193 1.91e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 1.91e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1907113554 147 TENEEGCTPLHLACRKGDSEILVELVQYcHAQMDVTDNKGETAFHYA 193
Cdd:pfam13857  11 RLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
171-227 2.10e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 2.10e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907113554 171 LVQYCHAQMDVTDNKGETAFHYAVQGDNPQVLQLLGKNASAgLNQVNNQGLTPLHLA 227
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD-LNLKDEEGLTALDLA 56
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 427-610 2.41e-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: 45.80  E-value: 2.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 427 LCLDGGGVKGLVIIQLLIAIEKAsGVatkdLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKdevfRGSRPYESGPL 506
Cdd:cd07198     1 LVLSGGGALGIYHVGVAKALRER-GP----LIDIIAGTSAGAIVAALLASGRDLEEALLLLLRLS----REVRLRFDGAF 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 507 EeflkREFgehtKMTDVkkpkvmltgtlsDRQPAELHLFRNYDAPEAVREPRCNQNI---NLKPPTQPADQLVWRAARSS 583
Cdd:cd07198    72 P----PTG----RLLGI------------LRQPLLSALPDDAHEDASGKLFISLTRLtdgENVLVSDTSKGELWSAVRAS 131

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1907113554 584 GAAPTYFRP------NGRFLDGGLLANNPTLDA 610
Cdd:cd07198   132 SSIPGYFGPvplsfrGRRYGDGGLSNNLPVAEL 164
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 268-392 3.29e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.75  E-value: 3.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 268 AEMIISMDSNqIHSKDPrYGASPLHWAK---NAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCV----------- 333
Cdd:PHA02876  161 AEMLLEGGAD-VNAKDI-YCITPIHYAAergNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIkaiidnrsnin 238

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907113554 334 ------------------MVLLTYGANAGARGEHGNTPLHLAMSKDNM-EMVKALIVFGAEVDTPNDFGETPALIASK 392
Cdd:PHA02876  239 kndlsllkairnedletsLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAK 316
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 349-377 3.33e-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: 3.33e-05
                           10        20
                   ....*....|....*....|....*....
gi 1907113554  349 HGNTPLHLAMSKDNMEMVKALIVFGAEVD 377
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 152-365 3.88e-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: 47.38  E-value: 3.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 152 GCTPLHLACRKGDSEILVELVQYCHAQMDVtdnkGETAFHYAVQGDNPQV---LQLLGKNASAGLNQ--VNNQ------- 219
Cdd:TIGR00870  52 GRSALFVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLEYVDAVeaiLLHLLAAFRKSGPLelANDQytseftp 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 220 GLTPLHLACKMGKQEMVRVLLL----CNARCNimgpggfpihtamkfsqkgCAEMIISMDSNQIhskdpRYGASPLHWAK 295
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLErgasVPARAC-------------------GDFFVKSQGVDSF-----YHGESPLNAAA 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 296 ---NAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFD-------CVMVLLTYGANAGARG----EH-----GNTPLHL 356
Cdd:TIGR00870 184 clgSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKaeyeelsCQMYNFALSLLDKLRDskelEVilnhqGLTPLKL 263


                  ....*....
gi 1907113554 357 AMSKDNMEM 365
Cdd:TIGR00870 264 AAKEGRIVL 272
PHA03095 PHA03095
ankyrin-like protein; Provisional
 327-386 4.31e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 4.31e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907113554 327 RNRFDCVMVLLTYGANAGARGEHGNTPLHLAM---SKDNMEMVKALIVFGAEVDTPNDFGETP 386
Cdd:PHA03095   24 NVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLhysSEKVKDIVRLLLEAGADVNAPERCGFTP 86
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 349-381 4.52e-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: 41.12  E-value: 4.52e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907113554 349 HGNTPLHLA-MSKDNMEMVKALIVFGAEVDTPND 381
Cdd:pfam00023   1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 152-240 9.61e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 46.29  E-value: 9.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 152 GCTPLHLACRKGDSEILVELVQYCHAQMDVTDNKGETAFHYAV------QGDNPQVLQL----LGKNASAGLNQV-NNQG 220
Cdd:cd22194   188 GETPLALAACTNQPEIVQLLMEKESTDITSQDSRGNTVLHALVtvaedsKTQNDFVKRMydmiLLKSENKNLETIrNNEG 267

                          90       100
                  ....*....|....*....|
gi 1907113554 221 LTPLHLACKMGKQEMVRVLL 240
Cdd:cd22194   268 LTPLQLAAKMGKAEILKYIL 287
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 349-378 1.06e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.93  E-value: 1.06e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907113554 349 HGNTPLHLAMSKDNMEMVKALIVFGAEVDT 378
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 154-262 1.20e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 154 TPLHLACRKGDSEILVELVQYcHAQMDVTDNKGETAFHYAVQGDNP--QVLQLLGKNASagLNQVNNQGLTPLHLACKMG 231
Cdd:PHA02876  377 TPIHYAAVRNNVVIINTLLDY-GADIEALSQKIGTALHFALCGTNPymSVKTLIDRGAN--VNSKNKDLSTPLHYACKKN 453

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907113554 232 -KQEMVRVLLLCNARCNIMG-PGGFPIHTAMKF 262
Cdd:PHA02876  454 cKLDVIEMLLDNGADVNAINiQNQYPLLIALEY 486
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 149-277 1.29e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.37  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 149 NEEGCTPLHLACRKGDSEiLVELVQYCHAQMDVTDNKGETAFHYAVQGDNPQVLQLLgKNASAGLNQVNNQG-LTPLHLA 227
Cdd:PHA02875  132 NTDKFSPLHLAVMMGDIK-GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML-LDSGANIDYFGKNGcVAALCYA 209

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907113554 228 CKMGKQEMVRVLLLCNARCNIMGPGGFPIHTAMkfsqkgcaEMIISMDSN 277
Cdd:PHA02875  210 IENNKIDIVRLFIKRGADCNIMFMIEGEECTIL--------DMICNMCTN 251
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 278-376 1.62e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 45.46  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 278 QIHSKDPrYGASPLHWA----KNAEMARMLLKRGCDVDStsssGNTALHVAVMRNRFDCVMVLLTYGANAGARGE----- 348
Cdd:TIGR00870  44 NINCPDR-LGRSALFVAaienENLELTELLLNLSCRGAV----GDTLLHAISLEYVDAVEAILLHLLAAFRKSGPlelan 118

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907113554 349 --------HGNTPLHLAMSKDNMEMVKALIVFGAEV 376
Cdd:TIGR00870 119 dqytseftPGITALHLAAHRQNYEIVKLLLERGASV 154
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 186-370 1.98e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 45.26  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 186 GETAFHYAVQGDNPQVLQ---LLGKNA--SAGLNQVNN--------QGLTPLHLACKMGKQEMVRVLLLCNARCNIMGPG 252
Cdd:cd21882    26 GKTCLHKAALNLNDGVNEaimLLLEAApdSGNPKELVNapctdefyQGQTALHIAIENRNLNLVRLLVENGADVSARATG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 253 GFpihtamkFSQKGCaemiismdsNQIHskdprYGASPLHWA---KNAEMARMLLKRGCD---VDSTSSSGNTALHVAVM 326
Cdd:cd21882   106 RF-------FRKSPG---------NLFY-----FGELPLSLAactNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHALVL 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907113554 327 -------RNRFDCVM--VLLTYganaGARGEH-----------GNTPLHLAMSKDNMEMVKALI 370
Cdd:cd21882   165 qadntpeNSAFVCQMynLLLSY----GAHLDPtqqleeipnhqGLTPLKLAAVEGKIVMFQHIL 224
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 299-370 2.04e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 2.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907113554 299 MARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLTYGANAGARGEHGNTPLHLAMSKDNMEMVKALI 370
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
Ank_4 pfam13637
Ankyrin repeats (many copies);
188-240 4.13e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 4.13e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907113554 188 TAFHYAVQGDNPQVLQ-LLGKNASagLNQVNNQGLTPLHLACKMGKQEMVRVLL 240
Cdd:pfam13637   3 TALHAAAASGHLELLRlLLEKGAD--INAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 317-342 4.90e-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: 37.95  E-value: 4.90e-04
                           10        20
                   ....*....|....*....|....*.
gi 1907113554  317 GNTALHVAVMRNRFDCVMVLLTYGAN 342
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 315-376 7.66e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 43.33  E-value: 7.66e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907113554 315 SSGNTALHVAVM---RNRFDCVMVLLTYGANAGARGE-----------HGNTPLHLAMSKDNMEMVKALIVFGAEV 376
Cdd:cd21882    24 ATGKTCLHKAALnlnDGVNEAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAIENRNLNLVRLLVENGADV 99
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 271-385 8.14e-04

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 40.95  E-value: 8.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 271 IISMDSNQIHSKDpRYGASPLHWA-----KNAEMA-RMLLKRGCDVDSTSS-SGNTALHVAVMRNRFDCVMVLL-TYGAN 342
Cdd:PHA02743   42 FISGDGHLLHRYD-HHGRQCTHMVawydrANAVMKiELLVNMGADINARELgTGNTLLHIAASTKNYELAEWLCrQLGVN 120

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1907113554 343 AGARGEHGNTPLHLAMSKDNMEMVKALIVFGAEVDTPNDFGET 385
Cdd:PHA02743  121 LGAINYQHETAYHIAYKMRDRRMMEILRANGAVCDDPLSIGLS 163
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 219-248 1.10e-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: 37.27  E-value: 1.10e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1907113554 219 QGLTPLHLAC-KMGKQEMVRVLLLCNARCNI 248
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNA 31
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 151-174 1.26e-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: 36.80  E-value: 1.26e-03
                           10        20
                   ....*....|....*....|....
gi 1907113554  151 EGCTPLHLACRKGDSEILVELVQY 174
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDK 24
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 317-346 1.41e-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: 36.88  E-value: 1.41e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1907113554 317 GNTALHVAVMR-NRFDCVMVLLTYGANAGAR 346
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNAR 32
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 317-376 2.93e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 41.40  E-value: 2.93e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907113554 317 GNTALHVAVMRNRFDCVMVLLTYGANAGAR----------------GEHgntPLHLAMSKDNMEMVKALIVFGAEV 376
Cdd:cd21882    73 GQTALHIAIENRNLNLVRLLVENGADVSARatgrffrkspgnlfyfGEL---PLSLAACTNQEEIVRLLLENGAQP 145
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 286-313 2.98e-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: 36.11  E-value: 2.98e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1907113554 286 YGASPLHWA----KNAEMARMLLKRGCDVDST 313
Cdd:pfam00023   1 DGNTPLHLAagrrGNLEIVKLLLSKGADVNAR 32
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 219-248 3.50e-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: 35.64  E-value: 3.50e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1907113554  219 QGLTPLHLACKMGKQEMVRVLLLCNARCNI 248
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 152-240 3.74e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.93  E-value: 3.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 152 GCTPLHLACRKGDSEILVELVQYCHAQMDV--TDNKGETAFHYAVQ-GDNPQ------------VLQLLGK-NASAGLNQ 215
Cdd:cd22193   123 GELPLSLAACTNQPDIVQYLLENEHQPADIeaQDSRGNTVLHALVTvADNTKentkfvtrmydmILIRGAKlCPTVELEE 202

                          90       100
                  ....*....|....*....|....*.
gi 1907113554 216 V-NNQGLTPLHLACKMGKQEMVRVLL 240
Cdd:cd22193   203 IrNNDGLTPLQLAAKMGKIEILKYIL 228
Ank_5 pfam13857
Ankyrin repeats (many copies);
213-248 4.23e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 4.23e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907113554 213 LNQVNNQGLTPLHLACKMGKQEMVRVLLLCNARCNI 248
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNL 44
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 184-247 4.67e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 39.03  E-value: 4.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907113554 184 NKGETAFHYAVQGDNPQVLQLLGKNASAGLNQVNNQGLTPLHLACKMGKQEMVRVLLLCNARCN 247
Cdd:PHA02743   92 GTGNTLLHIAASTKNYELAEWLCRQLGVNLGAINYQHETAYHIAYKMRDRRMMEILRANGAVCD 155
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 193-385 5.68e-03

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: 40.45  E-value: 5.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 193 AVQGDNPQVLQLLGKNASAGLNQVNNQGLTPLHLACKMGKQEMVRVLLLCNARCNIMGPGGfpIHTAMKFSQKGCaEMII 272
Cdd:TIGR00870  25 AERGDLASVYRDLEEPKKLNINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAVGDTL--LHAISLEYVDAV-EAIL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113554 273 SmdsnqiHSKDPRYGASPLHWAknaeMARMLlkrgcdvdSTSSSGNTALHVAVMRNRFDCVMVLLTYGANAGARGE---- 348
Cdd:TIGR00870 102 L------HLLAAFRKSGPLELA----NDQYT--------SEFTPGITALHLAAHRQNYEIVKLLLERGASVPARACgdff 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907113554 349 ----------HGNTPLHLAMSKDNMEMVKALIVFGAEVDTPNDFGET 385
Cdd:TIGR00870 164 vksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNT 210
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 151-184 6.61e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 6.61e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1907113554 151 EGCTPLHLAC-RKGDSEILVELVQYcHAQMDVTDN 184
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSK-GADVNARDK 34
 
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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