NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1743221411|ref|XP_030671428|]
View 

85/88 kDa calcium-independent phospholipase A2 isoform X3 [Nomascus leucogenys]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 426-739 0e+00

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


:

Pssm-ID: 132851 [Multi-domain]  Cd Length: 312  Bit Score: 583.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 426 LLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRPYESGP 505
Cdd:cd07212     1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGSRPYNSEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 506 LEEFLKREFGEHTKMTDVKKPKVMLTGTLSDRQPAELHLFRNYDAPETVREPRFNqnVNLRPPAQPSDQLVWRAARSSGA 585
Cdd:cd07212    81 LEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEEPEKN--ANFLPPTDPAEQLLWRAARSSGA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 586 APTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAK 665
Cdd:cd07212   159 APTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKSKGRKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSNPWELAK 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743221411 666 TVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVNALWETEVYIYEHR 739
Cdd:cd07212   239 TVFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTHR 312
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
105-392 1.21e-36

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.70  E-value: 1.21e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 105 EVLQHLTDLIRNHPSWSVAHLAVELGIRECFHHSRIISCANCTENEEGCTPLHLACRKGDGEILVELVQYCHAQMDVTDY 184
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 185 KGETVFHYAVQGDNSQVLQLLgKNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPNGYpihsamkfsq 264
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLL-LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN---------- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 265 kgcaemiismdssqihskdprygaSPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGA 341
Cdd:COG0666   155 ------------------------TPLHLAaanGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1743221411 342 NADARGEHGNTPLHLAMSKDNVEMVKALIVFGAEVDTLNDFGETPAFLASK 392
Cdd:COG0666   211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261
 
Name Accession Description Interval E-value
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
 426-739 0e+00

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


Pssm-ID: 132851 [Multi-domain]  Cd Length: 312  Bit Score: 583.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 426 LLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRPYESGP 505
Cdd:cd07212     1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGSRPYNSEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 506 LEEFLKREFGEHTKMTDVKKPKVMLTGTLSDRQPAELHLFRNYDAPETVREPRFNqnVNLRPPAQPSDQLVWRAARSSGA 585
Cdd:cd07212    81 LEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEEPEKN--ANFLPPTDPAEQLLWRAARSSGA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 586 APTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAK 665
Cdd:cd07212   159 APTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKSKGRKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSNPWELAK 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743221411 666 TVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVNALWETEVYIYEHR 739
Cdd:cd07212   239 TVFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTHR 312
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 416-717 2.48e-45

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 164.31  E-value: 2.48e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 416 MRDEKRTHdhLLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVF 495
Cdd:COG3621     1 MSANKPFR--ILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAAGYSAEEILDLYEEEGKEIF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 496 RGSRP-------------YESGPLEEFLKREFGEhTKMTDVKKPkVMLTGT-LSDRQPaelHLFRNYDAPetvreprFNQ 561
Cdd:COG3621    79 PKSRWrkllslrglfgpkYDSEGLEKVLKEYFGD-TTLGDLKTP-VLIPSYdLDNGKP---VFFKSPHAK-------FDR 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 562 NVNLrppaqpsdqLVWRAARSSGAAPTYFRP---------NGRFLDGGLLANNPTLDAMTE-IHEYNQDL--IRkgqank 629
Cdd:COG3621   147 DRDF---------LLVDVARATSAAPTYFPPaqiknltgeGYALIDGGVFANNPALCALAEaLKLLGPDLddIL------ 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 630 vkklsiVVSLGTGRSPQvpvtcvdvfrpSNPWELAKTvFGAKELGKMVVDCCTDPDGRAVDrarAWCEMV-GIQYFRLNP 708
Cdd:COG3621   212 ------VLSLGTGTAPR-----------SIPYKKVKN-WGALGWLLPLIDILMDAQSDAVD---YQLRQLlGDRYYRLDP 270


                  ....*....
gi 1743221411 709 QLGTDIMLD 717
Cdd:COG3621   271 ELPEEIALD 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
105-392 1.21e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.70  E-value: 1.21e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 105 EVLQHLTDLIRNHPSWSVAHLAVELGIRECFHHSRIISCANCTENEEGCTPLHLACRKGDGEILVELVQYCHAQMDVTDY 184
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 185 KGETVFHYAVQGDNSQVLQLLgKNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPNGYpihsamkfsq 264
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLL-LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN---------- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 265 kgcaemiismdssqihskdprygaSPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGA 341
Cdd:COG0666   155 ------------------------TPLHLAaanGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1743221411 342 NADARGEHGNTPLHLAMSKDNVEMVKALIVFGAEVDTLNDFGETPAFLASK 392
Cdd:COG0666   211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
425-635 5.66e-22

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 97.57  E-value: 5.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 425 HLLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSR----- 499
Cdd:NF041079    2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILALALALEIPARELVELFEEHGKDIFPKRKwprrl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 500 -------PYESGPLEEFLKREFGEhTKMTDVKKPKVMLTGTLSDRQPaelHLFRnydapeTVREPRFNQNVNLRppaqps 572
Cdd:NF041079   82 lgllkkpKYSSEPLREVLEEIFGD-KTIGDLKHRVLIPAVNYTTGKP---QVFK------TPHHPDFTRDHKLK------ 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743221411 573 dqLVwRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAMTEIHEY-NQdlirkgQANKVKKLSI 635
Cdd:NF041079  146 --LV-DVALATSAAPTYFPLhefdNEQFVDGGLVANNPGLLGLHEALHFlGV------PYDDVRILSI 204
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 427-611 1.55e-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: 93.06  E-value: 1.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 427 LCLDGGGVKGLVIIQLLIAIEKAsgvatKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRP------ 500
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEA-----GIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRkralsl 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 501 -------------YESGPLEEFLKREFGEHTKMTDVKKPKVMLTGTLSDRqpaelhlfrnydaPETVREPRFNQNVNLRP 567
Cdd:pfam01734  76 lallrgligegglFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRAL-------------LTVISTALGTRARILLP 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1743221411 568 PAQPSDQLVWRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAM 611
Cdd:pfam01734 143 DDLDDDEDLADAVLASSALPGVFPPvrldGELYVDGGLVDNVPVEAAL 190
Ank_2 pfam12796
Ankyrin repeats (3 copies);
291-380 1.62e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 1.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 291 LHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHgANADARgEHGNTPLHLAMSKDNVEMVK 367
Cdd:pfam12796   1 LHLAaknGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1743221411 368 ALIVFGAEVDTLN 380
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 167-390 1.78e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 85.49  E-value: 1.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 167 ILVELVQYCHAQMDVTDYKGE---TVFHYAVQGDNSQVLQLLGKNAvAGLNQVNNQGLTPLHLACQLGK-----QEMVRV 238
Cdd:PHA03100   13 IKVKNIKYIIMEDDLNDYSYKkpvLPLYLAKEARNIDVVKILLDNG-ADINSSTKNNSTPLHYLSNIKYnltdvKEIVKL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 239 LLLCNARCNIMGPNG-YPIHSAMkfSQKGCaemiismdssqihskdprygasplhwakNAEMARMLLKRGCNVNSTSSAG 317
Cdd:PHA03100   92 LLEYGANVNAPDNNGiTPLLYAI--SKKSN----------------------------SYSIVEYLLDNGANVNIKNSDG 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 318 NTALHVAVMRNRFDCAIV------------------LLTHGANADARGEHGNTPLHLAMSKDNVEMVKALIVFGAEVDTL 379
Cdd:PHA03100  142 ENLLHLYLESNKIDLKILkllidkgvdinaknrvnyLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV 221

                         250
                  ....*....|.
gi 1743221411 380 NDFGETPAFLA 390
Cdd:PHA03100  222 NKYGDTPLHIA 232
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 154-370 5.39e-10

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: 62.72  E-value: 5.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 154 TPLHLACRKGDGEILVELVQYCHAQMDVTDYKGETVFHYAVQGDNSQVLQLLgKNAVAGLnqVNN-------QGLTPLHL 226
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVL-MEAAPEL--VNEpmtsdlyQGETALHI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 227 ACQLGKQEMVRVLLlcnarcnimgpngypihsamkfsQKGcAEMIISMDSSQIHSKDPR----YGASPLHWAK---NAEM 299
Cdd:cd22192    96 AVVNQNLNLVRELI-----------------------ARG-ADVVSPRATGTFFRPGPKnliyYGEHPLSFAAcvgNEEI 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 300 ARMLLKRGCNVNSTSSAGNTALHVAVMRN--RFDCAI--VLLTHGANADA------RGEHGNTPLHLAMSKDNVEMVKAL 369
Cdd:cd22192   152 VRLLIEHGADIRAQDSLGNTVLHILVLQPnkTFACQMydLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHL 231


                  .
gi 1743221411 370 I 370
Cdd:cd22192   232 V 232
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 349-377 4.93e-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: 40.65  E-value: 4.93e-05
                           10        20
                   ....*....|....*....|....*....
gi 1743221411  349 HGNTPLHLAMSKDNVEMVKALIVFGAEVD 377
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 276-376 5.52e-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: 46.61  E-value: 5.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 276 SSQIHSKDPrYGASPLHWA----KNAEMARMLLKRGCNVnstsSAGNTALHVAVMR---NRFDCAIVLLTHG-------- 340
Cdd:TIGR00870  42 KLNINCPDR-LGRSALFVAaienENLELTELLLNLSCRG----AVGDTLLHAISLEyvdAVEAILLHLLAAFrksgplel 116

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1743221411 341 ANADARGE--HGNTPLHLAMSKDNVEMVKALIVFGAEV 376
Cdd:TIGR00870 117 ANDQYTSEftPGITALHLAAHRQNYEIVKLLLERGASV 154
 
Name Accession Description Interval E-value
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
 426-739 0e+00

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


Pssm-ID: 132851 [Multi-domain]  Cd Length: 312  Bit Score: 583.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 426 LLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRPYESGP 505
Cdd:cd07212     1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGSRPYNSEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 506 LEEFLKREFGEHTKMTDVKKPKVMLTGTLSDRQPAELHLFRNYDAPETVREPRFNqnVNLRPPAQPSDQLVWRAARSSGA 585
Cdd:cd07212    81 LEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEEPEKN--ANFLPPTDPAEQLLWRAARSSGA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 586 APTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAK 665
Cdd:cd07212   159 APTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKSKGRKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSNPWELAK 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743221411 666 TVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVNALWETEVYIYEHR 739
Cdd:cd07212   239 TVFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTHR 312
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
 427-735 1.85e-52

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: 182.53  E-value: 1.85e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 427 LCLDGGGVKGLVIIQLLIAIEKASGVATK--DLFDWVAGTSTGGILALAILHSK-SMAYMRGVYFRMKDEVFrgsrpyes 503
Cdd:cd07199     2 LSLDGGGIRGIIPAEILAELEKRLGKPSRiaDLFDLIAGTSTGGIIALGLALGRySAEELVELYEELGRKIF-------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 504 gpleeflkrefgehtkmtdvkkPKVMLTGTlsDRQPAELHLFRNYDAPETVREPRFnqnvnlrppaqpsdqLVWRAARSS 583
Cdd:cd07199    74 ----------------------PRVLVTAY--DLSTGKPVVFSNYDAEEPDDDDDF---------------KLWDVARAT 114

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 584 GAAPTYFRP--------NGRFLDGGLLANNPTLDAMTEiheynqdlIRKGQANKVKKLsIVVSLGTGRSPQVPVTCVDVF 655
Cdd:cd07199   115 SAAPTYFPPaviesggdEGAFVDGGVAANNPALLALAE--------ALRLLAPDKDDI-LVLSLGTGTSPSSSSSKKASR 185

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 656 RPSNPWelaktvfgAKELGKMVVDCCTDPDGRAVDRARAwCEMVGIQYFRLNPQLGTDIM-LDEVSDTVLVNALWETEVY 734
Cdd:cd07199   186 WGGLGW--------GRPLLDILMDAQSDGVDQWLDLLFG-SLDSKDNYLRINPPLPGPIPaLDDASEANLLALDSAAFEL 256


                  .
gi 1743221411 735 I 735
Cdd:cd07199   257 I 257
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 416-717 2.48e-45

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 164.31  E-value: 2.48e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 416 MRDEKRTHdhLLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVF 495
Cdd:COG3621     1 MSANKPFR--ILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAAGYSAEEILDLYEEEGKEIF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 496 RGSRP-------------YESGPLEEFLKREFGEhTKMTDVKKPkVMLTGT-LSDRQPaelHLFRNYDAPetvreprFNQ 561
Cdd:COG3621    79 PKSRWrkllslrglfgpkYDSEGLEKVLKEYFGD-TTLGDLKTP-VLIPSYdLDNGKP---VFFKSPHAK-------FDR 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 562 NVNLrppaqpsdqLVWRAARSSGAAPTYFRP---------NGRFLDGGLLANNPTLDAMTE-IHEYNQDL--IRkgqank 629
Cdd:COG3621   147 DRDF---------LLVDVARATSAAPTYFPPaqiknltgeGYALIDGGVFANNPALCALAEaLKLLGPDLddIL------ 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 630 vkklsiVVSLGTGRSPQvpvtcvdvfrpSNPWELAKTvFGAKELGKMVVDCCTDPDGRAVDrarAWCEMV-GIQYFRLNP 708
Cdd:COG3621   212 ------VLSLGTGTAPR-----------SIPYKKVKN-WGALGWLLPLIDILMDAQSDAVD---YQLRQLlGDRYYRLDP 270


                  ....*....
gi 1743221411 709 QLGTDIMLD 717
Cdd:COG3621   271 ELPEEIALD 279
Pat_PNPLA8 cd07211
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ...
 425-735 6.38e-39

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: 146.63  E-value: 6.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 425 HLLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILA--LAILHSkSMAYMRGVYFRMKDEVF-RGSRP- 500
Cdd:cd07211     9 RILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAflLGLKKM-SLDECEELYRKLGKDVFsQNTYIs 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 501 -----------YESGPLEEFLKREFGEHTKMTDVKK---PKVMLTGTLSDRQPAELHLFRNYDAPETVREPRFNQnvnlr 566
Cdd:cd07211    88 gtsrlvlshayYDTETWEKILKEMMGSDELIDTSADpncPKVACVSTQVNRTPLKPYVFRNYNHPPGTRSHYLGS----- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 567 ppaqpSDQLVWRAARSSGAAPTYF----RPNGRFLDGGLLANNPTLDAMTEIHEYNQDlirkgqankvKKLSIVVSLGTG 642
Cdd:cd07211   163 -----CKHKLWEAIRASSAAPGYFeefkLGNNLHQDGGLLANNPTALALHEAKLLWPD----------TPIQCLVSVGTG 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 643 RSpqvpvtcvdvfrPSNPWELAKTVFGAKELGKMVVDCCTDPDgrAVDrarawcEMV-----GIQYFRLNPQLGTDIMLD 717
Cdd:cd07211   228 RY------------PSSVRLETGGYTSLKTKLLNLIDSATDTE--RVH------TALddllpPDVYFRFNPVMSECVELD 287

                         330
                  ....*....|....*...
gi 1743221411 718 EVSDTVLVNALWETEVYI 735
Cdd:cd07211   288 ETRPEKLDQLQDDTLEYI 305
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
105-392 1.21e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.70  E-value: 1.21e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 105 EVLQHLTDLIRNHPSWSVAHLAVELGIRECFHHSRIISCANCTENEEGCTPLHLACRKGDGEILVELVQYCHAQMDVTDY 184
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 185 KGETVFHYAVQGDNSQVLQLLgKNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPNGYpihsamkfsq 264
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLL-LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN---------- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 265 kgcaemiismdssqihskdprygaSPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGA 341
Cdd:COG0666   155 ------------------------TPLHLAaanGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1743221411 342 NADARGEHGNTPLHLAMSKDNVEMVKALIVFGAEVDTLNDFGETPAFLASK 392
Cdd:COG0666   211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261
Pat17_PNPLA8_PNPLA9_like2 cd07215
Patatin-like phospholipase of bacteria; Patatin is a storage protein of the potato tuber that ...
 426-749 7.76e-29

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: 117.89  E-value: 7.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 426 LLCLDGGGVKGLVIIQLLIAIE----KASG---VATKDLFDWVAGTSTGGILALAIL-------HSKSMAYMRGVYFRMK 491
Cdd:cd07215     2 ILSIDGGGIRGIIPATILVSVEeklqKKTGnpeARLADYFDLVAGTSTGGILTCLYLcpnesgrPKFSAKEALNFYLERG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 492 DEVFRGSR-------------PYESGPLEEFLKREFGEhTKMTDVKKPKVMLTGTLSDRQPaelHLFRNYDApeTVREPR 558
Cdd:cd07215    82 NYIFKKKIwnkiksrggflneKYSHKPLEEVLLEYFGD-TKLSELLKPCLITSYDIERRSP---HFFKSHTA--IKNEQR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 559 fnqnvnlrppaqpsDQLVWRAARSSGAAPTYFRPNgRF----------LDGGLLANNPTLDAMTEiheynqdlIRKGQAN 628
Cdd:cd07215   156 --------------DFYVRDVARATSAAPTYFEPA-RIhsltgekytlIDGGVFANNPTLCAYAE--------ARKLKFE 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 629 KVKKLS----IVVSLGTGRSpqvpvtcvdvfRPSNPWELAKTvFGAKELGKMVVDCCTDPDGRAVDRARAW---CEMVGI 701
Cdd:cd07215   213 QPGKPTakdmIILSLGTGKN-----------KKSYTYEKVKD-WGLLGWAKPLIDIMMDGASQTVDYQLKQifdAEGDQQ 280

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1743221411 702 QYFRLNPQL-GTDIMLDEVSDTVLVNALWETEVYIYEHREEFQKLIQLL 749
Cdd:cd07215   281 QYLRIQPELeDADPEMDDASPENLEKLREVGQALAEDHKDQLDEIVDRL 329
Pat17_PNPLA8_PNPLA9_like3 cd07216
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 426-718 2.25e-26

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: 110.08  E-value: 2.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 426 LLCLDGGGVKG---LVIIQ-LLIAIEKASGVA----TKDLFDWVAGTSTGGILALailhsksmayMRG-----------V 486
Cdd:cd07216     3 LLSLDGGGVRGlssLLILKeIMERIDPKEGLDeppkPCDYFDLIGGTSTGGLIAI----------MLGrlrmtvdecidA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 487 YFRMKDEVFRGSRPYESGPLEEFLKREFG----------------EHTKMTDVKKP---KVMLTGTLSDrQPAELHLFRN 547
Cdd:cd07216    73 YTRLAKKIFSRKRLRLIIGDLRTGARFDSkklaeaikvilkelgnDEDDLLDEGEEdgcKVFVCATDKD-VTGKAVRLRS 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 548 YDAPetvREPRFNQNVNlrppaqpsdqlVWRAARSSGAAPTYFRP------NGRFLDGGLLANNPTLDAMTEIHEYNQDL 621
Cdd:cd07216   152 YPSK---DEPSLYKNAT-----------IWEAARATSAAPTFFDPvkigpgGRTFVDGGLGANNPIREVWSEAVSLWEGL 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 622 IRkgqankvkKLSIVVSLGTGRSPQVpvtcvdVFRPSnpwelAKTVFGAKELGKMVvdccTDPDGRAVDRARAWCEMVGI 701
Cdd:cd07216   218 AR--------LVGCLVSIGTGTPSIK------SLGRS-----AEGAGLLKGLKDLV----TDTEAEAKRFSAEHSELDEE 274

                         330
                  ....*....|....*....
gi 1743221411 702 -QYFRLN-PQLGTDIMLDE 718
Cdd:cd07216   275 gRYFRFNvPHGLEDVGLDE 293
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 427-721 1.99e-24

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: 103.91  E-value: 1.99e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 427 LCLDGGGVKGLVIIQLLIAIEKA--SGVATKDLFdwvAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRPYE-- 502
Cdd:cd07213     5 LSLDGGGVKGIVQLVLLKRLAEEfpSFLDQIDLF---AGTSAGSLIALGLALGYSPRQVLKLYEEVGLKVFSKSSAGGga 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 503 -------SGPLEEFLKREFGEhTKMTDVKKpKVMLTGTLSDRQPaelhlfrnydaPETVR--EPRFNQNVnlrPPAQPSD 573
Cdd:cd07213    82 gnnqyfaAGFLKAFAEVFFGD-LTLGDLKR-KVLVPSFQLDSGK-----------DDPNRrwKPKLFHNF---PGEPDLD 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 574 QLVWRAARSSGAAPTYFRPNGRFLDGGLLANNPTLDAMTEIheynqdLIRKGQANKVKKLSiVVSLGTGRSPQvPVTcvD 653
Cdd:cd07213   146 ELLVDVCLRSSAAPTYFPSYQGYVDGGVFANNPSLCAIAQA------IGEEGLNIDLKDIV-VLSLGTGRPPS-YLD--G 215

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1743221411 654 VFRPSNpWELAKTvfgAKELGKMVVdcctdpDGRaVDRARAWCEMV-GIQYFRLNPQLGTDIMLDEVSD 721
Cdd:cd07213   216 ANGYGD-WGLLQW---LPDLLDLFM------DAG-VDAADFQCRQLlGERYFRLDPVLPANIDLDDNKQ 273
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
425-635 5.66e-22

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 97.57  E-value: 5.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 425 HLLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSR----- 499
Cdd:NF041079    2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILALALALEIPARELVELFEEHGKDIFPKRKwprrl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 500 -------PYESGPLEEFLKREFGEhTKMTDVKKPKVMLTGTLSDRQPaelHLFRnydapeTVREPRFNQNVNLRppaqps 572
Cdd:NF041079   82 lgllkkpKYSSEPLREVLEEIFGD-KTIGDLKHRVLIPAVNYTTGKP---QVFK------TPHHPDFTRDHKLK------ 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743221411 573 dqLVwRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAMTEIHEY-NQdlirkgQANKVKKLSI 635
Cdd:NF041079  146 --LV-DVALATSAAPTYFPLhefdNEQFVDGGLVANNPGLLGLHEALHFlGV------PYDDVRILSI 204
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 427-611 1.55e-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: 93.06  E-value: 1.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 427 LCLDGGGVKGLVIIQLLIAIEKAsgvatKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRP------ 500
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEA-----GIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRkralsl 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 501 -------------YESGPLEEFLKREFGEHTKMTDVKKPKVMLTGTLSDRqpaelhlfrnydaPETVREPRFNQNVNLRP 567
Cdd:pfam01734  76 lallrgligegglFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRAL-------------LTVISTALGTRARILLP 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1743221411 568 PAQPSDQLVWRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAM 611
Cdd:pfam01734 143 DDLDDDEDLADAVLASSALPGVFPPvrldGELYVDGGLVDNVPVEAAL 190
Pat17_PNPLA8_PNPLA9_like4 cd07217
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 426-710 1.62e-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: 132856 [Multi-domain]  Cd Length: 344  Bit Score: 87.55  E-value: 1.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 426 LLCLDGGGVKGLVIIQLLIAIEKASGVATK-------DLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVF--- 495
Cdd:cd07217     3 ILALDGGGIRGLLSVEILGRIEKDLRTHLDdpefrlgDYFDFVGGTSTGSIIAACIALGMSVTDLLSFYTLNGVNMFdka 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 496 ------RGSRPYESGPLEEFLKR--EFGEHTKMTD--VKKPKVMLTGTLSDRQPAELHlfRNYDApetvrepRFNQNVnl 565
Cdd:cd07217    83 wlaqrlFLNKLYNQYDPTNLGKKlnTVFPETTLGDdtLRTLLMIVTRNATTGSPWPVC--NNPEA-------KYNDSD-- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 566 rPPAQPSDQLVWRAARSSGAAPTYFRPN---------GRFLDGGL-LANNPTLDAMTEIHEYNQDLIRKGQANKVkklsI 635
Cdd:cd07217   152 -RSDCNLDLPLWQLVRASTAAPTFFPPEvvsiapgtaFVFVDGGVtTYNNPAFQAFLMATAKPYKLNWEVGADNL----L 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 636 VVSLGTGRSPQVpvtcVDVFRPSNPWEL--AKTV-----FGAKELGKMVV----DCctdPDGRAVDR-------ARAWCE 697
Cdd:cd07217   227 LVSVGTGFAPEA----RPDLKAADMWALdhAKYIpsalmNAANAGQDMVCrvlgEC---RKGGLVDReigtmhvDPNWLG 299

                         330
                  ....*....|...
gi 1743221411 698 MVGIQYFRLNPQL 710
Cdd:cd07217   300 PKLFTYVRYDVSL 312
Ank_2 pfam12796
Ankyrin repeats (3 copies);
291-380 1.62e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 1.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 291 LHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHgANADARgEHGNTPLHLAMSKDNVEMVK 367
Cdd:pfam12796   1 LHLAaknGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1743221411 368 ALIVFGAEVDTLN 380
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 167-390 1.78e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 85.49  E-value: 1.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 167 ILVELVQYCHAQMDVTDYKGE---TVFHYAVQGDNSQVLQLLGKNAvAGLNQVNNQGLTPLHLACQLGK-----QEMVRV 238
Cdd:PHA03100   13 IKVKNIKYIIMEDDLNDYSYKkpvLPLYLAKEARNIDVVKILLDNG-ADINSSTKNNSTPLHYLSNIKYnltdvKEIVKL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 239 LLLCNARCNIMGPNG-YPIHSAMkfSQKGCaemiismdssqihskdprygasplhwakNAEMARMLLKRGCNVNSTSSAG 317
Cdd:PHA03100   92 LLEYGANVNAPDNNGiTPLLYAI--SKKSN----------------------------SYSIVEYLLDNGANVNIKNSDG 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 318 NTALHVAVMRNRFDCAIV------------------LLTHGANADARGEHGNTPLHLAMSKDNVEMVKALIVFGAEVDTL 379
Cdd:PHA03100  142 ENLLHLYLESNKIDLKILkllidkgvdinaknrvnyLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV 221

                         250
                  ....*....|.
gi 1743221411 380 NDFGETPAFLA 390
Cdd:PHA03100  222 NKYGDTPLHIA 232
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 190-401 2.08e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 82.62  E-value: 2.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 190 FHYAVQGDNSQVLQLL---GKNavagLNQVNNQGLTPLHLAC----QLGKQEMVRVLLLCNarcniMGPNGYPIHSAMKF 262
Cdd:PHA02878   41 LHQAVEARNLDVVKSLltrGHN----VNQPDHRDLTPLHIICkepnKLGMKEMIRSINKCS-----VFYTLVAIKDAFNN 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 263 SQKGCAEMII--------SMDSSQIHSKDP-------------RYGA-----------SPLHWA---KNAEMARMLLKRG 307
Cdd:PHA02878  112 RNVEIFKIILtnrykniqTIDLVYIDKKSKddiieaeitklllSYGAdinmkdrhkgnTALHYAtenKDQRLTELLLSYG 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 308 CNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSK-DNVEMVKALIVFGAEVDTLNDF-GET 385
Cdd:PHA02878  192 ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLT 271

                         250
                  ....*....|....*.
gi 1743221411 386 PAFLASKISRQLQDLM 401
Cdd:PHA02878  272 ALHSSIKSERKLKLLL 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
156-249 3.55e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 3.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 156 LHLACRKGDGEILVELVQyCHAQMDVTDYKGETVFHYAVQGDNSQVLQLLGKNAVAglnQVNNQGLTPLHLACQLGKQEM 235
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEI 76

                          90
                  ....*....|....
gi 1743221411 236 VRVLLLCNARCNIM 249
Cdd:pfam12796  77 VKLLLEKGADINVK 90
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 154-380 1.60e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 80.49  E-value: 1.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 154 TPLHLACRKGDGEILVELVQYcHAQMDVTDYKGETVFHYAVQGDNSQVLQLLGKNAvaglNQVNNQGLTPLHlacQLGKQ 233
Cdd:PHA02876  180 TPIHYAAERGNAKMVNLLLSY-GADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR----SNINKNDLSLLK---AIRNE 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 234 EMVRVLLLCNARCNIMGPNGY---PIHSAMKFSQKGCAEMIISMDSSQIHSKDPRyGASPLH-WAKNA---EMARMLLKR 306
Cdd:PHA02876  252 DLETSLLLYDAGFSVNSIDDCkntPLHHASQAPSLSRLVPKLLERGADVNAKNIK-GETPLYlMAKNGydtENIRTLIML 330

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1743221411 307 GCNVNSTSSAGNTALHVAVMRNRF-DCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMVKALIVFGAEVDTLN 380
Cdd:PHA02876  331 GADVNAADRLYITPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALS 405
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 220-377 2.06e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 79.26  E-value: 2.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 220 GLTPLHLACQLGKQEMVRVLLLCNARCNIMGPN-GYPIHSAMKFSQKGCAEMIISMDS--SQIHSKDpryGASPLHWA-- 294
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDiESELHDAVEEGDVKAVEELLDLGKfaDDVFYKD---GMTPLHLAti 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 295 -KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMVKALIVFG 373
Cdd:PHA02875  112 lKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191


                  ....
gi 1743221411 374 AEVD 377
Cdd:PHA02875  192 ANID 195
PHA03095 PHA03095
ankyrin-like protein; Provisional
 152-390 2.86e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.91  E-value: 2.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 152 GCTPLH--LACRKGDGEILVELVQYCHAQMDVTDYKGETVFHYAVQGDNS-QVLQLLGKNAvAGLNQVNNQGLTPLHlAC 228
Cdd:PHA03095   47 GKTPLHlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAG-ADVNAKDKVGRTPLH-VY 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 229 QLGKQ---EMVRVLLLCNARCNIMGPNGY-PIHSAMKFsqKGCA----EMIISMDSSqIHSKDPRyGASPLH-----WAK 295
Cdd:PHA03095  125 LSGFNinpKVIRLLLRKGADVNALDLYGMtPLAVLLKS--RNANvellRLLIDAGAD-VYAVDDR-FRSLLHhhlqsFKP 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 296 NAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIV--LLTHGANADARGEHGNTPLHLAMSKDNVEMVKALIVFG 373
Cdd:PHA03095  201 RARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280

                         250
                  ....*....|....*..
gi 1743221411 374 AEVDTLNDFGETPAFLA 390
Cdd:PHA03095  281 ADINAVSSDGNTPLSLM 297
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 150-392 2.03e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.99  E-value: 2.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 150 EEGCTPLHLACRKGDGEIlVELVQYCHAQMDVTDYKGETVFHYAVQGDNSQVLQLLGKNAV------------------- 210
Cdd:PHA02874   33 DETTTPLIDAIRSGDAKI-VELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVdtsilpipciekdmiktil 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 211 ---AGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPNG-YPIHSAMKFSQKGCAEMIISmDSSQIHSKDpRY 286
Cdd:PHA02874  112 dcgIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGcYPIHIAIKHNFFDIIKLLLE-KGAYANVKD-NN 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 287 GASPLHWAK---NAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRfdCAIVLLTHGANADARGEHGNTPLHLAMSKD-N 362
Cdd:PHA02874  190 GESPLHNAAeygDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR--SAIELLINNASINDQDIDGSTPLHHAINPPcD 267

                         250       260       270
                  ....*....|....*....|....*....|
gi 1743221411 363 VEMVKALIVFGAEVDTLNDFGETPAFLASK 392
Cdd:PHA02874  268 IDIIDILLYHKADISIKDNKGENPIDTAFK 297
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 151-344 3.35e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 69.25  E-value: 3.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 151 EGCTPLHLACRKGDGEILVELVQYcHAQMDVTDYKGETVFHYAV-QGDNSQVLQLLGKNAVAGlNQVNNQGLTPLHLACQ 229
Cdd:PHA02875   34 DGISPIKLAMKFRDSEAIKLLMKH-GAIPDVKYPDIESELHDAVeEGDVKAVEELLDLGKFAD-DVFYKDGMTPLHLATI 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 230 LGKQEMVRVLLLCNARCNIMGPNGY-PIHSAMKFSQKGCAEMIIsmDSSQIHSKDPRYGASPLHWA---KNAEMARMLLK 305
Cdd:PHA02875  112 LKKLDIMKLLIARGADPDIPNTDKFsPLHLAVMMGDIKGIELLI--DHKACLDIEDCCGCTPLIIAmakGDIAICKMLLD 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1743221411 306 RGCNVNSTSSAGN-TALHVAVMRNRFDCAIVLLTHGANAD 344
Cdd:PHA02875  190 SGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCN 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
224-346 4.21e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.83  E-value: 4.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 224 LHLACQLGKQEMVRVLLLCNARCNIMGPNGYpihsamkfsqkgcaemiismdssqihskdprygaSPLHWA---KNAEMA 300
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGR----------------------------------TALHLAaknGHLEIV 46

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1743221411 301 RMLLKRgCNVNSTSSaGNTALHVAVMRNRFDCAIVLLTHGANADAR 346
Cdd:pfam12796  47 KLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVK 90
Pat17_isozyme_like cd07214
Patatin-like phospholipase of plants; Pat17 is an isozyme of patatin cloned from Solanum ...
 426-646 1.69e-11

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


Pssm-ID: 132853 [Multi-domain]  Cd Length: 349  Bit Score: 66.31  E-value: 1.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 426 LLCLDGGGVKGLVIIQLLIAIEK------ASGVATKDLFDWVAGTSTGGILAlAIL-----HSKSMAYMRGV---YFRMK 491
Cdd:cd07214     6 VLSIDGGGIRGIIPATILEFLEGklqeldGPDARIADYFDVIAGTSTGGLIT-AMLtapneNKRPLFAAKDIvqfYLENG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 492 DEVFRGSR-PYES---------GP------LEEFLKREFGEhTKMTDVKKPKVMLTGTLSDRQPAelhLFRNYDApetVR 555
Cdd:cd07214    85 PKIFPQSTgQFEDdrkklrsllGPkydgvyLHDLLNELLGD-TRLSDTLTNVVIPTFDIKLLQPV---IFSSSKA---KN 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 556 EPRFNqnvnlrppAQPSDqlvwrAARSSGAAPTYFrPNGRF--------------LDGGLLANNPTLDAMT----EIHEY 617
Cdd:cd07214   158 DKLTN--------ARLAD-----VCISTSAAPTYF-PAHYFttedsngdirefnlVDGGVAANNPTLLAISevtkEIIKD 223

                         250       260
                  ....*....|....*....|....*....
gi 1743221411 618 NQDLIRKGQANKVKKLsiVVSLGTGRSPQ 646
Cdd:cd07214   224 NPFFASIKPLDYKKLL--VLSLGTGSAEE 250
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 181-402 2.90e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.01  E-value: 2.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 181 VTDYKgETVFHYAVQGDNSQVL--QLLGKNAvaGLNQVNNQGLTPLHLACQLG-KQEMVRVLLLCNARCNIMGP-NGYPI 256
Cdd:PHA02876  269 IDDCK-NTPLHHASQAPSLSRLvpKLLERGA--DVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRlYITPL 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 257 HSAMKFSQKGCAEMIISMDSSQIHSKDpRYGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVM-RNRFDC 332
Cdd:PHA02876  346 HQASTLDRNKDIVITLLELGANVNARD-YCDKTPIHYAavrNNVVIINTLLDYGADIEALSQKIGTALHFALCgTNPYMS 424

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1743221411 333 AIVLLTHGANADARGEHGNTPLHLAMSKD-NVEMVKALIVFGAEVDTLNDFGETPAFLASKISRQLQDLMH 402
Cdd:PHA02876  425 VKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGIVNILLH 495
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
268-392 4.51e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.59  E-value: 4.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 268 AEMIISMDSSQIHSKDPRYGASPLHWAKNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARG 347
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1743221411 348 EHGNTPLHLAMSKDNVEMVKALIVFGAEVDTLNDFGETPAFLASK 392
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAY 129
Ank_2 pfam12796
Ankyrin repeats (3 copies);
321-392 1.29e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.59  E-value: 1.29e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1743221411 321 LHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMVKALIVFgAEVDtLNDFGETPAFLASK 392
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAAR 70
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 194-395 1.62e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 64.31  E-value: 1.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 194 VQGDNSQVLQLLGKNAvAGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPNGYPI-HSAMKFSQKGCAEMII 272
Cdd:PHA02876  153 IQQDELLIAEMLLEGG-ADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVlECAVDSKNIDTIKAII 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 273 SmDSSQIHSKDprygASPLHWAKNA--EMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAI-VLLTHGANADARGEH 349
Cdd:PHA02876  232 D-NRSNINKND----LSLLKAIRNEdlETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVpKLLERGADVNAKNIK 306

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1743221411 350 GNTPLHLaMSKD--NVEMVKALIVFGAEVDTLNDFGETPAFLASKISR 395
Cdd:PHA02876  307 GETPLYL-MAKNgyDTENIRTLIMLGADVNAADRLYITPLHQASTLDR 353
PHA03095 PHA03095
ankyrin-like protein; Provisional
 152-332 2.51e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.51  E-value: 2.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 152 GCTPLHLACRKGDGEILVELVQYCHAQMDVTDYKGETVFHYAVQGDN---SQVLQLLGKNAvaGLNQVNNQGLTPLHL-- 226
Cdd:PHA03095   83 GFTPLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNinpKVIRLLLRKGA--DVNALDLYGMTPLAVll 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 227 ---ACQLgkqEMVRVLL---------------------------------LCNARCNIMGPNGY---PIHSAMKFSQkgC 267
Cdd:PHA03095  161 ksrNANV---ELLRLLIdagadvyavddrfrsllhhhlqsfkprarivreLIRAGCDPAATDMLgntPLHSMATGSS--C 235

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1743221411 268 AEMIIS---MDSSQIHSKDpRYGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDC 332
Cdd:PHA03095  236 KRSLVLpllIAGISINARN-RYGQTPLHYAavfNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRA 305
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 196-411 2.59e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.44  E-value: 2.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 196 GDNSQVLQLLgKNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPN-GYPIHSAMKFSQKGCAEMII-- 272
Cdd:PHA02874   12 GDIEAIEKII-KNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKiPHPLLTAIKIGAHDIIKLLIdn 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 273 SMDSSQIHSKDprygasplhwaKNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNT 352
Cdd:PHA02874   91 GVDTSILPIPC-----------IEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCY 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1743221411 353 PLHLAMSKDNVEMVKALIVFGAEVDTLNDFGETPAFLASK------ISRQLQDLMHISRARKPGF 411
Cdd:PHA02874  160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEygdyacIKLLIDHGNHIMNKCKNGF 224
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 147-381 4.65e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 62.29  E-value: 4.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 147 TENEEGCTPLHLACRKGDGEILVELVQYcHAQMDVTDYKGETVFHYAVQGDNSQVLQLLGKNAvAGLNQVNNQGLTPLHL 226
Cdd:PHA02874  119 IKDAELKTFLHYAIKKGDLESIKMLFEY-GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLHN 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 227 ACQLGKQEMVRVLLLCNARCNIMGPNGY-PIHSAMKFSqKGCAEMIISMDSSQIHSKDpryGASPLHWAknaemarmlLK 305
Cdd:PHA02874  197 AAEYGDYACIKLLIDHGNHIMNKCKNGFtPLHNAIIHN-RSAIELLINNASINDQDID---GSTPLHHA---------IN 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 306 RGCNVnstssagntalhvavmrnrfDCAIVLLTHGANADARGEHGNTPLHLAM---SKDNVemVKALI---VFGAEVDTL 379
Cdd:PHA02874  264 PPCDI--------------------DIIDILLYHKADISIKDNKGENPIDTAFkyiNKDPV--IKDIIanaVLIKEADKL 321


                  ..
gi 1743221411 380 ND 381
Cdd:PHA02874  322 KD 323
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 154-370 5.39e-10

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: 62.72  E-value: 5.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 154 TPLHLACRKGDGEILVELVQYCHAQMDVTDYKGETVFHYAVQGDNSQVLQLLgKNAVAGLnqVNN-------QGLTPLHL 226
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVL-MEAAPEL--VNEpmtsdlyQGETALHI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 227 ACQLGKQEMVRVLLlcnarcnimgpngypihsamkfsQKGcAEMIISMDSSQIHSKDPR----YGASPLHWAK---NAEM 299
Cdd:cd22192    96 AVVNQNLNLVRELI-----------------------ARG-ADVVSPRATGTFFRPGPKnliyYGEHPLSFAAcvgNEEI 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 300 ARMLLKRGCNVNSTSSAGNTALHVAVMRN--RFDCAI--VLLTHGANADA------RGEHGNTPLHLAMSKDNVEMVKAL 369
Cdd:cd22192   152 VRLLIEHGADIRAQDSLGNTVLHILVLQPnkTFACQMydLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHL 231


                  .
gi 1743221411 370 I 370
Cdd:cd22192   232 V 232
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 153-345 1.38e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.83  E-value: 1.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 153 CTPLHLACRKGDGEILVELVQ--YCHAQMDVTDYkgeTVFHY-----AVQGDNSQVLQLLGKNAvAGLNQVNNQGLTPLH 225
Cdd:PHA03100   36 VLPLYLAKEARNIDVVKILLDngADINSSTKNNS---TPLHYlsnikYNLTDVKEIVKLLLEYG-ANVNAPDNNGITPLL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 226 LA--CQLGKQEMVRVLLLCNARCNIMGPNGY-PIHSAMKFS------------------QKGCAEMIISMDSSqIHSKDp 284
Cdd:PHA03100  112 YAisKKSNSYSIVEYLLDNGANVNIKNSDGEnLLHLYLESNkidlkilkllidkgvdinAKNRVNYLLSYGVP-INIKD- 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743221411 285 RYGASPLH---WAKNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADA 345
Cdd:PHA03100  190 VYGFTPLHyavYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_5 pfam13857
Ankyrin repeats (many copies);
303-357 1.80e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.89  E-value: 1.80e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1743221411 303 LLKRG-CNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLA 357
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 287-385 5.78e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 59.50  E-value: 5.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 287 GASPLHWAKN---AEMARMLLKRGCNVNSTSSAGNTALHVAVM-------------------------------RNRFDC 332
Cdd:PLN03192  558 GRTPLHIAASkgyEDCVLVLLKHACNVHIRDANGNTALWNAISakhhkifrilyhfasisdphaagdllctaakRNDLTA 637

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1743221411 333 AIVLLTHGANADARGEHGNTPLHLAMSKDNVEMVKALIVFGAEVD---TLNDFGET 385
Cdd:PLN03192  638 MKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDkanTDDDFSPT 693
Ank_4 pfam13637
Ankyrin repeats (many copies);
317-370 6.81e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 6.81e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1743221411 317 GNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMVKALI 370
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 299-378 1.14e-08

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: 58.49  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 299 MARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHG---ANADARGE--HGNTPLHLAMSKDNVEMVKALIVFG 373
Cdd:cd22192    33 IKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelVNEPMTSDlyQGETALHIAVVNQNLNLVRELIARG 112


                  ....*
gi 1743221411 374 AEVDT 378
Cdd:cd22192   113 ADVVS 117
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 427-607 2.37e-08

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: 54.59  E-value: 2.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 427 LCLDGGGVKGLVIIQLLIAIEKAsGVatkdLFDWVAGTSTGGILA--LAI-LHSKSMAY--MRGVYFRMKDE----VFRG 497
Cdd:cd07207     2 LVFEGGGAKGIAYIGALKALEEA-GI----LKKRVAGTSAGAITAalLALgYSAADIKDilKETDFAKLLDSpvglLFLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 498 SRPYESG------PLEEFLKREFGEHTKMTDVKKpkvmLTGTLSDRQPAELHLF-RNYDapeTVREPRFNQNvnlrppaQ 570
Cdd:cd07207    77 PSLFKEGglykgdALEEWLRELLKEKTGNSFATS----LLRDLDDDLGKDLKVVaTDLT---TGALVVFSAE-------T 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1743221411 571 PSDQLVWRAARSSGAAPTYFRP-----NGRFLDGGLLANNPT 607
Cdd:cd07207   143 TPDMPVAKAVRASMSIPFVFKPvrlakGDVYVDGGVLDNYPV 184
PHA03095 PHA03095
ankyrin-like protein; Provisional
 301-386 2.69e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.96  E-value: 2.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 301 RMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCA-IV--LLTHGANADARGEHGNTPLHLAMSKDNVE-MVKALIVFGAEV 376
Cdd:PHA03095   31 RRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdIVrlLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADV 110

                          90
                  ....*....|
gi 1743221411 377 DTLNDFGETP 386
Cdd:PHA03095  111 NAKDKVGRTP 120
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 227-390 8.19e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.38  E-value: 8.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 227 ACQLGKQEMVRVLLLCNARCNIMGPNGY-PIHSAMKFSQKGCAEMIISmdssqiHSKDPRYGA----SPLHWA---KNAE 298
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGIsPIKLAMKFRDSEAIKLLMK------HGAIPDVKYpdieSELHDAveeGDVK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 299 MARMLLKRGCNVNST-SSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMVKALIVFGAEVD 377
Cdd:PHA02875   83 AVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162

                         170
                  ....*....|...
gi 1743221411 378 TLNDFGETPAFLA 390
Cdd:PHA02875  163 IEDCCGCTPLIIA 175
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 201-386 1.34e-07

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 55.30  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 201 VLQLLGKNAVaGLNQVNNQGLTPLHLACQLGK------QEMVRVLLLCNARC-NIMGPNGYPIHSAMKFSQKGCAEMIIS 273
Cdd:PHA02716  194 ILEWLCNNGV-NVNLQNNHLITPLHTYLITGNvcasviKKIIELGGDMDMKCvNGMSPIMTYIINIDNINPEITNIYIES 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 274 MDSSQIhSKDPRYGASPLHWAKNAEMARM--LLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIV--LLTHGANADARGEH 349
Cdd:PHA02716  273 LDGNKV-KNIPMILHSYITLARNIDISVVysFLQPGVKLHYKDSAGRTCLHQYILRHNISTDIIklLHEYGNDLNEPDNI 351

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1743221411 350 GNTPLHLAMSK-----------DN---VEMVKALIVFGAEVDTLNDFGETP 386
Cdd:PHA02716  352 GNTVLHTYLSMlsvvnildpetDNdirLDVIQCLISLGADITAVNCLGYTP 402
Ank_4 pfam13637
Ankyrin repeats (many copies);
289-337 4.83e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 4.83e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1743221411 289 SPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLL 337
Cdd:pfam13637   3 TALHAAaasGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 154-376 7.23e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.76  E-value: 7.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 154 TPLHLACRKGDGEILVELVQYCHAQMDVTDYKGETVFHYAVQG----DNSQVLQLLGknavAGLNQVNNQGLTPLHLACQ 229
Cdd:PHA02876  275 TPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNgydtENIRTLIMLG----ADVNAADRLYITPLHQAST 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 230 LGK-QEMVRVLLLCNARCNIMG-PNGYPIHSAMKFSQKGCAEMIISMdSSQIHSKDPRYGASpLHWA---KNAEMA-RML 303
Cdd:PHA02876  351 LDRnKDIVITLLELGANVNARDyCDKTPIHYAAVRNNVVIINTLLDY-GADIEALSQKIGTA-LHFAlcgTNPYMSvKTL 428

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743221411 304 LKRGCNVNSTSSAGNTALHVAVMRN-RFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVemVKALIVFGAEV 376
Cdd:PHA02876  429 IDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGI--VNILLHYGAEL 500
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 300-369 7.95e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.59  E-value: 7.95e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 300 ARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMVKAL 369
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 296-385 9.20e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.56  E-value: 9.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 296 NAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPL-------H------------- 355
Cdd:PLN03192  537 NAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHhkifrilyhfasi 616

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1743221411 356 -----------LAMSKDNVEMVKALIVFGAEVDTLNDFGET 385
Cdd:PLN03192  617 sdphaagdllcTAAKRNDLTAMKELLKQGLNVDSEDHQGAT 657
PHA02946 PHA02946
ankyin-like protein; Provisional
 303-381 9.66e-07

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 51.98  E-value: 9.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 303 LLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDN--VEMVKALIVFGAEVDTLN 380
Cdd:PHA02946   58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNSV 137


                  .
gi 1743221411 381 D 381
Cdd:PHA02946  138 D 138
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 335-390 1.83e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 1.83e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1743221411 335 VLLTHGANADARGEHGNTPLHLAMSKDNVEMVKALIVFGAEVDTLNDFGETPAFLA 390
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
Ank_5 pfam13857
Ankyrin repeats (many copies);
336-390 2.97e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 2.97e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1743221411 336 LLTHG-ANADARGEHGNTPLHLAMSKDNVEMVKALIVFGAEVDTLNDFGETPAFLA 390
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
154-205 4.57e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 4.57e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1743221411 154 TPLHLACRKGDGEILVELVQYcHAQMDVTDYKGETVFHYAVQGDNSQVLQLL 205
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLKLL 53
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 427-610 1.04e-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: 46.57  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 427 LCLDGGGVKGLVIIQLLIAIEKAsGVatkdLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKdevfRGSRPYESGPL 506
Cdd:cd07198     1 LVLSGGGALGIYHVGVAKALRER-GP----LIDIIAGTSAGAIVAALLASGRDLEEALLLLLRLS----REVRLRFDGAF 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 507 EeflkREFgehtKMTDVkkpkvmltgtlsDRQPAELHLFRNYDAPETVREPRFNQNV---NLRPPAQPSDQLVWRAARSS 583
Cdd:cd07198    72 P----PTG----RLLGI------------LRQPLLSALPDDAHEDASGKLFISLTRLtdgENVLVSDTSKGELWSAVRAS 131

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1743221411 584 GAAPTYFRP------NGRFLDGGLLANNPTLDA 610
Cdd:cd07198   132 SSIPGYFGPvplsfrGRRYGDGGLSNNLPVAEL 164
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 150-311 2.28e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.68  E-value: 2.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 150 EEGCTPLHLACRKGDGEILVELVQYcHAQMDVTDYKGETVFHYAVQGDNSQVLQLLGKNAvAGLNQVNNQGLTPLHLACQ 229
Cdd:PHA02875  100 KDGMTPLHLATILKKLDIMKLLIAR-GADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK-ACLDIEDCCGCTPLIIAMA 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 230 LGKQEMVRVLLLCNARCNImgpngypihsamkFSQKGC-AEMIISMDSSQIhskdprygasplhwaknaEMARMLLKRGC 308
Cdd:PHA02875  178 KGDIAICKMLLDSGANIDY-------------FGKNGCvAALCYAIENNKI------------------DIVRLFIKRGA 226


                  ...
gi 1743221411 309 NVN 311
Cdd:PHA02875  227 DCN 229
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 255-386 2.41e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.97  E-value: 2.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 255 PIHSAM--KFSQKGCAEMIISmDSSQIHSKDPRYGASPLH----WAKNA--EMARMLLKRGCNVNSTSSAGNTALHVaVM 326
Cdd:PHA02859   54 PIFSCLekDKVNVEILKFLIE-NGADVNFKTRDNNLSALHhylsFNKNVepEILKILIDSGSSITEEDEDGKNLLHM-YM 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743221411 327 RN---RFDCAIVLLTHGANADARGEHGNTPLH-LAMSKDNVEMVKALIVFGAEVDTLNDFGETP 386
Cdd:PHA02859  132 CNfnvRINVIKLLIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNC 195
Ank_4 pfam13637
Ankyrin repeats (many copies);
350-395 2.48e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 2.48e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1743221411 350 GNTPLHLAMSKDNVEMVKALIVFGAEVDTLNDFGETPAFLASKISR 395
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
Ank_5 pfam13857
Ankyrin repeats (many copies);
171-227 4.05e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 4.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1743221411 171 LVQYCHAQMDVTDYKGETVFHYAVQGDNSQVLQLLGKNAVAgLNQVNNQGLTPLHLA 227
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD-LNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
285-324 4.38e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 4.38e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1743221411 285 RYGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVA 324
Cdd:pfam13857  14 GEGYTPLHVAakyGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 164-339 4.80e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.41  E-value: 4.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 164 DGEILVELVQYCHAQMDVTDYKGETVFHYAVQGDNSQVLQLL---GKNaVAGLNQVNNqglTPLHLACQLGKQEMVRVLL 240
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLlsyGAN-VNIPDKTNN---SPLHHAVKHYNKPIVHILL 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 241 LCNARCNIMGPNG-YPIHSAMKFSQKGCAEMIISMDSSQIHSKDPRYGASPLHWA-KNAEMARMLLKRGCNVNSTSSAGN 318
Cdd:PHA02878  222 ENGASTDARDKCGnTPLHISVGYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSiKSERKLKLLLEYGADINSLNSYKL 301

                         170       180
                  ....*....|....*....|..
gi 1743221411 319 TALHVAVM-RNRFDCAIVLLTH 339
Cdd:PHA02878  302 TPLSSAVKqYLCINIGRILISN 323
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 349-377 4.93e-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: 40.65  E-value: 4.93e-05
                           10        20
                   ....*....|....*....|....*....
gi 1743221411  349 HGNTPLHLAMSKDNVEMVKALIVFGAEVD 377
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 276-376 5.52e-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: 46.61  E-value: 5.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 276 SSQIHSKDPrYGASPLHWA----KNAEMARMLLKRGCNVnstsSAGNTALHVAVMR---NRFDCAIVLLTHG-------- 340
Cdd:TIGR00870  42 KLNINCPDR-LGRSALFVAaienENLELTELLLNLSCRG----AVGDTLLHAISLEyvdAVEAILLHLLAAFrksgplel 116

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1743221411 341 ANADARGE--HGNTPLHLAMSKDNVEMVKALIVFGAEV 376
Cdd:TIGR00870 117 ANDQYTSEftPGITALHLAAHRQNYEIVKLLLERGASV 154
Ank_2 pfam12796
Ankyrin repeats (3 copies);
103-183 6.41e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.41  E-value: 6.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 103 HTEVLQHLTDL-----IRNHPSWSVAHLAVELGIRECFhhSRIISCANCTENEEGCTPLHLACRKGDGEIlVELVQYCHA 177
Cdd:pfam12796   9 NLELVKLLLENgadanLQDKNGRTALHLAAKNGHLEIV--KLLLEHADVNLKDNGRTALHYAARSGHLEI-VKLLLEKGA 85


                  ....*.
gi 1743221411 178 QMDVTD 183
Cdd:pfam12796  86 DINVKD 91
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 349-381 6.97e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 6.97e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1743221411 349 HGNTPLHLA-MSKDNVEMVKALIVFGAEVDTLND 381
Cdd:pfam00023   1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 152-240 8.01e-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: 45.90  E-value: 8.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 152 GCTPLHLACRKGDGEILVELVQYCHAQMDVTDYKGETVFHYAVQ-GDNSQVL---------QLLGKNAVAGLNQV-NNQG 220
Cdd:cd22194   188 GETPLALAACTNQPEIVQLLMEKESTDITSQDSRGNTVLHALVTvAEDSKTQndfvkrmydMILLKSENKNLETIrNNEG 267

                          90       100
                  ....*....|....*....|
gi 1743221411 221 LTPLHLACQLGKQEMVRVLL 240
Cdd:cd22194   268 LTPLQLAAKMGKAEILKYIL 287
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 349-378 1.43e-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: 39.55  E-value: 1.43e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1743221411 349 HGNTPLHLAMSKDNVEMVKALIVFGAEVDT 378
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 336-389 3.01e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.86  E-value: 3.01e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1743221411 336 LLTHGANADARGEHGNTPLHLAM---SKDNVEMVKALIVFGAEVDTLNDFGETPAFL 389
Cdd:PHA03095   33 LLAAGADVNFRGEYGKTPLHLYLhysSEKVKDIVRLLLEAGADVNAPERCGFTPLHL 89
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 317-345 6.40e-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: 37.57  E-value: 6.40e-04
                           10        20
                   ....*....|....*....|....*....
gi 1743221411  317 GNTALHVAVMRNRFDCAIVLLTHGANADA 345
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 149-249 8.87e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.29  E-value: 8.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 149 NEEGCTPLHLACRKGDGEiLVELVQYCHAQMDVTDYKGETVFHYAVQGDNSQVLQLLgKNAVAGLNQVNNQG-LTPLHLA 227
Cdd:PHA02875  132 NTDKFSPLHLAVMMGDIK-GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML-LDSGANIDYFGKNGcVAALCYA 209

                          90       100
                  ....*....|....*....|..
gi 1743221411 228 CQLGKQEMVRVLLLCNARCNIM 249
Cdd:PHA02875  210 IENNKIDIVRLFIKRGADCNIM 231
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 287-386 9.77e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 42.69  E-value: 9.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 287 GASPLHWA---KNAEMARMLLK---RGCNVNSTSS--AGNTALHVAVMRNRFDCAIVLLTHGAN-ADAR----------- 346
Cdd:cd22192    51 GETALHVAalyDNLEAAVVLMEaapELVNEPMTSDlyQGETALHIAVVNQNLNLVRELIARGADvVSPRatgtffrpgpk 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1743221411 347 -----GEHgntPLHLAMSKDNVEMVKALIVFGAEVDTLNDFGETP 386
Cdd:cd22192   131 nliyyGEH---PLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 317-346 1.06e-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: 1.06e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1743221411 317 GNTALHVAVMR-NRFDCAIVLLTHGANADAR 346
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNAR 32
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 286-313 2.45e-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: 2.45e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1743221411 286 YGASPLHWA----KNAEMARMLLKRGCNVNST 313
Cdd:pfam00023   1 DGNTPLHLAagrrGNLEIVKLLLSKGADVNAR 32
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 317-345 2.74e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.70  E-value: 2.74e-03
                          10        20
                  ....*....|....*....|....*....
gi 1743221411 317 GNTALHVAVMRNRFDCAIVLLTHGANADA 345
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 219-248 2.78e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 2.78e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1743221411 219 QGLTPLHLAC-QLGKQEMVRVLLLCNARCNI 248
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNA 31
PHA02798 PHA02798
ankyrin-like protein; Provisional
 298-385 3.94e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.59  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 298 EMARMLLKRGCNVNSTSSAGNTAL-----HVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSK---DNVEMVKAL 369
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFM 131

                          90
                  ....*....|....*.
gi 1743221411 370 IVFGAEVDTLNDFGET 385
Cdd:PHA02798  132 IENGADTTLLDKDGFT 147
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 214-447 4.06e-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: 4.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 214 NQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPNGypIHSAMKFSQKGCaEMIISmdssqiHSKDPRYGASPLHW 293
Cdd:TIGR00870  46 NCPDRLGRSALFVAAIENENLELTELLLNLSCRGAVGDTL--LHAISLEYVDAV-EAILL------HLLAAFRKSGPLEL 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 294 AknaeMARMLlkrgcnvnSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGE--------------HGNTPLHLAMS 359
Cdd:TIGR00870 117 A----NDQYT--------SEFTPGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAAC 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 360 KDNVEMVKALIVFGAEVDTLNDFGET--------PAFLA--SKISRQLQD--LMHISRARkpgfilGSMRDEK-RTHDHL 426
Cdd:TIGR00870 185 LGSPSIVALLSEDPADILTADSLGNTllhllvmeNEFKAeyEELSCQMYNfaLSLLDKLR------DSKELEViLNHQGL 258

                         250       260
                  ....*....|....*....|..
gi 1743221411 427 LCLDGGGVKGL-VIIQLLIAIE 447
Cdd:TIGR00870 259 TPLKLAAKEGRiVLFRLKLAIK 280
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 217-377 4.78e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 38.32  E-value: 4.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 217 NNQGLTPLHLACQLGKqemvrVLLLCNARCNIMGPNGYpihSAMKFSQKG--CAEMIISMDSSqihskDPRygasplhwa 294
Cdd:PHA02736   14 DIEGENILHYLCRNGG-----VTDLLAFKNAISDENRY---LVLEYNRHGkqCVHIVSNPDKA-----DPQ--------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 295 knaEMARMLLKRGCNVNSTSSA-GNTALHVAVMRNRFDCAIVLLTH-GANADARGEHGNTPLHLAMSKDNVEMVKALIVF 372
Cdd:PHA02736   72 ---EKLKLLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAK 148


                  ....*
gi 1743221411 373 GAEVD 377
Cdd:PHA02736  149 GAQCK 153
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 212-382 6.25e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.05  E-value: 6.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 212 GLNQVNNQGL--TPLHLACQLGKQEMVRVLLLCNARcnIMGPNGYPIHSAMKFS--QKGCAEMIISMDSSQIHSKDPRYG 287
Cdd:PHA02876   31 GANQCENESIpfTAIHQALQLRQIDIVEEIIQQNPE--LIYITDHKCHSTLHTIciIPNVMDIVISLTLDCDIILDIKYA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 288 ASPLHWAKNAEMARMLLKRGCNVNSTS--SAGNTALHVAVMRNRFD-----CAIVLLTHGANADARGEHGNTPLHLAMSK 360
Cdd:PHA02876  109 SIILNKHKLDEACIHILKEAISGNDIHydKINESIEYMKLIKERIQqdellIAEMLLEGGADVNAKDIYCITPIHYAAER 188

                         170       180
                  ....*....|....*....|....
gi 1743221411 361 DNVEMVKALIVFGAEVD--TLNDF 382
Cdd:PHA02876  189 GNAKMVNLLLSYGADVNiiALDDL 212
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 152-240 6.45e-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: 39.78  E-value: 6.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221411 152 GCTPLHLACRKGDGEILVELVQYCHAQMDV--TDYKGETVFHYAVQ-GDNSQ------------VLQLLGK-NAVAGLNQ 215
Cdd:cd22193   123 GELPLSLAACTNQPDIVQYLLENEHQPADIeaQDSRGNTVLHALVTvADNTKentkfvtrmydmILIRGAKlCPTVELEE 202

                          90       100
                  ....*....|....*....|....*.
gi 1743221411 216 V-NNQGLTPLHLACQLGKQEMVRVLL 240
Cdd:cd22193   203 IrNNDGLTPLQLAAKMGKIEILKYIL 228
Ank_5 pfam13857
Ankyrin repeats (many copies);
147-193 7.25e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 7.25e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1743221411 147 TENEEGCTPLHLACRKGDGEILVELVQYcHAQMDVTDYKGETVFHYA 193
Cdd:pfam13857  11 RLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALDLA 56
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH