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Conserved domains on  [gi|312222743|ref|NP_001185953|]
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85/88 kDa calcium-independent phospholipase A2 isoform 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
426-739 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: 577.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 426 LLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRPYESGP 505
Cdd:cd07212    1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGSRPYNSEP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 506 LEEFLKREFGEHTKMTDVKKPKVMLTGTLSDRQPAELHLFRNYDAPEAVREprCNQNINLKPPTQPADQLVWRAARSSGA 585
Cdd:cd07212   81 LEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEE--PEKNANFLPPTDPAEQLLWRAARSSGA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 586 APTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDMIRKGQGNKVKKLSIVVSLGTGKSPQVPVTCVDVFRPSNPWELAK 665
Cdd:cd07212  159 APTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKSKGRKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSNPWELAK 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312222743 666 TVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGSDIMLDEVSDAVLVNALWETEVYIYEHR 739
Cdd:cd07212  239 TVFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTHR 312
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
102-392 2.34e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.33  E-value: 2.34e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 102 LHVEVLQHLTDLIRNHPSWTVTHLAVELGIRECFHHSRIISCANSTENEEGCTPLHLACRKGDSEILVELVQYCHAQMDV 181
Cdd:COG0666    3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 182 TDNKGETAFHYAVQGDNPQVLQLLgKNASAGLNQVNNQGLTPLHLACKMGKQEMVRVLLLCNArcnimgpggfpihtamk 261
Cdd:COG0666   83 KDDGGNTLLHAAARNGDLEIVKLL-LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA----------------- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 262 fsqkgcaemiismdsnQIHSKDpRYGASPLHWA---KNAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLT 338
Cdd:COG0666  145 ----------------DVNAQD-NDGNTPLHLAaanGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 312222743 339 YGANAGARGEHGNTPLHLAMSKDNMEMVKALIVFGAEVDTPNDFGETPALIASK 392
Cdd:COG0666  208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261
 
Name Accession Description Interval E-value
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
426-739 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: 577.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 426 LLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRPYESGP 505
Cdd:cd07212    1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGSRPYNSEP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 506 LEEFLKREFGEHTKMTDVKKPKVMLTGTLSDRQPAELHLFRNYDAPEAVREprCNQNINLKPPTQPADQLVWRAARSSGA 585
Cdd:cd07212   81 LEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEE--PEKNANFLPPTDPAEQLLWRAARSSGA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 586 APTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDMIRKGQGNKVKKLSIVVSLGTGKSPQVPVTCVDVFRPSNPWELAK 665
Cdd:cd07212  159 APTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKSKGRKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSNPWELAK 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312222743 666 TVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGSDIMLDEVSDAVLVNALWETEVYIYEHR 739
Cdd:cd07212  239 TVFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTHR 312
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
416-723 4.28e-45

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 163.54  E-value: 4.28e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 416 MRDEKRSHdhLLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVF 495
Cdd:COG3621    1 MSANKPFR--ILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAAGYSAEEILDLYEEEGKEIF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 496 RGSRP-------------YESGPLEEFLKREFGEhTKMTDVKKPkVMLTGT-LSDRQPaelHLFRNYDAPeavrePRCNQ 561
Cdd:COG3621   79 PKSRWrkllslrglfgpkYDSEGLEKVLKEYFGD-TTLGDLKTP-VLIPSYdLDNGKP---VFFKSPHAK-----FDRDR 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 562 NInlkpptqpadqLVWRAARSSGAAPTYFRP---------NGRFLDGGLLANNPTLDAMTEIHEYNqdmirkgqGNKVKK 632
Cdd:COG3621  149 DF-----------LLVDVARATSAAPTYFPPaqiknltgeGYALIDGGVFANNPALCALAEALKLL--------GPDLDD 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 633 LsIVVSLGTGKSPQvpvtcvdvfrpSNPWELAKTvFGAKELGKMVVDCCTDPDGRAVDrarAWCEMV-GIQYFRLNPQLG 711
Cdd:COG3621  210 I-LVLSLGTGTAPR-----------SIPYKKVKN-WGALGWLLPLIDILMDAQSDAVD---YQLRQLlGDRYYRLDPELP 273
                        330
                 ....*....|..
gi 312222743 712 SDIMLDEVSDAV 723
Cdd:COG3621  274 EEIALDDNAENI 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
102-392 2.34e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.33  E-value: 2.34e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 102 LHVEVLQHLTDLIRNHPSWTVTHLAVELGIRECFHHSRIISCANSTENEEGCTPLHLACRKGDSEILVELVQYCHAQMDV 181
Cdd:COG0666    3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 182 TDNKGETAFHYAVQGDNPQVLQLLgKNASAGLNQVNNQGLTPLHLACKMGKQEMVRVLLLCNArcnimgpggfpihtamk 261
Cdd:COG0666   83 KDDGGNTLLHAAARNGDLEIVKLL-LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA----------------- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 262 fsqkgcaemiismdsnQIHSKDpRYGASPLHWA---KNAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLT 338
Cdd:COG0666  145 ----------------DVNAQD-NDGNTPLHLAaanGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 312222743 339 YGANAGARGEHGNTPLHLAMSKDNMEMVKALIVFGAEVDTPNDFGETPALIASK 392
Cdd:COG0666  208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
427-611 2.17e-21

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


Pssm-ID: 396341  Cd Length: 190  Bit Score: 92.29  E-value: 2.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743  427 LCLDGGGVKGLVIIQLLIAIEKAsgvatKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRP------ 500
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEA-----GIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRkralsl 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743  501 -------------YESGPLEEFLKREFGEHTKMTDVKKPKVMLTGTLSdrqpAELHLFRNYDAPEAvreprcnqnINLKP 567
Cdd:pfam01734  76 lallrgligegglFDGDALRELLRKLLGDLTLEELAARLSLLLVVALR----ALLTVISTALGTRA---------RILLP 142
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 312222743  568 PTQPADQLVWRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAM 611
Cdd:pfam01734 143 DDLDDDEDLADAVLASSALPGVFPPvrldGELYVDGGLVDNVPVEAAL 190
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
425-641 7.50e-21

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 94.10  E-value: 7.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 425 HLLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSR----- 499
Cdd:NF041079   2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILALALALEIPARELVELFEEHGKDIFPKRKwprrl 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 500 -------PYESGPLEEFLKREFGEhTKMTDVKKPKVMLTGTLSDRQPaelHLFRNYDAPEAVREPRCnqninlkpptqpa 572
Cdd:NF041079  82 lgllkkpKYSSEPLREVLEEIFGD-KTIGDLKHRVLIPAVNYTTGKP---QVFKTPHHPDFTRDHKL------------- 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312222743 573 dQLVwRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAMTEIHEYNqdmirkgqGNKVKKLSIvVSLGT 641
Cdd:NF041079 145 -KLV-DVALATSAAPTYFPLhefdNEQFVDGGLVANNPGLLGLHEALHFL--------GVPYDDVRI-LSIGT 206
Ank_2 pfam12796
Ankyrin repeats (3 copies);
156-249 3.51e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 3.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743  156 LHLACRKGDSEILVELVQyCHAQMDVTDNKGETAFHYAVQGDNPQVLQLLGKNASAglnQVNNQGLTPLHLACKMGKQEM 235
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEI 76
                          90
                  ....*....|....
gi 312222743  236 VRVLLLCNARCNIM 249
Cdd:pfam12796  77 VKLLLEKGADINVK 90
PHA02875 PHA02875
ankyrin repeat protein; Provisional
220-390 3.03e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 84.66  E-value: 3.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 220 GLTPLHLACKMGKQEMVRVLLLCNARCNIMGPG-GFPIHTAMKFSQKGCAEMIISMDS--NQIHSKDpryGASPLHWA-- 294
Cdd:PHA02875  35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDiESELHDAVEEGDVKAVEELLDLGKfaDDVFYKD---GMTPLHLAti 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 295 -KNAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLTYGANAGARGEHGNTPLHLAMSKDNMEMVKALIVFG 373
Cdd:PHA02875 112 lKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
                        170
                 ....*....|....*..
gi 312222743 374 AevdTPNDFGETPALIA 390
Cdd:PHA02875 192 A---NIDYFGKNGCVAA 205
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
154-370 2.67e-13

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 73.12  E-value: 2.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 154 TPLHLACRKGDSEILVELVQYCHAQMDVTDNKGETAFHYAVQGDNPQVLQLLGKNASAGLNQVNN----QGLTPLHLACK 229
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 230 MGKQEMVRVLL-----LCNARCnimgpggfpihTAMKFSQKGCaemiismdsNQIHskdprYGASPLHWAK---NAEMAR 301
Cdd:cd22192   99 NQNLNLVRELIargadVVSPRA-----------TGTFFRPGPK---------NLIY-----YGEHPLSFAAcvgNEEIVR 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312222743 302 MLLKRGCDVDSTSSSGNTALHVAVMRN--RFDCVM--VLLTYGANAGA------RGEHGNTPLHLAMSKDNMEMVKALI 370
Cdd:cd22192  154 LLIEHGADIRAQDSLGNTVLHILVLQPnkTFACQMydLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLV 232
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
152-365 3.09e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.38  E-value: 3.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743  152 GCTPLHLACRKGDSEILVELVQYCHAQMDVtdnkGETAFHYAVQGDNPQV---LQLLGKNASAGLNQ--VNNQ------- 219
Cdd:TIGR00870  52 GRSALFVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLEYVDAVeaiLLHLLAAFRKSGPLelANDQytseftp 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743  220 GLTPLHLACKMGKQEMVRVLLL----CNARCNimgpggfpihtamkfsqkgCAEMIISMDSNQIhskdpRYGASPLHWAK 295
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLErgasVPARAC-------------------GDFFVKSQGVDSF-----YHGESPLNAAA 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743  296 ---NAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFD-------CVMVLLTYGANAGARG----EH-----GNTPLHL 356
Cdd:TIGR00870 184 clgSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKaeyeelsCQMYNFALSLLDKLRDskelEVilnhqGLTPLKL 263

                  ....*....
gi 312222743  357 AMSKDNMEM 365
Cdd:TIGR00870 264 AAKEGRIVL 272
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
349-377 3.78e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.03  E-value: 3.78e-05
                           10        20
                   ....*....|....*....|....*....
gi 312222743   349 HGNTPLHLAMSKDNMEMVKALIVFGAEVD 377
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
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: 577.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 426 LLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRPYESGP 505
Cdd:cd07212    1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGSRPYNSEP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 506 LEEFLKREFGEHTKMTDVKKPKVMLTGTLSDRQPAELHLFRNYDAPEAVREprCNQNINLKPPTQPADQLVWRAARSSGA 585
Cdd:cd07212   81 LEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEE--PEKNANFLPPTDPAEQLLWRAARSSGA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 586 APTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDMIRKGQGNKVKKLSIVVSLGTGKSPQVPVTCVDVFRPSNPWELAK 665
Cdd:cd07212  159 APTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKSKGRKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSNPWELAK 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312222743 666 TVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGSDIMLDEVSDAVLVNALWETEVYIYEHR 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 1.44e-51

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: 180.22  E-value: 1.44e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 427 LCLDGGGVKGLVIIQLLIAIEKASGVATK--DLFDWVAGTSTGGILALAILHSK-SMAYMRGVYFRMKDEVFrgsrpyes 503
Cdd:cd07199    2 LSLDGGGIRGIIPAEILAELEKRLGKPSRiaDLFDLIAGTSTGGIIALGLALGRySAEELVELYEELGRKIF-------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 504 gpleeflkrefgehtkmtdvkkPKVMLTGTlsDRQPAELHLFRNYDAPEavreprcnqninlkpPTQPADQLVWRAARSS 583
Cdd:cd07199   74 ----------------------PRVLVTAY--DLSTGKPVVFSNYDAEE---------------PDDDDDFKLWDVARAT 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 584 GAAPTYFRP--------NGRFLDGGLLANNPTLDAMTEiheynqdmIRKGQGNKVKKLsIVVSLGTGKSPQVPVTCVDVF 655
Cdd:cd07199  115 SAAPTYFPPaviesggdEGAFVDGGVAANNPALLALAE--------ALRLLAPDKDDI-LVLSLGTGTSPSSSSSKKASR 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 656 RPSNPWelaktvfgAKELGKMVVDCCTDPDGRAVDRARAwCEMVGIQYFRLNPQLGSDIM-LDEVSDAVLVNALWETEVY 734
Cdd:cd07199  186 WGGLGW--------GRPLLDILMDAQSDGVDQWLDLLFG-SLDSKDNYLRINPPLPGPIPaLDDASEANLLALDSAAFEL 256

                 .
gi 312222743 735 I 735
Cdd:cd07199  257 I 257
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
416-723 4.28e-45

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 163.54  E-value: 4.28e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 416 MRDEKRSHdhLLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVF 495
Cdd:COG3621    1 MSANKPFR--ILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAAGYSAEEILDLYEEEGKEIF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 496 RGSRP-------------YESGPLEEFLKREFGEhTKMTDVKKPkVMLTGT-LSDRQPaelHLFRNYDAPeavrePRCNQ 561
Cdd:COG3621   79 PKSRWrkllslrglfgpkYDSEGLEKVLKEYFGD-TTLGDLKTP-VLIPSYdLDNGKP---VFFKSPHAK-----FDRDR 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 562 NInlkpptqpadqLVWRAARSSGAAPTYFRP---------NGRFLDGGLLANNPTLDAMTEIHEYNqdmirkgqGNKVKK 632
Cdd:COG3621  149 DF-----------LLVDVARATSAAPTYFPPaqiknltgeGYALIDGGVFANNPALCALAEALKLL--------GPDLDD 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 633 LsIVVSLGTGKSPQvpvtcvdvfrpSNPWELAKTvFGAKELGKMVVDCCTDPDGRAVDrarAWCEMV-GIQYFRLNPQLG 711
Cdd:COG3621  210 I-LVLSLGTGTAPR-----------SIPYKKVKN-WGALGWLLPLIDILMDAQSDAVD---YQLRQLlGDRYYRLDPELP 273
                        330
                 ....*....|..
gi 312222743 712 SDIMLDEVSDAV 723
Cdd:COG3621  274 EEIALDDNAENI 285
Pat_PNPLA8 cd07211
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ...
425-735 7.46e-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: 146.25  E-value: 7.46e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 425 HLLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILA--LAILHSkSMAYMRGVYFRMKDEVF-RGSRP- 500
Cdd:cd07211    9 RILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAflLGLKKM-SLDECEELYRKLGKDVFsQNTYIs 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 501 -----------YESGPLEEFLKREFGEHTKMTDVKK---PKVMLTGTLSDRQPAELHLFRNYDAPEAVREP---RCNqni 563
Cdd:cd07211   88 gtsrlvlshayYDTETWEKILKEMMGSDELIDTSADpncPKVACVSTQVNRTPLKPYVFRNYNHPPGTRSHylgSCK--- 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 564 nlkpptqpadQLVWRAARSSGAAPTYF----RPNGRFLDGGLLANNPTLDAMTEIHEYNQDmirkgqgnkvKKLSIVVSL 639
Cdd:cd07211  165 ----------HKLWEAIRASSAAPGYFeefkLGNNLHQDGGLLANNPTALALHEAKLLWPD----------TPIQCLVSV 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 640 GTGKSpqvpvtcvdvfrPSNPWELAKTVFGAKELGKMVVDCCTDPDgrAVDrarawcEMV-----GIQYFRLNPQLGSDI 714
Cdd:cd07211  225 GTGRY------------PSSVRLETGGYTSLKTKLLNLIDSATDTE--RVH------TALddllpPDVYFRFNPVMSECV 284
                        330       340
                 ....*....|....*....|.
gi 312222743 715 MLDEVSDAVLVNALWETEVYI 735
Cdd:cd07211  285 ELDETRPEKLDQLQDDTLEYI 305
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
102-392 2.34e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.33  E-value: 2.34e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 102 LHVEVLQHLTDLIRNHPSWTVTHLAVELGIRECFHHSRIISCANSTENEEGCTPLHLACRKGDSEILVELVQYCHAQMDV 181
Cdd:COG0666    3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 182 TDNKGETAFHYAVQGDNPQVLQLLgKNASAGLNQVNNQGLTPLHLACKMGKQEMVRVLLLCNArcnimgpggfpihtamk 261
Cdd:COG0666   83 KDDGGNTLLHAAARNGDLEIVKLL-LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA----------------- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 262 fsqkgcaemiismdsnQIHSKDpRYGASPLHWA---KNAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLT 338
Cdd:COG0666  145 ----------------DVNAQD-NDGNTPLHLAaanGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 312222743 339 YGANAGARGEHGNTPLHLAMSKDNMEMVKALIVFGAEVDTPNDFGETPALIASK 392
Cdd:COG0666  208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
101-387 4.67e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.08  E-value: 4.67e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 101 VLHVEVLQHLTDLIRNHPSWTVTHLAVELGIRECFHHSRIISCANSTENEEGCTPLHLACRKGDSEILVELVQYcHAQMD 180
Cdd:COG0666   36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVN 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 181 VTDNKGETAFHYAVQGDNPQVLQLLgKNASAGLNQVNNQGLTPLHLACKMGKQEMVRVLLLCNARCNImgpggfpihtam 260
Cdd:COG0666  115 ARDKDGETPLHLAAYNGNLEIVKLL-LEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA------------ 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 261 kfsqkgcaemiismdsnqihsKDpRYGASPLHWA---KNAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLL 337
Cdd:COG0666  182 ---------------------RD-NDGETPLHLAaenGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 312222743 338 TYGANAGARGEHGNTPLHLAMSKDNMEMVKALIVFGAEVDTPNDFGETPA 387
Cdd:COG0666  240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Pat17_PNPLA8_PNPLA9_like2 cd07215
Patatin-like phospholipase of bacteria; Patatin is a storage protein of the potato tuber that ...
426-749 6.07e-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: 118.28  E-value: 6.07e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 426 LLCLDGGGVKGLVIIQLLIAIE----KASG---VATKDLFDWVAGTSTGGILALAIL-------HSKSMAYMRGVYFRMK 491
Cdd:cd07215    2 ILSIDGGGIRGIIPATILVSVEeklqKKTGnpeARLADYFDLVAGTSTGGILTCLYLcpnesgrPKFSAKEALNFYLERG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 492 DEVFRGSR-------------PYESGPLEEFLKREFGEhTKMTDVKKPKVMLTGTLSDRQPaelHLFRNYDApeAVREPR 558
Cdd:cd07215   82 NYIFKKKIwnkiksrggflneKYSHKPLEEVLLEYFGD-TKLSELLKPCLITSYDIERRSP---HFFKSHTA--IKNEQR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 559 cnqninlkpptqpaDQLVWRAARSSGAAPTYFRPNgRF----------LDGGLLANNPTLDAMTEIheynQDMIRKGQGN 628
Cdd:cd07215  156 --------------DFYVRDVARATSAAPTYFEPA-RIhsltgekytlIDGGVFANNPTLCAYAEA----RKLKFEQPGK 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 629 KVKKLSIVVSLGTGKSpqvpvtcvdvfRPSNPWELAKTvFGAKELGKMVVDCCTDPDGRAVDRARAW---CEMVGIQYFR 705
Cdd:cd07215  217 PTAKDMIILSLGTGKN-----------KKSYTYEKVKD-WGLLGWAKPLIDIMMDGASQTVDYQLKQifdAEGDQQQYLR 284
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 312222743 706 LNPQL-GSDIMLDEVSDAVLVNALWETEVYIYEHREEFQKLVQLL 749
Cdd:cd07215  285 IQPELeDADPEMDDASPENLEKLREVGQALAEDHKDQLDEIVDRL 329
Pat17_PNPLA8_PNPLA9_like3 cd07216
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
426-718 5.32e-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: 109.31  E-value: 5.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 426 LLCLDGGGVKG---LVIIQ-LLIAIEKASGVA----TKDLFDWVAGTSTGGILALailhsksmayMRG-----------V 486
Cdd:cd07216    3 LLSLDGGGVRGlssLLILKeIMERIDPKEGLDeppkPCDYFDLIGGTSTGGLIAI----------MLGrlrmtvdecidA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 487 YFRMKDEVFRGSRPYESGPLEEFLKREFG----------------EHTKMTDVKKP---KVMLTGTLSDrQPAELHLFRN 547
Cdd:cd07216   73 YTRLAKKIFSRKRLRLIIGDLRTGARFDSkklaeaikvilkelgnDEDDLLDEGEEdgcKVFVCATDKD-VTGKAVRLRS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 548 YDAPeavREPrcNQNINLKpptqpadqlVWRAARSSGAAPTYFRP------NGRFLDGGLLANNPTLDAMTEIHEynqdm 621
Cdd:cd07216  152 YPSK---DEP--SLYKNAT---------IWEAARATSAAPTFFDPvkigpgGRTFVDGGLGANNPIREVWSEAVS----- 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 622 IRKGQGNKVKklsIVVSLGTGKSPQVpvtcvdVFRPSnpwelAKTVFGAKELGKMVvdccTDPDGRAVDRARAWCEMVGI 701
Cdd:cd07216  213 LWEGLARLVG---CLVSIGTGTPSIK------SLGRS-----AEGAGLLKGLKDLV----TDTEAEAKRFSAEHSELDEE 274
                        330
                 ....*....|....*....
gi 312222743 702 -QYFRLN-PQLGSDIMLDE 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 5.87e-23

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


Pssm-ID: 132852 [Multi-domain]  Cd Length: 288  Bit Score: 99.67  E-value: 5.87e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 427 LCLDGGGVKGLVIIQLLIAIEKA--SGVATKDLFdwvAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRPYE-- 502
Cdd:cd07213    5 LSLDGGGVKGIVQLVLLKRLAEEfpSFLDQIDLF---AGTSAGSLIALGLALGYSPRQVLKLYEEVGLKVFSKSSAGGga 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 503 -------SGPLEEFLKREFGEhTKMTDVKKpKVMLTGTLSDRQPaelhlfrnydaPEAVR--EPRCNQNInlkPPTQPAD 573
Cdd:cd07213   82 gnnqyfaAGFLKAFAEVFFGD-LTLGDLKR-KVLVPSFQLDSGK-----------DDPNRrwKPKLFHNF---PGEPDLD 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 574 QLVWRAARSSGAAPTYFRPNGRFLDGGLLANNPTLDAMTEIheynqdMIRKGQGNKVKKLSiVVSLGTGKSPQvPVTcvD 653
Cdd:cd07213  146 ELLVDVCLRSSAAPTYFPSYQGYVDGGVFANNPSLCAIAQA------IGEEGLNIDLKDIV-VLSLGTGRPPS-YLD--G 215
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312222743 654 VFRPSNpWELAKTvfgAKELGKMVVdcctdpDGRaVDRARAWCEMV-GIQYFRLNPQLGSDIMLDEVSD 721
Cdd:cd07213  216 ANGYGD-WGLLQW---LPDLLDLFM------DAG-VDAADFQCRQLlGERYFRLDPVLPANIDLDDNKQ 273
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
427-611 2.17e-21

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


Pssm-ID: 396341  Cd Length: 190  Bit Score: 92.29  E-value: 2.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743  427 LCLDGGGVKGLVIIQLLIAIEKAsgvatKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRP------ 500
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEA-----GIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRkralsl 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743  501 -------------YESGPLEEFLKREFGEHTKMTDVKKPKVMLTGTLSdrqpAELHLFRNYDAPEAvreprcnqnINLKP 567
Cdd:pfam01734  76 lallrgligegglFDGDALRELLRKLLGDLTLEELAARLSLLLVVALR----ALLTVISTALGTRA---------RILLP 142
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 312222743  568 PTQPADQLVWRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAM 611
Cdd:pfam01734 143 DDLDDDEDLADAVLASSALPGVFPPvrldGELYVDGGLVDNVPVEAAL 190
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
425-641 7.50e-21

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 94.10  E-value: 7.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 425 HLLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSR----- 499
Cdd:NF041079   2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILALALALEIPARELVELFEEHGKDIFPKRKwprrl 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 500 -------PYESGPLEEFLKREFGEhTKMTDVKKPKVMLTGTLSDRQPaelHLFRNYDAPEAVREPRCnqninlkpptqpa 572
Cdd:NF041079  82 lgllkkpKYSSEPLREVLEEIFGD-KTIGDLKHRVLIPAVNYTTGKP---QVFKTPHHPDFTRDHKL------------- 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312222743 573 dQLVwRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAMTEIHEYNqdmirkgqGNKVKKLSIvVSLGT 641
Cdd:NF041079 145 -KLV-DVALATSAAPTYFPLhefdNEQFVDGGLVANNPGLLGLHEALHFL--------GVPYDDVRI-LSIGT 206
Ank_2 pfam12796
Ankyrin repeats (3 copies);
156-249 3.51e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 3.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743  156 LHLACRKGDSEILVELVQyCHAQMDVTDNKGETAFHYAVQGDNPQVLQLLGKNASAglnQVNNQGLTPLHLACKMGKQEM 235
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEI 76
                          90
                  ....*....|....
gi 312222743  236 VRVLLLCNARCNIM 249
Cdd:pfam12796  77 VKLLLEKGADINVK 90
Pat17_PNPLA8_PNPLA9_like4 cd07217
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
426-722 5.96e-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: 86.01  E-value: 5.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 426 LLCLDGGGVKGLVIIQLLIAIEKASGVATK-------DLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVF--- 495
Cdd:cd07217    3 ILALDGGGIRGLLSVEILGRIEKDLRTHLDdpefrlgDYFDFVGGTSTGSIIAACIALGMSVTDLLSFYTLNGVNMFdka 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 496 ------RGSRPYESGPLEEFLKR--EFGEHTKMTD--VKKPKVMLTGTLSDRQPAELHlfrnyDAPEAVREPRCNQNINL 565
Cdd:cd07217   83 wlaqrlFLNKLYNQYDPTNLGKKlnTVFPETTLGDdtLRTLLMIVTRNATTGSPWPVC-----NNPEAKYNDSDRSDCNL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 566 kpptqpaDQLVWRAARSSGAAPTYFRPN---------GRFLDGGL-LANNPTLDA--MTEIHEYNQDMiRKGQGNkvkkl 633
Cdd:cd07217  158 -------DLPLWQLVRASTAAPTFFPPEvvsiapgtaFVFVDGGVtTYNNPAFQAflMATAKPYKLNW-EVGADN----- 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 634 SIVVSLGTGKSPQVpvtcVDVFRPSNPWEL--AKTV-----FGAKELGKMVV----DCctdPDGRAVDR-------ARAW 695
Cdd:cd07217  225 LLLVSVGTGFAPEA----RPDLKAADMWALdhAKYIpsalmNAANAGQDMVCrvlgEC---RKGGLVDReigtmhvDPNW 297
                        330       340
                 ....*....|....*....|....*..
gi 312222743 696 CEMVGIQYFRLNPQLGSDiMLDEVSDA 722
Cdd:cd07217  298 LGPKLFTYVRYDVSLSRS-GLDVLGLS 323
Ank_2 pfam12796
Ankyrin repeats (3 copies);
291-380 7.08e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 7.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743  291 LHWA---KNAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLTYgaNAGARGEHGNTPLHLAMSKDNMEMVK 367
Cdd:pfam12796   1 LHLAaknGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 312222743  368 ALIVFGAEVDTPN 380
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
220-390 3.03e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 84.66  E-value: 3.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 220 GLTPLHLACKMGKQEMVRVLLLCNARCNIMGPG-GFPIHTAMKFSQKGCAEMIISMDS--NQIHSKDpryGASPLHWA-- 294
Cdd:PHA02875  35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDiESELHDAVEEGDVKAVEELLDLGKfaDDVFYKD---GMTPLHLAti 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 295 -KNAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLTYGANAGARGEHGNTPLHLAMSKDNMEMVKALIVFG 373
Cdd:PHA02875 112 lKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
                        170
                 ....*....|....*..
gi 312222743 374 AevdTPNDFGETPALIA 390
Cdd:PHA02875 192 A---NIDYFGKNGCVAA 205
PHA03100 PHA03100
ankyrin repeat protein; Provisional
153-390 2.38e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 82.02  E-value: 2.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 153 CTPLHLAcRKGDSEILVELVQYCHAQMDVTDNKGETAFHY-----AVQGDNPQVLQLLGKNAsAGLNQVNNQGLTPLHLA 227
Cdd:PHA03100  36 VLPLYLA-KEARNIDVVKILLDNGADINSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYG-ANVNAPDNNGITPLLYA 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 228 --CKMGKQEMVRVLLLCNARCNIMGPGGF-PIHTAMKfsqkgcaemiismdSNQIhskdprygasplhwakNAEMARMLL 304
Cdd:PHA03100 114 isKKSNSYSIVEYLLDNGANVNIKNSDGEnLLHLYLE--------------SNKI----------------DLKILKLLI 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 305 KRGCDVDSTsssgntalhvavmrNRFDCvmvLLTYGANAGARGEHGNTPLHLAMSKDNMEMVKALIVFGAEVDTPNDFGE 384
Cdd:PHA03100 164 DKGVDINAK--------------NRVNY---LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226

                 ....*.
gi 312222743 385 TPALIA 390
Cdd:PHA03100 227 TPLHIA 232
PHA02878 PHA02878
ankyrin repeat protein; Provisional
190-391 4.03e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 81.85  E-value: 4.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 190 FHYAVQGDNPQVLQLL---GKNasagLNQVNNQGLTPLHLAC----KMGKQEMVRVLLLCNarcniMGPGGFPIHTAMKF 262
Cdd:PHA02878  41 LHQAVEARNLDVVKSLltrGHN----VNQPDHRDLTPLHIICkepnKLGMKEMIRSINKCS-----VFYTLVAIKDAFNN 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 263 SQKGCAEMIISMDSNQIHSKDPRY-GASPLHWAKNAEMARMLLKRGCDVD-STSSSGNTALHVAVMRNRFDCVMVLLTYG 340
Cdd:PHA02878 112 RNVEIFKIILTNRYKNIQTIDLVYiDKKSKDDIIEAEITKLLLSYGADINmKDRHKGNTALHYATENKDQRLTELLLSYG 191
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 312222743 341 ANAGARGEHGNTPLHLAMSKDNMEMVKALIVFGAEVDTPNDFGETPALIAS 391
Cdd:PHA02878 192 ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV 242
PHA03095 PHA03095
ankyrin-like protein; Provisional
152-390 2.18e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.22  E-value: 2.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 152 GCTPLHLACRKG---DSEILVELVQYcHAQMDVTDNKGETAFHYAVQGDN-PQVLQLLGKnASAGLNQVNNQGLTPLH-- 225
Cdd:PHA03095  47 GKTPLHLYLHYSsekVKDIVRLLLEA-GADVNAPERCGFTPLHLYLYNATtLDVIKLLIK-AGADVNAKDKVGRTPLHvy 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 226 LACKMGKQEMVRVLLLCNARCNIMGPGGF-PIHTAMKFsqKGCA----EMIISMDSNqIHSKDPRyGASPLH-----WAK 295
Cdd:PHA03095 125 LSGFNINPKVIRLLLRKGADVNALDLYGMtPLAVLLKS--RNANvellRLLIDAGAD-VYAVDDR-FRSLLHhhlqsFKP 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 296 NAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMV--LLTYGANAGARGEHGNTPLHLAMSKDNMEMVKALIVFG 373
Cdd:PHA03095 201 RARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280
                        250
                 ....*....|....*..
gi 312222743 374 AEVDTPNDFGETPALIA 390
Cdd:PHA03095 281 ADINAVSSDGNTPLSLM 297
PHA03095 PHA03095
ankyrin-like protein; Provisional
182-392 4.33e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.45  E-value: 4.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 182 TDNKGETAFHYAVQ---GDNPQVLQLLgKNASAGLNQVNNQGLTPLHL-ACKMGKQEMVRVLLLCNARCNIMGPGGF-PI 256
Cdd:PHA03095  43 RGEYGKTPLHLYLHyssEKVKDIVRLL-LEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRtPL 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 257 HTAM--KFSQKGCAEMIISMDSNqIHSKDpRYGASPLHW-----AKNAEMARMLLKRGCDVDSTSSSGNTALHV--AVMR 327
Cdd:PHA03095 122 HVYLsgFNINPKVIRLLLRKGAD-VNALD-LYGMTPLAVllksrNANVELLRLLIDAGADVYAVDDRFRSLLHHhlQSFK 199
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312222743 328 NRFDCVMVLLTYGANAGARGEHGNTPLH-LAM-SKDNMEMVKALIVFGAEVDTPNDFGETPALIASK 392
Cdd:PHA03095 200 PRARIVRELIRAGCDPAATDMLGNTPLHsMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAV 266
PHA02876 PHA02876
ankyrin repeat protein; Provisional
183-390 6.86e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 75.49  E-value: 6.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 183 DNKGETAFHYAVQGdnPQVLQLLGKNASAG--LNQVNNQGLTPLHLACKMG-KQEMVRVLLLCNARCNIMGP-GGFPIHT 258
Cdd:PHA02876 270 DDCKNTPLHHASQA--PSLSRLVPKLLERGadVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRlYITPLHQ 347
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 259 AMKFSQ-KGCAEMIISMDSNqIHSKDpRYGASPLHWA---KNAEMARMLLKRGCDVDSTSSSGNTALHVAVM-RNRFDCV 333
Cdd:PHA02876 348 ASTLDRnKDIVITLLELGAN-VNARD-YCDKTPIHYAavrNNVVIINTLLDYGADIEALSQKIGTALHFALCgTNPYMSV 425
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 312222743 334 MVLLTYGANAGARGEHGNTPLHLAMSKD-NMEMVKALIVFGAEVDTPNDFGETPALIA 390
Cdd:PHA02876 426 KTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA 483
PHA03095 PHA03095
ankyrin-like protein; Provisional
234-386 9.40e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 74.29  E-value: 9.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 234 EMVRVLLLCNARCNIMGP-GGFPIHTAMKFSQKGCAEMIISMDSNQIHSKDP-RYGASPLHW----AKNAEMARMLLKRG 307
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGEyGKTPLHLYLHYSSEKVKDIVRLLLEAGADVNAPeRCGFTPLHLylynATTLDVIKLLIKAG 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 308 CDVDSTSSSGNTALHV--AVMRNRFDCVMVLLTYGANAGARGEHGNTPLHLAM-SKD-NMEMVKALIVFGAEVDTPNDFG 383
Cdd:PHA03095 108 ADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLkSRNaNVELLRLLIDAGADVYAVDDRF 187

                 ...
gi 312222743 384 ETP 386
Cdd:PHA03095 188 RSL 190
PHA02875 PHA02875
ankyrin repeat protein; Provisional
151-343 1.94e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 73.10  E-value: 1.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 151 EGCTPLHLACRKGDSEILVELVQYcHAQMDVTDNKGETAFHYAV-QGDNPQVLQLLGKNASAGlNQVNNQGLTPLHLACK 229
Cdd:PHA02875  34 DGISPIKLAMKFRDSEAIKLLMKH-GAIPDVKYPDIESELHDAVeEGDVKAVEELLDLGKFAD-DVFYKDGMTPLHLATI 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 230 MGKQEMVRVLLLCNARCNIMGPGGF-PIHTAMKFSQKGCAEMIIsmDSNQIHSKDPRYGASPLHWA---KNAEMARMLLK 305
Cdd:PHA02875 112 LKKLDIMKLLIARGADPDIPNTDKFsPLHLAVMMGDIKGIELLI--DHKACLDIEDCCGCTPLIIAmakGDIAICKMLLD 189
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 312222743 306 RGCDVDSTSSSGN-TALHVAVMRNRFDCVMVLLTYGANA 343
Cdd:PHA02875 190 SGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADC 228
PHA02874 PHA02874
ankyrin repeat protein; Provisional
193-386 2.19e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.07  E-value: 2.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 193 AVQGDNPQVLQLLgKNASAGLNQVNNQGLTPLHLACKMGKQEMVRVLLLCNARCNIMgpggfPIHTAMKFSQKGCAEMII 272
Cdd:PHA02874  42 AIRSGDAKIVELF-IKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIL-----PIPCIEKDMIKTILDCGI 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 273 SMDSNQIHSKdprygaSPLHWA-KNA--EMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLTYGANAGARGEH 349
Cdd:PHA02874 116 DVNIKDAELK------TFLHYAiKKGdlESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 312222743 350 GNTPLHLAMSKDNMEMVKALIVFGAEVDTPNDFGETP 386
Cdd:PHA02874 190 GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
154-370 2.67e-13

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 73.12  E-value: 2.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 154 TPLHLACRKGDSEILVELVQYCHAQMDVTDNKGETAFHYAVQGDNPQVLQLLGKNASAGLNQVNN----QGLTPLHLACK 229
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 230 MGKQEMVRVLL-----LCNARCnimgpggfpihTAMKFSQKGCaemiismdsNQIHskdprYGASPLHWAK---NAEMAR 301
Cdd:cd22192   99 NQNLNLVRELIargadVVSPRA-----------TGTFFRPGPK---------NLIY-----YGEHPLSFAAcvgNEEIVR 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312222743 302 MLLKRGCDVDSTSSSGNTALHVAVMRN--RFDCVM--VLLTYGANAGA------RGEHGNTPLHLAMSKDNMEMVKALI 370
Cdd:cd22192  154 LLIEHGADIRAQDSLGNTVLHILVLQPnkTFACQMydLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLV 232
PHA02876 PHA02876
ankyrin repeat protein; Provisional
154-377 3.72e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 73.17  E-value: 3.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 154 TPLHLACRKGDSEILVELVQYcHAQMDVTDNKGETAFHYAVQGDNPQVLQLLGKNASaglnQVNNQGLTPLHlacKMGKQ 233
Cdd:PHA02876 180 TPIHYAAERGNAKMVNLLLSY-GADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS----NINKNDLSLLK---AIRNE 251
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 234 EMVRVLLLCNARCNIMGPGGF---PIHTAM----------KFSQKGcaemiisMDSNQIHSKdpryGASPLH-WAKNA-- 297
Cdd:PHA02876 252 DLETSLLLYDAGFSVNSIDDCkntPLHHASqapslsrlvpKLLERG-------ADVNAKNIK----GETPLYlMAKNGyd 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 298 -EMARMLLKRGCDVDSTSSSGNTALHVAVMRNRF-DCVMVLLTYGANAGARGEHGNTPLHLAMSKDNMEMVKALIVFGAE 375
Cdd:PHA02876 321 tENIRTLIMLGADVNAADRLYITPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400

                 ..
gi 312222743 376 VD 377
Cdd:PHA02876 401 IE 402
Pat17_isozyme_like cd07214
Patatin-like phospholipase of plants; Pat17 is an isozyme of patatin cloned from Solanum ...
426-646 2.08e-12

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: 69.39  E-value: 2.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 426 LLCLDGGGVKGLVIIQLLIAIEK------ASGVATKDLFDWVAGTSTGGILAlAIL-----HSKSMAYMRGV---YFRMK 491
Cdd:cd07214    6 VLSIDGGGIRGIIPATILEFLEGklqeldGPDARIADYFDVIAGTSTGGLIT-AMLtapneNKRPLFAAKDIvqfYLENG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 492 DEVFRGSR-PYES---------GP------LEEFLKREFGEhTKMTDVKKPKVMLTGTLSDRQPAelhLFRNYDApeavr 555
Cdd:cd07214   85 PKIFPQSTgQFEDdrkklrsllGPkydgvyLHDLLNELLGD-TRLSDTLTNVVIPTFDIKLLQPV---IFSSSKA----- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 556 epRCNQNINLKPptqpADqlvwrAARSSGAAPTYFrPNGRF--------------LDGGLLANNPTLDAMT----EIHEY 617
Cdd:cd07214  156 --KNDKLTNARL----AD-----VCISTSAAPTYF-PAHYFttedsngdirefnlVDGGVAANNPTLLAISevtkEIIKD 223
                        250       260
                 ....*....|....*....|....*....
gi 312222743 618 NQDMIRKGQGNKVKKLsiVVSLGTGKSPQ 646
Cdd:cd07214  224 NPFFASIKPLDYKKLL--VLSLGTGSAEE 250
PHA03095 PHA03095
ankyrin-like protein; Provisional
152-336 2.53e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 69.67  E-value: 2.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 152 GCTPLHLACRKGDSEILVELVQYCHAQMDVTDNKGETAFHYAVQGDN--PQVLQLLgKNASAGLNQVNNQGLTPLHL--- 226
Cdd:PHA03095  83 GFTPLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNinPKVIRLL-LRKGADVNALDLYGMTPLAVllk 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 227 --ACKMgkqEMVRVLL---------------------------------LCNARCNIMGP---GGFPIHTAMKFSQkgCA 268
Cdd:PHA03095 162 srNANV---ELLRLLIdagadvyavddrfrsllhhhlqsfkprarivreLIRAGCDPAATdmlGNTPLHSMATGSS--CK 236
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312222743 269 EMIIS--MDSN-QIHSKDpRYGASPLHWA---KNAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCV-MVL 336
Cdd:PHA03095 237 RSLVLplLIAGiSINARN-RYGQTPLHYAavfNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVrAAL 310
PHA02878 PHA02878
ankyrin repeat protein; Provisional
218-360 9.73e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.98  E-value: 9.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 218 NQGLTPLHLACKMGKQEMVRVLLLCNARCNIMGPGG-FPIHTAMKFSQKGCAEMIISMDSNqIHSKDpRYGASPLHWA-- 294
Cdd:PHA02878 166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNnSPLHHAVKHYNKPIVHILLENGAS-TDARD-KCGNTPLHISvg 243
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312222743 295 --KNAEMARMLLKRGCDVDSTSS-SGNTALHVAVMRNRfdCVMVLLTYGANAGARGEHGNTPLHLAMSK 360
Cdd:PHA02878 244 ycKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
Ank_2 pfam12796
Ankyrin repeats (3 copies);
124-205 2.12e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.51  E-value: 2.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743  124 HLAVELGIRECFHHSRIISCANSTENEEGCTPLHLACRKGDSEILVELVQYCHAQMdvtDNKGETAFHYAVQGDNPQVLQ 203
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIVK 78

                  ..
gi 312222743  204 LL 205
Cdd:pfam12796  79 LL 80
Ank_2 pfam12796
Ankyrin repeats (3 copies);
224-313 7.54e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 7.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743  224 LHLACKMGKQEMVRVLLLCNARCNIMGPGGF-PIHTAMKFSQKGCAEMIIsmdsNQIHSKDPRYGASPLHWA---KNAEM 299
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRtALHLAAKNGHLEIVKLLL----EHADVNLKDNGRTALHYAarsGHLEI 76
                          90
                  ....*....|....
gi 312222743  300 ARMLLKRGCDVDST 313
Cdd:pfam12796  77 VKLLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
146-353 8.94e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.60  E-value: 8.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 146 STENEEGCTPLHLACRKGDSEILVELVQYcHAQMDVTDNKGETAFHYAVQGDNPQVLQLLGKNAsAGLNQVNNQGLTPLH 225
Cdd:PHA02874 118 NIKDAELKTFLHYAIKKGDLESIKMLFEY-GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLH 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 226 LACKMGKQEMVRVLLLCNARCNIMGPGGF-PIHTAMKFSqKGCAEMIISMDSNQIHSKDpryGASPLHWAKN----AEMA 300
Cdd:PHA02874 196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFtPLHNAIIHN-RSAIELLINNASINDQDID---GSTPLHHAINppcdIDII 271
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 312222743 301 RMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLTygANAGARGEHGNTP 353
Cdd:PHA02874 272 DILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDII--ANAVLIKEADKLK 322
PHA02874 PHA02874
ankyrin repeat protein; Provisional
175-377 1.46e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.21  E-value: 1.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 175 CHAQMDVTDNKGETAFHYAVQGDNPQVLQLLGKnASAGLNQVNNQGLTPLHLACKMGKQEMVRVLLLCNARCNIMG-PGG 253
Cdd:PHA02874 113 CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFE-YGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDnNGE 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 254 FPIHTAMKFSQKGCAEMIISmDSNQIHSKDPRyGASPLHWA--KNAEMARMLLKRGcDVDSTSSSGNTALHVAVMRN-RF 330
Cdd:PHA02874 192 SPLHNAAEYGDYACIKLLID-HGNHIMNKCKN-GFTPLHNAiiHNRSAIELLINNA-SINDQDIDGSTPLHHAINPPcDI 268
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 312222743 331 DCVMVLLTYGANAGARGEHGNTPLHLAMSKDN-MEMVKALI---VFGAEVD 377
Cdd:PHA02874 269 DIIDILLYHKADISIKDNKGENPIDTAFKYINkDPVIKDIIanaVLIKEAD 319
Ank_2 pfam12796
Ankyrin repeats (3 copies);
321-392 1.51e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.20  E-value: 1.51e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312222743  321 LHVAVMRNRFDCVMVLLTYGANAGARGEHGNTPLHLAMSKDNMEMVKALIVFgAEVDtPNDFGETPALIASK 392
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAAR 70
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
299-379 2.65e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 60.41  E-value: 2.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 299 MARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLTYG---ANAGARGE--HGNTPLHLAMSKDNMEMVKALIVFG 373
Cdd:cd22192   33 IKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelVNEPMTSDlyQGETALHIAVVNQNLNLVRELIARG 112

                 ....*.
gi 312222743 374 AEVDTP 379
Cdd:cd22192  113 ADVVSP 118
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
300-405 4.09e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.91  E-value: 4.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 300 ARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLTYGANAGARGEHGNTPLHLAMSKDNMEMVKALI-----VFGA 374
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSrhsqcHFEL 177
                         90       100       110
                 ....*....|....*....|....*....|...
gi 312222743 375 EVDTPND--FGETPALIASKISKQLQDLMPISR 405
Cdd:PTZ00322 178 GANAKPDsfTGKPPSLEDSPISSHHPDFSAVPQ 210
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
427-607 4.45e-09

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


Pssm-ID: 132846  Cd Length: 194  Bit Score: 56.90  E-value: 4.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 427 LCLDGGGVKGLVIIQLLIAIEKAsGVatkdLFDWVAGTSTGGILA--LAI-LHSKSMAY--MRGVYFRMKDE----VFRG 497
Cdd:cd07207    2 LVFEGGGAKGIAYIGALKALEEA-GI----LKKRVAGTSAGAITAalLALgYSAADIKDilKETDFAKLLDSpvglLFLL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 498 SRPYESG------PLEEFLKREFGEHTKMTDVKKpkvmLTGTLSDRQPAELHLFrnydapeAVREPRCnQNINLKPPTQP 571
Cdd:cd07207   77 PSLFKEGglykgdALEEWLRELLKEKTGNSFATS----LLRDLDDDLGKDLKVV-------ATDLTTG-ALVVFSAETTP 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 312222743 572 aDQLVWRAARSSGAAPTYFRP-----NGRFLDGGLLANNPT 607
Cdd:cd07207  145 -DMPVAKAVRASMSIPFVFKPvrlakGDVYVDGGVLDNYPV 184
PHA02874 PHA02874
ankyrin repeat protein; Provisional
114-262 6.20e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.82  E-value: 6.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 114 IRNHPSWTVTHLAVELGIRECFHHSRIISCANSTENEEGCTPLHLACRKGDSEILVELVQYcHAQMDVTDNKGETAFHYA 193
Cdd:PHA02874 119 IKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK-GAYANVKDNNGESPLHNA 197
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 194 VQGDNPQVLQLLGKNASAGLNQVNNqGLTPLHLACKMGKQemVRVLLLCNARCNIMGPGGF-PIHTAMKF 262
Cdd:PHA02874 198 AEYGDYACIKLLIDHGNHIMNKCKN-GFTPLHNAIIHNRS--AIELLINNASINDQDIDGStPLHHAINP 264
Ank_4 pfam13637
Ankyrin repeats (many copies);
317-370 6.94e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 6.94e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 312222743  317 GNTALHVAVMRNRFDCVMVLLTYGANAGARGEHGNTPLHLAMSKDNMEMVKALI 370
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
296-390 7.53e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 59.11  E-value: 7.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 296 NAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLTYGANAGARGEHGNTPL-------H------------- 355
Cdd:PLN03192 537 NAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHhkifrilyhfasi 616
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 312222743 356 -----------LAMSKDNMEMVKALIVFGAEVDTPNDFGETPALIA 390
Cdd:PLN03192 617 sdphaagdllcTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVA 662
Ank_5 pfam13857
Ankyrin repeats (many copies);
303-357 7.97e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.35  E-value: 7.97e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 312222743  303 LLKRG-CDVDSTSSSGNTALHVAVMRNRFDCVMVLLTYGANAGARGEHGNTPLHLA 357
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
154-205 1.04e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 1.04e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 312222743  154 TPLHLACRKGDSEILVELVQYcHAQMDVTDNKGETAFHYAVQGDNPQVLQLL 205
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
289-337 4.74e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 4.74e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 312222743  289 SPLHWA---KNAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLL 337
Cdd:pfam13637   3 TALHAAaasGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
201-386 5.72e-07

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 52.99  E-value: 5.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 201 VLQLLGKNAsAGLNQVNNQGLTPLHLACKMGK------QEMVRVLLLCNARC-NIMGPGGFPIHTAMKFSQKGCAEMIIS 273
Cdd:PHA02716 194 ILEWLCNNG-VNVNLQNNHLITPLHTYLITGNvcasviKKIIELGGDMDMKCvNGMSPIMTYIINIDNINPEITNIYIES 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 274 MDSNQIhSKDPRYGASPLHWAKNAEMARM--LLKRGCDVDSTSSSGNTALHVAVMRNRF--DCVMVLLTYGANAGARGEH 349
Cdd:PHA02716 273 LDGNKV-KNIPMILHSYITLARNIDISVVysFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNI 351
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 312222743 350 GNTPLHLAMSK-----------DN---MEMVKALIVFGAEVDTPNDFGETP 386
Cdd:PHA02716 352 GNTVLHTYLSMlsvvnildpetDNdirLDVIQCLISLGADITAVNCLGYTP 402
PHA02875 PHA02875
ankyrin repeat protein; Provisional
144-309 7.78e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.30  E-value: 7.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 144 ANSTENEEGCTPLHLACRKGDSEILVELVQYcHAQMDVTDNKGETAFHYAVQGDNPQVLQLLGKNaSAGLNQVNNQGLTP 223
Cdd:PHA02875  94 ADDVFYKDGMTPLHLATILKKLDIMKLLIAR-GADPDIPNTDKFSPLHLAVMMGDIKGIELLIDH-KACLDIEDCCGCTP 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 224 LHLACKMGKQEMVRVLLLCNARCNImgpggfpihtamkFSQKGC-AEMIISMDSNQIhskdprygasplhwaknaEMARM 302
Cdd:PHA02875 172 LIIAMAKGDIAICKMLLDSGANIDY-------------FGKNGCvAALCYAIENNKI------------------DIVRL 220

                 ....*..
gi 312222743 303 LLKRGCD 309
Cdd:PHA02875 221 FIKRGAD 227
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
287-385 1.05e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.18  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 287 GASPLHWAKN---AEMARMLLKRGCDVDSTSSSGNTALHVAVM-------------------------------RNRFDC 332
Cdd:PLN03192 558 GRTPLHIAASkgyEDCVLVLLKHACNVHIRDANGNTALWNAISakhhkifrilyhfasisdphaagdllctaakRNDLTA 637
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 312222743 333 VMVLLTYGANAGARGEHGNTPLHLAMSKDNMEMVKALIVFGAEVD---TPNDFGET 385
Cdd:PLN03192 638 MKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDkanTDDDFSPT 693
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
206-342 1.32e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.79  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 206 GKNASAGlnqvNNQGLTPLHLACKMGKQEMVRVLLLCNARCNIMGPGGfpiHTAMKFSQKGCAEMIISMDSNQIHSKDPR 285
Cdd:PLN03192 548 KLDPDIG----DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANG---NTALWNAISAKHHKIFRILYHFASISDPH 620
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 286 YGASPLHWA---KNAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLTYGAN 342
Cdd:PLN03192 621 AAGDLLCTAakrNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
PHA03100 PHA03100
ankyrin repeat protein; Provisional
180-249 1.80e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.20  E-value: 1.80e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 180 DVTDNKGETAFHYAVQGDNPQVLQLLgKNASAGLNQVNNQGLTPLHLACKMGKQEMVRVLLLCNARCNIM 249
Cdd:PHA03100 186 NIKDVYGFTPLHYAVYNNNPEFVKYL-LDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
222-430 2.51e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.78  E-value: 2.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 222 TPLHLACKMGKQEMVRVLLLCNaRCNIMGPGGF---PIHTAMKFSQKGCAEMIISMDS---NQIHSKDPRYGASPLHWA- 294
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKCP-SCDLFQRGALgetALHVAALYDNLEAAVVLMEAAPelvNEPMTSDLYQGETALHIAv 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 295 --KNAEMARMLLKRGCDVDSTSSSGntalhvAVMRNRFDCvmvLLTYganagarGEHgntPLHLAMSKDNMEMVKALIVF 372
Cdd:cd22192   98 vnQNLNLVRELIARGADVVSPRATG------TFFRPGPKN---LIYY-------GEH---PLSFAACVGNEEIVRLLIEH 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312222743 373 GAEVDTPNDFGETP----ALIASK-ISKQLQDlmpisrarkpaFILSSMRdekrsHDHLLCLD 430
Cdd:cd22192  159 GADIRAQDSLGNTVlhilVLQPNKtFACQMYD-----------LILSYDK-----EDDLQPLD 205
PHA02946 PHA02946
ankyin-like protein; Provisional
303-381 7.23e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 49.28  E-value: 7.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 303 LLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLTYGANAGARGEHGNTPLHLAMSKDN--MEMVKALIVFGAEVDTPN 380
Cdd:PHA02946  58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNSV 137

                 .
gi 312222743 381 D 381
Cdd:PHA02946 138 D 138
Ank_5 pfam13857
Ankyrin repeats (many copies);
336-390 9.01e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 9.01e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 312222743  336 LLTYG-ANAGARGEHGNTPLHLAMSKDNMEMVKALIVFGAEVDTPNDFGETPALIA 390
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
103-183 1.28e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.34  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743  103 HVEVLQHLTDL-----IRNHPSWTVTHLAVELGIRECFhhSRIISCANSTENEEGCTPLHLACRKGDSEIlVELVQYCHA 177
Cdd:pfam12796   9 NLELVKLLLENgadanLQDKNGRTALHLAAKNGHLEIV--KLLLEHADVNLKDNGRTALHYAARSGHLEI-VKLLLEKGA 85

                  ....*.
gi 312222743  178 QMDVTD 183
Cdd:pfam12796  86 DINVKD 91
Ank_5 pfam13857
Ankyrin repeats (many copies);
285-324 1.43e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 1.43e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 312222743  285 RYGASPLHWA---KNAEMARMLLKRGCDVDSTSSSGNTALHVA 324
Cdd:pfam13857  14 GEGYTPLHVAakyGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
427-610 1.71e-05

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


Pssm-ID: 132837 [Multi-domain]  Cd Length: 172  Bit Score: 45.80  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 427 LCLDGGGVKGLVIIQLLIAIEKAsGVatkdLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKdevfRGSRPYESGPL 506
Cdd:cd07198    1 LVLSGGGALGIYHVGVAKALRER-GP----LIDIIAGTSAGAIVAALLASGRDLEEALLLLLRLS----REVRLRFDGAF 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 507 EeflkREFgehtKMTDVkkpkvmltgtlsDRQPAELHLFRNYDAPEAVREPRCNQNI---NLKPPTQPADQLVWRAARSS 583
Cdd:cd07198   72 P----PTG----RLLGI------------LRQPLLSALPDDAHEDASGKLFISLTRLtdgENVLVSDTSKGELWSAVRAS 131
                        170       180       190
                 ....*....|....*....|....*....|...
gi 312222743 584 GAAPTYFRP------NGRFLDGGLLANNPTLDA 610
Cdd:cd07198  132 SSIPGYFGPvplsfrGRRYGDGGLSNNLPVAEL 164
Ank_4 pfam13637
Ankyrin repeats (many copies);
350-393 1.77e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 1.77e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 312222743  350 GNTPLHLAMSKDNMEMVKALIVFGAEVDTPNDFGETPALIASKI 393
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASN 44
Ank_5 pfam13857
Ankyrin repeats (many copies);
147-193 2.20e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 2.20e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 312222743  147 TENEEGCTPLHLACRKGDSEILVELVQYcHAQMDVTDNKGETAFHYA 193
Cdd:pfam13857  11 RLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
171-227 2.43e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 2.43e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 312222743  171 LVQYCHAQMDVTDNKGETAFHYAVQGDNPQVLQLLGKNASAgLNQVNNQGLTPLHLA 227
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD-LNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
268-392 2.62e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.75  E-value: 2.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 268 AEMIISMDSNqIHSKDPrYGASPLHWAK---NAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCV----------- 333
Cdd:PHA02876 161 AEMLLEGGAD-VNAKDI-YCITPIHYAAergNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIkaiidnrsnin 238
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312222743 334 ------------------MVLLTYGANAGARGEHGNTPLHLAMSKDNM-EMVKALIVFGAEVDTPNDFGETPALIASK 392
Cdd:PHA02876 239 kndlsllkairnedletsLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAK 316
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
152-365 3.09e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.38  E-value: 3.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743  152 GCTPLHLACRKGDSEILVELVQYCHAQMDVtdnkGETAFHYAVQGDNPQV---LQLLGKNASAGLNQ--VNNQ------- 219
Cdd:TIGR00870  52 GRSALFVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLEYVDAVeaiLLHLLAAFRKSGPLelANDQytseftp 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743  220 GLTPLHLACKMGKQEMVRVLLL----CNARCNimgpggfpihtamkfsqkgCAEMIISMDSNQIhskdpRYGASPLHWAK 295
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLErgasVPARAC-------------------GDFFVKSQGVDSF-----YHGESPLNAAA 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743  296 ---NAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFD-------CVMVLLTYGANAGARG----EH-----GNTPLHL 356
Cdd:TIGR00870 184 clgSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKaeyeelsCQMYNFALSLLDKLRDskelEVilnhqGLTPLKL 263

                  ....*....
gi 312222743  357 AMSKDNMEM 365
Cdd:TIGR00870 264 AAKEGRIVL 272
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
349-377 3.78e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.03  E-value: 3.78e-05
                           10        20
                   ....*....|....*....|....*....
gi 312222743   349 HGNTPLHLAMSKDNMEMVKALIVFGAEVD 377
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA03095 PHA03095
ankyrin-like protein; Provisional
327-386 4.27e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 4.27e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312222743 327 RNRFDCVMVLLTYGANAGARGEHGNTPLHLAM---SKDNMEMVKALIVFGAEVDTPNDFGETP 386
Cdd:PHA03095  24 NVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLhysSEKVKDIVRLLLEAGADVNAPERCGFTP 86
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
349-381 4.80e-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: 40.74  E-value: 4.80e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 312222743  349 HGNTPLHLA-MSKDNMEMVKALIVFGAEVDTPND 381
Cdd:pfam00023   1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
152-240 9.34e-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: 9.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 152 GCTPLHLACRKGDSEILVELVQYCHAQMDVTDNKGETAFHYAV------QGDNPQVLQL----LGKNASAGLNQV-NNQG 220
Cdd:cd22194  188 GETPLALAACTNQPEIVQLLMEKESTDITSQDSRGNTVLHALVtvaedsKTQNDFVKRMydmiLLKSENKNLETIrNNEG 267
                         90       100
                 ....*....|....*....|
gi 312222743 221 LTPLHLACKMGKQEMVRVLL 240
Cdd:cd22194  268 LTPLQLAAKMGKAEILKYIL 287
PHA02876 PHA02876
ankyrin repeat protein; Provisional
154-262 9.62e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 9.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 154 TPLHLACRKGDSEILVELVQYcHAQMDVTDNKGETAFHYAVQGDNP--QVLQLLGKNASagLNQVNNQGLTPLHLACKMG 231
Cdd:PHA02876 377 TPIHYAAVRNNVVIINTLLDY-GADIEALSQKIGTALHFALCGTNPymSVKTLIDRGAN--VNSKNKDLSTPLHYACKKN 453
                         90       100       110
                 ....*....|....*....|....*....|...
gi 312222743 232 -KQEMVRVLLLCNARCNIMG-PGGFPIHTAMKF 262
Cdd:PHA02876 454 cKLDVIEMLLDNGADVNAINiQNQYPLLIALEY 486
PHA02875 PHA02875
ankyrin repeat protein; Provisional
149-277 1.03e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.37  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 149 NEEGCTPLHLACRKGDSEiLVELVQYCHAQMDVTDNKGETAFHYAVQGDNPQVLQLLgKNASAGLNQVNNQG-LTPLHLA 227
Cdd:PHA02875 132 NTDKFSPLHLAVMMGDIK-GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML-LDSGANIDYFGKNGcVAALCYA 209
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 312222743 228 CKMGKQEMVRVLLLCNARCNIMGPGGFPIHTAMkfsqkgcaEMIISMDSN 277
Cdd:PHA02875 210 IENNKIDIVRLFIKRGADCNIMFMIEGEECTIL--------DMICNMCTN 251
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
349-378 1.15e-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: 1.15e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 312222743  349 HGNTPLHLAMSKDNMEMVKALIVFGAEVDT 378
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
278-376 1.30e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 45.46  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743  278 QIHSKDPrYGASPLHWA----KNAEMARMLLKRGCDVDStsssGNTALHVAVMRNRFDCVMVLLTYGANAGARGE----- 348
Cdd:TIGR00870  44 NINCPDR-LGRSALFVAaienENLELTELLLNLSCRGAV----GDTLLHAISLEYVDAVEAILLHLLAAFRKSGPlelan 118
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 312222743  349 --------HGNTPLHLAMSKDNMEMVKALIVFGAEV 376
Cdd:TIGR00870 119 dqytseftPGITALHLAAHRQNYEIVKLLLERGASV 154
PHA02876 PHA02876
ankyrin repeat protein; Provisional
299-370 1.64e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 1.64e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312222743 299 MARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLTYGANAGARGEHGNTPLHLAMSKDNMEMVKALI 370
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
186-370 1.73e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 44.87  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 186 GETAFHYAVQGDNPQVLQ---LLGKNA--SAGLNQVNN--------QGLTPLHLACKMGKQEMVRVLLLCNARCNIMGPG 252
Cdd:cd21882   26 GKTCLHKAALNLNDGVNEaimLLLEAApdSGNPKELVNapctdefyQGQTALHIAIENRNLNLVRLLVENGADVSARATG 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 253 GFpihtamkFSQKGCaemiismdsNQIHskdprYGASPLHWA---KNAEMARMLLKRGCD---VDSTSSSGNTALHVAVM 326
Cdd:cd21882  106 RF-------FRKSPG---------NLFY-----FGELPLSLAactNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHALVL 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312222743 327 -------RNRFDCVM--VLLTYganaGARGEH-----------GNTPLHLAMSKDNMEMVKALI 370
Cdd:cd21882  165 qadntpeNSAFVCQMynLLLSY----GAHLDPtqqleeipnhqGLTPLKLAAVEGKIVMFQHIL 224
Ank_4 pfam13637
Ankyrin repeats (many copies);
188-240 4.46e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 4.46e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 312222743  188 TAFHYAVQGDNPQVLQ-LLGKNASagLNQVNNQGLTPLHLACKMGKQEMVRVLL 240
Cdd:pfam13637   3 TALHAAAASGHLELLRlLLEKGAD--INAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
317-342 5.68e-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: 5.68e-04
                           10        20
                   ....*....|....*....|....*.
gi 312222743   317 GNTALHVAVMRNRFDCVMVLLTYGAN 342
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
315-376 6.59e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.94  E-value: 6.59e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312222743 315 SSGNTALHVAVM---RNRFDCVMVLLTYGANAGARGE-----------HGNTPLHLAMSKDNMEMVKALIVFGAEV 376
Cdd:cd21882   24 ATGKTCLHKAALnlnDGVNEAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAIENRNLNLVRLLVENGADV 99
PHA02743 PHA02743
Viral ankyrin protein; Provisional
271-385 1.08e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 40.57  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 271 IISMDSNQIHSKDpRYGASPLHWA-----KNAEMA-RMLLKRGCDVDSTSS-SGNTALHVAVMRNRFDCVMVLL-TYGAN 342
Cdd:PHA02743  42 FISGDGHLLHRYD-HHGRQCTHMVawydrANAVMKiELLVNMGADINARELgTGNTLLHIAASTKNYELAEWLCrQLGVN 120
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 312222743 343 AGARGEHGNTPLHLAMSKDNMEMVKALIVFGAEVDTPNDFGET 385
Cdd:PHA02743 121 LGAINYQHETAYHIAYKMRDRRMMEILRANGAVCDDPLSIGLS 163
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
219-248 1.17e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 1.17e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 312222743  219 QGLTPLHLAC-KMGKQEMVRVLLLCNARCNI 248
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNA 31
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
151-174 1.43e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 1.43e-03
                           10        20
                   ....*....|....*....|....
gi 312222743   151 EGCTPLHLACRKGDSEILVELVQY 174
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDK 24
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
317-346 1.48e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 1.48e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 312222743  317 GNTALHVAVMR-NRFDCVMVLLTYGANAGAR 346
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNAR 32
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
317-376 2.44e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 41.40  E-value: 2.44e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312222743 317 GNTALHVAVMRNRFDCVMVLLTYGANAGAR----------------GEHgntPLHLAMSKDNMEMVKALIVFGAEV 376
Cdd:cd21882   73 GQTALHIAIENRNLNLVRLLVENGADVSARatgrffrkspgnlfyfGEL---PLSLAACTNQEEIVRLLLENGAQP 145
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
286-313 3.07e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 3.07e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 312222743  286 YGASPLHWA----KNAEMARMLLKRGCDVDST 313
Cdd:pfam00023   1 DGNTPLHLAagrrGNLEIVKLLLSKGADVNAR 32
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
152-240 3.63e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.55  E-value: 3.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743 152 GCTPLHLACRKGDSEILVELVQYCHAQMDV--TDNKGETAFHYAVQ-GDNPQ------------VLQLLGK-NASAGLNQ 215
Cdd:cd22193  123 GELPLSLAACTNQPDIVQYLLENEHQPADIeaQDSRGNTVLHALVTvADNTKentkfvtrmydmILIRGAKlCPTVELEE 202
                         90       100
                 ....*....|....*....|....*.
gi 312222743 216 V-NNQGLTPLHLACKMGKQEMVRVLL 240
Cdd:cd22193  203 IrNNDGLTPLQLAAKMGKIEILKYIL 228
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
219-248 3.94e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 3.94e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 312222743   219 QGLTPLHLACKMGKQEMVRVLLLCNARCNI 248
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
213-248 4.26e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 4.26e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 312222743  213 LNQVNNQGLTPLHLACKMGKQEMVRVLLLCNARCNI 248
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNL 44
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
193-385 4.57e-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: 4.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743  193 AVQGDNPQVLQLLGKNASAGLNQVNNQGLTPLHLACKMGKQEMVRVLLLCNARCNIMGPGGfpIHTAMKFSQKGCaEMII 272
Cdd:TIGR00870  25 AERGDLASVYRDLEEPKKLNINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAVGDTL--LHAISLEYVDAV-EAIL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312222743  273 SmdsnqiHSKDPRYGASPLHWAknaeMARMLlkrgcdvdSTSSSGNTALHVAVMRNRFDCVMVLLTYGANAGARGE---- 348
Cdd:TIGR00870 102 L------HLLAAFRKSGPLELA----NDQYT--------SEFTPGITALHLAAHRQNYEIVKLLLERGASVPARACgdff 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 312222743  349 ----------HGNTPLHLAMSKDNMEMVKALIVFGAEVDTPNDFGET 385
Cdd:TIGR00870 164 vksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNT 210
PHA02743 PHA02743
Viral ankyrin protein; Provisional
184-247 4.93e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 38.64  E-value: 4.93e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312222743 184 NKGETAFHYAVQGDNPQVLQLLGKNASAGLNQVNNQGLTPLHLACKMGKQEMVRVLLLCNARCN 247
Cdd:PHA02743  92 GTGNTLLHIAASTKNYELAEWLCRQLGVNLGAINYQHETAYHIAYKMRDRRMMEILRANGAVCD 155
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
151-184 7.09e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.57  E-value: 7.09e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 312222743  151 EGCTPLHLAC-RKGDSEILVELVQYcHAQMDVTDN 184
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSK-GADVNARDK 34
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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