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Conserved domains on  [gi|1169292910|ref|NP_001336796|]
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85/88 kDa calcium-independent phospholipase A2 isoform c [Homo sapiens]

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 ...
302-615 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: 555.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 302 LLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVFRGSRPYESGP 381
Cdd:cd07212     1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGSRPYNSEP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 382 LEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRQPAELHLFRNYDAPETVREPRFNqnVNLRPPAQPSDQLVWRAARSSGA 461
Cdd:cd07212    81 LEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEEPEKN--ANFLPPTDPAEQLLWRAARSSGA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 462 APTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAK 541
Cdd:cd07212   159 APTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKSKGRKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSNPWELAK 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169292910 542 TVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVNALWETEVYIYEHR 615
Cdd:cd07212   239 TVFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTHR 312
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-229 7.05e-35

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 7.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910   1 MDVTDYKGETVFHYAVQGDNSQVLQLLgRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPNGY-PIH 79
Cdd:COG0666    47 LALADALGALLLLAAALAGDLLVALLL-LAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGEtPLH 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  80 SAMKFSQKGCAEMIISMDSSqIHSKDpRYGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAI 156
Cdd:COG0666   126 LAAYNGNLEIVKLLLEAGAD-VNAQD-NDGNTPLHLAaanGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169292910 157 VLLTHGANADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRLVTRKAILTLLR 229
Cdd:COG0666   204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
 
Name Accession Description Interval E-value
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
302-615 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: 555.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 302 LLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVFRGSRPYESGP 381
Cdd:cd07212     1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGSRPYNSEP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 382 LEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRQPAELHLFRNYDAPETVREPRFNqnVNLRPPAQPSDQLVWRAARSSGA 461
Cdd:cd07212    81 LEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEEPEKN--ANFLPPTDPAEQLLWRAARSSGA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 462 APTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAK 541
Cdd:cd07212   159 APTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKSKGRKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSNPWELAK 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169292910 542 TVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVNALWETEVYIYEHR 615
Cdd:cd07212   239 TVFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTHR 312
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
292-593 5.64e-40

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 148.13  E-value: 5.64e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 292 MRDEKRTHdhLLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVF 371
Cdd:COG3621     1 MSANKPFR--ILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAAGYSAEEILDLYEEEGKEIF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 372 RGSRP-------------YESGPLEEFLKREFGEhTKMTDVRKPkVMLTGT-LSDRQPaelHLFRNYDAPetvreprFNQ 437
Cdd:COG3621    79 PKSRWrkllslrglfgpkYDSEGLEKVLKEYFGD-TTLGDLKTP-VLIPSYdLDNGKP---VFFKSPHAK-------FDR 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 438 NVNLrppaqpsdqLVWRAARSSGAAPTYFRP---------NGRFLDGGLLANNPTLDAMTE-IHEYNQDL--IRkgqank 505
Cdd:COG3621   147 DRDF---------LLVDVARATSAAPTYFPPaqiknltgeGYALIDGGVFANNPALCALAEaLKLLGPDLddIL------ 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 506 vkklsiVVSLGTGRSPQvpvtcvdvfrpSNPWELAKTvFGAKELGKMVVDCCTDPDGRAVDrarAWCEMV-GIQYFRLNP 584
Cdd:COG3621   212 ------VLSLGTGTAPR-----------SIPYKKVKN-WGALGWLLPLIDILMDAQSDAVD---YQLRQLlGDRYYRLDP 270

                  ....*....
gi 1169292910 585 QLGTDIMLD 593
Cdd:COG3621   271 ELPEEIALD 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-229 7.05e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 7.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910   1 MDVTDYKGETVFHYAVQGDNSQVLQLLgRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPNGY-PIH 79
Cdd:COG0666    47 LALADALGALLLLAAALAGDLLVALLL-LAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGEtPLH 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  80 SAMKFSQKGCAEMIISMDSSqIHSKDpRYGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAI 156
Cdd:COG0666   126 LAAYNGNLEIVKLLLEAGAD-VNAQD-NDGNTPLHLAaanGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169292910 157 VLLTHGANADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRLVTRKAILTLLR 229
Cdd:COG0666   204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
303-487 1.05e-18

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: 84.58  E-value: 1.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 303 LCLDGGGVKGLIiiqlliaiekASGVA-----TKDLFDWVAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVFRGSRP- 376
Cdd:pfam01734   1 LVLSGGGARGAY----------HLGVLkalgeAGIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRk 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 377 ------------------YESGPLEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRqpaelhlfrnydaPETVREPRFNQN 438
Cdd:pfam01734  71 ralsllallrgligegglFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRAL-------------LTVISTALGTRA 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1169292910 439 VNLRPPAQPSDQLVWRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAM 487
Cdd:pfam01734 138 RILLPDDLDDDEDLADAVLASSALPGVFPPvrldGELYVDGGLVDNVPVEAAL 190
Ank_2 pfam12796
Ankyrin repeats (3 copies);
113-202 1.33e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 1.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 113 LHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHgANADARgEHGNTPLHLAMSKDNVEMIK 189
Cdd:pfam12796   1 LHLAaknGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1169292910 190 ALIVFGAEVDTPN 202
Cdd:pfam12796  79 LLLEKGADINVKD 91
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
301-511 2.18e-17

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 83.32  E-value: 2.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 301 HLLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVFRGSR----- 375
Cdd:NF041079    2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILALALALEIPARELVELFEEHGKDIFPKRKwprrl 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 376 -------PYESGPLEEFLKREFGEhTKMTDVRKPKVMLTGTLSDRQPaelHLFRnydapeTVREPRFNQNVNLRppaqps 448
Cdd:NF041079   82 lgllkkpKYSSEPLREVLEEIFGD-KTIGDLKHRVLIPAVNYTTGKP---QVFK------TPHHPDFTRDHKLK------ 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169292910 449 dqLVwRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAMTEIHEY-NQdlirkgQANKVKKLSI 511
Cdd:NF041079  146 --LV-DVALATSAAPTYFPLhefdNEQFVDGGLVANNPGLLGLHEALHFlGV------PYDDVRILSI 204
PHA02878 PHA02878
ankyrin repeat protein; Provisional
12-199 8.01e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 83.39  E-value: 8.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  12 FHYAVQGDNSQVLQ-LLGRNAvaGLNQVNNQGLTPLHLAC----QLGKQEMVRVLLLCNarcniMGPNGYPIHSAMKFSQ 86
Cdd:PHA02878   41 LHQAVEARNLDVVKsLLTRGH--NVNQPDHRDLTPLHIICkepnKLGMKEMIRSINKCS-----VFYTLVAIKDAFNNRN 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  87 KGCAEMII--------SMDSSQIHSKDPR-------------YGA-----------SPLHWA---KNAEMARMLLKRGCN 131
Cdd:PHA02878  114 VEIFKIILtnrykniqTIDLVYIDKKSKDdiieaeitklllsYGAdinmkdrhkgnTALHYAtenKDQRLTELLLSYGAN 193
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169292910 132 VNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSK-DNVEMIKALIVFGAEVD 199
Cdd:PHA02878  194 VNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVN 262
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
121-201 3.72e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 59.64  E-value: 3.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 121 MARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHG---ANADARGE--HGNTPLHLAMSKDNVEMIKALIVFG 195
Cdd:cd22192    33 IKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelVNEPMTSDlyQGETALHIAVVNQNLNLVRELIARG 112

                  ....*.
gi 1169292910 196 AEVDTP 201
Cdd:cd22192   113 ADVVSP 118
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
171-199 4.74e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.65  E-value: 4.74e-05
                           10        20
                   ....*....|....*....|....*....
gi 1169292910  171 HGNTPLHLAMSKDNVEMIKALIVFGAEVD 199
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
42-187 5.41e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.23  E-value: 5.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  42 GLTPLHLACQLGKQEMVRVLLL----CNARCNimgpngypihsamkfsqkgCAEMIISMDSSQIhskdpRYGASPLHWAK 117
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLErgasVPARAC-------------------GDFFVKSQGVDSF-----YHGESPLNAAA 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 118 ---NAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFD---------CAIVLLTHGANADARGE-------HGNTPLHL 178
Cdd:TIGR00870 184 clgSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKaeyeelscqMYNFALSLLDKLRDSKElevilnhQGLTPLKL 263

                  ....*....
gi 1169292910 179 AMSKDNVEM 187
Cdd:TIGR00870 264 AAKEGRIVL 272
 
Name Accession Description Interval E-value
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
302-615 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: 555.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 302 LLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVFRGSRPYESGP 381
Cdd:cd07212     1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGSRPYNSEP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 382 LEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRQPAELHLFRNYDAPETVREPRFNqnVNLRPPAQPSDQLVWRAARSSGA 461
Cdd:cd07212    81 LEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEEPEKN--ANFLPPTDPAEQLLWRAARSSGA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 462 APTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAK 541
Cdd:cd07212   159 APTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKSKGRKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSNPWELAK 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169292910 542 TVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVNALWETEVYIYEHR 615
Cdd:cd07212   239 TVFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTHR 312
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
303-611 2.42e-46

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


Pssm-ID: 132838 [Multi-domain]  Cd Length: 258  Bit Score: 164.43  E-value: 2.42e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 303 LCLDGGGVKGLIIIQLLIAIEKASGVATK--DLFDWVAGTSTGGILALAILHSK-SMAYMRGMYFRMKDEVFrgsrpyes 379
Cdd:cd07199     2 LSLDGGGIRGIIPAEILAELEKRLGKPSRiaDLFDLIAGTSTGGIIALGLALGRySAEELVELYEELGRKIF-------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 380 gpleeflkrefgehtkmtdvrkPKVMLTGTlsDRQPAELHLFRNYDAPETVREPRFnqnvnlrppaqpsdqLVWRAARSS 459
Cdd:cd07199    74 ----------------------PRVLVTAY--DLSTGKPVVFSNYDAEEPDDDDDF---------------KLWDVARAT 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 460 GAAPTYFRP--------NGRFLDGGLLANNPTLDAMTEiheynqdlIRKGQANKVKKLsIVVSLGTGRSPQVPVTCVDVF 531
Cdd:cd07199   115 SAAPTYFPPaviesggdEGAFVDGGVAANNPALLALAE--------ALRLLAPDKDDI-LVLSLGTGTSPSSSSSKKASR 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 532 RPSNPWelaktvfgAKELGKMVVDCCTDPDGRAVDRARAwCEMVGIQYFRLNPQLGTDIM-LDEVSDTVLVNALWETEVY 610
Cdd:cd07199   186 WGGLGW--------GRPLLDILMDAQSDGVDQWLDLLFG-SLDSKDNYLRINPPLPGPIPaLDDASEANLLALDSAAFEL 256

                  .
gi 1169292910 611 I 611
Cdd:cd07199   257 I 257
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
292-593 5.64e-40

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 148.13  E-value: 5.64e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 292 MRDEKRTHdhLLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVF 371
Cdd:COG3621     1 MSANKPFR--ILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAAGYSAEEILDLYEEEGKEIF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 372 RGSRP-------------YESGPLEEFLKREFGEhTKMTDVRKPkVMLTGT-LSDRQPaelHLFRNYDAPetvreprFNQ 437
Cdd:COG3621    79 PKSRWrkllslrglfgpkYDSEGLEKVLKEYFGD-TTLGDLKTP-VLIPSYdLDNGKP---VFFKSPHAK-------FDR 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 438 NVNLrppaqpsdqLVWRAARSSGAAPTYFRP---------NGRFLDGGLLANNPTLDAMTE-IHEYNQDL--IRkgqank 505
Cdd:COG3621   147 DRDF---------LLVDVARATSAAPTYFPPaqiknltgeGYALIDGGVFANNPALCALAEaLKLLGPDLddIL------ 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 506 vkklsiVVSLGTGRSPQvpvtcvdvfrpSNPWELAKTvFGAKELGKMVVDCCTDPDGRAVDrarAWCEMV-GIQYFRLNP 584
Cdd:COG3621   212 ------VLSLGTGTAPR-----------SIPYKKVKN-WGALGWLLPLIDILMDAQSDAVD---YQLRQLlGDRYYRLDP 270

                  ....*....
gi 1169292910 585 QLGTDIMLD 593
Cdd:COG3621   271 ELPEEIALD 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-229 7.05e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 7.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910   1 MDVTDYKGETVFHYAVQGDNSQVLQLLgRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPNGY-PIH 79
Cdd:COG0666    47 LALADALGALLLLAAALAGDLLVALLL-LAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGEtPLH 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  80 SAMKFSQKGCAEMIISMDSSqIHSKDpRYGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAI 156
Cdd:COG0666   126 LAAYNGNLEIVKLLLEAGAD-VNAQD-NDGNTPLHLAaanGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169292910 157 VLLTHGANADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRLVTRKAILTLLR 229
Cdd:COG0666   204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
Pat_PNPLA8 cd07211
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ...
301-611 8.14e-34

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


Pssm-ID: 132850 [Multi-domain]  Cd Length: 308  Bit Score: 131.22  E-value: 8.14e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 301 HLLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILA--LAILHSkSMAYMRGMYFRMKDEVF-RGSRP- 376
Cdd:cd07211     9 RILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAflLGLKKM-SLDECEELYRKLGKDVFsQNTYIs 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 377 -----------YESGPLEEFLKREFGEHTKMTDVRK---PKVMLTGTLSDRQPAELHLFRNYDAPETVREPRFNQnvnlr 442
Cdd:cd07211    88 gtsrlvlshayYDTETWEKILKEMMGSDELIDTSADpncPKVACVSTQVNRTPLKPYVFRNYNHPPGTRSHYLGS----- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 443 ppaqpSDQLVWRAARSSGAAPTYF----RPNGRFLDGGLLANNPTLDAMTEIHEYNQDlirkgqankvKKLSIVVSLGTG 518
Cdd:cd07211   163 -----CKHKLWEAIRASSAAPGYFeefkLGNNLHQDGGLLANNPTALALHEAKLLWPD----------TPIQCLVSVGTG 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 519 RSpqvpvtcvdvfrPSNPWELAKTVFGAKELGKMVVDCCTDPDgrAVDrarawcEMV-----GIQYFRLNPQLGTDIMLD 593
Cdd:cd07211   228 RY------------PSSVRLETGGYTSLKTKLLNLIDSATDTE--RVH------TALddllpPDVYFRFNPVMSECVELD 287
                         330
                  ....*....|....*...
gi 1169292910 594 EVSDTVLVNALWETEVYI 611
Cdd:cd07211   288 ETRPEKLDQLQDDTLEYI 305
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-207 1.08e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.90  E-value: 1.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910   2 DVTDYKGETVFHYAVQGDNSQVLQLLgRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPNGY-PIHS 80
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLL-LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNtPLHL 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  81 AMKFSQKGCAEMIISMDSsQIHSKDpRYGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIV 157
Cdd:COG0666   160 AAANGNLEIVKLLLEAGA-DVNARD-NDGETPLHLAaenGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1169292910 158 LLTHGANADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGET 207
Cdd:COG0666   238 LLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
Pat17_PNPLA8_PNPLA9_like2 cd07215
Patatin-like phospholipase of bacteria; Patatin is a storage protein of the potato tuber that ...
302-625 1.22e-25

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: 108.26  E-value: 1.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 302 LLCLDGGGVKGLIIIQLLIAIE----KASG---VATKDLFDWVAGTSTGGILALAIL-------HSKSMAYMRGMYFRMK 367
Cdd:cd07215     2 ILSIDGGGIRGIIPATILVSVEeklqKKTGnpeARLADYFDLVAGTSTGGILTCLYLcpnesgrPKFSAKEALNFYLERG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 368 DEVFRGSR-------------PYESGPLEEFLKREFGEhTKMTDVRKPKVMLTGTLSDRQPaelHLFRNYDApeTVREPR 434
Cdd:cd07215    82 NYIFKKKIwnkiksrggflneKYSHKPLEEVLLEYFGD-TKLSELLKPCLITSYDIERRSP---HFFKSHTA--IKNEQR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 435 fnqnvnlrppaqpsDQLVWRAARSSGAAPTYFRPNgRF----------LDGGLLANNPTLDAMTEiheynqdlIRKGQAN 504
Cdd:cd07215   156 --------------DFYVRDVARATSAAPTYFEPA-RIhsltgekytlIDGGVFANNPTLCAYAE--------ARKLKFE 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 505 KVKKLS----IVVSLGTGRSpqvpvtcvdvfRPSNPWELAKTvFGAKELGKMVVDCCTDPDGRAVDRARAW---CEMVGI 577
Cdd:cd07215   213 QPGKPTakdmIILSLGTGKN-----------KKSYTYEKVKD-WGLLGWAKPLIDIMMDGASQTVDYQLKQifdAEGDQQ 280
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1169292910 578 QYFRLNPQL-GTDIMLDEVSDTVLVNALWETEVYIYEHREEFQKLIQLL 625
Cdd:cd07215   281 QYLRIQPELeDADPEMDDASPENLEKLREVGQALAEDHKDQLDEIVDRL 329
Pat17_PNPLA8_PNPLA9_like3 cd07216
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
302-594 1.27e-22

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


Pssm-ID: 132855 [Multi-domain]  Cd Length: 309  Bit Score: 98.91  E-value: 1.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 302 LLCLDGGGVKGLII--------IQLLIAIEKASGVATKDLFDWVAGTSTGGILALailhsksmaymrgMYFRMK---DE- 369
Cdd:cd07216     3 LLSLDGGGVRGLSSllilkeimERIDPKEGLDEPPKPCDYFDLIGGTSTGGLIAI-------------MLGRLRmtvDEc 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 370 ----------VFRGSRPYESGPLEEFLKREFG----------------EHTKMTDVRKP---KVMLTGTLSDrQPAELHL 420
Cdd:cd07216    70 idaytrlakkIFSRKRLRLIIGDLRTGARFDSkklaeaikvilkelgnDEDDLLDEGEEdgcKVFVCATDKD-VTGKAVR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 421 FRNYDAPetvREPRFNQNVNlrppaqpsdqlVWRAARSSGAAPTYFRP------NGRFLDGGLLANNPTLDAMTEIHEYN 494
Cdd:cd07216   149 LRSYPSK---DEPSLYKNAT-----------IWEAARATSAAPTFFDPvkigpgGRTFVDGGLGANNPIREVWSEAVSLW 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 495 QDLIRkgqankvkKLSIVVSLGTGRSPQVpvtcvdVFRPSnpwelAKTVFGAKELGKMVvdccTDPDGRAVDRARAWCEM 574
Cdd:cd07216   215 EGLAR--------LVGCLVSIGTGTPSIK------SLGRS-----AEGAGLLKGLKDLV----TDTEAEAKRFSAEHSEL 271
                         330       340
                  ....*....|....*....|..
gi 1169292910 575 VGI-QYFRLN-PQLGTDIMLDE 594
Cdd:cd07216   272 DEEgRYFRFNvPHGLEDVGLDE 293
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
303-597 7.45e-20

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: 90.04  E-value: 7.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 303 LCLDGGGVKGLIIIQLLIAIEKA--SGVATKDLFdwvAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVFRGSRPYE-- 378
Cdd:cd07213     5 LSLDGGGVKGIVQLVLLKRLAEEfpSFLDQIDLF---AGTSAGSLIALGLALGYSPRQVLKLYEEVGLKVFSKSSAGGga 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 379 -------SGPLEEFLKREFGEhTKMTDVRKpKVMLTGTLSDRQPaelhlfrnydaPETVR--EPRFNQNVnlrPPAQPSD 449
Cdd:cd07213    82 gnnqyfaAGFLKAFAEVFFGD-LTLGDLKR-KVLVPSFQLDSGK-----------DDPNRrwKPKLFHNF---PGEPDLD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 450 QLVWRAARSSGAAPTYFRPNGRFLDGGLLANNPTLDAMTEIheynqdLIRKGQANKVKKLSiVVSLGTGRSPQvPVTcvD 529
Cdd:cd07213   146 ELLVDVCLRSSAAPTYFPSYQGYVDGGVFANNPSLCAIAQA------IGEEGLNIDLKDIV-VLSLGTGRPPS-YLD--G 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169292910 530 VFRPSNpWELAKTvfgAKELGKMVVdcctdpDGRaVDRARAWCEMV-GIQYFRLNPQLGTDIMLDEVSD 597
Cdd:cd07213   216 ANGYGD-WGLLQW---LPDLLDLFM------DAG-VDAADFQCRQLlGERYFRLDPVLPANIDLDDNKQ 273
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
303-487 1.05e-18

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: 84.58  E-value: 1.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 303 LCLDGGGVKGLIiiqlliaiekASGVA-----TKDLFDWVAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVFRGSRP- 376
Cdd:pfam01734   1 LVLSGGGARGAY----------HLGVLkalgeAGIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRk 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 377 ------------------YESGPLEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRqpaelhlfrnydaPETVREPRFNQN 438
Cdd:pfam01734  71 ralsllallrgligegglFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRAL-------------LTVISTALGTRA 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1169292910 439 VNLRPPAQPSDQLVWRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAM 487
Cdd:pfam01734 138 RILLPDDLDDDEDLADAVLASSALPGVFPPvrldGELYVDGGLVDNVPVEAAL 190
Ank_2 pfam12796
Ankyrin repeats (3 copies);
113-202 1.33e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 1.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 113 LHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHgANADARgEHGNTPLHLAMSKDNVEMIK 189
Cdd:pfam12796   1 LHLAaknGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1169292910 190 ALIVFGAEVDTPN 202
Cdd:pfam12796  79 LLLEKGADINVKD 91
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
301-511 2.18e-17

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 83.32  E-value: 2.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 301 HLLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVFRGSR----- 375
Cdd:NF041079    2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILALALALEIPARELVELFEEHGKDIFPKRKwprrl 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 376 -------PYESGPLEEFLKREFGEhTKMTDVRKPKVMLTGTLSDRQPaelHLFRnydapeTVREPRFNQNVNLRppaqps 448
Cdd:NF041079   82 lgllkkpKYSSEPLREVLEEIFGD-KTIGDLKHRVLIPAVNYTTGKP---QVFK------TPHHPDFTRDHKLK------ 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169292910 449 dqLVwRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAMTEIHEY-NQdlirkgQANKVKKLSI 511
Cdd:NF041079  146 --LV-DVALATSAAPTYFPLhefdNEQFVDGGLVANNPGLLGLHEALHFlGV------PYDDVRILSI 204
PHA02878 PHA02878
ankyrin repeat protein; Provisional
12-199 8.01e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 83.39  E-value: 8.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  12 FHYAVQGDNSQVLQ-LLGRNAvaGLNQVNNQGLTPLHLAC----QLGKQEMVRVLLLCNarcniMGPNGYPIHSAMKFSQ 86
Cdd:PHA02878   41 LHQAVEARNLDVVKsLLTRGH--NVNQPDHRDLTPLHIICkepnKLGMKEMIRSINKCS-----VFYTLVAIKDAFNNRN 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  87 KGCAEMII--------SMDSSQIHSKDPR-------------YGA-----------SPLHWA---KNAEMARMLLKRGCN 131
Cdd:PHA02878  114 VEIFKIILtnrykniqTIDLVYIDKKSKDdiieaeitklllsYGAdinmkdrhkgnTALHYAtenKDQRLTELLLSYGAN 193
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169292910 132 VNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSK-DNVEMIKALIVFGAEVD 199
Cdd:PHA02878  194 VNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVN 262
PHA02875 PHA02875
ankyrin repeat protein; Provisional
42-236 1.54e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 82.35  E-value: 1.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  42 GLTPLHLACQLGKQEMVRVLLLCNARCNIMGPN-GYPIHSAMKFSQKGCAEMIISMDS--SQIHSKDpryGASPLHWA-- 116
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDiESELHDAVEEGDVKAVEELLDLGKfaDDVFYKD---GMTPLHLAti 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 117 -KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMIKALIVFG 195
Cdd:PHA02875  112 lKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1169292910 196 AevdTPNDFGETPTFLA----------SKIGRLVTRKAILTLLRTVGAEYC 236
Cdd:PHA02875  192 A---NIDYFGKNGCVAAlcyaiennkiDIVRLFIKRGADCNIMFMIEGEEC 239
PHA03100 PHA03100
ankyrin repeat protein; Provisional
44-225 1.61e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 82.02  E-value: 1.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  44 TPLHLACQLGKQEMVRVLLlcNARCNI-------MGPngYPIHSAMKFSQKGCAEM--IISMDSSQIHSKDpRYGASPLH 114
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILL--DNGADInsstknnSTP--LHYLSNIKYNLTDVKEIvkLLLEYGANVNAPD-NNGITPLL 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 115 WA-----KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIV------------------LLTHGANADARGEH 171
Cdd:PHA03100  112 YAiskksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILkllidkgvdinaknrvnyLLSYGVPINIKDVY 191
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1169292910 172 GNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRLVTRKAIL 225
Cdd:PHA03100  192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
Pat17_PNPLA8_PNPLA9_like4 cd07217
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
302-586 1.14e-15

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


Pssm-ID: 132856 [Multi-domain]  Cd Length: 344  Bit Score: 78.69  E-value: 1.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 302 LLCLDGGGVKGLIIIQLLIAIEKASGVATK-------DLFDWVAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVF--- 371
Cdd:cd07217     3 ILALDGGGIRGLLSVEILGRIEKDLRTHLDdpefrlgDYFDFVGGTSTGSIIAACIALGMSVTDLLSFYTLNGVNMFdka 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 372 ------RGSRPYESGPLEEFLKR--EFGEHTKMTD--VRKPKVMLTGTLSDRQPAELHlfRNYDApetvrepRFNQNVnl 441
Cdd:cd07217    83 wlaqrlFLNKLYNQYDPTNLGKKlnTVFPETTLGDdtLRTLLMIVTRNATTGSPWPVC--NNPEA-------KYNDSD-- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 442 rPPAQPSDQLVWRAARSSGAAPTYFRPN---------GRFLDGGL-LANNPTLDAMTEIHEYNQDLIRKGQANKVkklsI 511
Cdd:cd07217   152 -RSDCNLDLPLWQLVRASTAAPTFFPPEvvsiapgtaFVFVDGGVtTYNNPAFQAFLMATAKPYKLNWEVGADNL----L 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 512 VVSLGTGRSPQVpvtcVDVFRPSNPWEL--AKTV-----FGAKELGKMVV----DCctdPDGRAVDR-------ARAWCE 573
Cdd:cd07217   227 LVSVGTGFAPEA----RPDLKAADMWALdhAKYIpsalmNAANAGQDMVCrvlgEC---RKGGLVDReigtmhvDPNWLG 299
                         330
                  ....*....|...
gi 1169292910 574 MVGIQYFRLNPQL 586
Cdd:cd07217   300 PKLFTYVRYDVSL 312
PHA03095 PHA03095
ankyrin-like protein; Provisional
56-208 4.97e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 74.68  E-value: 4.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  56 EMVRVLLLCNARCNIMGPNGY-PIHSAMKFSQKGCAEMIISMDSSQIHSKDP-RYGASPLHW----AKNAEMARMLLKRG 129
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKtPLHLYLHYSSEKVKDIVRLLLEAGADVNAPeRCGFTPLHLylynATTLDVIKLLIKAG 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 130 CNVNSTSSAGNTALHV--AVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAM-SKD-NVEMIKALIVFGAEVDTPNDFG 205
Cdd:PHA03095  108 ADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLkSRNaNVELLRLLIDAGADVYAVDDRF 187

                  ...
gi 1169292910 206 ETP 208
Cdd:PHA03095  188 RSL 190
PHA02874 PHA02874
ankyrin repeat protein; Provisional
15-208 2.60e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.22  E-value: 2.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  15 AVQGDNSQVLQLLgRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMgpngyPIHSAMKFSQKGCAEMII 94
Cdd:PHA02874   42 AIRSGDAKIVELF-IKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIL-----PIPCIEKDMIKTILDCGI 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  95 SMDSSQIHSKdprygaSPLHWA-KNA--EMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEH 171
Cdd:PHA02874  116 DVNIKDAELK------TFLHYAiKKGdlESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1169292910 172 GNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETP 208
Cdd:PHA02874  190 GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226
PHA02874 PHA02874
ankyrin repeat protein; Provisional
18-226 4.61e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.45  E-value: 4.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  18 GDNSQVLQLLgRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPN-GYPIHSAMKFSQKGCAEMII-- 94
Cdd:PHA02874   12 GDIEAIEKII-KNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKiPHPLLTAIKIGAHDIIKLLIdn 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  95 SMDSSQIHSKDprygasplhwaKNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNT 174
Cdd:PHA02874   91 GVDTSILPIPC-----------IEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCY 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169292910 175 PLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRLVTRKAILT 226
Cdd:PHA02874  160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLID 211
PHA02878 PHA02878
ankyrin repeat protein; Provisional
40-182 5.81e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.37  E-value: 5.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  40 NQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGP-NGYPIHSAMKFSQKGCAEMIISMDSSqIHSKDpRYGASPLHWA-- 116
Cdd:PHA02878  166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKtNNSPLHHAVKHYNKPIVHILLENGAS-TDARD-KCGNTPLHISvg 243
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169292910 117 --KNAEMARMLLKRGCNVNSTSSA-GNTALHVAVMRNRfdCAIVLLTHGANADARGEHGNTPLHLAMSK 182
Cdd:PHA02878  244 ycKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
90-225 1.05e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 66.13  E-value: 1.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  90 AEMIISMDSSQIHSKDPRYGASPLHWAKNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARG 169
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1169292910 170 EHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRLVTRKAIL 225
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL 140
PHA02876 PHA02876
ankyrin repeat protein; Provisional
16-241 1.15e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.78  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  16 VQGDNSQVLQLLGRNAvAGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPNGYPI-HSAMKFSQKGCAEMII 94
Cdd:PHA02876  153 IQQDELLIAEMLLEGG-ADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVlECAVDSKNIDTIKAII 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  95 SmDSSQIHSKDprygASPLHWAKNA--EMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAI-VLLTHGANADARGEH 171
Cdd:PHA02876  232 D-NRSNINKND----LSLLKAIRNEdlETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVpKLLERGADVNAKNIK 306
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169292910 172 GNTPLHLaMSKD--NVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRlvTRKAILTLLRtVGA-----EYC-FPPIH 241
Cdd:PHA02876  307 GETPLYL-MAKNgyDTENIRTLIMLGADVNAADRLYITPLHQASTLDR--NKDIVITLLE-LGAnvnarDYCdKTPIH 380
PHA03095 PHA03095
ankyrin-like protein; Provisional
13-214 1.32e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.97  E-value: 1.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  13 HYAVQGDNSQVLQLLgrNAVAGLNQVNNQGLTPLHLACQLGKQE-MVRVLLLCNARCNIMGPNGY-PIHSAM--KFSQKG 88
Cdd:PHA03095   56 HYSSEKVKDIVRLLL--EAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRtPLHVYLsgFNINPK 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  89 CAEMIISMDSSqIHSKDpRYGASPLHW-----AKNAEMARMLLKRGCNVNSTSSAGNTALHV--AVMRNRFDCAIVLLTH 161
Cdd:PHA03095  134 VIRLLLRKGAD-VNALD-LYGMTPLAVllksrNANVELLRLLIDAGADVYAVDDRFRSLLHHhlQSFKPRARIVRELIRA 211
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1169292910 162 GANADARGEHGNTPLH-LAM-SKDNVEMIKALIVFGAEVDTPNDFGETPTFLASK 214
Cdd:PHA03095  212 GCDPAATDMLGNTPLHsMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAV 266
PHA02874 PHA02874
ankyrin repeat protein; Provisional
35-225 1.72e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.53  E-value: 1.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  35 LNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPNG-YPIHSAMKFSQKGCAEMIISmDSSQIHSKDpRYGASPL 113
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGcYPIHIAIKHNFFDIIKLLLE-KGAYANVKD-NNGESPL 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 114 HWAK---NAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRfdCAIVLLTHGANADARGEHGNTPLHLAMSKD-NVEMIK 189
Cdd:PHA02874  195 HNAAeygDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR--SAIELLINNASINDQDIDGSTPLHHAINPPcDIDIID 272
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1169292910 190 ALIVFGAEVDTPNDFGETPTFLASK-IGRLVTRKAIL 225
Cdd:PHA02874  273 ILLYHKADISIKDNKGENPIDTAFKyINKDPVIKDII 309
PHA02876 PHA02876
ankyrin repeat protein; Provisional
8-216 2.34e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 66.63  E-value: 2.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910   8 GETVFHYAVQGDNSQVLQLLGRNAvaglNQVNNQGLTPLHlacQLGKQEMVRVLLLCNARCNIMGPNGY---PIHSAMKF 84
Cdd:PHA02876  211 DLSVLECAVDSKNIDTIKAIIDNR----SNINKNDLSLLK---AIRNEDLETSLLLYDAGFSVNSIDDCkntPLHHASQA 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  85 SQKGCAEMIISMDSSQIHSKDPRyGASPLH-WAKNA---EMARMLLKRGCNVNSTSSAGNTALHVAVMRNRF-DCAIVLL 159
Cdd:PHA02876  284 PSLSRLVPKLLERGADVNAKNIK-GETPLYlMAKNGydtENIRTLIMLGADVNAADRLYITPLHQASTLDRNkDIVITLL 362
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169292910 160 THGANADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTpndfgetptfLASKIG 216
Cdd:PHA02876  363 ELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA----------LSQKIG 409
Ank_2 pfam12796
Ankyrin repeats (3 copies);
12-135 2.52e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.13  E-value: 2.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  12 FHYAVQGDNSQVLQLLgRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLLlcnarcnimgpngypihsamkfsqkgcae 91
Cdd:pfam12796   1 LHLAAKNGNLELVKLL-LENGADANLQDKNGRTALHLAAKNGHLEIVKLLL----------------------------- 50
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1169292910  92 miismdsSQIHSKDPRYGASPLHWA---KNAEMARMLLKRGCNVNST 135
Cdd:pfam12796  51 -------EHADVNLKDNGRTALHYAarsGHLEIVKLLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
1-199 5.04e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.98  E-value: 5.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910   1 MDVTDYKGETVFHYAVQGDNSQVLQLLGRNAvAGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPNG-YPIH 79
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYG-ADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGeSPLH 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  80 SAMKFSQKGCAEMIISmDSSQIHSKDPRyGASPLHWA--KNAEMARMLLKRGcNVNSTSSAGNTALHVAVmrnRFDCAI- 156
Cdd:PHA02874  196 NAAEYGDYACIKLLID-HGNHIMNKCKN-GFTPLHNAiiHNRSAIELLINNA-SINDQDIDGSTPLHHAI---NPPCDId 269
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169292910 157 ---VLLTHGANADARGEHGNTPLHLAM---SKDNVemIKALI---VFGAEVD 199
Cdd:PHA02874  270 iidILLYHKADISIKDNKGENPIDTAFkyiNKDPV--IKDIIanaVLIKEAD 319
PHA02876 PHA02876
ankyrin repeat protein; Provisional
3-214 9.07e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.08  E-value: 9.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910   3 VTDYKgETVFHYAVQGDNSQVL--QLLGRNAvaGLNQVNNQGLTPLHLacqlgkqemvrvlllcnarcniMGPNGYPIHS 80
Cdd:PHA02876  269 IDDCK-NTPLHHASQAPSLSRLvpKLLERGA--DVNAKNIKGETPLYL----------------------MAKNGYDTEN 323
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  81 AMKFSQKGcaemiismdsSQIHSKDPRYgASPLHWA----KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAI 156
Cdd:PHA02876  324 IRTLIMLG----------ADVNAADRLY-ITPLHQAstldRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIIN 392
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1169292910 157 VLLTHGANADARGEHGNTPLHLAMSKDNVEM-IKALIVFGAEVDTPNDFGETPTFLASK 214
Cdd:PHA02876  393 TLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACK 451
PHA03100 PHA03100
ankyrin repeat protein; Provisional
2-200 1.02e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.92  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910   2 DVTDYKGETVFHYAVQGDNSQVLQLLGRNAvAGLNQVNNQGLTPLHLACQLGK-----QEMVRVLLLCNARCNIMGPNG- 75
Cdd:PHA03100   29 DYSYKKPVLPLYLAKEARNIDVVKILLDNG-ADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGi 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  76 YPIHSAM--KFSQKGCAEMIISMdSSQIHSKDPrYGASPLHWA-----KNAEMARMLLKRGCNVNSTSSA---------- 138
Cdd:PHA03100  108 TPLLYAIskKSNSYSIVEYLLDN-GANVNIKNS-DGENLLHLYlesnkIDLKILKLLIDKGVDINAKNRVnyllsygvpi 185
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169292910 139 ------GNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDT 200
Cdd:PHA03100  186 nikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
143-235 1.24e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.20  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 143 LHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMIKALIVFgAEVDtPNDFGETPTFLASKIGRLvtrk 222
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHL---- 74
                          90
                  ....*....|...
gi 1169292910 223 AILTLLRTVGAEY 235
Cdd:pfam12796  75 EIVKLLLEKGADI 87
PHA02875 PHA02875
ankyrin repeat protein; Provisional
9-166 4.43e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.93  E-value: 4.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910   9 ETVFHYAV-QGDNSQVLQLLGRNAVAGlNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPNGY-PIHSAMKFSQ 86
Cdd:PHA02875   69 ESELHDAVeEGDVKAVEELLDLGKFAD-DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFsPLHLAVMMGD 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  87 KGCAEMIIsmDSSQIHSKDPRYGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGN-TALHVAVMRNRFDCAIVLLTHG 162
Cdd:PHA02875  148 IKGIELLI--DHKACLDIEDCCGCTPLIIAmakGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRG 225

                  ....
gi 1169292910 163 ANAD 166
Cdd:PHA02875  226 ADCN 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1-71 8.67e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.89  E-value: 8.67e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169292910   1 MDVTDYKGETVFHYAVQGDNSQVLQLLGRNAVAglnQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIM 71
Cdd:pfam12796  23 ANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
Ank_5 pfam13857
Ankyrin repeats (many copies);
125-179 1.23e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 54.27  E-value: 1.23e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1169292910 125 LLKRG-CNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLA 179
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
109-237 1.55e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.39  E-value: 1.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 109 GASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANA-DARGEHGNTPLHLAMSKDN 184
Cdd:PHA02875   35 GISPIKLAmkfRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKK 114
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1169292910 185 VEMIKALIVFGAEVDTPNDFGETPTFLASKIGRLVTRKAILTLLRTVGAEYCF 237
Cdd:PHA02875  115 LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167
Pat17_isozyme_like cd07214
Patatin-like phospholipase of plants; Pat17 is an isozyme of patatin cloned from Solanum ...
302-522 2.30e-09

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


Pssm-ID: 132853 [Multi-domain]  Cd Length: 349  Bit Score: 59.37  E-value: 2.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 302 LLCLDGGGVKGLIIIQLLIAIEK------ASGVATKDLFDWVAGTSTGGILAlAILHSKSmAYMRGM---------YFRM 366
Cdd:cd07214     6 VLSIDGGGIRGIIPATILEFLEGklqeldGPDARIADYFDVIAGTSTGGLIT-AMLTAPN-ENKRPLfaakdivqfYLEN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 367 KDEVFRGSR-PYES---------GP------LEEFLKREFGEhTKMTDVRKPKVMLTGTLSDRQPAelhLFRNYDApetV 430
Cdd:cd07214    84 GPKIFPQSTgQFEDdrkklrsllGPkydgvyLHDLLNELLGD-TRLSDTLTNVVIPTFDIKLLQPV---IFSSSKA---K 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 431 REPRFNqnvnlrppAQPSDqlvwrAARSSGAAPTYFrPNGRF--------------LDGGLLANNPTLDAMT----EIHE 492
Cdd:cd07214   157 NDKLTN--------ARLAD-----VCISTSAAPTYF-PAHYFttedsngdirefnlVDGGVAANNPTLLAISevtkEIIK 222
                         250       260       270
                  ....*....|....*....|....*....|
gi 1169292910 493 YNQDLIRKGQANKVKKLsiVVSLGTGRSPQ 522
Cdd:cd07214   223 DNPFFASIKPLDYKKLL--VLSLGTGSAEE 250
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
121-201 3.72e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 59.64  E-value: 3.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 121 MARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHG---ANADARGE--HGNTPLHLAMSKDNVEMIKALIVFG 195
Cdd:cd22192    33 IKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelVNEPMTSDlyQGETALHIAVVNQNLNLVRELIARG 112

                  ....*.
gi 1169292910 196 AEVDTP 201
Cdd:cd22192   113 ADVVSP 118
Ank_4 pfam13637
Ankyrin repeats (many copies);
139-192 3.84e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 3.84e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1169292910 139 GNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMIKALI 192
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
15-199 6.03e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.52  E-value: 6.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  15 AVQGDNSQVLQLLGRNAvAGLNQVNNQGLTPLHLA--CQLGKQEMVRVLLLCNARCNIMGPNGY-PIHSAMKFS------ 85
Cdd:PHA03100   80 YNLTDVKEIVKLLLEYG-ANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGEnLLHLYLESNkidlki 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  86 ------------QKGCAEMIISMDSSqIHSKDpRYGASPLH---WAKNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRN 150
Cdd:PHA03100  159 lkllidkgvdinAKNRVNYLLSYGVP-INIKD-VYGFTPLHyavYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNN 236
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1169292910 151 RFDCAIVLLTHGANADARGEH----GNTPLHlamSKDNVEMIKALIVFGAEVD 199
Cdd:PHA03100  237 NKEIFKLLLNNGPSIKTIIETllyfKDKDLN---TITKIKMLKKSIMYMFLLD 286
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
109-207 7.47e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.73  E-value: 7.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 109 GASPLHWAKN---AEMARMLLKRGCNVNSTSSAGNTALHVAVM-------------------------------RNRFDC 154
Cdd:PLN03192  558 GRTPLHIAASkgyEDCVLVLLKHACNVHIRDANGNTALWNAISakhhkifrilyhfasisdphaagdllctaakRNDLTA 637
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1169292910 155 AIVLLTHGANADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVD---TPNDFGET 207
Cdd:PLN03192  638 MKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDkanTDDDFSPT 693
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
8-192 1.19e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 58.10  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910   8 GETVFHYAVQGDNSQVLQLLGRNAVAGLNQVNN----QGLTPLHLACQLGKQEMVRVLLlcnarcnimgpngypihsamk 83
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVVNQNLNLVRELI--------------------- 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  84 fsQKGcAEMIISMDSSQIHSKDPR----YGASPLHWAK---NAEMARMLLKRGCNVNSTSSAGNTALHVAVMRN--RFDC 154
Cdd:cd22192   110 --ARG-ADVVSPRATGTFFRPGPKnliyYGEHPLSFAAcvgNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPnkTFAC 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1169292910 155 AI--VLLTHGANADA------RGEHGNTPLHLAMSKDNVEMIKALI 192
Cdd:cd22192   187 QMydLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLV 232
PHA03095 PHA03095
ankyrin-like protein; Provisional
38-154 2.78e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.57  E-value: 2.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  38 VNNQGLTPLHLACQLGK--QEMVRVL--LLCNARCNIMGPNGyPIHSAMKFSQkgCAEMIIS---MDSSQIHSKDpRYGA 110
Cdd:PHA03095  183 VDDRFRSLLHHHLQSFKprARIVRELirAGCDPAATDMLGNT-PLHSMATGSS--CKRSLVLpllIAGISINARN-RYGQ 258
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1169292910 111 SPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDC 154
Cdd:PHA03095  259 TPLHYAavfNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRA 305
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
23-208 6.74e-08

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 55.69  E-value: 6.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  23 VLQLLGRNAVaGLNQVNNQGLTPLHLACQLGK------QEMVRVLLLCNARC-NIMGPNGYPIHSAMKFSQKGCAEMIIS 95
Cdd:PHA02716  194 ILEWLCNNGV-NVNLQNNHLITPLHTYLITGNvcasviKKIIELGGDMDMKCvNGMSPIMTYIINIDNINPEITNIYIES 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  96 MDSSQIhSKDPRYGASPLHWAKNAEMARM--LLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIV--LLTHGANADARGEH 171
Cdd:PHA02716  273 LDGNKV-KNIPMILHSYITLARNIDISVVysFLQPGVKLHYKDSAGRTCLHQYILRHNISTDIIklLHEYGNDLNEPDNI 351
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1169292910 172 GNTPLHLAMSK-----------DN---VEMIKALIVFGAEVDTPNDFGETP 208
Cdd:PHA02716  352 GNTVLHTYLSMlsvvnildpetDNdirLDVIQCLISLGADITAVNCLGYTP 402
PHA03095 PHA03095
ankyrin-like protein; Provisional
8-192 1.26e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 54.65  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910   8 GETVFHYAVQGDNS-QVLQLLGRNAvAGLNQVNNQGLTPLHlACQLGKQ---EMVRVLLLCNARCNIMGPNGY-PIHSAM 82
Cdd:PHA03095   83 GFTPLHLYLYNATTlDVIKLLIKAG-ADVNAKDKVGRTPLH-VYLSGFNinpKVIRLLLRKGADVNALDLYGMtPLAVLL 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  83 KFsqKGCA----EMIISMDSSqIHSKDPRyGASPLH-----WAKNAEMARMLLKRGCNVNSTSSAGNTALHVAVM----- 148
Cdd:PHA03095  161 KS--RNANvellRLLIDAGAD-VYAVDDR-FRSLLHhhlqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATgssck 236
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169292910 149 ----------------RNRF-------------DCAIV-LLTHGANADARGEHGNTPLHLAMSKDNVEMIKALI 192
Cdd:PHA03095  237 rslvlplliagisinaRNRYgqtplhyaavfnnPRACRrLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
118-254 1.66e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.49  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 118 NAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMIKALIVFgAE 197
Cdd:PLN03192  537 NAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-AS 615
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169292910 198 VDTPNDFGETPTFlASKIGRLVTRKAILTLLRTVGAEycfpPIHGVPAEQGSAAPHH 254
Cdd:PLN03192  616 ISDPHAAGDLLCT-AAKRNDLTAMKELLKQGLNVDSE----DHQGATALQVAMAEDH 667
Ank_4 pfam13637
Ankyrin repeats (many copies);
111-159 2.37e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 2.37e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169292910 111 SPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLL 159
Cdd:pfam13637   3 TALHAAaasGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
125-203 2.81e-07

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 53.13  E-value: 2.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 125 LLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDN--VEMIKALIVFGAEVDTPN 202
Cdd:PHA02946   58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNSV 137

                  .
gi 1169292910 203 D 203
Cdd:PHA02946  138 D 138
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
157-266 8.18e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 8.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 157 VLLTHGANADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRlvtRKAILTLLRTVG---- 232
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF---REVVQLLSRHSQchfe 176
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1169292910 233 AEYCFPP--IHGVPA--EQGSAAPHHP-FSlerAQPPPI 266
Cdd:PTZ00322  177 LGANAKPdsFTGKPPslEDSPISSHHPdFS---AVPQPM 212
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
122-191 1.41e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 1.41e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 122 ARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMIKAL 191
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_5 pfam13857
Ankyrin repeats (many copies);
158-208 8.95e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 8.95e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169292910 158 LLTHG-ANADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETP 208
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
Ank_4 pfam13637
Ankyrin repeats (many copies);
172-218 1.01e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 1.01e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1169292910 172 GNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRL 218
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNV 47
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
303-483 1.55e-05

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: 46.12  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 303 LCLDGGGVKGLIIIQLLIAIEKAsGVatkdLFDWVAGTSTGGILA--LAI-LHSKSMAY--MRGMYFRMKDE----VFRG 373
Cdd:cd07207     2 LVFEGGGAKGIAYIGALKALEEA-GI----LKKRVAGTSAGAITAalLALgYSAADIKDilKETDFAKLLDSpvglLFLL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 374 SRPYESG------PLEEFLKREFGEHTKMTDVRKpkvmLTGTLSDRQPAELHLF-RNYDapeTVREPRFNQNvnlrppaQ 446
Cdd:cd07207    77 PSLFKEGglykgdALEEWLRELLKEKTGNSFATS----LLRDLDDDLGKDLKVVaTDLT---TGALVVFSAE-------T 142
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1169292910 447 PSDQLVWRAARSSGAAPTYFRP-----NGRFLDGGLLANNPT 483
Cdd:cd07207   143 TPDMPVAKAVRASMSIPFVFKPvrlakGDVYVDGGVLDNYPV 184
Ank_5 pfam13857
Ankyrin repeats (many copies);
107-146 3.21e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 3.21e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1169292910 107 RYGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVA 146
Cdd:pfam13857  14 GEGYTPLHVAakyGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
171-199 4.74e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.65  E-value: 4.74e-05
                           10        20
                   ....*....|....*....|....*....
gi 1169292910  171 HGNTPLHLAMSKDNVEMIKALIVFGAEVD 199
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
333-486 5.15e-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: 44.25  E-value: 5.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 333 LFDWVAGTSTGGILALAILHSKSMAYMrgmYFRMkDEVFRGSRPYESGPLEeflkREFgehtKMTDVRKPKvmltgtLSD 412
Cdd:cd07198    26 LIDIIAGTSAGAIVAALLASGRDLEEA---LLLL-LRLSREVRLRFDGAFP----PTG----RLLGILRQP------LLS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 413 RQPAELHLFRNYdapetvrepRFNQNVN------LRPPAQPSDQLVWRAARSSGAAPTYFRP------NGRFLDGGLLAN 480
Cdd:cd07198    88 ALPDDAHEDASG---------KLFISLTrltdgeNVLVSDTSKGELWSAVRASSSIPGYFGPvplsfrGRRYGDGGLSNN 158

                  ....*.
gi 1169292910 481 NPTLDA 486
Cdd:cd07198   159 LPVAEL 164
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
42-187 5.41e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.23  E-value: 5.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  42 GLTPLHLACQLGKQEMVRVLLL----CNARCNimgpngypihsamkfsqkgCAEMIISMDSSQIhskdpRYGASPLHWAK 117
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLErgasVPARAC-------------------GDFFVKSQGVDSF-----YHGESPLNAAA 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 118 ---NAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFD---------CAIVLLTHGANADARGE-------HGNTPLHL 178
Cdd:TIGR00870 184 clgSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKaeyeelscqMYNFALSLLDKLRDSKElevilnhQGLTPLKL 263

                  ....*....
gi 1169292910 179 AMSKDNVEM 187
Cdd:TIGR00870 264 AAKEGRIVL 272
PHA02859 PHA02859
ankyrin repeat protein; Provisional
77-208 6.94e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 44.42  E-value: 6.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  77 PIHSAM--KFSQKGCAEMIISmDSSQIHSKDPRYGASPLH----WAKNA--EMARMLLKRGCNVNSTSSAGNTALHVaVM 148
Cdd:PHA02859   54 PIFSCLekDKVNVEILKFLIE-NGADVNFKTRDNNLSALHhylsFNKNVepEILKILIDSGSSITEEDEDGKNLLHM-YM 131
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169292910 149 RN---RFDCAIVLLTHGANADARGEHGNTPLH-LAMSKDNVEMIKALIVFGAEVDTPNDFGETP 208
Cdd:PHA02859  132 CNfnvRINVIKLLIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNC 195
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
98-198 7.24e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 45.84  E-value: 7.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  98 SSQIHSKDPrYGASPLHWA----KNAEMARMLLKRGCNVnstsSAGNTALHVAVMR---NRFDCAIVLLTHG-------- 162
Cdd:TIGR00870  42 KLNINCPDR-LGRSALFVAaienENLELTELLLNLSCRG----AVGDTLLHAISLEyvdAVEAILLHLLAAFrksgplel 116
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1169292910 163 ANADARGE--HGNTPLHLAMSKDNVEMIKALIVFGAEV 198
Cdd:TIGR00870 117 ANDQYTSEftPGITALHLAAHRQNYEIVKLLLERGASV 154
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
171-200 1.09e-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: 1.09e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1169292910 171 HGNTPLHLAMSKDNVEMIKALIVFGAEVDT 200
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
171-203 1.18e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 39.58  E-value: 1.18e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1169292910 171 HGNTPLHLA-MSKDNVEMIKALIVFGAEVDTPND 203
Cdd:pfam00023   1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
139-167 4.15e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 4.15e-04
                           10        20
                   ....*....|....*....|....*....
gi 1169292910  139 GNTALHVAVMRNRFDCAIVLLTHGANADA 167
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02743 PHA02743
Viral ankyrin protein; Provisional
93-210 7.19e-04

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 40.57  E-value: 7.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  93 IISMDSSQIHSKDpRYGASPLHWA-----KNAEMA-RMLLKRGCNVNSTSS-AGNTALHVAVMRNRFDCAIVLLTH-GAN 164
Cdd:PHA02743   42 FISGDGHLLHRYD-HHGRQCTHMVawydrANAVMKiELLVNMGADINARELgTGNTLLHIAASTKNYELAEWLCRQlGVN 120
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1169292910 165 ADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTF 210
Cdd:PHA02743  121 LGAINYQHETAYHIAYKMRDRRMMEILRANGAVCDDPLSIGLSDET 166
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
139-168 7.80e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 7.80e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1169292910 139 GNTALHVAVMR-NRFDCAIVLLTHGANADAR 168
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNAR 32
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
109-208 1.09e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.92  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 109 GASPLHWA---KNAEMARMLLK---RGCNVNSTSS--AGNTALHVAVMRNRFDCAIVLLTHGAN-ADAR----------- 168
Cdd:cd22192    51 GETALHVAalyDNLEAAVVLMEaapELVNEPMTSDlyQGETALHIAVVNQNLNLVRELIARGADvVSPRatgtffrpgpk 130
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1169292910 169 -----GEHgntPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETP 208
Cdd:cd22192   131 nliyyGEH---PLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
139-167 1.80e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.08  E-value: 1.80e-03
                          10        20
                  ....*....|....*....|....*....
gi 1169292910 139 GNTALHVAVMRNRFDCAIVLLTHGANADA 167
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
108-135 1.85e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 1.85e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1169292910 108 YGASPLHWA----KNAEMARMLLKRGCNVNST 135
Cdd:pfam00023   1 DGNTPLHLAagrrGNLEIVKLLLSKGADVNAR 32
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
41-70 2.09e-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: 36.11  E-value: 2.09e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1169292910  41 QGLTPLHLAC-QLGKQEMVRVLLLCNARCNI 70
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNA 31
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
109-225 2.30e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 40.94  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 109 GASPLHWA---KNAEMARMLLKRGCNVNSTSSA--------------GNTALHVAVMRNRFDCAIVLLTH---GANADAR 168
Cdd:cd22196    94 GQTALHIAierRNMHLVELLVQNGADVHARASGeffkkkkggpgfyfGELPLSLAACTNQLDIVKFLLENphsPADISAR 173
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169292910 169 GEHGNTPLH-LAMSKDN--------VEMIKALIVFGAEV-------DTPNDFGETPTFLASKIGRLVTRKAIL 225
Cdd:cd22196   174 DSMGNTVLHaLVEVADNtpentkfvTKMYNEILILGAKIrpllkleEITNKKGLTPLKLAAKTGKIGIFAYIL 246
PHA02736 PHA02736
Viral ankyrin protein; Provisional
39-199 2.53e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.09  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  39 NNQGLTPLHLACQLGKqemvrVLLLCNARCNIMGPNGYpihSAMKFSQKG--CAEMIISMDSSqihskDPRygasplhwa 116
Cdd:PHA02736   14 DIEGENILHYLCRNGG-----VTDLLAFKNAISDENRY---LVLEYNRHGkqCVHIVSNPDKA-----DPQ--------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 117 knaEMARMLLKRGCNVNSTSSA-GNTALHVAVMRNRFDCAIVLLTH-GANADARGEHGNTPLHLAMSKDNVEMIKALIVF 194
Cdd:PHA02736   72 ---EKLKLLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAK 148

                  ....*
gi 1169292910 195 GAEVD 199
Cdd:PHA02736  149 GAQCK 153
Ank_5 pfam13857
Ankyrin repeats (many copies);
2-49 3.37e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 3.37e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1169292910   2 DVTDYKGETVFHYAVQGDNSQVLQLLGRNAVAgLNQVNNQGLTPLHLA 49
Cdd:pfam13857  10 NRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD-LNLKDEEGLTALDLA 56
PHA02946 PHA02946
ankyin-like protein; Provisional
36-226 4.38e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.04  E-value: 4.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910  36 NQVNNQGLTPLHLACQLGKQEMVRVLLLCNArcnimGPNGYPIHSAMK-FSQKGCAEMIIS------MDSSQIHSKDPRY 108
Cdd:PHA02946   66 NETDDDGNYPLHIASKINNNRIVAMLLTHGA-----DPNACDKQHKTPlYYLSGTDDEVIErinllvQYGAKINNSVDEE 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 109 GASPLHWAKNA--EMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIV--LLTHGANADARGEHGNTPLHLAMSK-- 182
Cdd:PHA02946  141 GCGPLLACTDPseRVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKASTIswMMKLGISPSKPDHDGNTPLHIVCSKtv 220
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1169292910 183 DNVEMIKaLIVFGAEVDTPNDFGETPTFLASK-------IGRLVTRKAILT 226
Cdd:PHA02946  221 KNVDIIN-LLLPSTDVNKQNKFGDSPLTLLIKtlspahlINKLLSTSNVIT 270
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
109-241 6.05e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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 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.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 39.84  E-value: 6.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 109 GASPLHWA---KNAEMARMLLKRGCNVNSTSSA-------------GNTALHVAVMRNRFDCAIVLLTHG---ANADARG 169
Cdd:cd22197    94 GHSALHIAiekRSLQCVKLLVENGADVHARACGrffqkkqgtcfyfGELPLSLAACTKQWDVVNYLLENPhqpASLQAQD 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169292910 170 EHGNTPLH-LAMSKDN--------VEMIKALIVFGAEVD-------TPNDFGETPTFLASKIGRLVTRKAILTllRTVGA 233
Cdd:cd22197   174 SLGNTVLHaLVMIADNspensalvIKMYDGLLQAGARLCptvqleeISNHEGLTPLKLAAKEGKIEIFRHILQ--REFSG 251
                         170
                  ....*....|....*...
gi 1169292910 234 ----------EYCFPPIH 241
Cdd:cd22197   252 pyqhlsrkftEWCYGPVR 269
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
108-133 7.76e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.49  E-value: 7.76e-03
                           10        20
                   ....*....|....*....|....*....
gi 1169292910  108 YGASPLHWA---KNAEMARMLLKRGCNVN 133
Cdd:smart00248   1 DGRTPLHLAaenGNLEVVKLLLDKGADIN 29
 
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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