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Conserved domains on  [gi|1743221413|ref|XP_030671429|]
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85/88 kDa calcium-independent phospholipase A2 isoform X4 [Nomascus leucogenys]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 12791065)

ankyrin repeat (ANK) domain-containing protein mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
 254-567 0e+00

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


:

Pssm-ID: 132851 [Multi-domain]  Cd Length: 312  Bit Score: 577.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 254 LLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRPYESGP 333
Cdd:cd07212     1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGSRPYNSEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 334 LEEFLKREFGEHTKMTDVKKPKVMLTGTLSDRQPAELHLFRNYDAPETVREPRFNqnVNLRPPAQPSDQLVWRAARSSGA 413
Cdd:cd07212    81 LEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEEPEKN--ANFLPPTDPAEQLLWRAARSSGA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 414 APTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAK 493
Cdd:cd07212   159 APTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKSKGRKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSNPWELAK 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743221413 494 TVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVNALWETEVYIYEHR 567
Cdd:cd07212   239 TVFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTHR 312
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-185 1.14e-30

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.60  E-value: 1.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  53 IHSKDpRYGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLH 129
Cdd:COG0666   113 VNARD-KDGETPLHLAaynGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLH 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1743221413 130 LAMSKDNVEMVKALIVFGAEVDTLNDFGETPAFLASKISrlvtRKAILTLLRTVGA 185
Cdd:COG0666   192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENG----NLEIVKLLLEAGA 243
 
Name Accession Description Interval E-value
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
 254-567 0e+00

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


Pssm-ID: 132851 [Multi-domain]  Cd Length: 312  Bit Score: 577.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 254 LLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRPYESGP 333
Cdd:cd07212     1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGSRPYNSEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 334 LEEFLKREFGEHTKMTDVKKPKVMLTGTLSDRQPAELHLFRNYDAPETVREPRFNqnVNLRPPAQPSDQLVWRAARSSGA 413
Cdd:cd07212    81 LEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEEPEKN--ANFLPPTDPAEQLLWRAARSSGA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 414 APTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAK 493
Cdd:cd07212   159 APTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKSKGRKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSNPWELAK 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743221413 494 TVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVNALWETEVYIYEHR 567
Cdd:cd07212   239 TVFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTHR 312
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 244-545 3.89e-46

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 164.31  E-value: 3.89e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 244 MRDEKRTHdhLLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVF 323
Cdd:COG3621     1 MSANKPFR--ILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAAGYSAEEILDLYEEEGKEIF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 324 RGSRP-------------YESGPLEEFLKREFGEhTKMTDVKKPkVMLTGT-LSDRQPaelHLFRNYDAPetvreprFNQ 389
Cdd:COG3621    79 PKSRWrkllslrglfgpkYDSEGLEKVLKEYFGD-TTLGDLKTP-VLIPSYdLDNGKP---VFFKSPHAK-------FDR 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 390 NVNLrppaqpsdqLVWRAARSSGAAPTYFRP---------NGRFLDGGLLANNPTLDAMTE-IHEYNQDL--IRkgqank 457
Cdd:COG3621   147 DRDF---------LLVDVARATSAAPTYFPPaqiknltgeGYALIDGGVFANNPALCALAEaLKLLGPDLddIL------ 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 458 vkklsiVVSLGTGRSPQvpvtcvdvfrpSNPWELAKTvFGAKELGKMVVDCCTDPDGRAVDrarAWCEMV-GIQYFRLNP 536
Cdd:COG3621   212 ------VLSLGTGTAPR-----------SIPYKKVKN-WGALGWLLPLIDILMDAQSDAVD---YQLRQLlGDRYYRLDP 270


                  ....*....
gi 1743221413 537 QLGTDIMLD 545
Cdd:COG3621   271 ELPEEIALD 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-185 1.14e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.60  E-value: 1.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  53 IHSKDpRYGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLH 129
Cdd:COG0666   113 VNARD-KDGETPLHLAaynGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLH 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1743221413 130 LAMSKDNVEMVKALIVFGAEVDTLNDFGETPAFLASKISrlvtRKAILTLLRTVGA 185
Cdd:COG0666   192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENG----NLEIVKLLLEAGA 243
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
253-463 3.67e-22

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 97.57  E-value: 3.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 253 HLLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSR----- 327
Cdd:NF041079    2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILALALALEIPARELVELFEEHGKDIFPKRKwprrl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 328 -------PYESGPLEEFLKREFGEhTKMTDVKKPKVMLTGTLSDRQPaelHLFRnydapeTVREPRFNQNVNLRppaqps 400
Cdd:NF041079   82 lgllkkpKYSSEPLREVLEEIFGD-KTIGDLKHRVLIPAVNYTTGKP---QVFK------TPHHPDFTRDHKLK------ 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743221413 401 dqLVwRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAMTEIHEY-NQdlirkgQANKVKKLSI 463
Cdd:NF041079  146 --LV-DVALATSAAPTYFPLhefdNEQFVDGGLVANNPGLLGLHEALHFlGV------PYDDVRILSI 204
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 255-439 1.84e-21

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


Pssm-ID: 396341  Cd Length: 190  Bit Score: 92.29  E-value: 1.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 255 LCLDGGGVKGLVIIQLLIAIEKAsgvatKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRP------ 328
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEA-----GIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRkralsl 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 329 -------------YESGPLEEFLKREFGEHTKMTDVKKPKVMLTGTLSDRqpaelhlfrnydaPETVREPRFNQNVNLRP 395
Cdd:pfam01734  76 lallrgligegglFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRAL-------------LTVISTALGTRARILLP 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1743221413 396 PAQPSDQLVWRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAM 439
Cdd:pfam01734 143 DDLDDDEDLADAVLASSALPGVFPPvrldGELYVDGGLVDNVPVEAAL 190
Ank_2 pfam12796
Ankyrin repeats (3 copies);
65-154 2.96e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 2.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  65 LHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHgANADARgEHGNTPLHLAMSKDNVEMVK 141
Cdd:pfam12796   1 LHLAaknGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1743221413 142 ALIVFGAEVDTLN 154
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 59-177 5.73e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.18  E-value: 5.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  59 RYGASPLHWA-----KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIV------------------LLTHGA 115
Cdd:PHA03100  104 NNGITPLLYAiskksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILkllidkgvdinaknrvnyLLSYGV 183

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1743221413 116 NADARGEHGNTPLHLAMSKDNVEMVKALIVFGAEVDTLNDFGETPAFLASKISRLVTRKAIL 177
Cdd:PHA03100  184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 73-152 7.24e-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: 58.49  E-value: 7.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  73 MARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHG---ANADARGE--HGNTPLHLAMSKDNVEMVKALIVFG 147
Cdd:cd22192    33 IKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelVNEPMTSDlyQGETALHIAVVNQNLNLVRELIARG 112


                  ....*
gi 1743221413 148 AEVDT 152
Cdd:cd22192   113 ADVVS 117
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 123-151 1.63e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 1.63e-05
                           10        20
                   ....*....|....*....|....*....
gi 1743221413  123 HGNTPLHLAMSKDNVEMVKALIVFGAEVD 151
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 50-150 3.87e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.61  E-value: 3.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  50 SSQIHSKDPrYGASPLHWA----KNAEMARMLLKRGCNVnstsSAGNTALHVAVMR---NRFDCAIVLLTHG-------- 114
Cdd:TIGR00870  42 KLNINCPDR-LGRSALFVAaienENLELTELLLNLSCRG----AVGDTLLHAISLEyvdAVEAILLHLLAAFrksgplel 116

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1743221413 115 ANADARGE--HGNTPLHLAMSKDNVEMVKALIVFGAEV 150
Cdd:TIGR00870 117 ANDQYTSEftPGITALHLAAHRQNYEIVKLLLERGASV 154
 
Name Accession Description Interval E-value
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
 254-567 0e+00

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


Pssm-ID: 132851 [Multi-domain]  Cd Length: 312  Bit Score: 577.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 254 LLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRPYESGP 333
Cdd:cd07212     1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGSRPYNSEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 334 LEEFLKREFGEHTKMTDVKKPKVMLTGTLSDRQPAELHLFRNYDAPETVREPRFNqnVNLRPPAQPSDQLVWRAARSSGA 413
Cdd:cd07212    81 LEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEEPEKN--ANFLPPTDPAEQLLWRAARSSGA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 414 APTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAK 493
Cdd:cd07212   159 APTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKSKGRKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSNPWELAK 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743221413 494 TVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVNALWETEVYIYEHR 567
Cdd:cd07212   239 TVFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTHR 312
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
 255-563 1.77e-53

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


Pssm-ID: 132838 [Multi-domain]  Cd Length: 258  Bit Score: 182.53  E-value: 1.77e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 255 LCLDGGGVKGLVIIQLLIAIEKASGVATK--DLFDWVAGTSTGGILALAILHSK-SMAYMRGVYFRMKDEVFrgsrpyes 331
Cdd:cd07199     2 LSLDGGGIRGIIPAEILAELEKRLGKPSRiaDLFDLIAGTSTGGIIALGLALGRySAEELVELYEELGRKIF-------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 332 gpleeflkrefgehtkmtdvkkPKVMLTGTlsDRQPAELHLFRNYDAPETVREPRFnqnvnlrppaqpsdqLVWRAARSS 411
Cdd:cd07199    74 ----------------------PRVLVTAY--DLSTGKPVVFSNYDAEEPDDDDDF---------------KLWDVARAT 114

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 412 GAAPTYFRP--------NGRFLDGGLLANNPTLDAMTEiheynqdlIRKGQANKVKKLsIVVSLGTGRSPQVPVTCVDVF 483
Cdd:cd07199   115 SAAPTYFPPaviesggdEGAFVDGGVAANNPALLALAE--------ALRLLAPDKDDI-LVLSLGTGTSPSSSSSKKASR 185

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 484 RPSNPWelaktvfgAKELGKMVVDCCTDPDGRAVDRARAwCEMVGIQYFRLNPQLGTDIM-LDEVSDTVLVNALWETEVY 562
Cdd:cd07199   186 WGGLGW--------GRPLLDILMDAQSDGVDQWLDLLFG-SLDSKDNYLRINPPLPGPIPaLDDASEANLLALDSAAFEL 256


                  .
gi 1743221413 563 I 563
Cdd:cd07199   257 I 257
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 244-545 3.89e-46

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 164.31  E-value: 3.89e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 244 MRDEKRTHdhLLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVF 323
Cdd:COG3621     1 MSANKPFR--ILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAAGYSAEEILDLYEEEGKEIF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 324 RGSRP-------------YESGPLEEFLKREFGEhTKMTDVKKPkVMLTGT-LSDRQPaelHLFRNYDAPetvreprFNQ 389
Cdd:COG3621    79 PKSRWrkllslrglfgpkYDSEGLEKVLKEYFGD-TTLGDLKTP-VLIPSYdLDNGKP---VFFKSPHAK-------FDR 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 390 NVNLrppaqpsdqLVWRAARSSGAAPTYFRP---------NGRFLDGGLLANNPTLDAMTE-IHEYNQDL--IRkgqank 457
Cdd:COG3621   147 DRDF---------LLVDVARATSAAPTYFPPaqiknltgeGYALIDGGVFANNPALCALAEaLKLLGPDLddIL------ 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 458 vkklsiVVSLGTGRSPQvpvtcvdvfrpSNPWELAKTvFGAKELGKMVVDCCTDPDGRAVDrarAWCEMV-GIQYFRLNP 536
Cdd:COG3621   212 ------VLSLGTGTAPR-----------SIPYKKVKN-WGALGWLLPLIDILMDAQSDAVD---YQLRQLlGDRYYRLDP 270


                  ....*....
gi 1743221413 537 QLGTDIMLD 545
Cdd:COG3621   271 ELPEEIALD 279
Pat_PNPLA8 cd07211
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ...
 253-563 1.66e-39

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


Pssm-ID: 132850 [Multi-domain]  Cd Length: 308  Bit Score: 146.63  E-value: 1.66e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 253 HLLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILA--LAILHSkSMAYMRGVYFRMKDEVF-RGSRP- 328
Cdd:cd07211     9 RILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAflLGLKKM-SLDECEELYRKLGKDVFsQNTYIs 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 329 -----------YESGPLEEFLKREFGEHTKMTDVKK---PKVMLTGTLSDRQPAELHLFRNYDAPETVREPRFNQnvnlr 394
Cdd:cd07211    88 gtsrlvlshayYDTETWEKILKEMMGSDELIDTSADpncPKVACVSTQVNRTPLKPYVFRNYNHPPGTRSHYLGS----- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 395 ppaqpSDQLVWRAARSSGAAPTYF----RPNGRFLDGGLLANNPTLDAMTEIHEYNQDlirkgqankvKKLSIVVSLGTG 470
Cdd:cd07211   163 -----CKHKLWEAIRASSAAPGYFeefkLGNNLHQDGGLLANNPTALALHEAKLLWPD----------TPIQCLVSVGTG 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 471 RSpqvpvtcvdvfrPSNPWELAKTVFGAKELGKMVVDCCTDPDgrAVDrarawcEMV-----GIQYFRLNPQLGTDIMLD 545
Cdd:cd07211   228 RY------------PSSVRLETGGYTSLKTKLLNLIDSATDTE--RVH------TALddllpPDVYFRFNPVMSECVELD 287

                         330
                  ....*....|....*...
gi 1743221413 546 EVSDTVLVNALWETEVYI 563
Cdd:cd07211   288 ETRPEKLDQLQDDTLEYI 305
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-185 1.14e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.60  E-value: 1.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  53 IHSKDpRYGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLH 129
Cdd:COG0666   113 VNARD-KDGETPLHLAaynGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLH 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1743221413 130 LAMSKDNVEMVKALIVFGAEVDTLNDFGETPAFLASKISrlvtRKAILTLLRTVGA 185
Cdd:COG0666   192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENG----NLEIVKLLLEAGA 243
Pat17_PNPLA8_PNPLA9_like2 cd07215
Patatin-like phospholipase of bacteria; Patatin is a storage protein of the potato tuber that ...
 254-577 4.02e-29

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


Pssm-ID: 132854 [Multi-domain]  Cd Length: 329  Bit Score: 117.89  E-value: 4.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 254 LLCLDGGGVKGLVIIQLLIAIE----KASG---VATKDLFDWVAGTSTGGILALAIL-------HSKSMAYMRGVYFRMK 319
Cdd:cd07215     2 ILSIDGGGIRGIIPATILVSVEeklqKKTGnpeARLADYFDLVAGTSTGGILTCLYLcpnesgrPKFSAKEALNFYLERG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 320 DEVFRGSR-------------PYESGPLEEFLKREFGEhTKMTDVKKPKVMLTGTLSDRQPaelHLFRNYDApeTVREPR 386
Cdd:cd07215    82 NYIFKKKIwnkiksrggflneKYSHKPLEEVLLEYFGD-TKLSELLKPCLITSYDIERRSP---HFFKSHTA--IKNEQR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 387 fnqnvnlrppaqpsDQLVWRAARSSGAAPTYFRPNgRF----------LDGGLLANNPTLDAMTEiheynqdlIRKGQAN 456
Cdd:cd07215   156 --------------DFYVRDVARATSAAPTYFEPA-RIhsltgekytlIDGGVFANNPTLCAYAE--------ARKLKFE 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 457 KVKKLS----IVVSLGTGRSpqvpvtcvdvfRPSNPWELAKTvFGAKELGKMVVDCCTDPDGRAVDRARAW---CEMVGI 529
Cdd:cd07215   213 QPGKPTakdmIILSLGTGKN-----------KKSYTYEKVKD-WGLLGWAKPLIDIMMDGASQTVDYQLKQifdAEGDQQ 280

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1743221413 530 QYFRLNPQL-GTDIMLDEVSDTVLVNALWETEVYIYEHREEFQKLIQLL 577
Cdd:cd07215   281 QYLRIQPELeDADPEMDDASPENLEKLREVGQALAEDHKDQLDEIVDRL 329
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
60-185 5.90e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.59  E-value: 5.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  60 YGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDN 136
Cdd:COG0666    86 GGNTLLHAAarnGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1743221413 137 VEMVKALIVFGAEVDTLNDFGETPAFLASKISRLvtrkAILTLLRTVGA 185
Cdd:COG0666   166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHL----EIVKLLLEAGA 210
Pat17_PNPLA8_PNPLA9_like3 cd07216
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 254-546 4.05e-26

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


Pssm-ID: 132855 [Multi-domain]  Cd Length: 309  Bit Score: 108.93  E-value: 4.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 254 LLCLDGGGVKG---LVII-QLLIAIEKASGVA----TKDLFDWVAGTSTGGILALailhsksmayMRG-----------V 314
Cdd:cd07216     3 LLSLDGGGVRGlssLLILkEIMERIDPKEGLDeppkPCDYFDLIGGTSTGGLIAI----------MLGrlrmtvdecidA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 315 YFRMKDEVFRGSRPYESGPLEEFLKREFG----------------EHTKMTDVKKP---KVMLTGTLSDrQPAELHLFRN 375
Cdd:cd07216    73 YTRLAKKIFSRKRLRLIIGDLRTGARFDSkklaeaikvilkelgnDEDDLLDEGEEdgcKVFVCATDKD-VTGKAVRLRS 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 376 YDAPetvREPRFNQNVNlrppaqpsdqlVWRAARSSGAAPTYFRP------NGRFLDGGLLANNPTLDAMTEIHEYNQDL 449
Cdd:cd07216   152 YPSK---DEPSLYKNAT-----------IWEAARATSAAPTFFDPvkigpgGRTFVDGGLGANNPIREVWSEAVSLWEGL 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 450 IRkgqankvkKLSIVVSLGTGRSPQVpvtcvdVFRPSnpwelAKTVFGAKELGKMVvdccTDPDGRAVDRARAWCEMVGI 529
Cdd:cd07216   218 AR--------LVGCLVSIGTGTPSIK------SLGRS-----AEGAGLLKGLKDLV----TDTEAEAKRFSAEHSELDEE 274

                         330
                  ....*....|....*....
gi 1743221413 530 -QYFRLN-PQLGTDIMLDE 546
Cdd:cd07216   275 gRYFRFNvPHGLEDVGLDE 293
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-181 2.59e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 106.19  E-value: 2.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  53 IHSKDpRYGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLH 129
Cdd:COG0666   146 VNAQD-NDGNTPLHLAaanGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALD 224

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1743221413 130 LAMSKDNVEMVKALIVFGAEVDTLNDFGETPAFLASKISRLVTRKAILTLLR 181
Cdd:COG0666   225 LAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 255-549 1.26e-24

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


Pssm-ID: 132852 [Multi-domain]  Cd Length: 288  Bit Score: 103.91  E-value: 1.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 255 LCLDGGGVKGLVIIQLLIAIEKA--SGVATKDLFdwvAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRPYE-- 330
Cdd:cd07213     5 LSLDGGGVKGIVQLVLLKRLAEEfpSFLDQIDLF---AGTSAGSLIALGLALGYSPRQVLKLYEEVGLKVFSKSSAGGga 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 331 -------SGPLEEFLKREFGEhTKMTDVKKpKVMLTGTLSDRQPaelhlfrnydaPETVR--EPRFNQNVnlrPPAQPSD 401
Cdd:cd07213    82 gnnqyfaAGFLKAFAEVFFGD-LTLGDLKR-KVLVPSFQLDSGK-----------DDPNRrwKPKLFHNF---PGEPDLD 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 402 QLVWRAARSSGAAPTYFRPNGRFLDGGLLANNPTLDAMTEIheynqdLIRKGQANKVKKLSiVVSLGTGRSPQvPVTcvD 481
Cdd:cd07213   146 ELLVDVCLRSSAAPTYFPSYQGYVDGGVFANNPSLCAIAQA------IGEEGLNIDLKDIV-VLSLGTGRPPS-YLD--G 215

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1743221413 482 VFRPSNpWELAKTvfgAKELGKMVVdcctdpDGRaVDRARAWCEMV-GIQYFRLNPQLGTDIMLDEVSD 549
Cdd:cd07213   216 ANGYGD-WGLLQW---LPDLLDLFM------DAG-VDAADFQCRQLlGERYFRLDPVLPANIDLDDNKQ 273
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
253-463 3.67e-22

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 97.57  E-value: 3.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 253 HLLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSR----- 327
Cdd:NF041079    2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILALALALEIPARELVELFEEHGKDIFPKRKwprrl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 328 -------PYESGPLEEFLKREFGEhTKMTDVKKPKVMLTGTLSDRQPaelHLFRnydapeTVREPRFNQNVNLRppaqps 400
Cdd:NF041079   82 lgllkkpKYSSEPLREVLEEIFGD-KTIGDLKHRVLIPAVNYTTGKP---QVFK------TPHHPDFTRDHKLK------ 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743221413 401 dqLVwRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAMTEIHEY-NQdlirkgQANKVKKLSI 463
Cdd:NF041079  146 --LV-DVALATSAAPTYFPLhefdNEQFVDGGLVANNPGLLGLHEALHFlGV------PYDDVRILSI 204
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 255-439 1.84e-21

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


Pssm-ID: 396341  Cd Length: 190  Bit Score: 92.29  E-value: 1.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 255 LCLDGGGVKGLVIIQLLIAIEKAsgvatKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRP------ 328
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEA-----GIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRkralsl 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 329 -------------YESGPLEEFLKREFGEHTKMTDVKKPKVMLTGTLSDRqpaelhlfrnydaPETVREPRFNQNVNLRP 395
Cdd:pfam01734  76 lallrgligegglFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRAL-------------LTVISTALGTRARILLP 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1743221413 396 PAQPSDQLVWRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAM 439
Cdd:pfam01734 143 DDLDDDEDLADAVLASSALPGVFPPvrldGELYVDGGLVDNVPVEAAL 190
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
68-166 1.01e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 89.63  E-value: 1.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  68 AKNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMVKALIVFG 147
Cdd:COG0666    64 AGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG 143

                          90
                  ....*....|....*....
gi 1743221413 148 AEVDTLNDFGETPAFLASK 166
Cdd:COG0666   144 ADVNAQDNDGNTPLHLAAA 162
Pat17_PNPLA8_PNPLA9_like4 cd07217
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 254-538 1.07e-18

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


Pssm-ID: 132856 [Multi-domain]  Cd Length: 344  Bit Score: 87.55  E-value: 1.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 254 LLCLDGGGVKGLVIIQLLIAIEKASGVATK-------DLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVF--- 323
Cdd:cd07217     3 ILALDGGGIRGLLSVEILGRIEKDLRTHLDdpefrlgDYFDFVGGTSTGSIIAACIALGMSVTDLLSFYTLNGVNMFdka 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 324 ------RGSRPYESGPLEEFLKR--EFGEHTKMTD--VKKPKVMLTGTLSDRQPAELHlfRNYDApetvrepRFNQNVnl 393
Cdd:cd07217    83 wlaqrlFLNKLYNQYDPTNLGKKlnTVFPETTLGDdtLRTLLMIVTRNATTGSPWPVC--NNPEA-------KYNDSD-- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 394 rPPAQPSDQLVWRAARSSGAAPTYFRPN---------GRFLDGGL-LANNPTLDAMTEIHEYNQDLIRKGQANKVkklsI 463
Cdd:cd07217   152 -RSDCNLDLPLWQLVRASTAAPTFFPPEvvsiapgtaFVFVDGGVtTYNNPAFQAFLMATAKPYKLNWEVGADNL----L 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 464 VVSLGTGRSPQVpvtcVDVFRPSNPWEL--AKTV-----FGAKELGKMVV----DCctdPDGRAVDR-------ARAWCE 525
Cdd:cd07217   227 LVSVGTGFAPEA----RPDLKAADMWALdhAKYIpsalmNAANAGQDMVCrvlgEC---RKGGLVDReigtmhvDPNWLG 299

                         330
                  ....*....|...
gi 1743221413 526 MVGIQYFRLNPQL 538
Cdd:cd07217   300 PKLFTYVRYDVSL 312
Ank_2 pfam12796
Ankyrin repeats (3 copies);
65-154 2.96e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 2.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  65 LHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHgANADARgEHGNTPLHLAMSKDNVEMVK 141
Cdd:pfam12796   1 LHLAaknGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1743221413 142 ALIVFGAEVDTLN 154
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 59-177 5.73e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.18  E-value: 5.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  59 RYGASPLHWA-----KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIV------------------LLTHGA 115
Cdd:PHA03100  104 NNGITPLLYAiskksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILkllidkgvdinaknrvnyLLSYGV 183

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1743221413 116 NADARGEHGNTPLHLAMSKDNVEMVKALIVFGAEVDTLNDFGETPAFLASKISRLVTRKAIL 177
Cdd:PHA03100  184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
59-161 6.26e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 75.76  E-value: 6.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  59 RYGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKD 135
Cdd:COG0666   184 NDGETPLHLAaenGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263

                          90       100
                  ....*....|....*....|....*.
gi 1743221413 136 NVEMVKALIVFGAEVDTLNDFGETPA 161
Cdd:COG0666   264 AALIVKLLLLALLLLAAALLDLLTLL 289
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 51-151 3.22e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.22  E-value: 3.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  51 SQIHSKDPRYGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTP 127
Cdd:PHA02878  158 ADINMKDRHKGNTALHYAtenKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTP 237

                          90       100
                  ....*....|....*....|....*
gi 1743221413 128 LHLAMSK-DNVEMVKALIVFGAEVD 151
Cdd:PHA02878  238 LHISVGYcKDYDILKLLLEHGVDVN 262
PHA03095 PHA03095
ankyrin-like protein; Provisional
 59-160 8.48e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.82  E-value: 8.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  59 RYGASPLHW----AKNAEMARMLLKRGCNVNSTSSAGNTALHV--AVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAM 132
Cdd:PHA03095   81 RCGFTPLHLylynATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLL 160

                          90       100       110
                  ....*....|....*....|....*....|
gi 1743221413 133 -SKD-NVEMVKALIVFGAEVDTLNDFGETP 160
Cdd:PHA03095  161 kSRNaNVELLRLLIDAGADVYAVDDRFRSL 190
PHA03095 PHA03095
ankyrin-like protein; Provisional
 44-180 9.51e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.44  E-value: 9.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  44 MIISMDSSqIHSKDPrYGASPLH------WAKNAEMARMLLKRGCNVNSTSSAGNTALHVAVM-RNRFDCAIVLLTHGAN 116
Cdd:PHA03095   32 RLLAAGAD-VNFRGE-YGKTPLHlylhysSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYnATTLDVIKLLIKAGAD 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 117 ADARGEHGNTPLHLAMSKDNV--EMVKALIVFGAEVDTLNDFGETPA---------------FLASKISRLVTRKAIL-T 178
Cdd:PHA03095  110 VNAKDKVGRTPLHVYLSGFNInpKVIRLLLRKGADVNALDLYGMTPLavllksrnanvellrLLIDAGADVYAVDDRFrS 189


                  ..
gi 1743221413 179 LL 180
Cdd:PHA03095  190 LL 191
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 61-188 2.48e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 68.86  E-value: 2.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  61 GASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNV 137
Cdd:PHA02875  102 GMTPLHLAtilKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDI 181

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1743221413 138 EMVKALIVFGAEVDTLNDFGETPAFLAS-------KISRLVTRKAILTLLRTVGAEYC 188
Cdd:PHA02875  182 AICKMLLDSGANIDYFGKNGCVAALCYAiennkidIVRLFIKRGADCNIMFMIEGEEC 239
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 61-154 1.13e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.78  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  61 GASPLH-WAKNA---EMARMLLKRGCNVNSTSSAGNTALHVAVMRNRF-DCAIVLLTHGANADARGEHGNTPLHLAMSKD 135
Cdd:PHA02876  307 GETPLYlMAKNGydtENIRTLIMLGADVNAADRLYITPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRN 386

                          90
                  ....*....|....*....
gi 1743221413 136 NVEMVKALIVFGAEVDTLN 154
Cdd:PHA02876  387 NVVIINTLLDYGADIEALS 405
Pat17_isozyme_like cd07214
Patatin-like phospholipase of plants; Pat17 is an isozyme of patatin cloned from Solanum ...
 254-474 1.15e-11

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


Pssm-ID: 132853 [Multi-domain]  Cd Length: 349  Bit Score: 66.31  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 254 LLCLDGGGVKGLVIIQLLIAIEK------ASGVATKDLFDWVAGTSTGGILAlAIL-----HSKSMAYMRGV---YFRMK 319
Cdd:cd07214     6 VLSIDGGGIRGIIPATILEFLEGklqeldGPDARIADYFDVIAGTSTGGLIT-AMLtapneNKRPLFAAKDIvqfYLENG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 320 DEVFRGSR-PYES---------GP------LEEFLKREFGEhTKMTDVKKPKVMLTGTLSDRQPAelhLFRNYDApetVR 383
Cdd:cd07214    85 PKIFPQSTgQFEDdrkklrsllGPkydgvyLHDLLNELLGD-TRLSDTLTNVVIPTFDIKLLQPV---IFSSSKA---KN 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 384 EPRFNqnvnlrppAQPSDqlvwrAARSSGAAPTYFrPNGRF--------------LDGGLLANNPTLDAMT----EIHEY 445
Cdd:cd07214   158 DKLTN--------ARLAD-----VCISTSAAPTYF-PAHYFttedsngdirefnlVDGGVAANNPTLLAISevtkEIIKD 223

                         250       260
                  ....*....|....*....|....*....
gi 1743221413 446 NQDLIRKGQANKVKKLsiVVSLGTGRSPQ 474
Cdd:cd07214   224 NPFFASIKPLDYKKLL--VLSLGTGSAEE 250
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-166 1.86e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.98  E-value: 1.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  42 AEMIISMDSSQIHSKDPRYGASPLHWAKNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARG 121
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1743221413 122 EHGNTPLHLAMSKDNVEMVKALIVFGAEVDTLNDFGETPAFLASK 166
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAY 129
Ank_2 pfam12796
Ankyrin repeats (3 copies);
95-166 3.38e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 3.38e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1743221413  95 LHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMVKALIVFgAEVDtLNDFGETPAFLASK 166
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAAR 70
Ank_5 pfam13857
Ankyrin repeats (many copies);
77-131 6.02e-10

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 55.05  E-value: 6.02e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1743221413  77 LLKRG-CNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLA 131
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 71-180 6.07e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.82  E-value: 6.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  71 AEMARMLLKRGCNVN-STSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMVKALIVFGAE 149
Cdd:PHA02878  147 AEITKLLLSYGADINmKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1743221413 150 VDTLNDFGETPAFLASkiSRLVTRKAILTLL 180
Cdd:PHA02878  227 TDARDKCGNTPLHISV--GYCKDYDILKLLL 255
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 70-178 1.13e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.75  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  70 NAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMVKALIVFGAE 149
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                          90       100
                  ....*....|....*....|....*....
gi 1743221413 150 VDTLNDFGETPAFLASKISRLVTRKAILT 178
Cdd:PHA02874  183 ANVKDNNGESPLHNAAEYGDYACIKLLID 211
Ank_4 pfam13637
Ankyrin repeats (many copies);
91-144 2.69e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 2.69e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1743221413  91 GNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMVKALI 144
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 61-159 3.94e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 59.50  E-value: 3.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  61 GASPLHWAKN---AEMARMLLKRGCNVNSTSSAGNTALHVAVM-------------------------------RNRFDC 106
Cdd:PLN03192  558 GRTPLHIAASkgyEDCVLVLLKHACNVHIRDANGNTALWNAISakhhkifrilyhfasisdphaagdllctaakRNDLTA 637

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1743221413 107 AIVLLTHGANADARGEHGNTPLHLAMSKDNVEMVKALIVFGAEVD---TLNDFGET 159
Cdd:PLN03192  638 MKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDkanTDDDFSPT 693
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 73-152 7.24e-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: 58.49  E-value: 7.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  73 MARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHG---ANADARGE--HGNTPLHLAMSKDNVEMVKALIVFG 147
Cdd:cd22192    33 IKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelVNEPMTSDlyQGETALHIAVVNQNLNLVRELIARG 112


                  ....*
gi 1743221413 148 AEVDT 152
Cdd:cd22192   113 ADVVS 117
PHA03095 PHA03095
ankyrin-like protein; Provisional
 69-164 1.32e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.34  E-value: 1.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  69 KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIV--LLTHGANADARGEHGNTPLHLAMSKDNVEMVKALIVF 146
Cdd:PHA03095  200 PRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIAL 279

                          90
                  ....*....|....*...
gi 1743221413 147 GAEVDTLNDFGETPAFLA 164
Cdd:PHA03095  280 GADINAVSSDGNTPLSLM 297
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 65-160 1.42e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  65 LHWA-KNA--EMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMVK 141
Cdd:PHA02874  128 LHYAiKKGdlESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207

                          90
                  ....*....|....*....
gi 1743221413 142 ALIVFGAEVDTLNDFGETP 160
Cdd:PHA02874  208 LLIDHGNHIMNKCKNGFTP 226
PHA03095 PHA03095
ankyrin-like protein; Provisional
 75-160 1.48e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.34  E-value: 1.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  75 RMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCA-IV--LLTHGANADARGEHGNTPLHLAMSKDNVE-MVKALIVFGAEV 150
Cdd:PHA03095   31 RRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdIVrlLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADV 110

                          90
                  ....*....|
gi 1743221413 151 DTLNDFGETP 160
Cdd:PHA03095  111 NAKDKVGRTP 120
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 255-435 1.73e-08

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


Pssm-ID: 132846  Cd Length: 194  Bit Score: 54.59  E-value: 1.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 255 LCLDGGGVKGLVIIQLLIAIEKAsGVatkdLFDWVAGTSTGGILA--LAI-LHSKSMAY--MRGVYFRMKDE----VFRG 325
Cdd:cd07207     2 LVFEGGGAKGIAYIGALKALEEA-GI----LKKRVAGTSAGAITAalLALgYSAADIKDilKETDFAKLLDSpvglLFLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 326 SRPYESG------PLEEFLKREFGEHTKMTDVKKpkvmLTGTLSDRQPAELHLF-RNYDapeTVREPRFNQNvnlrppaQ 398
Cdd:cd07207    77 PSLFKEGglykgdALEEWLRELLKEKTGNSFATS----LLRDLDDDLGKDLKVVaTDLT---TGALVVFSAE-------T 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1743221413 399 PSDQLVWRAARSSGAAPTYFRP-----NGRFLDGGLLANNPT 435
Cdd:cd07207   143 TPDMPVAKAVRASMSIPFVFKPvrlakGDVYVDGGVLDNYPV 184
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 76-156 2.46e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.60  E-value: 2.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  76 MLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMVKALIVFGAEVDTLND 155
Cdd:PHA03100  177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256


                  .
gi 1743221413 156 F 156
Cdd:PHA03100  257 T 257
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 61-195 3.36e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 3.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  61 GASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANA-DARGEHGNTPLHLAMSKDN 136
Cdd:PHA02875   35 GISPIKLAmkfRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKK 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1743221413 137 VEMVKALIVFGAEVDTLNDFGETPAFLA------SKISRLVTRKAILTLLRTVGaeyCFPPIHGV 195
Cdd:PHA02875  115 LDIMKLLIARGADPDIPNTDKFSPLHLAvmmgdiKGIELLIDHKACLDIEDCCG---CTPLIIAM 176
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 48-166 3.77e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 56.23  E-value: 3.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  48 MDSSQIHSKDPRYgASPLHWA----KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEH 123
Cdd:PHA02876  329 MLGADVNAADRLY-ITPLHQAstldRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQK 407

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1743221413 124 GNTPLHLAMSKDNVEM-VKALIVFGAEVDTLNDFGETPAFLASK 166
Cdd:PHA02876  408 IGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACK 451
PHA03095 PHA03095
ankyrin-like protein; Provisional
 60-166 6.26e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.42  E-value: 6.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  60 YGASPLHW-----AKNAEMARMLLKRGCNVNSTSSAGNTALHV--AVMRNRFDCAIVLLTHGANADARGEHGNTPLH-LA 131
Cdd:PHA03095  151 YGMTPLAVllksrNANVELLRLLIDAGADVYAVDDRFRSLLHHhlQSFKPRARIVRELIRAGCDPAATDMLGNTPLHsMA 230

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1743221413 132 M-SKDNVEMVKALIVFGAEVDTLNDFGETPAFLASK 166
Cdd:PHA03095  231 TgSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAV 266
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 64-166 1.21e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.29  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  64 PLHWAK---NAEMARMLLKRGCNVNSTSSAGNTALH-----VAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSK- 134
Cdd:PHA03100   38 PLYLAKearNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKk 117

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1743221413 135 -DNVEMVKALIVFGAEVDTLNDFGETPAFLASK 166
Cdd:PHA03100  118 sNSYSIVEYLLDNGANVNIKNSDGENLLHLYLE 150
Ank_4 pfam13637
Ankyrin repeats (many copies);
63-111 1.93e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 1.93e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1743221413  63 SPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLL 111
Cdd:pfam13637   3 TALHAAaasGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 77-174 2.35e-07

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 53.52  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  77 LLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDN--VEMVKALIVFGAEV-DTL 153
Cdd:PHA02946   58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKInNSV 137

                          90       100
                  ....*....|....*....|.
gi 1743221413 154 NDFGETPAFLASKISRLVTRK 174
Cdd:PHA02946  138 DEEGCGPLLACTDPSERVFKK 158
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 72-193 3.80e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.14  E-value: 3.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  72 EMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAI-VLLTHGANADARGEHGNTPLHLaMSKD--NVEMVKALIVFGA 148
Cdd:PHA02876  254 ETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVpKLLERGADVNAKNIKGETPLYL-MAKNgyDTENIRTLIMLGA 332

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1743221413 149 EVDTLNDFGETPAFLASKISRlvTRKAILTLLRtVGA-----EYC-FPPIH 193
Cdd:PHA02876  333 DVNAADRLYITPLHQASTLDR--NKDIVITLLE-LGAnvnarDYCdKTPIH 380
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 74-143 5.46e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.59  E-value: 5.46e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  74 ARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMVKAL 143
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 70-159 6.47e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.56  E-value: 6.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  70 NAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPL-------H------------- 129
Cdd:PLN03192  537 NAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHhkifrilyhfasi 616

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1743221413 130 -----------LAMSKDNVEMVKALIVFGAEVDTLNDFGET 159
Cdd:PLN03192  617 sdphaagdllcTAAKRNDLTAMKELLKQGLNVDSEDHQGAT 657
Ank_5 pfam13857
Ankyrin repeats (many copies);
110-164 1.16e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 1.16e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1743221413 110 LLTHG-ANADARGEHGNTPLHLAMSKDNVEMVKALIVFGAEVDTLNDFGETPAFLA 164
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 109-164 1.26e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 1.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1743221413 109 VLLTHGANADARGEHGNTPLHLAMSKDNVEMVKALIVFGAEVDTLNDFGETPAFLA 164
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
PHA03095 PHA03095
ankyrin-like protein; Provisional
 39-106 2.55e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.02  E-value: 2.55e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743221413  39 CRCAEMIIS---MDSSQIHSKDpRYGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDC 106
Cdd:PHA03095  233 SSCKRSLVLpllIAGISINARN-RYGQTPLHYAavfNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRA 305
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 40-166 3.39e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.06  E-value: 3.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  40 RCAEMIISmDSSQIHSKDPrYGASPLHWAK---NAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFD----------- 105
Cdd:PHA02876  159 LIAEMLLE-GGADVNAKDI-YCITPIHYAAergNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDtikaiidnrsn 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 106 ------------------CAIVLLTHGANADARGEHGNTPLHLAMSKDNV-EMVKALIVFGAEVDTLNDFGETPAFLASK 166
Cdd:PHA02876  237 inkndlsllkairnedleTSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAK 316
Ank_4 pfam13637
Ankyrin repeats (many copies);
124-170 6.58e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 6.58e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1743221413 124 GNTPLHLAMSKDNVEMVKALIVFGAEVDTLNDFGETPAFLASKISRL 170
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNV 47
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 60-177 8.02e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.42  E-value: 8.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  60 YGASPLHWAK---NAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRfdCAIVLLTHGANADARGEHGNTPLHLAMSKD- 135
Cdd:PHA02874  189 NGESPLHNAAeygDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR--SAIELLINNASINDQDIDGSTPLHHAINPPc 266

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1743221413 136 NVEMVKALIVFGAEVDTLNDFGETPAFLASK-ISRLVTRKAIL 177
Cdd:PHA02874  267 DIDIIDILLYHKADISIKDNKGENPIDTAFKyINKDPVIKDII 309
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 255-438 1.51e-05

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


Pssm-ID: 132837 [Multi-domain]  Cd Length: 172  Bit Score: 45.80  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 255 LCLDGGGVKGLVIIQLLIAIEKAsGVatkdLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKdevfRGSRPYESGPL 334
Cdd:cd07198     1 LVLSGGGALGIYHVGVAKALRER-GP----LIDIIAGTSAGAIVAALLASGRDLEEALLLLLRLS----REVRLRFDGAF 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413 335 EeflkREFgehtKMTDVkkpkvmltgtlsDRQPAELHLFRNYDAPETVREPRFNQNV---NLRPPAQPSDQLVWRAARSS 411
Cdd:cd07198    72 P----PTG----RLLGI------------LRQPLLSALPDDAHEDASGKLFISLTRLtdgENVLVSDTSKGELWSAVRAS 131

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1743221413 412 GAAPTYFRP------NGRFLDGGLLANNPTLDA 438
Cdd:cd07198   132 SSIPGYFGPvplsfrGRRYGDGGLSNNLPVAEL 164
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 123-151 1.63e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 1.63e-05
                           10        20
                   ....*....|....*....|....*....
gi 1743221413  123 HGNTPLHLAMSKDNVEMVKALIVFGAEVD 151
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
59-98 1.77e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 1.77e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1743221413  59 RYGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVA 98
Cdd:pfam13857  14 GEGYTPLHVAakyGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 123-155 2.43e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.51  E-value: 2.43e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1743221413 123 HGNTPLHLA-MSKDNVEMVKALIVFGAEVDTLND 155
Cdd:pfam00023   1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 50-150 3.87e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.61  E-value: 3.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  50 SSQIHSKDPrYGASPLHWA----KNAEMARMLLKRGCNVnstsSAGNTALHVAVMR---NRFDCAIVLLTHG-------- 114
Cdd:TIGR00870  42 KLNINCPDR-LGRSALFVAaienENLELTELLLNLSCRG----AVGDTLLHAISLEyvdAVEAILLHLLAAFrksgplel 116

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1743221413 115 ANADARGE--HGNTPLHLAMSKDNVEMVKALIVFGAEV 150
Cdd:TIGR00870 117 ANDQYTSEftPGITALHLAAHRQNYEIVKLLLERGASV 154
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 45-160 4.65e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 46.44  E-value: 4.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  45 IISMDSSQIhSKDPRYGASPLHWAKNAEMARM--LLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIV--LLTHGANADAR 120
Cdd:PHA02716  270 IESLDGNKV-KNIPMILHSYITLARNIDISVVysFLQPGVKLHYKDSAGRTCLHQYILRHNISTDIIklLHEYGNDLNEP 348

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1743221413 121 GEHGNTPLHLAMSK-----------DN---VEMVKALIVFGAEVDTLNDFGETP 160
Cdd:PHA02716  349 DNIGNTVLHTYLSMlsvvnildpetDNdirLDVIQCLISLGADITAVNCLGYTP 402
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 61-132 4.95e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 4.95e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1743221413  61 GASPLHWAKNA---EMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAM 132
Cdd:PHA02874  157 GCYPIHIAIKHnffDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 123-152 5.95e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 40.32  E-value: 5.95e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1743221413 123 HGNTPLHLAMSKDNVEMVKALIVFGAEVDT 152
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 43-119 1.46e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 44.27  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  43 EMIISMDSSqIHSKDpRYGASPLH---WAKNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADA 119
Cdd:PHA03100  176 NYLLSYGVP-INIKD-VYGFTPLHyavYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA03095 PHA03095
ankyrin-like protein; Provisional
 59-144 1.78e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  59 RYGASPLHWAKNAEMARM-----LLKRGCNVNSTSSAGNTALHVA-VMRNR--FDCAIVLlthGANADARGEHGNTPLHL 130
Cdd:PHA03095  220 MLGNTPLHSMATGSSCKRslvlpLLIAGISINARNRYGQTPLHYAaVFNNPraCRRLIAL---GADINAVSSDGNTPLSL 296

                          90
                  ....*....|....
gi 1743221413 131 AMSKDNVEMVKALI 144
Cdd:PHA03095  297 MVRNNNGRAVRAAL 310
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 60-134 1.82e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  60 YGASPLHWA----KNAEMARMLLKRGCNVNSTSSA-GNTALHVAVMRNRfdCAIVLLTHGANADARGEHGNTPLHLAMSK 134
Cdd:PHA02878  233 CGNTPLHISvgycKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 51-160 2.07e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.88  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  51 SQIHSKDPRYGASPLH----WAKNA--EMARMLLKRGCNVNSTSSAGNTALHVaVMRN---RFDCAIVLLTHGANADARG 121
Cdd:PHA02859   77 ADVNFKTRDNNLSALHhylsFNKNVepEILKILIDSGSSITEEDEDGKNLLHM-YMCNfnvRINVIKLLIDSGVSFLNKD 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1743221413 122 EHGNTPLH-LAMSKDNVEMVKALIVFGAEVDTLNDFGETP 160
Cdd:PHA02859  156 FDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNC 195
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 91-119 2.26e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 2.26e-04
                           10        20
                   ....*....|....*....|....*....
gi 1743221413   91 GNTALHVAVMRNRFDCAIVLLTHGANADA 119
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 22-160 2.65e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.85  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  22 RERPSSIMLSRVTILRCCRCAEMIISMDSSQIHSKDPrYGASPLHWA---KNAEMARMLLK---RGCNVNSTSS--AGNT 93
Cdd:cd22192    13 QKRISESPLLLAAKENDVQAIKKLLKCPSCDLFQRGA-LGETALHVAalyDNLEAAVVLMEaapELVNEPMTSDlyQGET 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  94 ALHVAVMRNRFDCAIVLLTHGAN-ADAR----------------GEHgntPLHLAMSKDNVEMVKALIVFGAEVDTLNDF 156
Cdd:cd22192    92 ALHIAVVNQNLNLVRELIARGADvVSPRatgtffrpgpknliyyGEH---PLSFAACVGNEEIVRLLIEHGADIRAQDSL 168


                  ....
gi 1743221413 157 GETP 160
Cdd:cd22192   169 GNTV 172
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 91-120 3.96e-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: 38.04  E-value: 3.96e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1743221413  91 GNTALHVAVMR-NRFDCAIVLLTHGANADAR 120
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNAR 32
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 60-144 5.75e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 42.69  E-value: 5.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  60 YGASPLHWAK---NAEMARMLLKRGCNVNSTSSAGNTALHVAVMRN--RFDCAI--VLLTHGANADA------RGEHGNT 126
Cdd:cd22192   135 YGEHPLSFAAcvgNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPnkTFACQMydLILSYDKEDDLqpldlvPNNQGLT 214

                          90
                  ....*....|....*...
gi 1743221413 127 PLHLAMSKDNVEMVKALI 144
Cdd:cd22192   215 PFKLAAKEGNIVMFQHLV 232
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 70-177 8.68e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 8.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  70 NAEMARMLLKRGCNVNSTSSAGNTALHVAvMRNRFDCAI-VLLTHGANADARGEHGNTPLHLAMSKDNVEMVKALIVFGA 148
Cdd:PHA02875   14 ELDIARRLLDIGINPNFEIYDGISPIKLA-MKFRDSEAIkLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                          90       100       110
                  ....*....|....*....|....*....|
gi 1743221413 149 EV-DTLNDFGETPAFLASKISRLVTRKAIL 177
Cdd:PHA02875   93 FAdDVFYKDGMTPLHLATILKKLDIMKLLI 122
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 60-87 9.22e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 9.22e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1743221413  60 YGASPLHWA----KNAEMARMLLKRGCNVNST 87
Cdd:pfam00023   1 DGNTPLHLAagrrGNLEIVKLLLSKGADVNAR 32
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 54-168 1.04e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.16  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  54 HSKDPRYGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGN-TPLH 129
Cdd:PLN03192  615 SISDPHAAGDLLCTAakrNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDfSPTE 694

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1743221413 130 LAMSKDNVEMVKALIVFGA----EVDTLNDFGETPAFLASKIS 168
Cdd:PLN03192  695 LRELLQKRELGHSITIVDSvpadEPDLGRDGGSRPGRLQGTSS 737
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 91-119 1.17e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.47  E-value: 1.17e-03
                          10        20
                  ....*....|....*....|....*....
gi 1743221413  91 GNTALHVAVMRNRFDCAIVLLTHGANADA 119
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 34-162 1.24e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 39.80  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  34 TILRCCRCAEM--------IISMDSSQIHSKDpRYGASPLHWA-----KNAEMA-RMLLKRGCNVNSTSS-AGNTALHVA 98
Cdd:PHA02743   23 TFLRICRTGNIyelmevapFISGDGHLLHRYD-HHGRQCTHMVawydrANAVMKiELLVNMGADINARELgTGNTLLHIA 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1743221413  99 VMRNRFDCAIVLLTH-GANADARGEHGNTPLHLAMSKDNVEMVKALIVFGAEVDTLNDFGETPAF 162
Cdd:PHA02743  102 ASTKNYELAEWLCRQlGVNLGAINYQHETAYHIAYKMRDRRMMEILRANGAVCDDPLSIGLSDET 166
PHA02798 PHA02798
ankyrin-like protein; Provisional
 72-159 2.83e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.59  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  72 EMARMLLKRGCNVNSTSSAGNTAL-----HVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSK---DNVEMVKAL 143
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFM 131

                          90
                  ....*....|....*.
gi 1743221413 144 IVFGAEVDTLNDFGET 159
Cdd:PHA02798  132 IENGADTTLLDKDGFT 147
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 60-85 4.06e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 4.06e-03
                           10        20
                   ....*....|....*....|....*....
gi 1743221413   60 YGASPLHWA---KNAEMARMLLKRGCNVN 85
Cdd:smart00248   1 DGRTPLHLAaenGNLEVVKLLLDKGADIN 29
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 75-151 4.26e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 38.32  E-value: 4.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1743221413  75 RMLLKRGCNVNSTSSA-GNTALHVAVMRNRFDCAIVLLTH-GANADARGEHGNTPLHLAMSKDNVEMVKALIVFGAEVD 151
Cdd:PHA02736   75 KLLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQCK 153
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 65-150 4.44e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.05  E-value: 4.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  65 LHWA---KNAEMA-RMLLKRGCNVNSTSSAGNTALHVAVMRN-RFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVem 139
Cdd:PHA02876  412 LHFAlcgTNPYMSvKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGI-- 489

                          90
                  ....*....|.
gi 1743221413 140 VKALIVFGAEV 150
Cdd:PHA02876  490 VNILLHYGAEL 500
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 91-150 7.81e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 39.09  E-value: 7.81e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1743221413  91 GNTALHVAVMRNRFDCAIVLLTHGANADAR----------------GEHgntPLHLAMSKDNVEMVKALIVFGAEV 150
Cdd:cd21882    73 GQTALHIAIENRNLNLVRLLVENGADVSARatgrffrkspgnlfyfGEL---PLSLAACTNQEEIVRLLLENGAQP 145
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 36-139 8.32e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 39.29  E-value: 8.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743221413  36 LRCCrCAEMIISMDSSQIhskdpRYGASPLHWAK---NAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFD------- 105
Cdd:TIGR00870 156 ARAC-GDFFVKSQGVDSF-----YHGESPLNAAAclgSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKaeyeels 229

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1743221413 106 --CAIVLLTHGANADARGE-------HGNTPLHLAMSKDNVEM 139
Cdd:TIGR00870 230 cqMYNFALSLLDKLRDSKElevilnhQGLTPLKLAAKEGRIVL 272
 
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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