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Conserved domains on  [gi|52486194|ref|NP_003551|]
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85/88 kDa calcium-independent phospholipase A2 isoform a [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
480-793 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: 556.56  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 480 LLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVFRGSRPYESGP 559
Cdd:cd07212   1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGSRPYNSEP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 560 LEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRQPAELHLFRNYDAPETVREPRFNqnVNLRPPAQPSDQLVWRAARSSGA 639
Cdd:cd07212  81 LEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEEPEKN--ANFLPPTDPAEQLLWRAARSSGA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 640 APTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAK 719
Cdd:cd07212 159 APTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKSKGRKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSNPWELAK 238
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52486194 720 TVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVNALWETEVYIYEHR 793
Cdd:cd07212 239 TVFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTHR 312
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
105-407 2.63e-37

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 141.63  E-value: 2.63e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 105 EVLQHLTDLIRNHPSWSVAHLAVELGIRECFHHSRIISCANCAENEEGCTPLHLACRKGDGEILVELVQYCHTQMDVTDY 184
Cdd:COG0666   6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 185 KGETVFHYAVQGDNSQVLQLLgRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPNGYpihsamkfsq 264
Cdd:COG0666  86 GGNTLLHAAARNGDLEIVKLL-LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN---------- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 265 kgcaemiismdssqihskdprygaSPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGA 341
Cdd:COG0666 155 ------------------------TPLHLAaanGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52486194 342 NADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRLVTRKAILTLLR 407
Cdd:COG0666 211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
 
Name Accession Description Interval E-value
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
480-793 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: 556.56  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 480 LLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVFRGSRPYESGP 559
Cdd:cd07212   1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGSRPYNSEP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 560 LEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRQPAELHLFRNYDAPETVREPRFNqnVNLRPPAQPSDQLVWRAARSSGA 639
Cdd:cd07212  81 LEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEEPEKN--ANFLPPTDPAEQLLWRAARSSGA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 640 APTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAK 719
Cdd:cd07212 159 APTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKSKGRKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSNPWELAK 238
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52486194 720 TVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVNALWETEVYIYEHR 793
Cdd:cd07212 239 TVFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTHR 312
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
470-771 1.60e-39

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 148.13  E-value: 1.60e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 470 MRDEKRTHdhLLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVF 549
Cdd:COG3621   1 MSANKPFR--ILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAAGYSAEEILDLYEEEGKEIF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 550 RGSRP-------------YESGPLEEFLKREFGEhTKMTDVRKPkVMLTGT-LSDRQPaelHLFRNYDAPetvreprFNQ 615
Cdd:COG3621  79 PKSRWrkllslrglfgpkYDSEGLEKVLKEYFGD-TTLGDLKTP-VLIPSYdLDNGKP---VFFKSPHAK-------FDR 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 616 NVNLrppaqpsdqLVWRAARSSGAAPTYFRP---------NGRFLDGGLLANNPTLDAMTE-IHEYNQDL--IRkgqank 683
Cdd:COG3621 147 DRDF---------LLVDVARATSAAPTYFPPaqiknltgeGYALIDGGVFANNPALCALAEaLKLLGPDLddIL------ 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 684 vkklsiVVSLGTGRSPQvpvtcvdvfrpSNPWELAKTvFGAKELGKMVVDCCTDPDGRAVDrarAWCEMV-GIQYFRLNP 762
Cdd:COG3621 212 ------VLSLGTGTAPR-----------SIPYKKVKN-WGALGWLLPLIDILMDAQSDAVD---YQLRQLlGDRYYRLDP 270

                ....*....
gi 52486194 763 QLGTDIMLD 771
Cdd:COG3621 271 ELPEEIALD 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
105-407 2.63e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 141.63  E-value: 2.63e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 105 EVLQHLTDLIRNHPSWSVAHLAVELGIRECFHHSRIISCANCAENEEGCTPLHLACRKGDGEILVELVQYCHTQMDVTDY 184
Cdd:COG0666   6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 185 KGETVFHYAVQGDNSQVLQLLgRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPNGYpihsamkfsq 264
Cdd:COG0666  86 GGNTLLHAAARNGDLEIVKLL-LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN---------- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 265 kgcaemiismdssqihskdprygaSPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGA 341
Cdd:COG0666 155 ------------------------TPLHLAaanGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52486194 342 NADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRLVTRKAILTLLR 407
Cdd:COG0666 211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
481-665 1.19e-18

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


Pssm-ID: 396341  Cd Length: 190  Bit Score: 84.58  E-value: 1.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194   481 LCLDGGGVKGLIiiqlliaiekASGVA-----TKDLFDWVAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVFRGSRP- 554
Cdd:pfam01734   1 LVLSGGGARGAY----------HLGVLkalgeAGIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRk 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194   555 ------------------YESGPLEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRqpaelhlfrnydaPETVREPRFNQN 616
Cdd:pfam01734  71 ralsllallrgligegglFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRAL-------------LTVISTALGTRA 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 52486194   617 VNLRPPAQPSDQLVWRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAM 665
Cdd:pfam01734 138 RILLPDDLDDDEDLADAVLASSALPGVFPPvrldGELYVDGGLVDNVPVEAAL 190
Ank_2 pfam12796
Ankyrin repeats (3 copies);
291-380 1.94e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 1.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194   291 LHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHgANADARgEHGNTPLHLAMSKDNVEMIK 367
Cdd:pfam12796   1 LHLAaknGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 52486194   368 ALIVFGAEVDTPN 380
Cdd:pfam12796  79 LLLEKGADINVKD 91
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
479-689 2.96e-17

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 83.70  E-value: 2.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  479 HLLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVFRGSR----- 553
Cdd:NF041079   2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILALALALEIPARELVELFEEHGKDIFPKRKwprrl 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  554 -------PYESGPLEEFLKREFGEhTKMTDVRKPKVMLTGTLSDRQPaelHLFRnydapeTVREPRFNQNVNLRppaqps 626
Cdd:NF041079  82 lgllkkpKYSSEPLREVLEEIFGD-KTIGDLKHRVLIPAVNYTTGKP---QVFK------TPHHPDFTRDHKLK------ 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52486194  627 dqLVwRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAMTEIHEY-NQdlirkgQANKVKKLSI 689
Cdd:NF041079 146 --LV-DVALATSAAPTYFPLhefdNEQFVDGGLVANNPGLLGLHEALHFlGV------PYDDVRILSI 204
PHA03100 PHA03100
ankyrin repeat protein; Provisional
167-403 1.17e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.18  E-value: 1.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  167 ILVELVQYCHTQMDVTDYKGE---TVFHYAVQGDNSQVLQLLGRNAvAGLNQVNNQGLTPLHLACQLGK-----QEMVRV 238
Cdd:PHA03100  13 IKVKNIKYIIMEDDLNDYSYKkpvLPLYLAKEARNIDVVKILLDNG-ADINSSTKNNSTPLHYLSNIKYnltdvKEIVKL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  239 LLLCNARCNIMGPNG-YPIHSAMkfSQKGCaemiismdssqihskdprygasplhwakNAEMARMLLKRGCNVNSTSSAG 317
Cdd:PHA03100  92 LLEYGANVNAPDNNGiTPLLYAI--SKKSN----------------------------SYSIVEYLLDNGANVNIKNSDG 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  318 NTALHVAVMRNRFDCAIV------------------LLTHGANADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTP 379
Cdd:PHA03100 142 ENLLHLYLESNKIDLKILkllidkgvdinaknrvnyLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV 221
                        250       260
                 ....*....|....*....|....
gi 52486194  380 NDFGETPTFLASKIGRLVTRKAIL 403
Cdd:PHA03100 222 NKYGDTPLHIAILNNNKEIFKLLL 245
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
154-370 1.20e-10

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 65.03  E-value: 1.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 154 TPLHLACRKGDGEILVELVQYCHTQMDVTDYKGETVFHYAVQGDNSQVLQLLGRNAVAGLNQVNN----QGLTPLHLACQ 229
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVV 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 230 LGKQEMVRVLLlcnarcnimgpngypihsamkfsQKGcAEMIISMDSSQIHSKDPR----YGASPLHWAK---NAEMARM 302
Cdd:cd22192  99 NQNLNLVRELI-----------------------ARG-ADVVSPRATGTFFRPGPKnliyYGEHPLSFAAcvgNEEIVRL 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52486194 303 LLKRGCNVNSTSSAGNTALHVAVMRN--RFDCAI--VLLTHGANADA------RGEHGNTPLHLAMSKDNVEMIKALI 370
Cdd:cd22192 155 LIEHGADIRAQDSLGNTVLHILVLQPnkTFACQMydLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLV 232
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
349-377 6.75e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.26  E-value: 6.75e-05
                           10        20
                   ....*....|....*....|....*....
gi 52486194    349 HGNTPLHLAMSKDNVEMIKALIVFGAEVD 377
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
220-365 7.54e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.23  E-value: 7.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194   220 GLTPLHLACQLGKQEMVRVLLL----CNARCNimgpngypihsamkfsqkgCAEMIISMDSSQIhskdpRYGASPLHWAK 295
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLErgasVPARAC-------------------GDFFVKSQGVDSF-----YHGESPLNAAA 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194   296 ---NAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFD---------CAIVLLTHGANADARGE-------HGNTPLHL 356
Cdd:TIGR00870 184 clgSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKaeyeelscqMYNFALSLLDKLRDSKElevilnhQGLTPLKL 263

                  ....*....
gi 52486194   357 AMSKDNVEM 365
Cdd:TIGR00870 264 AAKEGRIVL 272
 
Name Accession Description Interval E-value
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
480-793 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: 556.56  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 480 LLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVFRGSRPYESGP 559
Cdd:cd07212   1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGSRPYNSEP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 560 LEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRQPAELHLFRNYDAPETVREPRFNqnVNLRPPAQPSDQLVWRAARSSGA 639
Cdd:cd07212  81 LEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEEPEKN--ANFLPPTDPAEQLLWRAARSSGA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 640 APTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAK 719
Cdd:cd07212 159 APTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKSKGRKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSNPWELAK 238
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52486194 720 TVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVNALWETEVYIYEHR 793
Cdd:cd07212 239 TVFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTHR 312
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
481-789 1.04e-45

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


Pssm-ID: 132838 [Multi-domain]  Cd Length: 258  Bit Score: 164.43  E-value: 1.04e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 481 LCLDGGGVKGLIIIQLLIAIEKASGVATK--DLFDWVAGTSTGGILALAILHSK-SMAYMRGMYFRMKDEVFrgsrpyes 557
Cdd:cd07199   2 LSLDGGGIRGIIPAEILAELEKRLGKPSRiaDLFDLIAGTSTGGIIALGLALGRySAEELVELYEELGRKIF-------- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 558 gpleeflkrefgehtkmtdvrkPKVMLTGTlsDRQPAELHLFRNYDAPETVREPRFnqnvnlrppaqpsdqLVWRAARSS 637
Cdd:cd07199  74 ----------------------PRVLVTAY--DLSTGKPVVFSNYDAEEPDDDDDF---------------KLWDVARAT 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 638 GAAPTYFRP--------NGRFLDGGLLANNPTLDAMTEiheynqdlIRKGQANKVKKLsIVVSLGTGRSPQVPVTCVDVF 709
Cdd:cd07199 115 SAAPTYFPPaviesggdEGAFVDGGVAANNPALLALAE--------ALRLLAPDKDDI-LVLSLGTGTSPSSSSSKKASR 185
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 710 RPSNPWelaktvfgAKELGKMVVDCCTDPDGRAVDRARAwCEMVGIQYFRLNPQLGTDIM-LDEVSDTVLVNALWETEVY 788
Cdd:cd07199 186 WGGLGW--------GRPLLDILMDAQSDGVDQWLDLLFG-SLDSKDNYLRINPPLPGPIPaLDDASEANLLALDSAAFEL 256

                .
gi 52486194 789 I 789
Cdd:cd07199 257 I 257
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
470-771 1.60e-39

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 148.13  E-value: 1.60e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 470 MRDEKRTHdhLLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVF 549
Cdd:COG3621   1 MSANKPFR--ILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAAGYSAEEILDLYEEEGKEIF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 550 RGSRP-------------YESGPLEEFLKREFGEhTKMTDVRKPkVMLTGT-LSDRQPaelHLFRNYDAPetvreprFNQ 615
Cdd:COG3621  79 PKSRWrkllslrglfgpkYDSEGLEKVLKEYFGD-TTLGDLKTP-VLIPSYdLDNGKP---VFFKSPHAK-------FDR 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 616 NVNLrppaqpsdqLVWRAARSSGAAPTYFRP---------NGRFLDGGLLANNPTLDAMTE-IHEYNQDL--IRkgqank 683
Cdd:COG3621 147 DRDF---------LLVDVARATSAAPTYFPPaqiknltgeGYALIDGGVFANNPALCALAEaLKLLGPDLddIL------ 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 684 vkklsiVVSLGTGRSPQvpvtcvdvfrpSNPWELAKTvFGAKELGKMVVDCCTDPDGRAVDrarAWCEMV-GIQYFRLNP 762
Cdd:COG3621 212 ------VLSLGTGTAPR-----------SIPYKKVKN-WGALGWLLPLIDILMDAQSDAVD---YQLRQLlGDRYYRLDP 270

                ....*....
gi 52486194 763 QLGTDIMLD 771
Cdd:COG3621 271 ELPEEIALD 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
105-407 2.63e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 141.63  E-value: 2.63e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 105 EVLQHLTDLIRNHPSWSVAHLAVELGIRECFHHSRIISCANCAENEEGCTPLHLACRKGDGEILVELVQYCHTQMDVTDY 184
Cdd:COG0666   6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 185 KGETVFHYAVQGDNSQVLQLLgRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPNGYpihsamkfsq 264
Cdd:COG0666  86 GGNTLLHAAARNGDLEIVKLL-LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN---------- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 265 kgcaemiismdssqihskdprygaSPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGA 341
Cdd:COG0666 155 ------------------------TPLHLAaanGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52486194 342 NADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRLVTRKAILTLLR 407
Cdd:COG0666 211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
156-411 2.66e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.85  E-value: 2.66e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 156 LHLACRKGDGEILVELVQYCHTQMDVTDYKGETVFHYAVQGDNSQVLQLLgRNAVAGLNQVNNQGLTPLHLACQLGKQEM 235
Cdd:COG0666  24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLL-LAAGADINAKDDGGNTLLHAAARNGDLEI 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 236 VRVLLLCNARCNIMGPNGYpihsamkfsqkgcaemiismdssqihskdprygaSPLHWA---KNAEMARMLLKRGCNVNS 312
Cdd:COG0666 103 VKLLLEAGADVNARDKDGE----------------------------------TPLHLAaynGNLEIVKLLLEAGADVNA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 313 TSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASK 392
Cdd:COG0666 149 QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228
                       250
                ....*....|....*....
gi 52486194 393 IGrlvtRKAILTLLRTVGA 411
Cdd:COG0666 229 NG----NLEIVKLLLEAGA 243
Pat_PNPLA8 cd07211
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ...
479-789 1.69e-33

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


Pssm-ID: 132850 [Multi-domain]  Cd Length: 308  Bit Score: 131.22  E-value: 1.69e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 479 HLLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILA--LAILHSkSMAYMRGMYFRMKDEVF-RGSRP- 554
Cdd:cd07211   9 RILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAflLGLKKM-SLDECEELYRKLGKDVFsQNTYIs 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 555 -----------YESGPLEEFLKREFGEHTKMTDVRK---PKVMLTGTLSDRQPAELHLFRNYDAPETVREPRFNQnvnlr 620
Cdd:cd07211  88 gtsrlvlshayYDTETWEKILKEMMGSDELIDTSADpncPKVACVSTQVNRTPLKPYVFRNYNHPPGTRSHYLGS----- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 621 ppaqpSDQLVWRAARSSGAAPTYF----RPNGRFLDGGLLANNPTLDAMTEIHEYNQDlirkgqankvKKLSIVVSLGTG 696
Cdd:cd07211 163 -----CKHKLWEAIRASSAAPGYFeefkLGNNLHQDGGLLANNPTALALHEAKLLWPD----------TPIQCLVSVGTG 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 697 RSpqvpvtcvdvfrPSNPWELAKTVFGAKELGKMVVDCCTDPDgrAVDrarawcEMV-----GIQYFRLNPQLGTDIMLD 771
Cdd:cd07211 228 RY------------PSSVRLETGGYTSLKTKLLNLIDSATDTE--RVH------TALddllpPDVYFRFNPVMSECVELD 287
                       330
                ....*....|....*...
gi 52486194 772 EVSDTVLVNALWETEVYI 789
Cdd:cd07211 288 ETRPEKLDQLQDDTLEYI 305
Pat17_PNPLA8_PNPLA9_like2 cd07215
Patatin-like phospholipase of bacteria; Patatin is a storage protein of the potato tuber that ...
480-803 1.84e-25

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


Pssm-ID: 132854 [Multi-domain]  Cd Length: 329  Bit Score: 108.26  E-value: 1.84e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 480 LLCLDGGGVKGLIIIQLLIAIE----KASG---VATKDLFDWVAGTSTGGILALAIL-------HSKSMAYMRGMYFRMK 545
Cdd:cd07215   2 ILSIDGGGIRGIIPATILVSVEeklqKKTGnpeARLADYFDLVAGTSTGGILTCLYLcpnesgrPKFSAKEALNFYLERG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 546 DEVFRGSR-------------PYESGPLEEFLKREFGEhTKMTDVRKPKVMLTGTLSDRQPaelHLFRNYDApeTVREPR 612
Cdd:cd07215  82 NYIFKKKIwnkiksrggflneKYSHKPLEEVLLEYFGD-TKLSELLKPCLITSYDIERRSP---HFFKSHTA--IKNEQR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 613 fnqnvnlrppaqpsDQLVWRAARSSGAAPTYFRPNgRF----------LDGGLLANNPTLDAMTEiheynqdlIRKGQAN 682
Cdd:cd07215 156 --------------DFYVRDVARATSAAPTYFEPA-RIhsltgekytlIDGGVFANNPTLCAYAE--------ARKLKFE 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 683 KVKKLS----IVVSLGTGRSpqvpvtcvdvfRPSNPWELAKTvFGAKELGKMVVDCCTDPDGRAVDRARAW---CEMVGI 755
Cdd:cd07215 213 QPGKPTakdmIILSLGTGKN-----------KKSYTYEKVKD-WGLLGWAKPLIDIMMDGASQTVDYQLKQifdAEGDQQ 280
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 52486194 756 QYFRLNPQL-GTDIMLDEVSDTVLVNALWETEVYIYEHREEFQKLIQLL 803
Cdd:cd07215 281 QYLRIQPELeDADPEMDDASPENLEKLREVGQALAEDHKDQLDEIVDRL 329
Pat17_PNPLA8_PNPLA9_like3 cd07216
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
480-772 1.90e-22

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


Pssm-ID: 132855 [Multi-domain]  Cd Length: 309  Bit Score: 98.91  E-value: 1.90e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 480 LLCLDGGGVKGLII--------IQLLIAIEKASGVATKDLFDWVAGTSTGGILALailhsksmaymrgMYFRMK---DE- 547
Cdd:cd07216   3 LLSLDGGGVRGLSSllilkeimERIDPKEGLDEPPKPCDYFDLIGGTSTGGLIAI-------------MLGRLRmtvDEc 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 548 ----------VFRGSRPYESGPLEEFLKREFG----------------EHTKMTDVRKP---KVMLTGTLSDrQPAELHL 598
Cdd:cd07216  70 idaytrlakkIFSRKRLRLIIGDLRTGARFDSkklaeaikvilkelgnDEDDLLDEGEEdgcKVFVCATDKD-VTGKAVR 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 599 FRNYDAPetvREPRFNQNVNlrppaqpsdqlVWRAARSSGAAPTYFRP------NGRFLDGGLLANNPTLDAMTEIHEYN 672
Cdd:cd07216 149 LRSYPSK---DEPSLYKNAT-----------IWEAARATSAAPTFFDPvkigpgGRTFVDGGLGANNPIREVWSEAVSLW 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 673 QDLIRkgqankvkKLSIVVSLGTGRSPQVpvtcvdVFRPSnpwelAKTVFGAKELGKMVvdccTDPDGRAVDRARAWCEM 752
Cdd:cd07216 215 EGLAR--------LVGCLVSIGTGTPSIK------SLGRS-----AEGAGLLKGLKDLV----TDTEAEAKRFSAEHSEL 271
                       330       340
                ....*....|....*....|..
gi 52486194 753 VGI-QYFRLN-PQLGTDIMLDE 772
Cdd:cd07216 272 DEEgRYFRFNvPHGLEDVGLDE 293
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
481-775 9.48e-20

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


Pssm-ID: 132852 [Multi-domain]  Cd Length: 288  Bit Score: 90.42  E-value: 9.48e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 481 LCLDGGGVKGLIIIQLLIAIEKA--SGVATKDLFdwvAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVFRGSRPYE-- 556
Cdd:cd07213   5 LSLDGGGVKGIVQLVLLKRLAEEfpSFLDQIDLF---AGTSAGSLIALGLALGYSPRQVLKLYEEVGLKVFSKSSAGGga 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 557 -------SGPLEEFLKREFGEhTKMTDVRKpKVMLTGTLSDRQPaelhlfrnydaPETVR--EPRFNQNVnlrPPAQPSD 627
Cdd:cd07213  82 gnnqyfaAGFLKAFAEVFFGD-LTLGDLKR-KVLVPSFQLDSGK-----------DDPNRrwKPKLFHNF---PGEPDLD 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 628 QLVWRAARSSGAAPTYFRPNGRFLDGGLLANNPTLDAMTEIheynqdLIRKGQANKVKKLSiVVSLGTGRSPQvPVTcvD 707
Cdd:cd07213 146 ELLVDVCLRSSAAPTYFPSYQGYVDGGVFANNPSLCAIAQA------IGEEGLNIDLKDIV-VLSLGTGRPPS-YLD--G 215
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52486194 708 VFRPSNpWELAKTvfgAKELGKMVVdcctdpDGRaVDRARAWCEMV-GIQYFRLNPQLGTDIMLDEVSD 775
Cdd:cd07213 216 ANGYGD-WGLLQW---LPDLLDLFM------DAG-VDAADFQCRQLlGERYFRLDPVLPANIDLDDNKQ 273
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
481-665 1.19e-18

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


Pssm-ID: 396341  Cd Length: 190  Bit Score: 84.58  E-value: 1.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194   481 LCLDGGGVKGLIiiqlliaiekASGVA-----TKDLFDWVAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVFRGSRP- 554
Cdd:pfam01734   1 LVLSGGGARGAY----------HLGVLkalgeAGIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRk 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194   555 ------------------YESGPLEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRqpaelhlfrnydaPETVREPRFNQN 616
Cdd:pfam01734  71 ralsllallrgligegglFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRAL-------------LTVISTALGTRA 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 52486194   617 VNLRPPAQPSDQLVWRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAM 665
Cdd:pfam01734 138 RILLPDDLDDDEDLADAVLASSALPGVFPPvrldGELYVDGGLVDNVPVEAAL 190
Ank_2 pfam12796
Ankyrin repeats (3 copies);
291-380 1.94e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 1.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194   291 LHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHgANADARgEHGNTPLHLAMSKDNVEMIK 367
Cdd:pfam12796   1 LHLAaknGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 52486194   368 ALIVFGAEVDTPN 380
Cdd:pfam12796  79 LLLEKGADINVKD 91
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
479-689 2.96e-17

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 83.70  E-value: 2.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  479 HLLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVFRGSR----- 553
Cdd:NF041079   2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILALALALEIPARELVELFEEHGKDIFPKRKwprrl 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  554 -------PYESGPLEEFLKREFGEhTKMTDVRKPKVMLTGTLSDRQPaelHLFRnydapeTVREPRFNQNVNLRppaqps 626
Cdd:NF041079  82 lgllkkpKYSSEPLREVLEEIFGD-KTIGDLKHRVLIPAVNYTTGKP---QVFK------TPHHPDFTRDHKLK------ 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52486194  627 dqLVwRAARSSGAAPTYFRP----NGRFLDGGLLANNPTLDAMTEIHEY-NQdlirkgQANKVKKLSI 689
Cdd:NF041079 146 --LV-DVALATSAAPTYFPLhefdNEQFVDGGLVANNPGLLGLHEALHFlGV------PYDDVRILSI 204
PHA03100 PHA03100
ankyrin repeat protein; Provisional
167-403 1.17e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.18  E-value: 1.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  167 ILVELVQYCHTQMDVTDYKGE---TVFHYAVQGDNSQVLQLLGRNAvAGLNQVNNQGLTPLHLACQLGK-----QEMVRV 238
Cdd:PHA03100  13 IKVKNIKYIIMEDDLNDYSYKkpvLPLYLAKEARNIDVVKILLDNG-ADINSSTKNNSTPLHYLSNIKYnltdvKEIVKL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  239 LLLCNARCNIMGPNG-YPIHSAMkfSQKGCaemiismdssqihskdprygasplhwakNAEMARMLLKRGCNVNSTSSAG 317
Cdd:PHA03100  92 LLEYGANVNAPDNNGiTPLLYAI--SKKSN----------------------------SYSIVEYLLDNGANVNIKNSDG 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  318 NTALHVAVMRNRFDCAIV------------------LLTHGANADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTP 379
Cdd:PHA03100 142 ENLLHLYLESNKIDLKILkllidkgvdinaknrvnyLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV 221
                        250       260
                 ....*....|....*....|....
gi 52486194  380 NDFGETPTFLASKIGRLVTRKAIL 403
Cdd:PHA03100 222 NKYGDTPLHIAILNNNKEIFKLLL 245
PHA02878 PHA02878
ankyrin repeat protein; Provisional
190-377 1.24e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 83.39  E-value: 1.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  190 FHYAVQGDNSQVLQ-LLGRNAvaGLNQVNNQGLTPLHLAC----QLGKQEMVRVLLLCNarcniMGPNGYPIHSAMKFSQ 264
Cdd:PHA02878  41 LHQAVEARNLDVVKsLLTRGH--NVNQPDHRDLTPLHIICkepnKLGMKEMIRSINKCS-----VFYTLVAIKDAFNNRN 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  265 KGCAEMII--------SMDSSQIHSKDPR-------------YGA-----------SPLHWA---KNAEMARMLLKRGCN 309
Cdd:PHA02878 114 VEIFKIILtnrykniqTIDLVYIDKKSKDdiieaeitklllsYGAdinmkdrhkgnTALHYAtenKDQRLTELLLSYGAN 193
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52486194  310 VNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSK-DNVEMIKALIVFGAEVD 377
Cdd:PHA02878 194 VNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVN 262
PHA02875 PHA02875
ankyrin repeat protein; Provisional
220-414 2.31e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 82.35  E-value: 2.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  220 GLTPLHLACQLGKQEMVRVLLLCNARCNIMGPN-GYPIHSAMKFSQKGCAEMIISMDS--SQIHSKDpryGASPLHWA-- 294
Cdd:PHA02875  35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDiESELHDAVEEGDVKAVEELLDLGKfaDDVFYKD---GMTPLHLAti 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  295 -KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMIKALIVFG 373
Cdd:PHA02875 112 lKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 52486194  374 AevdTPNDFGETPTFLA----------SKIGRLVTRKAILTLLRTVGAEYC 414
Cdd:PHA02875 192 A---NIDYFGKNGCVAAlcyaiennkiDIVRLFIKRGADCNIMFMIEGEEC 239
Ank_2 pfam12796
Ankyrin repeats (3 copies);
156-249 1.04e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 1.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194   156 LHLACRKGDGEILVELVQyCHTQMDVTDYKGETVFHYAVQGDNSQVLQLLGRNAVAglnQVNNQGLTPLHLACQLGKQEM 235
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEI 76
                          90
                  ....*....|....
gi 52486194   236 VRVLLLCNARCNIM 249
Cdd:pfam12796  77 VKLLLEKGADINVK 90
Pat17_PNPLA8_PNPLA9_like4 cd07217
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
480-764 1.70e-15

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


Pssm-ID: 132856 [Multi-domain]  Cd Length: 344  Bit Score: 78.69  E-value: 1.70e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 480 LLCLDGGGVKGLIIIQLLIAIEKASGVATK-------DLFDWVAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVF--- 549
Cdd:cd07217   3 ILALDGGGIRGLLSVEILGRIEKDLRTHLDdpefrlgDYFDFVGGTSTGSIIAACIALGMSVTDLLSFYTLNGVNMFdka 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 550 ------RGSRPYESGPLEEFLKR--EFGEHTKMTD--VRKPKVMLTGTLSDRQPAELHlfRNYDApetvrepRFNQNVnl 619
Cdd:cd07217  83 wlaqrlFLNKLYNQYDPTNLGKKlnTVFPETTLGDdtLRTLLMIVTRNATTGSPWPVC--NNPEA-------KYNDSD-- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 620 rPPAQPSDQLVWRAARSSGAAPTYFRPN---------GRFLDGGL-LANNPTLDAMTEIHEYNQDLIRKGQANKVkklsI 689
Cdd:cd07217 152 -RSDCNLDLPLWQLVRASTAAPTFFPPEvvsiapgtaFVFVDGGVtTYNNPAFQAFLMATAKPYKLNWEVGADNL----L 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 690 VVSLGTGRSPQVpvtcVDVFRPSNPWEL--AKTV-----FGAKELGKMVV----DCctdPDGRAVDR-------ARAWCE 751
Cdd:cd07217 227 LVSVGTGFAPEA----RPDLKAADMWALdhAKYIpsalmNAANAGQDMVCrvlgEC---RKGGLVDReigtmhvDPNWLG 299
                       330
                ....*....|...
gi 52486194 752 MVGIQYFRLNPQL 764
Cdd:cd07217 300 PKLFTYVRYDVSL 312
PHA02876 PHA02876
ankyrin repeat protein; Provisional
154-394 1.63e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.41  E-value: 1.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  154 TPLHLACRKGDGEILVELVQYcHTQMDVTDYKGETVFHYAVQGDNSQVLQLLGRNAvaglNQVNNQGLTPLHlacQLGKQ 233
Cdd:PHA02876 180 TPIHYAAERGNAKMVNLLLSY-GADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR----SNINKNDLSLLK---AIRNE 251
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  234 EMVRVLLLCNARCNIMGPNGY---PIHSAMKFSQKGCAEMIISMDSSQIHSKDPRyGASPLH-WAKNA---EMARMLLKR 306
Cdd:PHA02876 252 DLETSLLLYDAGFSVNSIDDCkntPLHHASQAPSLSRLVPKLLERGADVNAKNIK-GETPLYlMAKNGydtENIRTLIML 330
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  307 GCNVNSTSSAGNTALHVAVMRNRF-DCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTpndfget 385
Cdd:PHA02876 331 GADVNAADRLYITPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA------- 403

                 ....*....
gi 52486194  386 ptfLASKIG 394
Cdd:PHA02876 404 ---LSQKIG 409
PHA03095 PHA03095
ankyrin-like protein; Provisional
234-386 6.98e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 74.68  E-value: 6.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  234 EMVRVLLLCNARCNIMGPNGY-PIHSAMKFSQKGCAEMIISMDSSQIHSKDP-RYGASPLHW----AKNAEMARMLLKRG 307
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGEYGKtPLHLYLHYSSEKVKDIVRLLLEAGADVNAPeRCGFTPLHLylynATTLDVIKLLIKAG 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  308 CNVNSTSSAGNTALHV--AVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAM-SKD-NVEMIKALIVFGAEVDTPNDFG 383
Cdd:PHA03095 108 ADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLkSRNaNVELLRLLIDAGADVYAVDDRF 187

                 ...
gi 52486194  384 ETP 386
Cdd:PHA03095 188 RSL 190
Ank_2 pfam12796
Ankyrin repeats (3 copies);
224-346 2.70e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 2.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194   224 LHLACQLGKQEMVRVLLLCNARCNIMGPNGYpihsamkfsqkgcaemiismdssqihskdprygaSPLHWA---KNAEMA 300
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGR----------------------------------TALHLAaknGHLEIV 46
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 52486194   301 RMLLKRgCNVNSTSSaGNTALHVAVMRNRFDCAIVLLTHGANADAR 346
Cdd:pfam12796  47 KLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02875 PHA02875
ankyrin repeat protein; Provisional
151-344 3.36e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 69.25  E-value: 3.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  151 EGCTPLHLACRKGDGEILVELVQYcHTQMDVTDYKGETVFHYAV-QGDNSQVLQLLGRNAVAGlNQVNNQGLTPLHLACQ 229
Cdd:PHA02875  34 DGISPIKLAMKFRDSEAIKLLMKH-GAIPDVKYPDIESELHDAVeEGDVKAVEELLDLGKFAD-DVFYKDGMTPLHLATI 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  230 LGKQEMVRVLLLCNARCNIMGPNGY-PIHSAMKFSQKGCAEMIIsmDSSQIHSKDPRYGASPLHWA---KNAEMARMLLK 305
Cdd:PHA02875 112 LKKLDIMKLLIARGADPDIPNTDKFsPLHLAVMMGDIKGIELLI--DHKACLDIEDCCGCTPLIIAmakGDIAICKMLLD 189
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 52486194  306 RGCNVNSTSSAGN-TALHVAVMRNRFDCAIVLLTHGANAD 344
Cdd:PHA02875 190 SGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02874 PHA02874
ankyrin repeat protein; Provisional
193-386 3.82e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.22  E-value: 3.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  193 AVQGDNSQVLQLLgRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMgpngyPIHSAMKFSQKGCAEMII 272
Cdd:PHA02874  42 AIRSGDAKIVELF-IKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIL-----PIPCIEKDMIKTILDCGI 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  273 SMDSSQIHSKdprygaSPLHWA-KNA--EMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEH 349
Cdd:PHA02874 116 DVNIKDAELK------TFLHYAiKKGdlESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 52486194  350 GNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETP 386
Cdd:PHA02874 190 GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226
PHA02874 PHA02874
ankyrin repeat protein; Provisional
150-403 3.99e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.22  E-value: 3.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  150 EEGCTPLHLACRKGDGEIlVELVQYCHTQMDVTDYKGETVFHYAVQGDNSQVLQLLGRNAV------------------- 210
Cdd:PHA02874  33 DETTTPLIDAIRSGDAKI-VELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVdtsilpipciekdmiktil 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  211 ---AGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPNG-YPIHSAMKFSQKGCAEMIISmDSSQIHSKDpRY 286
Cdd:PHA02874 112 dcgIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGcYPIHIAIKHNFFDIIKLLLE-KGAYANVKD-NN 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  287 GASPLHWAK---NAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRfdCAIVLLTHGANADARGEHGNTPLHLAMSKD-N 362
Cdd:PHA02874 190 GESPLHNAAeygDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR--SAIELLINNASINDQDIDGSTPLHHAINPPcD 267
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 52486194  363 VEMIKALIVFGAEVDTPNDFGETPTFLASK-IGRLVTRKAIL 403
Cdd:PHA02874 268 IDIIDILLYHKADISIKDNKGENPIDTAFKyINKDPVIKDII 309
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
268-403 5.17e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.29  E-value: 5.17e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 268 AEMIISMDSSQIHSKDPRYGASPLHWAKNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARG 347
Cdd:COG0666   5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 52486194 348 EHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRLVTRKAIL 403
Cdd:COG0666  85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL 140
PHA02874 PHA02874
ankyrin repeat protein; Provisional
196-404 6.77e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.45  E-value: 6.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  196 GDNSQVLQLLgRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPN-GYPIHSAMKFSQKGCAEMII-- 272
Cdd:PHA02874  12 GDIEAIEKII-KNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKiPHPLLTAIKIGAHDIIKLLIdn 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  273 SMDSSQIHSKDprygasplhwaKNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNT 352
Cdd:PHA02874  91 GVDTSILPIPC-----------IEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCY 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 52486194  353 PLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRLVTRKAILT 404
Cdd:PHA02874 160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLID 211
PHA02878 PHA02878
ankyrin repeat protein; Provisional
218-360 8.60e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.37  E-value: 8.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  218 NQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGP-NGYPIHSAMKFSQKGCAEMIISMDSSqIHSKDpRYGASPLHWA-- 294
Cdd:PHA02878 166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKtNNSPLHHAVKHYNKPIVHILLENGAS-TDARD-KCGNTPLHISvg 243
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52486194  295 --KNAEMARMLLKRGCNVNSTSSA-GNTALHVAVMRNRfdCAIVLLTHGANADARGEHGNTPLHLAMSK 360
Cdd:PHA02878 244 ycKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA03095 PHA03095
ankyrin-like protein; Provisional
191-392 1.59e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.36  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  191 HYAVQGDNSQVLQLLgrNAVAGLNQVNNQGLTPLHLACQLGKQE-MVRVLLLCNARCNIMGPNGY-PIHSAM--KFSQKG 266
Cdd:PHA03095  56 HYSSEKVKDIVRLLL--EAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRtPLHVYLsgFNINPK 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  267 CAEMIISMDSSqIHSKDpRYGASPLHW-----AKNAEMARMLLKRGCNVNSTSSAGNTALHV--AVMRNRFDCAIVLLTH 339
Cdd:PHA03095 134 VIRLLLRKGAD-VNALD-LYGMTPLAVllksrNANVELLRLLIDAGADVYAVDDRFRSLLHHhlQSFKPRARIVRELIRA 211
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 52486194  340 GANADARGEHGNTPLH-LAM-SKDNVEMIKALIVFGAEVDTPNDFGETPTFLASK 392
Cdd:PHA03095 212 GCDPAATDMLGNTPLHsMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAV 266
PHA02876 PHA02876
ankyrin repeat protein; Provisional
194-419 1.72e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.78  E-value: 1.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  194 VQGDNSQVLQLLGRNAvAGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPNGYPI-HSAMKFSQKGCAEMII 272
Cdd:PHA02876 153 IQQDELLIAEMLLEGG-ADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVlECAVDSKNIDTIKAII 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  273 SmDSSQIHSKDprygASPLHWAKNA--EMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAI-VLLTHGANADARGEH 349
Cdd:PHA02876 232 D-NRSNINKND----LSLLKAIRNEdlETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVpKLLERGADVNAKNIK 306
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52486194  350 GNTPLHLaMSKD--NVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRlvTRKAILTLLRtVGA-----EYC-FPPIH 419
Cdd:PHA02876 307 GETPLYL-MAKNgyDTENIRTLIMLGADVNAADRLYITPLHQASTLDR--NKDIVITLLE-LGAnvnarDYCdKTPIH 380
PHA03095 PHA03095
ankyrin-like protein; Provisional
152-386 2.82e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.59  E-value: 2.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  152 GCTPLHLACRKGDGEILVELVQYCHTQMDVTDYKGETVFHYAVQGDN--SQVLQLLGRNAvAGLNQVNNQGLTPLHlacq 229
Cdd:PHA03095  83 GFTPLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKG-ADVNALDLYGMTPLA---- 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  230 lgkqemvrvLLLCNARCNImgpngypihsamkfsqkGCAEMIISMDSSqIHSKDPRyGASPLH-----WAKNAEMARMLL 304
Cdd:PHA03095 158 ---------VLLKSRNANV-----------------ELLRLLIDAGAD-VYAVDDR-FRSLLHhhlqsFKPRARIVRELI 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  305 KRGCNVNSTSSAGNTALHVAVMRNRFDCAIV--LLTHGANADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDF 382
Cdd:PHA03095 210 RAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSD 289

                 ....
gi 52486194  383 GETP 386
Cdd:PHA03095 290 GNTP 293
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
154-370 1.20e-10

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 65.03  E-value: 1.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 154 TPLHLACRKGDGEILVELVQYCHTQMDVTDYKGETVFHYAVQGDNSQVLQLLGRNAVAGLNQVNN----QGLTPLHLACQ 229
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVV 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 230 LGKQEMVRVLLlcnarcnimgpngypihsamkfsQKGcAEMIISMDSSQIHSKDPR----YGASPLHWAK---NAEMARM 302
Cdd:cd22192  99 NQNLNLVRELI-----------------------ARG-ADVVSPRATGTFFRPGPKnliyYGEHPLSFAAcvgNEEIVRL 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52486194 303 LLKRGCNVNSTSSAGNTALHVAVMRN--RFDCAI--VLLTHGANADA------RGEHGNTPLHLAMSKDNVEMIKALI 370
Cdd:cd22192 155 LIEHGADIRAQDSLGNTVLHILVLQPnkTFACQMydLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLV 232
Ank_2 pfam12796
Ankyrin repeats (3 copies);
321-413 1.84e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.20  E-value: 1.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194   321 LHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMIKALIVFgAEVDtPNDFGETPTFLASKIGRLvtrk 400
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHL---- 74
                          90
                  ....*....|...
gi 52486194   401 AILTLLRTVGAEY 413
Cdd:pfam12796  75 EIVKLLLEKGADI 87
PHA03100 PHA03100
ankyrin repeat protein; Provisional
153-377 9.33e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.60  E-value: 9.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  153 CTPLHLACRKGDGEILVELV-QYCHTQMDVTDYKGETVFH---YAVQGDNSQVLQLLGRNAvAGLNQVNNQGLTPLHLA- 227
Cdd:PHA03100  36 VLPLYLAKEARNIDVVKILLdNGADINSSTKNNSTPLHYLsniKYNLTDVKEIVKLLLEYG-ANVNAPDNNGITPLLYAi 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  228 -CQLGKQEMVRVLLLCNARCNIMGPNGY-PIHSAMKFS------------------QKGCAEMIISMDSSqIHSKDpRYG 287
Cdd:PHA03100 115 sKKSNSYSIVEYLLDNGANVNIKNSDGEnLLHLYLESNkidlkilkllidkgvdinAKNRVNYLLSYGVP-INIKD-VYG 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  288 ASPLH---WAKNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEH----GNTPLHlamSK 360
Cdd:PHA03100 193 FTPLHyavYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIETllyfKDKDLN---TI 269
                        250
                 ....*....|....*..
gi 52486194  361 DNVEMIKALIVFGAEVD 377
Cdd:PHA03100 270 TKIKMLKKSIMYMFLLD 286
Ank_5 pfam13857
Ankyrin repeats (many copies);
303-357 1.68e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 54.27  E-value: 1.68e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 52486194   303 LLKRG-CNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLA 357
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
287-415 2.22e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.39  E-value: 2.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  287 GASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANA-DARGEHGNTPLHLAMSKDN 362
Cdd:PHA02875  35 GISPIKLAmkfRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKK 114
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 52486194  363 VEMIKALIVFGAEVDTPNDFGETPTFLASKIGRLVTRKAILTLLRTVGAEYCF 415
Cdd:PHA02875 115 LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167
Pat17_isozyme_like cd07214
Patatin-like phospholipase of plants; Pat17 is an isozyme of patatin cloned from Solanum ...
480-700 3.25e-09

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


Pssm-ID: 132853 [Multi-domain]  Cd Length: 349  Bit Score: 59.37  E-value: 3.25e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 480 LLCLDGGGVKGLIIIQLLIAIEK------ASGVATKDLFDWVAGTSTGGILAlAILHSKSmAYMRGM---------YFRM 544
Cdd:cd07214   6 VLSIDGGGIRGIIPATILEFLEGklqeldGPDARIADYFDVIAGTSTGGLIT-AMLTAPN-ENKRPLfaakdivqfYLEN 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 545 KDEVFRGSR-PYES---------GP------LEEFLKREFGEhTKMTDVRKPKVMLTGTLSDRQPAelhLFRNYDApetV 608
Cdd:cd07214  84 GPKIFPQSTgQFEDdrkklrsllGPkydgvyLHDLLNELLGD-TRLSDTLTNVVIPTFDIKLLQPV---IFSSSKA---K 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 609 REPRFNqnvnlrppAQPSDqlvwrAARSSGAAPTYFrPNGRF--------------LDGGLLANNPTLDAMT----EIHE 670
Cdd:cd07214 157 NDKLTN--------ARLAD-----VCISTSAAPTYF-PAHYFttedsngdirefnlVDGGVAANNPTLLAISevtkEIIK 222
                       250       260       270
                ....*....|....*....|....*....|
gi 52486194 671 YNQDLIRKGQANKVKKLsiVVSLGTGRSPQ 700
Cdd:cd07214 223 DNPFFASIKPLDYKKLL--VLSLGTGSAEE 250
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
299-379 5.98e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 59.64  E-value: 5.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 299 MARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHG---ANADARGE--HGNTPLHLAMSKDNVEMIKALIVFG 373
Cdd:cd22192  33 IKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelVNEPMTSDlyQGETALHIAVVNQNLNLVRELIARG 112

                ....*.
gi 52486194 374 AEVDTP 379
Cdd:cd22192 113 ADVVSP 118
Ank_4 pfam13637
Ankyrin repeats (many copies);
317-370 7.59e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 7.59e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 52486194   317 GNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMIKALI 370
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
287-389 1.08e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.73  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  287 GASPLHWAKN---AEMARMLLKRGCNVNSTSSAGNTALHVAVM-------------------------------RNRFDC 332
Cdd:PLN03192 558 GRTPLHIAASkgyEDCVLVLLKHACNVHIRDANGNTALWNAISakhhkifrilyhfasisdphaagdllctaakRNDLTA 637
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 52486194  333 AIVLLTHGANADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGE-TPTFL 389
Cdd:PLN03192 638 MKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDfSPTEL 695
PHA02874 PHA02874
ankyrin repeat protein; Provisional
148-377 3.51e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.51  E-value: 3.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  148 ENEEGCTPLHLACRKGDGEILVELVQYcHTQMDVTDYKGETVFHYAVQGDNSQVLQLLGRNAvAGLNQVNNQGLTPLHLA 227
Cdd:PHA02874 120 KDAELKTFLHYAIKKGDLESIKMLFEY-GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLHNA 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  228 CQLGKQEMVRVLLLCNARCNIMGPNGY-PIHSAMKFSqKGCAEMIISMDSSQIHSKDpryGASPLHWAknaemarmlLKR 306
Cdd:PHA02874 198 AEYGDYACIKLLIDHGNHIMNKCKNGFtPLHNAIIHN-RSAIELLINNASINDQDID---GSTPLHHA---------INP 264
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52486194  307 GCNVnstssagntalhvavmrnrfDCAIVLLTHGANADARGEHGNTPLHLAM---SKDNVemIKALI---VFGAEVD 377
Cdd:PHA02874 265 PCDI--------------------DIIDILLYHKADISIKDNKGENPIDTAFkyiNKDPV--IKDIIanaVLIKEAD 319
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
201-386 9.67e-08

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 55.69  E-value: 9.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  201 VLQLLGRNAVaGLNQVNNQGLTPLHLACQLGK------QEMVRVLLLCNARC-NIMGPNGYPIHSAMKFSQKGCAEMIIS 273
Cdd:PHA02716 194 ILEWLCNNGV-NVNLQNNHLITPLHTYLITGNvcasviKKIIELGGDMDMKCvNGMSPIMTYIINIDNINPEITNIYIES 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  274 MDSSQIhSKDPRYGASPLHWAKNAEMARM--LLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIV--LLTHGANADARGEH 349
Cdd:PHA02716 273 LDGNKV-KNIPMILHSYITLARNIDISVVysFLQPGVKLHYKDSAGRTCLHQYILRHNISTDIIklLHEYGNDLNEPDNI 351
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 52486194  350 GNTPLHLAMSK-----------DN---VEMIKALIVFGAEVDTPNDFGETP 386
Cdd:PHA02716 352 GNTVLHTYLSMlsvvnildpetDNdirLDVIQCLISLGADITAVNCLGYTP 402
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
296-432 2.37e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.49  E-value: 2.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  296 NAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMIKALIVFgAE 375
Cdd:PLN03192 537 NAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-AS 615
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 52486194  376 VDTPNDFGETPTFlASKIGRLVTRKAILTLLRTVGAEycfpPIHGVPAEQGSAAPHH 432
Cdd:PLN03192 616 ISDPHAAGDLLCT-AAKRNDLTAMKELLKQGLNVDSE----DHQGATALQVAMAEDH 667
PHA02946 PHA02946
ankyin-like protein; Provisional
303-381 4.22e-07

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 53.13  E-value: 4.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  303 LLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDN--VEMIKALIVFGAEVDTPN 380
Cdd:PHA02946  58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNSV 137

                 .
gi 52486194  381 D 381
Cdd:PHA02946 138 D 138
Ank_4 pfam13637
Ankyrin repeats (many copies);
289-337 4.43e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 4.43e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 52486194   289 SPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLL 337
Cdd:pfam13637   3 TALHAAaasGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
335-444 1.37e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  335 VLLTHGANADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRlvtRKAILTLLRTVG---- 410
Cdd:PTZ00322 100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF---REVVQLLSRHSQchfe 176
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 52486194  411 AEYCFPP--IHGVPA--EQGSAAPHHP-FSlerAQPPPI 444
Cdd:PTZ00322 177 LGANAKPdsFTGKPPslEDSPISSHHPdFS---AVPQPM 212
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
300-369 2.18e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 2.18e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  300 ARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMIKAL 369
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PHA02876 PHA02876
ankyrin repeat protein; Provisional
154-376 2.66e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.83  E-value: 2.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  154 TPLHLACRKGDGEILVELVQYCHTQMDVTDYKGETVFHYAVQG--DNSQVLQLLGRNAvaGLNQVNNQGLTPLHLACQLG 231
Cdd:PHA02876 275 TPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNgyDTENIRTLIMLGA--DVNAADRLYITPLHQASTLD 352
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  232 K-QEMVRVLLLCNARCNIMG-PNGYPIHSAMKFSQKGCAEMIISMdSSQIHSKDPRYGASpLHWA---KNAEMA-RMLLK 305
Cdd:PHA02876 353 RnKDIVITLLELGANVNARDyCDKTPIHYAAVRNNVVIINTLLDY-GADIEALSQKIGTA-LHFAlcgTNPYMSvKTLID 430
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52486194  306 RGCNVNSTSSAGNTALHVAVMRN-RFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVemIKALIVFGAEV 376
Cdd:PHA02876 431 RGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGI--VNILLHYGAEL 500
Ank_5 pfam13857
Ankyrin repeats (many copies);
336-386 1.24e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 1.24e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 52486194   336 LLTHG-ANADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETP 386
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
Ank_4 pfam13637
Ankyrin repeats (many copies);
350-396 1.76e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 1.76e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 52486194   350 GNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRL 396
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNV 47
Ank_4 pfam13637
Ankyrin repeats (many copies);
154-205 2.02e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 2.02e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 52486194   154 TPLHLACRKGDGEILVELVQYcHTQMDVTDYKGETVFHYAVQGDNSQVLQLL 205
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLKLL 53
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
152-240 2.08e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 48.22  E-value: 2.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 152 GCTPLHLACRKGDGEILVELVQYCHTQMDVTDYKGETVFHYAVQ-GDNSQVL---------QLLGRNAVAGLNQV-NNQG 220
Cdd:cd22194 188 GETPLALAACTNQPEIVQLLMEKESTDITSQDSRGNTVLHALVTvAEDSKTQndfvkrmydMILLKSENKNLETIrNNEG 267
                        90       100
                ....*....|....*....|
gi 52486194 221 LTPLHLACQLGKQEMVRVLL 240
Cdd:cd22194 268 LTPLQLAAKMGKAEILKYIL 287
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
481-661 2.28e-05

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


Pssm-ID: 132846  Cd Length: 194  Bit Score: 46.12  E-value: 2.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 481 LCLDGGGVKGLIIIQLLIAIEKAsGVatkdLFDWVAGTSTGGILA--LAI-LHSKSMAY--MRGMYFRMKDE----VFRG 551
Cdd:cd07207   2 LVFEGGGAKGIAYIGALKALEEA-GI----LKKRVAGTSAGAITAalLALgYSAADIKDilKETDFAKLLDSpvglLFLL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 552 SRPYESG------PLEEFLKREFGEHTKMTDVRKpkvmLTGTLSDRQPAELHLF-RNYDapeTVREPRFNQNvnlrppaQ 624
Cdd:cd07207  77 PSLFKEGglykgdALEEWLRELLKEKTGNSFATS----LLRDLDDDLGKDLKVVaTDLT---TGALVVFSAE-------T 142
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 52486194 625 PSDQLVWRAARSSGAAPTYFRP-----NGRFLDGGLLANNPT 661
Cdd:cd07207 143 TPDMPVAKAVRASMSIPFVFKPvrlakGDVYVDGGVLDNYPV 184
Ank_5 pfam13857
Ankyrin repeats (many copies);
285-324 4.39e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 4.39e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 52486194   285 RYGASPLHWA---KNAEMARMLLKRGCNVNSTSSAGNTALHVA 324
Cdd:pfam13857  14 GEGYTPLHVAakyGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
511-664 6.49e-05

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


Pssm-ID: 132837 [Multi-domain]  Cd Length: 172  Bit Score: 44.25  E-value: 6.49e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 511 LFDWVAGTSTGGILALAILHSKSMAYMrgmYFRMkDEVFRGSRPYESGPLEeflkREFgehtKMTDVRKPKvmltgtLSD 590
Cdd:cd07198  26 LIDIIAGTSAGAIVAALLASGRDLEEA---LLLL-LRLSREVRLRFDGAFP----PTG----RLLGILRQP------LLS 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 591 RQPAELHLFRNYdapetvrepRFNQNVN------LRPPAQPSDQLVWRAARSSGAAPTYFRP------NGRFLDGGLLAN 658
Cdd:cd07198  88 ALPDDAHEDASG---------KLFISLTrltdgeNVLVSDTSKGELWSAVRASSSIPGYFGPvplsfrGRRYGDGGLSNN 158

                ....*.
gi 52486194 659 NPTLDA 664
Cdd:cd07198 159 LPVAEL 164
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
349-377 6.75e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.26  E-value: 6.75e-05
                           10        20
                   ....*....|....*....|....*....
gi 52486194    349 HGNTPLHLAMSKDNVEMIKALIVFGAEVD 377
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
220-365 7.54e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.23  E-value: 7.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194   220 GLTPLHLACQLGKQEMVRVLLL----CNARCNimgpngypihsamkfsqkgCAEMIISMDSSQIhskdpRYGASPLHWAK 295
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLErgasVPARAC-------------------GDFFVKSQGVDSF-----YHGESPLNAAA 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194   296 ---NAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFD---------CAIVLLTHGANADARGE-------HGNTPLHL 356
Cdd:TIGR00870 184 clgSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKaeyeelscqMYNFALSLLDKLRDSKElevilnhQGLTPLKL 263

                  ....*....
gi 52486194   357 AMSKDNVEM 365
Cdd:TIGR00870 264 AAKEGRIVL 272
PHA02859 PHA02859
ankyrin repeat protein; Provisional
255-386 9.36e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 44.42  E-value: 9.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  255 PIHSAM--KFSQKGCAEMIISmDSSQIHSKDPRYGASPLH----WAKNA--EMARMLLKRGCNVNSTSSAGNTALHVaVM 326
Cdd:PHA02859  54 PIFSCLekDKVNVEILKFLIE-NGADVNFKTRDNNLSALHhylsFNKNVepEILKILIDSGSSITEEDEDGKNLLHM-YM 131
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52486194  327 RN---RFDCAIVLLTHGANADARGEHGNTPLH-LAMSKDNVEMIKALIVFGAEVDTPNDFGETP 386
Cdd:PHA02859 132 CNfnvRINVIKLLIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNC 195
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
276-376 1.01e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 45.84  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194   276 SSQIHSKDPrYGASPLHWA----KNAEMARMLLKRGCNVnstsSAGNTALHVAVMR---NRFDCAIVLLTHG-------- 340
Cdd:TIGR00870  42 KLNINCPDR-LGRSALFVAaienENLELTELLLNLSCRG----AVGDTLLHAISLEyvdAVEAILLHLLAAFrksgplel 116
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 52486194   341 ANADARGE--HGNTPLHLAMSKDNVEMIKALIVFGAEV 376
Cdd:TIGR00870 117 ANDQYTSEftPGITALHLAAHRQNYEIVKLLLERGASV 154
Ank_2 pfam12796
Ankyrin repeats (3 copies);
103-174 1.45e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.25  E-value: 1.45e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52486194   103 HTEVLQHLTDL-----IRNHPSWSVAHLAVELGIRECFhhSRIISCANCAENEEGCTPLHLACRKGDGEILVELVQY 174
Cdd:pfam12796   9 NLELVKLLLENgadanLQDKNGRTALHLAAKNGHLEIV--KLLLEHADVNLKDNGRTALHYAARSGHLEIVKLLLEK 83
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
349-381 1.51e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 1.51e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 52486194   349 HGNTPLHLA-MSKDNVEMIKALIVFGAEVDTPND 381
Cdd:pfam00023   1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
349-378 1.73e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 1.73e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 52486194   349 HGNTPLHLAMSKDNVEMIKALIVFGAEVDT 378
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
171-227 4.21e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 4.21e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 52486194   171 LVQYCHTQMDVTDYKGETVFHYAVQGDNSQVLQLLGRNAVAgLNQVNNQGLTPLHLA 227
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD-LNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
317-345 5.80e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 5.80e-04
                           10        20
                   ....*....|....*....|....*....
gi 52486194    317 GNTALHVAVMRNRFDCAIVLLTHGANADA 345
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
317-346 9.99e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 9.99e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 52486194   317 GNTALHVAVMR-NRFDCAIVLLTHGANADAR 346
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNAR 32
PHA02743 PHA02743
Viral ankyrin protein; Provisional
271-388 1.23e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 40.57  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  271 IISMDSSQIHSKDpRYGASPLHWA-----KNAEMA-RMLLKRGCNVNSTSS-AGNTALHVAVMRNRFDCAIVLLTH-GAN 342
Cdd:PHA02743  42 FISGDGHLLHRYD-HHGRQCTHMVawydrANAVMKiELLVNMGADINARELgTGNTLLHIAASTKNYELAEWLCRQlGVN 120
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 52486194  343 ADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTF 388
Cdd:PHA02743 121 LGAINYQHETAYHIAYKMRDRRMMEILRANGAVCDDPLSIGLSDET 166
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
287-386 1.61e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.92  E-value: 1.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 287 GASPLHWA---KNAEMARMLLK---RGCNVNSTSS--AGNTALHVAVMRNRFDCAIVLLTHGAN-ADAR----------- 346
Cdd:cd22192  51 GETALHVAalyDNLEAAVVLMEaapELVNEPMTSDlyQGETALHIAVVNQNLNLVRELIARGADvVSPRatgtffrpgpk 130
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 52486194 347 -----GEHgntPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETP 386
Cdd:cd22192 131 nliyyGEH---PLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
286-313 2.38e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 2.38e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 52486194   286 YGASPLHWA----KNAEMARMLLKRGCNVNST 313
Cdd:pfam00023   1 DGNTPLHLAagrrGNLEIVKLLLSKGADVNAR 32
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
152-240 2.45e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 41.32  E-value: 2.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 152 GCTPLHLACRKGDGEILVELVQYCHTQMDV--TDYKGETVFHYAVQ-GDNSQ------------VLQLLGR-NAVAGLNQ 215
Cdd:cd22193 123 GELPLSLAACTNQPDIVQYLLENEHQPADIeaQDSRGNTVLHALVTvADNTKentkfvtrmydmILIRGAKlCPTVELEE 202
                        90       100
                ....*....|....*....|....*.
gi 52486194 216 V-NNQGLTPLHLACQLGKQEMVRVLL 240
Cdd:cd22193 203 IrNNDGLTPLQLAAKMGKIEILKYIL 228
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
219-248 2.70e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 2.70e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 52486194   219 QGLTPLHLAC-QLGKQEMVRVLLLCNARCNI 248
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNA 31
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
317-345 2.72e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.08  E-value: 2.72e-03
                          10        20
                  ....*....|....*....|....*....
gi 52486194   317 GNTALHVAVMRNRFDCAIVLLTHGANADA 345
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
149-249 2.83e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 40.74  E-value: 2.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  149 NEEGCTPLHLACRKGDGEILVELVQYCHTqMDVTDYKGETVFHYAVQGDNSQVLQLLgRNAVAGLNQVNNQG-LTPLHLA 227
Cdd:PHA02875 132 NTDKFSPLHLAVMMGDIKGIELLIDHKAC-LDIEDCCGCTPLIIAMAKGDIAICKML-LDSGANIDYFGKNGcVAALCYA 209
                         90       100
                 ....*....|....*....|..
gi 52486194  228 CQLGKQEMVRVLLLCNARCNIM 249
Cdd:PHA02875 210 IENNKIDIVRLFIKRGADCNIM 231
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
287-403 3.16e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 40.94  E-value: 3.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194 287 GASPLHWA---KNAEMARMLLKRGCNVNSTSSA--------------GNTALHVAVMRNRFDCAIVLLTH---GANADAR 346
Cdd:cd22196  94 GQTALHIAierRNMHLVELLVQNGADVHARASGeffkkkkggpgfyfGELPLSLAACTNQLDIVKFLLENphsPADISAR 173
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52486194 347 GEHGNTPLH-LAMSKDN--------VEMIKALIVFGAEV-------DTPNDFGETPTFLASKIGRLVTRKAIL 403
Cdd:cd22196 174 DSMGNTVLHaLVEVADNtpentkfvTKMYNEILILGAKIrpllkleEITNKKGLTPLKLAAKTGKIGIFAYIL 246
PHA02736 PHA02736
Viral ankyrin protein; Provisional
217-377 3.75e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 38.70  E-value: 3.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  217 NNQGLTPLHLACQLGKqemvrVLLLCNARCNIMGPNGYpihSAMKFSQKG--CAEMIISMDSSqihskDPRygasplhwa 294
Cdd:PHA02736  14 DIEGENILHYLCRNGG-----VTDLLAFKNAISDENRY---LVLEYNRHGkqCVHIVSNPDKA-----DPQ--------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  295 knaEMARMLLKRGCNVNSTSSA-GNTALHVAVMRNRFDCAIVLLTH-GANADARGEHGNTPLHLAMSKDNVEMIKALIVF 372
Cdd:PHA02736  72 ---EKLKLLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAK 148

                 ....*
gi 52486194  373 GAEVD 377
Cdd:PHA02736 149 GAQCK 153
PHA02946 PHA02946
ankyin-like protein; Provisional
214-404 7.28e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 39.65  E-value: 7.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  214 NQVNNQGLTPLHLACQLGKQEMVRVLLLCNArcnimGPNGYPIHSAMK-FSQKGCAEMIIS------MDSSQIHSKDPRY 286
Cdd:PHA02946  66 NETDDDGNYPLHIASKINNNRIVAMLLTHGA-----DPNACDKQHKTPlYYLSGTDDEVIErinllvQYGAKINNSVDEE 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486194  287 GASPLHWAKNA--EMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIV--LLTHGANADARGEHGNTPLHLAMSK-- 360
Cdd:PHA02946 141 GCGPLLACTDPseRVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKASTIswMMKLGISPSKPDHDGNTPLHIVCSKtv 220
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 52486194  361 DNVEMIKaLIVFGAEVDTPNDFGETPTFLASK-------IGRLVTRKAILT 404
Cdd:PHA02946 221 KNVDIIN-LLLPSTDVNKQNKFGDSPLTLLIKtlspahlINKLLSTSNVIT 270
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
151-174 9.84e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.49  E-value: 9.84e-03
                           10        20
                   ....*....|....*....|....
gi 52486194    151 EGCTPLHLACRKGDGEILVELVQY 174
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDK 24
 
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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