|
Name |
Accession |
Description |
Interval |
E-value |
| Pat_PNPLA9 |
cd07212 |
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ... |
747-1045 |
1.09e-158 |
|
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: 471.82 E-value: 1.09e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 747 LISMDGGGIRGLVIIQTLIAIEERLGDDIFKYFDWSAGTSTGSLIMAGLATGKSLREMQQTYLLLKDRVFDGImPPYDTV 826
Cdd:cd07212 1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGS-RPYNSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 827 QLEKFIQDQFGTGT-VWEIPYPRLMISAVNSEKLPVRLEMARNYKPAKDVA----------PETPKEMPLWMALRRSTAA 895
Cdd:cd07212 80 PLEEFLKREFGEDTkMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEepeknanflpPTDPAEQLLWRAARSSGAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 896 PVLFKPSeDRYIDGGIISNNPALDLMSEVHAYNRELQLSGRKSDAVQMNVLVSFGTGQIPSTVIETLSIDSNS----PLQ 971
Cdd:cd07212 160 PTYFRPM-GRFLDGGLIANNPTLDAMTEIHEYNKTLKSKGRKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSnpweLAK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17567809 972 SIKTIKNLAAMFIDQATASEGAPVARSRQWADSLEIPFFRFSAPLSKNIFLSSTSDLDVCTMMWDSFIYCRKHR 1045
Cdd:cd07212 239 TVFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTHR 312
|
|
| PATA |
COG3621 |
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ... |
741-1034 |
4.21e-37 |
|
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function prediction only];
Pssm-ID: 442839 [Multi-domain] Cd Length: 296 Bit Score: 141.58 E-value: 4.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 741 KKAKVNLISMDGGGIRGLVIIQTLIAIEERLGDDIFKYFDWSAGTSTGSLIMAGLATGKSLREMQQTYLLLKDRVF---- 816
Cdd:COG3621 3 ANKPFRILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAAGYSAEEILDLYEEEGKEIFpksr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 817 -------DGIMPP-YDTVQLEKFIQDQFGTGTVWEIPyPRLMISAVNseklpvrlemARNYKPA----KDVAPETPKEMP 884
Cdd:COG3621 83 wrkllslRGLFGPkYDSEGLEKVLKEYFGDTTLGDLK-TPVLIPSYD----------LDNGKPVffksPHAKFDRDRDFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 885 LWMALRRSTAAPVLFKP--------SEDRYIDGGIISNNPALdlmsevHAYNRELQLSGRKSDAVQMnvlVSFGTGqips 956
Cdd:COG3621 152 LVDVARATSAAPTYFPPaqiknltgEGYALIDGGVFANNPAL------CALAEALKLLGPDLDDILV---LSLGTG---- 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17567809 957 TVIETLSIDSNSPLQSIKTIKNLAAMFIDqatASEGAPVARSRQWADSleiPFFRFSAPLSKNIflsstSDLDVCTMM 1034
Cdd:COG3621 219 TAPRSIPYKKVKNWGALGWLLPLIDILMD---AQSDAVDYQLRQLLGD---RYYRLDPELPEEI-----ALDDNAENI 285
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
409-722 |
5.78e-26 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 109.27 E-value: 5.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 409 HTENCYPVHLALTMDRQKIVERLLELDPTLFCETDKAGNNVWHHVNSSFCAQIIWDRCPASQHFIDERNMDGQSPLNEAV 488
Cdd:COG0666 16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 489 STAKPLVATFLIGKGAKftrgdrnelfvamtsknaqsvvevvltdkpeiANERDALGNSAIHVALYKESLNA--LLnrkV 566
Cdd:COG0666 96 RNGDLEIVKLLLEAGAD--------------------------------VNARDKDGETPLHLAAYNGNLEIvkLL---L 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 567 ELGLDIDVKNNAGETALLLFITTRKPDLLPLLVtlyAHGANMNATDPHGNTALHksAAlvdAKKISLECVKFLISAGSNP 646
Cdd:COG0666 141 EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL---EAGADVNARDNDGETPLH--LA---AENGHLEIVKLLLEAGADV 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17567809 647 NKINLRGESPRHLAASLQNQEMLAILKAAGATRCPKGYKGCRSNCRHDCSSAEDEYEETLQKIRIGNESDYEKTEF 722
Cdd:COG0666 213 NAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| CBASS_lipase |
NF041079 |
CBASS cGAMP-activated phospholipase; |
745-918 |
3.14e-21 |
|
CBASS cGAMP-activated phospholipase;
Pssm-ID: 469006 [Multi-domain] Cd Length: 317 Bit Score: 96.03 E-value: 3.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 745 VNLISMDGGGIRGLVIIQTLIAIEERLGDDIFKYFDWSAGTSTGSLIMAGLATGKSLREMQQTYLLLKDRVFD------- 817
Cdd:NF041079 1 FQILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILALALALEIPARELVELFEEHGKDIFPkrkwprr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 818 --GI--MPPYDTVQLEKFIQDQFGTGTVWEIpYPRLMISAVN-SE------KLPVRLEMARNYK-PAKDVApetpkempl 885
Cdd:NF041079 81 llGLlkKPKYSSEPLREVLEEIFGDKTIGDL-KHRVLIPAVNyTTgkpqvfKTPHHPDFTRDHKlKLVDVA--------- 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 17567809 886 wMAlrrSTAAPVLFKPSE---DRYIDGGIISNNPAL 918
Cdd:NF041079 151 -LA---TSAAPTYFPLHEfdnEQFVDGGLVANNPGL 182
|
|
| Patatin |
pfam01734 |
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ... |
748-921 |
4.84e-20 |
|
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: 89.21 E-value: 4.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 748 ISMDGGGIRGLVIIQTLIAIEERLgdDIFKYFdwsAGTSTGSLIMAGLATGKSLREMQQTYLLLKDRVFDGIMPP----- 822
Cdd:pfam01734 1 LVLSGGGARGAYHLGVLKALGEAG--IRFDVI---SGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRKralsl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 823 -------------YDTVQLEKFIQDQFGTGTVWEIPYPRLMISAVNSEKLPVRLEMARNYKPAKDVAPETPKEMPLWMAL 889
Cdd:pfam01734 76 lallrgligegglFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRARILLPDDLDDDEDLADAV 155
|
170 180 190
....*....|....*....|....*....|....*
gi 17567809 890 RRSTAAPVLFKPSE---DRYIDGGIISNNPALDLM 921
Cdd:pfam01734 156 LASSALPGVFPPVRldgELYVDGGLVDNVPVEAAL 190
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
495-677 |
5.92e-12 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 69.28 E-value: 5.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 495 VATFLIGKGAKFTRGD---RNELFVAMTSKNAQ-SVVEVVLTDKPEIaNERDALGNSAIHVALykESLNA---LLNRKVE 567
Cdd:PHA03095 99 VIKLLIKAGADVNAKDkvgRTPLHVYLSGFNINpKVIRLLLRKGADV-NALDLYGMTPLAVLL--KSRNAnveLLRLLID 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 568 LGLDIDVKNNAGETALLLFITTRKPDLlPLLVTLYAHGANMNATDPHGNTALHkSAALVDAKKISLecVKFLISAGSNPN 647
Cdd:PHA03095 176 AGADVYAVDDRFRSLLHHHLQSFKPRA-RIVRELIRAGCDPAATDMLGNTPLH-SMATGSSCKRSL--VLPLLIAGISIN 251
|
170 180 190
....*....|....*....|....*....|
gi 17567809 648 KINLRGESPRHLAASLQNQEMLAILKAAGA 677
Cdd:PHA03095 252 ARNRYGQTPLHYAAVFNNPRACRRLIALGA 281
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
549-650 |
5.57e-07 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 48.57 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 549 IHVALYKESLNaLLNRKVELGLDIDVKNNAGETALLLFITTRKPDLLPLLVTlyahGANMNATDpHGNTALHkSAALVDa 628
Cdd:pfam12796 1 LHLAAKNGNLE-LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE----HADVNLKD-NGRTALH-YAARSG- 72
|
90 100
....*....|....*....|..
gi 17567809 629 kkiSLECVKFLISAGSNPNKIN 650
Cdd:pfam12796 73 ---HLEIVKLLLEKGADINVKD 91
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
520-674 |
1.04e-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: 46.23 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 520 SKNAQSVVEVVL---------TDKPEIANERDA----LGNSAIHVALYKESLN---ALLNRkvelGLDIDVKNNA----- 578
Cdd:TIGR00870 90 SLEYVDAVEAILlhllaafrkSGPLELANDQYTseftPGITALHLAAHRQNYEivkLLLER----GASVPARACGdffvk 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 579 ---------GETALLLFITTRKPDLLPLLVTlyaHGANMNATDPHGNTALHKSA----ALVDAKKISLECVKFLISAGSN 645
Cdd:TIGR00870 166 sqgvdsfyhGESPLNAAACLGSPSIVALLSE---DPADILTADSLGNTLLHLLVmeneFKAEYEELSCQMYNFALSLLDK 242
|
170 180 190
....*....|....*....|....*....|....*.
gi 17567809 646 PNK-------INLRGESPRHLAASLQNQEMLAILKA 674
Cdd:TIGR00870 243 LRDskeleviLNHQGLTPLKLAAKEGRIVLFRLKLA 278
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
581-677 |
4.11e-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: 41.15 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 581 TALLLFITTRKPDLLPLLVTLYAHGANMNATDPHGNTALHkSAALVDakkiSLECVKFLISAGsnPNKINL-------RG 653
Cdd:cd22192 17 SESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALH-VAALYD----NLEAAVVLMEAA--PELVNEpmtsdlyQG 89
|
90 100
....*....|....*....|....
gi 17567809 654 ESPRHLAASLQNQEMLAILKAAGA 677
Cdd:cd22192 90 ETALHIAVVNQNLNLVRELIARGA 113
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Pat_PNPLA9 |
cd07212 |
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ... |
747-1045 |
1.09e-158 |
|
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: 471.82 E-value: 1.09e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 747 LISMDGGGIRGLVIIQTLIAIEERLGDDIFKYFDWSAGTSTGSLIMAGLATGKSLREMQQTYLLLKDRVFDGImPPYDTV 826
Cdd:cd07212 1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGS-RPYNSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 827 QLEKFIQDQFGTGT-VWEIPYPRLMISAVNSEKLPVRLEMARNYKPAKDVA----------PETPKEMPLWMALRRSTAA 895
Cdd:cd07212 80 PLEEFLKREFGEDTkMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEepeknanflpPTDPAEQLLWRAARSSGAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 896 PVLFKPSeDRYIDGGIISNNPALDLMSEVHAYNRELQLSGRKSDAVQMNVLVSFGTGQIPSTVIETLSIDSNS----PLQ 971
Cdd:cd07212 160 PTYFRPM-GRFLDGGLIANNPTLDAMTEIHEYNKTLKSKGRKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSnpweLAK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17567809 972 SIKTIKNLAAMFIDQATASEGAPVARSRQWADSLEIPFFRFSAPLSKNIFLSSTSDLDVCTMMWDSFIYCRKHR 1045
Cdd:cd07212 239 TVFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTHR 312
|
|
| PATA |
COG3621 |
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ... |
741-1034 |
4.21e-37 |
|
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function prediction only];
Pssm-ID: 442839 [Multi-domain] Cd Length: 296 Bit Score: 141.58 E-value: 4.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 741 KKAKVNLISMDGGGIRGLVIIQTLIAIEERLGDDIFKYFDWSAGTSTGSLIMAGLATGKSLREMQQTYLLLKDRVF---- 816
Cdd:COG3621 3 ANKPFRILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAAGYSAEEILDLYEEEGKEIFpksr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 817 -------DGIMPP-YDTVQLEKFIQDQFGTGTVWEIPyPRLMISAVNseklpvrlemARNYKPA----KDVAPETPKEMP 884
Cdd:COG3621 83 wrkllslRGLFGPkYDSEGLEKVLKEYFGDTTLGDLK-TPVLIPSYD----------LDNGKPVffksPHAKFDRDRDFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 885 LWMALRRSTAAPVLFKP--------SEDRYIDGGIISNNPALdlmsevHAYNRELQLSGRKSDAVQMnvlVSFGTGqips 956
Cdd:COG3621 152 LVDVARATSAAPTYFPPaqiknltgEGYALIDGGVFANNPAL------CALAEALKLLGPDLDDILV---LSLGTG---- 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17567809 957 TVIETLSIDSNSPLQSIKTIKNLAAMFIDqatASEGAPVARSRQWADSleiPFFRFSAPLSKNIflsstSDLDVCTMM 1034
Cdd:COG3621 219 TAPRSIPYKKVKNWGALGWLLPLIDILMD---AQSDAVDYQLRQLLGD---RYYRLDPELPEEI-----ALDDNAENI 285
|
|
| Pat17_PNPLA8_PNPLA9_like |
cd07199 |
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ... |
749-1020 |
1.12e-33 |
|
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: 130.53 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 749 SMDGGGIRGLVIIQTLIAIEERLGDD--IFKYFDWSAGTSTGSLIMAGLATGK-SLREMQQTYLLLKDRVFdgimppydt 825
Cdd:cd07199 3 SLDGGGIRGIIPAEILAELEKRLGKPsrIADLFDLIAGTSTGGIIALGLALGRySAEELVELYEELGRKIF--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 826 vqlekfiqdqfgtgtvweipyPRLMISAVNSEKLpvRLEMARNYKPAKDVApetPKEMPLWMALRRSTAAPVLFKP---- 901
Cdd:cd07199 74 ---------------------PRVLVTAYDLSTG--KPVVFSNYDAEEPDD---DDDFKLWDVARATSAAPTYFPPavie 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 902 ---SEDRYIDGGIISNNPALDLMSEVhaynRELQLSGRKSDavqmnVLVSFGTGQIPSTVietLSIDSNSPLQSIKTIKN 978
Cdd:cd07199 128 sggDEGAFVDGGVAANNPALLALAEA----LRLLAPDKDDI-----LVLSLGTGTSPSSS---SSKKASRWGGLGWGRPL 195
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 17567809 979 LAAMFIDQATASEGApvARSRQWADSLEIPFFRFSAPLSKNI 1020
Cdd:cd07199 196 LDILMDAQSDGVDQW--LDLLFGSLDSKDNYLRINPPLPGPI 235
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
409-722 |
5.78e-26 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 109.27 E-value: 5.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 409 HTENCYPVHLALTMDRQKIVERLLELDPTLFCETDKAGNNVWHHVNSSFCAQIIWDRCPASQHFIDERNMDGQSPLNEAV 488
Cdd:COG0666 16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 489 STAKPLVATFLIGKGAKftrgdrnelfvamtsknaqsvvevvltdkpeiANERDALGNSAIHVALYKESLNA--LLnrkV 566
Cdd:COG0666 96 RNGDLEIVKLLLEAGAD--------------------------------VNARDKDGETPLHLAAYNGNLEIvkLL---L 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 567 ELGLDIDVKNNAGETALLLFITTRKPDLLPLLVtlyAHGANMNATDPHGNTALHksAAlvdAKKISLECVKFLISAGSNP 646
Cdd:COG0666 141 EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL---EAGADVNARDNDGETPLH--LA---AENGHLEIVKLLLEAGADV 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17567809 647 NKINLRGESPRHLAASLQNQEMLAILKAAGATRCPKGYKGCRSNCRHDCSSAEDEYEETLQKIRIGNESDYEKTEF 722
Cdd:COG0666 213 NAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| Pat_PNPLA8 |
cd07211 |
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ... |
738-993 |
3.25e-24 |
|
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: 104.64 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 738 RRGKKAKVNLISMDGGGIRGLVIIQTLIAIEERLGDDIFKYFDWSAGTSTGSLIMAGLA-TGKSLREMQQTYLLLKDRVF 816
Cdd:cd07211 1 PPVKGRGIRILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAFLLGlKKMSLDECEELYRKLGKDVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 817 DGIMPP------------YDTVQLEKFIQDQFGTGTVWEI----PYPRLMISAVNSEKLPVRLEMARNYKPAKDVAPETP 880
Cdd:cd07211 81 SQNTYIsgtsrlvlshayYDTETWEKILKEMMGSDELIDTsadpNCPKVACVSTQVNRTPLKPYVFRNYNHPPGTRSHYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 881 K--EMPLWMALRRSTAAPV---LFKPSEDRYIDGGIISNNP-ALDLmsevhaynRELQLSGRKsdaVQMNVLVSFGTGQI 954
Cdd:cd07211 161 GscKHKLWEAIRASSAAPGyfeEFKLGNNLHQDGGLLANNPtALAL--------HEAKLLWPD---TPIQCLVSVGTGRY 229
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 17567809 955 PSTVIETLSIDSnsplqSIKT-IKNLaamfIDQATASEGA 993
Cdd:cd07211 230 PSSVRLETGGYT-----SLKTkLLNL----IDSATDTERV 260
|
|
| CBASS_lipase |
NF041079 |
CBASS cGAMP-activated phospholipase; |
745-918 |
3.14e-21 |
|
CBASS cGAMP-activated phospholipase;
Pssm-ID: 469006 [Multi-domain] Cd Length: 317 Bit Score: 96.03 E-value: 3.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 745 VNLISMDGGGIRGLVIIQTLIAIEERLGDDIFKYFDWSAGTSTGSLIMAGLATGKSLREMQQTYLLLKDRVFD------- 817
Cdd:NF041079 1 FQILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILALALALEIPARELVELFEEHGKDIFPkrkwprr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 818 --GI--MPPYDTVQLEKFIQDQFGTGTVWEIpYPRLMISAVN-SE------KLPVRLEMARNYK-PAKDVApetpkempl 885
Cdd:NF041079 81 llGLlkKPKYSSEPLREVLEEIFGDKTIGDL-KHRVLIPAVNyTTgkpqvfKTPHHPDFTRDHKlKLVDVA--------- 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 17567809 886 wMAlrrSTAAPVLFKPSE---DRYIDGGIISNNPAL 918
Cdd:NF041079 151 -LA---TSAAPTYFPLHEfdnEQFVDGGLVANNPGL 182
|
|
| Patatin |
pfam01734 |
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ... |
748-921 |
4.84e-20 |
|
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: 89.21 E-value: 4.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 748 ISMDGGGIRGLVIIQTLIAIEERLgdDIFKYFdwsAGTSTGSLIMAGLATGKSLREMQQTYLLLKDRVFDGIMPP----- 822
Cdd:pfam01734 1 LVLSGGGARGAYHLGVLKALGEAG--IRFDVI---SGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRKralsl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 823 -------------YDTVQLEKFIQDQFGTGTVWEIPYPRLMISAVNSEKLPVRLEMARNYKPAKDVAPETPKEMPLWMAL 889
Cdd:pfam01734 76 lallrgligegglFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRARILLPDDLDDDEDLADAV 155
|
170 180 190
....*....|....*....|....*....|....*
gi 17567809 890 RRSTAAPVLFKPSE---DRYIDGGIISNNPALDLM 921
Cdd:pfam01734 156 LASSALPGVFPPVRldgELYVDGGLVDNVPVEAAL 190
|
|
| Pat17_PNPLA8_PNPLA9_like4 |
cd07217 |
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ... |
747-955 |
5.23e-18 |
|
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes subfamily of PNPLA8 (iPLA2-gamma) and PNPLA9 (iPLA2-beta) like phospholipases from human as well as the Pat17 isozyme from Solanum cardiophyllum.
Pssm-ID: 132856 [Multi-domain] Cd Length: 344 Bit Score: 86.78 E-value: 5.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 747 LISMDGGGIRGLVIIQTLIAIEE-----------RLGDdifkYFDWSAGTSTGSLIMAGLATGKSLREMQQTYLLLKDRV 815
Cdd:cd07217 3 ILALDGGGIRGLLSVEILGRIEKdlrthlddpefRLGD----YFDFVGGTSTGSIIAACIALGMSVTDLLSFYTLNGVNM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 816 FDG-----------IMPPYDTVQLEKFIQDQFGTGTVWEiPYPR--LMISAVNSEKLPVRLemARNYKPAK--DVAPETP 880
Cdd:cd07217 79 FDKawlaqrlflnkLYNQYDPTNLGKKLNTVFPETTLGD-DTLRtlLMIVTRNATTGSPWP--VCNNPEAKynDSDRSDC 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 881 K-EMPLWMALRRSTAAPVLFKP--------SEDRYIDGGIIS-NNPALD--LMSEVHAYNrelqlSGRKSDAVQMnVLVS 948
Cdd:cd07217 156 NlDLPLWQLVRASTAAPTFFPPevvsiapgTAFVFVDGGVTTyNNPAFQafLMATAKPYK-----LNWEVGADNL-LLVS 229
|
....*..
gi 17567809 949 FGTGQIP 955
Cdd:cd07217 230 VGTGFAP 236
|
|
| Pat17_PNPLA8_PNPLA9_like2 |
cd07215 |
Patatin-like phospholipase of bacteria; Patatin is a storage protein of the potato tuber that ... |
747-952 |
9.35e-18 |
|
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: 85.92 E-value: 9.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 747 LISMDGGGIRGLVIIQTLIAIEERL----GD---DIFKYFDWSAGTSTGSLIMAG-LATGKSLR------EMQQTYLLLK 812
Cdd:cd07215 2 ILSIDGGGIRGIIPATILVSVEEKLqkktGNpeaRLADYFDLVAGTSTGGILTCLyLCPNESGRpkfsakEALNFYLERG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 813 DRVFD-----------GIM-PPYDTVQLEKFIQDQFGTGTVWEIPYPRLMISAVNSEKLPV-------RLEMARNYKpAK 873
Cdd:cd07215 82 NYIFKkkiwnkiksrgGFLnEKYSHKPLEEVLLEYFGDTKLSELLKPCLITSYDIERRSPHffkshtaIKNEQRDFY-VR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 874 DVApetpkemplwmalRRSTAAPVLFKPS------EDRY--IDGGIISNNPALDLMSEVhaynRELQLSGRKSDAVQMNV 945
Cdd:cd07215 161 DVA-------------RATSAAPTYFEPArihsltGEKYtlIDGGVFANNPTLCAYAEA----RKLKFEQPGKPTAKDMI 223
|
....*..
gi 17567809 946 LVSFGTG 952
Cdd:cd07215 224 ILSLGTG 230
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
494-677 |
3.42e-17 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 83.46 E-value: 3.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 494 LVATFLIGKGAKFTRGDRNELFVAMTSKNAQSVVEVVLTDKPEIANERDALGNSAIHVALYKESLNALLNRKVELGLDID 573
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 574 VKNNAGETALLLFITTRKPDLLPLLVtlyAHGANMNATDPHGNTALHKSAalvdaKKISLECVKFLISAGSNPNKINLRG 653
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLL---EAGADVNARDKDGETPLHLAA-----YNGNLEIVKLLLEAGADVNAQDNDG 153
|
170 180
....*....|....*....|....
gi 17567809 654 ESPRHLAASLQNQEMLAILKAAGA 677
Cdd:COG0666 154 NTPLHLAAANGNLEIVKLLLEAGA 177
|
|
| Pat17_PNPLA8_PNPLA9_like1 |
cd07213 |
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ... |
748-1046 |
5.20e-16 |
|
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: 79.64 E-value: 5.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 748 ISMDGGGIRGLVIIQTLiaieERLGDDIFKYF---DWSAGTSTGSLIMAGLATGKSLREMQQTYLLLKDRVFDGIMPPY- 823
Cdd:cd07213 5 LSLDGGGVKGIVQLVLL----KRLAEEFPSFLdqiDLFAGTSAGSLIALGLALGYSPRQVLKLYEEVGLKVFSKSSAGGg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 824 -------DTVQLEKFIQDQFGTGTVWEIPYpRLMISAV---NSEKLPVRLEMAR---NYKPAKDVapetpkEMPLWMALR 890
Cdd:cd07213 81 agnnqyfAAGFLKAFAEVFFGDLTLGDLKR-KVLVPSFqldSGKDDPNRRWKPKlfhNFPGEPDL------DELLVDVCL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 891 RSTAAPVLFkPSEDRYIDGGIISNNPALDLMSevhaynrelQLSGRKSDAVQMN--VLVSFGTGQIPSTVietlsIDSNS 968
Cdd:cd07213 154 RSSAAPTYF-PSYQGYVDGGVFANNPSLCAIA---------QAIGEEGLNIDLKdiVVLSLGTGRPPSYL-----DGANG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 969 PLQ--SIKTIKNLAAMFIDqATAS----EGAPVARSRqwadsleipFFRFSAPLSKNIflsstsDLDVCTMMwDSFIYCR 1042
Cdd:cd07213 219 YGDwgLLQWLPDLLDLFMD-AGVDaadfQCRQLLGER---------YFRLDPVLPANI------DLDDNKQI-EELVEIA 281
|
....
gi 17567809 1043 KHRD 1046
Cdd:cd07213 282 NTVD 285
|
|
| Pat17_PNPLA8_PNPLA9_like3 |
cd07216 |
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ... |
745-953 |
9.03e-16 |
|
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: 79.27 E-value: 9.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 745 VNLISMDGGGIRG---LVIIQTL-IAIEERLGDD-IFK---YFDWSAGTSTGSL--IMAGlatgkSLReMQ-----QTYL 809
Cdd:cd07216 1 LNLLSLDGGGVRGlssLLILKEImERIDPKEGLDePPKpcdYFDLIGGTSTGGLiaIMLG-----RLR-MTvdeciDAYT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 810 LLKDRVF-----------DGIMPPYDTVQLE---KFIQDQFG---TGTVWEIPYPR------LMISAVNSEklPVRLema 866
Cdd:cd07216 75 RLAKKIFsrkrlrliigdLRTGARFDSKKLAeaiKVILKELGndeDDLLDEGEEDGckvfvcATDKDVTGK--AVRL--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 867 RNYKPAKDVAPEtpKEMPLWMALRRSTAAPVLFKP-----SEDRYIDGGIISNNPALDLMSEVHAYNRELqlsgrksdAV 941
Cdd:cd07216 150 RSYPSKDEPSLY--KNATIWEAARATSAAPTFFDPvkigpGGRTFVDGGLGANNPIREVWSEAVSLWEGL--------AR 219
|
250
....*....|..
gi 17567809 942 QMNVLVSFGTGQ 953
Cdd:cd07216 220 LVGCLVSIGTGT 231
|
|
| Pat17_isozyme_like |
cd07214 |
Patatin-like phospholipase of plants; Pat17 is an isozyme of patatin cloned from Solanum ... |
744-954 |
1.91e-13 |
|
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: 72.85 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 744 KVNLISMDGGGIRGLVIIQTLIAIEERL----GDD--IFKYFDWSAGTSTGSLIMAGLAT-GKSLREM------------ 804
Cdd:cd07214 3 FITVLSIDGGGIRGIIPATILEFLEGKLqeldGPDarIADYFDVIAGTSTGGLITAMLTApNENKRPLfaakdivqfyle 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 805 -------QQTYLLLKDRVFDGIM--PPYDTVQLEKFIQDQFGTGTVWEIPYPrLMISAVNSEKL-PVrleMARNYKPAKD 874
Cdd:cd07214 83 ngpkifpQSTGQFEDDRKKLRSLlgPKYDGVYLHDLLNELLGDTRLSDTLTN-VVIPTFDIKLLqPV---IFSSSKAKND 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 875 VApetpKEMPLWMALRRSTAAPVLFKP----SEDR--------YIDGGIISNNPALDLMSEVhayNRELQLSGRKSDAVQ 942
Cdd:cd07214 159 KL----TNARLADVCISTSAAPTYFPAhyftTEDSngdirefnLVDGGVAANNPTLLAISEV---TKEIIKDNPFFASIK 231
|
250
....*....|....*..
gi 17567809 943 M----NVLV-SFGTGQI 954
Cdd:cd07214 232 PldykKLLVlSLGTGSA 248
|
|
| RssA |
COG1752 |
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ... |
752-926 |
6.95e-13 |
|
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function prediction only];
Pssm-ID: 441358 [Multi-domain] Cd Length: 261 Bit Score: 69.93 E-value: 6.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 752 GGGIRGLVIIQTLIAIEERlgdDIfkYFDWSAGTSTGSLIMAGLATGKSLREMQQTYL-LLKDRVFDGIMP--------- 821
Cdd:COG1752 13 GGGARGAAHIGVLKALEEA---GI--PPDVIAGTSAGAIVGALYAAGYSADELEELWRsLDRRDLFDLSLPrrllrldlg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 822 -----PYDTVQLEKFIQDQFGTGTVWEIPyPRLMISAVNseklpvrLEMARnykpakdvaPETPKEMPLWMALRRSTAAP 896
Cdd:COG1752 88 lspggLLDGDPLRRLLERLLGDRDFEDLP-IPLAVVATD-------LETGR---------EVVFDSGPLADAVRASAAIP 150
|
170 180 190
....*....|....*....|....*....|...
gi 17567809 897 VLFKPSE---DRYIDGGIiSNNPALDLMSEVHA 926
Cdd:COG1752 151 GVFPPVEidgRLYVDGGV-VNNLPVDPARALGA 182
|
|
| Pat_ExoU_VipD_like |
cd07207 |
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ... |
748-917 |
8.11e-13 |
|
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: 68.07 E-value: 8.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 748 ISMDGGGIRGLVIIQTLIAIEERlgdDIFKY-FdwsAGTSTGSLIMAGLATGKSLREMQQtylLLKDRVFDGIMPPYDTV 826
Cdd:cd07207 2 LVFEGGGAKGIAYIGALKALEEA---GILKKrV---AGTSAGAITAALLALGYSAADIKD---ILKETDFAKLLDSPVGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 827 Q-----------------LEKFIQDQFGtgtvweipypRLMISAVNSEKLPVrlEMARNYKPAKDVA------------P 877
Cdd:cd07207 73 LfllpslfkegglykgdaLEEWLRELLK----------EKTGNSFATSLLRD--LDDDLGKDLKVVAtdlttgalvvfsA 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17567809 878 ETPKEMPLWMALRRSTAAPVLFKP----SEDRYIDGGIISNNPA 917
Cdd:cd07207 141 ETTPDMPVAKAVRASMSIPFVFKPvrlaKGDVYVDGGVLDNYPV 184
|
|
| Pat_PNPLA6_PNPLA7_NTE1_like |
cd07205 |
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ... |
752-926 |
2.02e-12 |
|
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; Patatin-like phospholipase domain containing protein 6 (PNPLA6) and protein 7 (PNPLA7) are included in this family. PNPLA6 is commonly known as Neuropathy Target Esterase (NTE). NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. PNPLA7 is an insulin-regulated phospholipase that is homologus to Neuropathy Target Esterase (NTE or PNPLA6) and is also known as NTE-related esterase (NRE). Human NRE is predominantly expressed in prostate, white adipose, and pancreatic tissue. NRE hydrolyzes sn-1 esters in lysophosphatidylcholine and lysophosphatidic acid, but shows no lipase activity with substrates like triacylglycerols (TG), cholesteryl esters, retinyl esters (RE), phosphatidylcholine (PC), or monoacylglycerol (MG). This family includes subfamily of PNPLA6 (NTE) and PNPLA7 (NRE)-like phospholipases.
Pssm-ID: 132844 [Multi-domain] Cd Length: 175 Bit Score: 66.42 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 752 GGGIRGLVIIQTLIAIEERlgdDIfkYFDWSAGTSTGSLIMAGLATGKSLREMQQTYLLLKDRVFDGIMPPYDTVQL--- 828
Cdd:cd07205 7 GGGARGLAHIGVLKALEEA---GI--PIDIVSGTSAGAIVGALYAAGYSPEEIEERAKLRSTDLKALSDLTIPTAGLlrg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 829 ---EKFIQDQFGtgtvweipyprlmisAVNSEKLPVRLemarnYKPAKDVAPETPK---EMPLWMALRRSTAAPVLFKPS 902
Cdd:cd07205 82 dkfLELLDEYFG---------------DRDIEDLWIPF-----FIVATDLTSGKLVvfrSGSLVRAVRASMSIPGIFPPV 141
|
170 180
....*....|....*....|....*..
gi 17567809 903 ED---RYIDGGIISNNPAlDLMSEVHA 926
Cdd:cd07205 142 KIdgqLLVDGGVLNNLPV-DVLRELGA 167
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
495-677 |
5.92e-12 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 69.28 E-value: 5.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 495 VATFLIGKGAKFTRGD---RNELFVAMTSKNAQ-SVVEVVLTDKPEIaNERDALGNSAIHVALykESLNA---LLNRKVE 567
Cdd:PHA03095 99 VIKLLIKAGADVNAKDkvgRTPLHVYLSGFNINpKVIRLLLRKGADV-NALDLYGMTPLAVLL--KSRNAnveLLRLLID 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 568 LGLDIDVKNNAGETALLLFITTRKPDLlPLLVTLYAHGANMNATDPHGNTALHkSAALVDAKKISLecVKFLISAGSNPN 647
Cdd:PHA03095 176 AGADVYAVDDRFRSLLHHHLQSFKPRA-RIVRELIRAGCDPAATDMLGNTPLH-SMATGSSCKRSL--VLPLLIAGISIN 251
|
170 180 190
....*....|....*....|....*....|
gi 17567809 648 KINLRGESPRHLAASLQNQEMLAILKAAGA 677
Cdd:PHA03095 252 ARNRYGQTPLHYAAVFNNPRACRRLIALGA 281
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
465-678 |
2.30e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 67.00 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 465 RCPASQHFIDERNMDGQSPLNEAVSTAKPLVATFLIGKGAKFTRGDRNEL----FVAMTSKNAQSVVEVV--LTDKPEIA 538
Cdd:PHA03100 20 YIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNStplhYLSNIKYNLTDVKEIVklLLEYGANV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 539 NERDALGNSAIHVALYKES-----LNALLNRkvelGLDIDVKNNAGETALLLFITTRKPDLlPLLVTLYAHGANMNA--- 610
Cdd:PHA03100 100 NAPDNNGITPLLYAISKKSnsysiVEYLLDN----GANVNIKNSDGENLLHLYLESNKIDL-KILKLLIDKGVDINAknr 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 611 -------------TDPHGNTALHKSAalvdaKKISLECVKFLISAGSNPNKINLRGESPRHLAASLQNQEMLAILKAAGA 677
Cdd:PHA03100 175 vnyllsygvpiniKDVYGFTPLHYAV-----YNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
|
.
gi 17567809 678 T 678
Cdd:PHA03100 250 S 250
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
510-677 |
1.10e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 59.31 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 510 DRNELFVAMTSKNAQSVVEVVLTDKPEIANERDALGNSAIHVALYKESLNALLNRKVELGLDIDVKNNAGETAllLFITT 589
Cdd:PHA02876 238 NKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETP--LYLMA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 590 RKPDLLPLLVTLYAHGANMNATDPHGNTALHKSAALVDAKKIslecVKFLISAGSNPNKINLRGESPRHLAASLQNQEML 669
Cdd:PHA02876 316 KNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDI----VITLLELGANVNARDYCDKTPIHYAAVRNNVVII 391
|
....*...
gi 17567809 670 AILKAAGA 677
Cdd:PHA02876 392 NTLLDYGA 399
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
549-650 |
5.57e-07 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 48.57 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 549 IHVALYKESLNaLLNRKVELGLDIDVKNNAGETALLLFITTRKPDLLPLLVTlyahGANMNATDpHGNTALHkSAALVDa 628
Cdd:pfam12796 1 LHLAAKNGNLE-LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE----HADVNLKD-NGRTALH-YAARSG- 72
|
90 100
....*....|....*....|..
gi 17567809 629 kkiSLECVKFLISAGSNPNKIN 650
Cdd:pfam12796 73 ---HLEIVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
595-677 |
1.28e-06 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 47.42 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 595 LPLLVTLYAHGANMNATDPHGNTALHKSaalvdAKKISLECVKFLISagSNPNKINLRGESPRHLAASLQNQEMLAILKA 674
Cdd:pfam12796 10 LELVKLLLENGADANLQDKNGRTALHLA-----AKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVKLLLE 82
|
...
gi 17567809 675 AGA 677
Cdd:pfam12796 83 KGA 85
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
539-672 |
6.45e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 49.96 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 539 NERDALGNSAIHVALYK---ESLNALLnrkvELGLDIDVKNNAGETALLLFITTRKPDLLPLLVTlyaHGANMNATDPHG 615
Cdd:PHA02874 118 NIKDAELKTFLHYAIKKgdlESIKMLF----EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE---KGAYANVKDNNG 190
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 17567809 616 NTALHKSAALVDAKkisleCVKFLISAGSN-PNKINlRGESPRHlAASLQNQEMLAIL 672
Cdd:PHA02874 191 ESPLHNAAEYGDYA-----CIKLLIDHGNHiMNKCK-NGFTPLH-NAIIHNRSAIELL 241
|
|
| Pat_hypo_Ecoli_Z1214_like |
cd07209 |
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ... |
752-920 |
2.19e-05 |
|
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase similar to Z1214 protein of Escherichia coli. This family predominantly consists of bacterial patatin glycoproteins and some representatives from eukaryotes and archaea. 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 a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates.
Pssm-ID: 132848 [Multi-domain] Cd Length: 215 Bit Score: 46.90 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 752 GGGIRGLVIIQTLIAIEERlgddiFKYFDWSAGTSTGSLIMAGLATGKSLReMQQTYlllkdRVFDGIMPPydTVQLEKF 831
Cdd:cd07209 5 GGGALGAYQAGVLKALAEA-----GIEPDIISGTSIGAINGALIAGGDPEA-VERLE-----KLWRELSRE--DVFLRGL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 832 IQDQ--FGTGTVWEIPYPRLMISAVNSEK-LPVRLEmarnykpakdvapETPKE-MPLW-MAlrrSTAAPVLFKPSE--- 903
Cdd:cd07209 72 LDRAldFDTLRLLAILFAGLVIVAVNVLTgEPVYFD-------------DIPDGiLPEHlLA---SAALPPFFPPVEidg 135
|
170 180
....*....|....*....|
gi 17567809 904 DRYIDGGIISN---NPALDL 920
Cdd:cd07209 136 RYYWDGGVVDNtplSPAIDL 155
|
|
| Pat_NTE_like_bacteria |
cd07228 |
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ... |
748-917 |
2.42e-05 |
|
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like phospholipase domain containing protein 6. PNPLA6 is commonly known as Neuropathy Target Esterase (NTE). NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. This group includes YCHK and rssA from Escherichia coli as well as Ylbk from Bacillus amyloliquefaciens.
Pssm-ID: 132866 [Multi-domain] Cd Length: 175 Bit Score: 46.11 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 748 ISMDGGGIRGLVIIQTLIAIEERlGDDIfkyfDWSAGTSTGSLIMAGLATGKSLREM-------QQTYLLLKDRVF--DG 818
Cdd:cd07228 3 LALGSGGARGWAHIGVLRALEEE-GIEI----DIIAGSSIGALVGALYAAGHLDALEewvrslsQRDVLRLLDLSAsrSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 819 ImppydtVQLEKFIQdqfgtgtvweipYPRLMISAVNSEKLPVRLemarnYKPAKDVapETPKEM-----PLWMALRRST 893
Cdd:cd07228 78 L------LKGEKVLE------------YLREIMGGVTIEELPIPF-----AAVATDL--QTGKEVwfregSLIDAIRASI 132
|
170 180
....*....|....*....|....*..
gi 17567809 894 AAPVLFKPSEDR---YIDGGIISNNPA 917
Cdd:cd07228 133 SIPGIFAPVEHNgrlLVDGGVVNPIPV 159
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
473-677 |
5.69e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 47.37 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 473 IDERNMDGQSPL---------NEAVSTakplvatfLIGKGAKFTRGDR---NELFVAMTSKNAQSVVeVVLTDKPEIANE 540
Cdd:PHA02876 300 VNAKNIKGETPLylmakngydTENIRT--------LIMLGADVNAADRlyiTPLHQASTLDRNKDIV-ITLLELGANVNA 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 541 RDALGNSAIHVALYKESLnALLNRKVELGLDIDVKNNAGETALLLFITTRKPDLLplLVTLYAHGANMNATDPHGNTALH 620
Cdd:PHA02876 371 RDYCDKTPIHYAAVRNNV-VIINTLLDYGADIEALSQKIGTALHFALCGTNPYMS--VKTLIDRGANVNSKNKDLSTPLH 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17567809 621 KSAalvdAKKISLECVKFLISAGSNPNKINLRGESPrhLAASLQNQEMLAILKAAGA 677
Cdd:PHA02876 448 YAC----KKNCKLDVIEMLLDNGADVNAINIQNQYP--LLIALEYHGIVNILLHYGA 498
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
483-677 |
6.82e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 46.80 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 483 PLNEAVSTAKPLVATFLIGKGAKFTRGDRNELF---VAMTSKNAQSVVEVVltdkpEIANERDaLGNSaihvalYKESLN 559
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTplhIICKEPNKLGMKEMI-----RSINKCS-VFYT------LVAIKD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 560 ALLNRKVELG--LDIDVKNNAGETALLLFITTRKPDLLPLLVT--LYAHGANMNATDPH-GNTALHKSAALVDAKkisle 634
Cdd:PHA02878 108 AFNNRNVEIFkiILTNRYKNIQTIDLVYIDKKSKDDIIEAEITklLLSYGADINMKDRHkGNTALHYATENKDQR----- 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17567809 635 CVKFLISAGSNPNKINLRGESPRHLAASLQNQEMLAILKAAGA 677
Cdd:PHA02878 183 LTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
538-677 |
1.03e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 46.17 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 538 ANERDALGNSAIhVALYKESLNA------LLNRKVELGLDIDVKNNAGETALLLFITTRKPDLLPLLVTLYAHGANMNAT 611
Cdd:PHA03095 1 DEEDESVDIIME-AALYDYLLNAsnvtveEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEAGADVNAP 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17567809 612 DPHGNTALHksaaLVDAKKISLECVKFLISAGSNPNKINLRGESPRHLAASLQN--QEMLAILKAAGA 677
Cdd:PHA03095 80 ERCGFTPLH----LYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGA 143
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
520-674 |
1.04e-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: 46.23 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 520 SKNAQSVVEVVL---------TDKPEIANERDA----LGNSAIHVALYKESLN---ALLNRkvelGLDIDVKNNA----- 578
Cdd:TIGR00870 90 SLEYVDAVEAILlhllaafrkSGPLELANDQYTseftPGITALHLAAHRQNYEivkLLLER----GASVPARACGdffvk 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 579 ---------GETALLLFITTRKPDLLPLLVTlyaHGANMNATDPHGNTALHKSA----ALVDAKKISLECVKFLISAGSN 645
Cdd:TIGR00870 166 sqgvdsfyhGESPLNAAACLGSPSIVALLSE---DPADILTADSLGNTLLHLLVmeneFKAEYEELSCQMYNFALSLLDK 242
|
170 180 190
....*....|....*....|....*....|....*.
gi 17567809 646 PNK-------INLRGESPRHLAASLQNQEMLAILKA 674
Cdd:TIGR00870 243 LRDskeleviLNHQGLTPLKLAAKEGRIVLFRLKLA 278
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
475-628 |
1.04e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 46.17 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 475 ERNMDGQSPLNEAVSTAKPLVAT--FLIGKGAK-FTRGDR-NELF--VAMTSKNAQSVVEVvLTDKPEIANERDALGNSA 548
Cdd:PHA03095 147 ALDLYGMTPLAVLLKSRNANVELlrLLIDAGADvYAVDDRfRSLLhhHLQSFKPRARIVRE-LIRAGCDPAATDMLGNTP 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 549 IHVALYKESLNALLNRK-VELGLDIDVKNNAGETALLLFITTRKPDLLPLLVTLyahGANMNATDPHGNTAL-----HKS 622
Cdd:PHA03095 226 LHSMATGSSCKRSLVLPlLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIAL---GADINAVSSDGNTPLslmvrNNN 302
|
....*.
gi 17567809 623 AALVDA 628
Cdd:PHA03095 303 GRAVRA 308
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
632-672 |
1.69e-04 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 41.64 E-value: 1.69e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 17567809 632 SLECVKFLISAGSNPNKINLRGESPRHLAASLQNQEMLAIL 672
Cdd:pfam12796 9 NLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
601-660 |
8.25e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.48 E-value: 8.25e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 601 LYAHGANMNATDPHGNTALHKSAalvdaKKISLECVKFLISAGSNPNKINLRGESPRHLA 660
Cdd:pfam13857 2 LEHGPIDLNRLDGEGYTPLHVAA-----KYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
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| Pat_hypo_W_succinogenes_WS1459_like |
cd07210 |
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ... |
783-926 |
1.03e-03 |
|
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. This family predominantly consists of bacterial patatin glycoproteins. 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 a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates.
Pssm-ID: 132849 [Multi-domain] Cd Length: 221 Bit Score: 41.95 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 783 AGTSTGSLIMAGLATGKSLREMQQTYLLLKDRVFDGI---MPPYDTVQLEKFIQ---DQFGTGTVWEIPYPrLMISAVNs 856
Cdd:cd07210 33 SGTSAGALVGGLFASGISPDEMAELLLSLERKDFWMFwdpPLRGGLLSGDRFAAllrEHLPPDRFEELRIP-LAVSVVD- 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17567809 857 eklpvrlemarnykpAKDVAPETPKEMPLWMALRRSTAAPVLFKPSE---DRYIDGGIISNNPALDLMSEVHA 926
Cdd:cd07210 111 ---------------LTSRETLLLSEGDLAEAVAASCAVPPLFQPVEiggRPFVDGGVADRLPFDALRPEIER 168
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|
| Patatin_and_cPLA2 |
cd01819 |
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ... |
748-797 |
1.07e-03 |
|
Patatins and Phospholipases; 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 a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates. This family also includes the catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms.
Pssm-ID: 132836 [Multi-domain] Cd Length: 155 Bit Score: 40.86 E-value: 1.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 17567809 748 ISMDGGGIRGLVIIQTLIAIEERLGDDIFKYFdwsAGTSTGSLIMAGLAT 797
Cdd:cd01819 1 LSFSGGGFRGMYHAGVLSALAERGLLDCVTYL---AGTSGGAWVAATLYP 47
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|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
614-650 |
1.24e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 37.27 E-value: 1.24e-03
10 20 30
....*....|....*....|....*....|....*..
gi 17567809 614 HGNTALHKSAALVDakkiSLECVKFLISAGSNPNKIN 650
Cdd:pfam00023 1 DGNTPLHLAAGRRG----NLEIVKLLLSKGADVNARD 33
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|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
595-640 |
3.44e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 36.48 E-value: 3.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 17567809 595 LPLLVTLYAHGANMNATDPHGNTALHKSaalvdAKKISLECVKFLI 640
Cdd:pfam13637 14 LELLRLLLEKGADINAVDGNGETALHFA-----ASNGNVEVLKLLL 54
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| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
581-677 |
4.11e-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: 41.15 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 581 TALLLFITTRKPDLLPLLVTLYAHGANMNATDPHGNTALHkSAALVDakkiSLECVKFLISAGsnPNKINL-------RG 653
Cdd:cd22192 17 SESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALH-VAALYD----NLEAAVVLMEAA--PELVNEpmtsdlyQG 89
|
90 100
....*....|....*....|....
gi 17567809 654 ESPRHLAASLQNQEMLAILKAAGA 677
Cdd:cd22192 90 ETALHIAVVNQNLNLVRELIARGA 113
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|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
540-669 |
9.67e-03 |
|
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: 40.13 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17567809 540 ERDALGNSAIHVALYKESLNaLLNRKVELGLDIDVKNNA--------------GETALLLFITTRKPDLLPLLvtLYAHG 605
Cdd:cd22194 136 EEAYEGQTALNIAIERRQGD-IVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLL--MEKES 212
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17567809 606 ANMNATDPHGNTALHksaALVDAKKISLECVKFLI---------SAGSNPNKI-NLRGESPRHLAASLQNQEML 669
Cdd:cd22194 213 TDITSQDSRGNTVLH---ALVTVAEDSKTQNDFVKrmydmillkSENKNLETIrNNEGLTPLQLAAKMGKAEIL 283
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