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Conserved domains on  [gi|1757305629|ref|NP_001361552|]
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omega-hydroxyceramide transacylase isoform 4 [Homo sapiens]

Protein Classification

patatin-like phospholipase domain-containing protein( domain architecture ID 10163438)

patatin-like phospholipase domain-containing protein may function as a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Pat_PNPLA1 cd07219
Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin ...
 2-388 0e+00

Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin domain, initially discovered in potato tubers. Some members of PNPLA1 subfamily do not have the lipase consensus sequence Gly-X-Ser-X-Gly which is essential for hydrolase activity. This family includes PNPLA1 from Homo sapiens and Gallus gallus. Currently, there is no literature available on the physiological role, structure, or enzymatic activity of PNPLA1. It is expressed in various human tissues in low mRNA levels.


:

Pssm-ID: 132858  Cd Length: 382  Bit Score: 726.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629   2 EEQVFKGDPDTPHSISFSGSGFLSFYQAGAVDALRDLAPRMLETAHRFAGTSAGAVIAALAICGIEMDEYLRVLNVGVAE 81
Cdd:cd07219     1 MEQVFKGDPDTPHSISFSGSGFLSFYQAGVVDALRDLAPRMLETAHRVAGTSAGSVIAALVVCGISMDEYLRVLNVGVAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  82 VKKSFLGPLSPSCKMVQMMRQFLYRVLPEDSYKVTTGKLHVSLTRLTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLI 161
Cdd:cd07219    81 VRKSFLGPLSPSCKMVQMMRQFLYRVLPEDSYKVATGKLHVSLTRVTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 162 PPTYRGVRYIDGGFTGMQPCAFWTDAITISTFSGQQDICPRDCPAIFHDFRMFNCSFQFSLENIARMTHALFPPDLVILH 241
Cdd:cd07219   161 PPTYRGVRYIDGGFTGMQPCSFWTDSITISTFSGQQDICPRDCPAIFHDFRIFNCSFQFSLENIARMTHALFPPDLMVLH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 242 DYYYRGYEDAVLYLRRLNAVYLNSSSKRVIFPRVEVYCQielALGNECPERSQPSLRARQASLEGATQPHKEWVPKGDGR 321
Cdd:cd07219   241 DYYYRGYQDTVLYLRRLNAVYLNSPSKRVIFPRVEVYCQ---ALGKECPQRSQPSLQDGQASLEESWQPHLARAPKGDGR 317

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1757305629 322 GSHGPPVSQPVQ----TLEFTCESPVSAPVSPLEQPPAQplasstPLSLSGMPPVSFPAVHKPPSSTPGSS 388
Cdd:cd07219   318 GLHDPPLSPPLAapesTAEWVVESPVSSPASPLESSPSL------PGSLTDLSPASLPAVHSLPSSTPGLS 382
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 295-493 2.52e-06

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 50.54  E-value: 2.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 295 PSLRARQASLEGATQPHKEwvPKGDGRGSHGPPVSQPVQTLEFTCESPVSAPVSPLEQPPAqPLASSTPLSLSGMPPVSF 374
Cdd:pfam03154 310 PPGPSPAAPGQSQQRIHTP--PSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPN-PQSHKHPPHLSGPSPFQM 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 375 PA---------------VHKPPSSTP--------GSSLPTPPPGLSPLSPQQQVQPSGS---PARSLHSQAPTSPRPS-- 426
Cdd:pfam03154 387 NSnlppppalkplsslsTHHPPSAHPpplqlmpqSQQLPPPPAQPPVLTQSQSLPPPAAshpPTSGLHQVPSQSPFPQhp 466

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1757305629 427 ---LGPSTVGAPQTLPRSSLSAFPA-QPPveelgQEQPQAVALLVSSKPKSAVPLVHVK-ETVSKPYVTESP 493
Cdd:pfam03154 467 fvpGGPPPITPPSGPPTSTSSAMPGiQPP-----SSASVSSSGPVPAAVSCPLPPVQIKeEALDEAEEPESP 533
 
Name Accession Description Interval E-value
Pat_PNPLA1 cd07219
Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin ...
 2-388 0e+00

Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin domain, initially discovered in potato tubers. Some members of PNPLA1 subfamily do not have the lipase consensus sequence Gly-X-Ser-X-Gly which is essential for hydrolase activity. This family includes PNPLA1 from Homo sapiens and Gallus gallus. Currently, there is no literature available on the physiological role, structure, or enzymatic activity of PNPLA1. It is expressed in various human tissues in low mRNA levels.


Pssm-ID: 132858  Cd Length: 382  Bit Score: 726.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629   2 EEQVFKGDPDTPHSISFSGSGFLSFYQAGAVDALRDLAPRMLETAHRFAGTSAGAVIAALAICGIEMDEYLRVLNVGVAE 81
Cdd:cd07219     1 MEQVFKGDPDTPHSISFSGSGFLSFYQAGVVDALRDLAPRMLETAHRVAGTSAGSVIAALVVCGISMDEYLRVLNVGVAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  82 VKKSFLGPLSPSCKMVQMMRQFLYRVLPEDSYKVTTGKLHVSLTRLTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLI 161
Cdd:cd07219    81 VRKSFLGPLSPSCKMVQMMRQFLYRVLPEDSYKVATGKLHVSLTRVTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 162 PPTYRGVRYIDGGFTGMQPCAFWTDAITISTFSGQQDICPRDCPAIFHDFRMFNCSFQFSLENIARMTHALFPPDLVILH 241
Cdd:cd07219   161 PPTYRGVRYIDGGFTGMQPCSFWTDSITISTFSGQQDICPRDCPAIFHDFRIFNCSFQFSLENIARMTHALFPPDLMVLH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 242 DYYYRGYEDAVLYLRRLNAVYLNSSSKRVIFPRVEVYCQielALGNECPERSQPSLRARQASLEGATQPHKEWVPKGDGR 321
Cdd:cd07219   241 DYYYRGYQDTVLYLRRLNAVYLNSPSKRVIFPRVEVYCQ---ALGKECPQRSQPSLQDGQASLEESWQPHLARAPKGDGR 317

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1757305629 322 GSHGPPVSQPVQ----TLEFTCESPVSAPVSPLEQPPAQplasstPLSLSGMPPVSFPAVHKPPSSTPGSS 388
Cdd:cd07219   318 GLHDPPLSPPLAapesTAEWVVESPVSSPASPLESSPSL------PGSLTDLSPASLPAVHSLPSSTPGLS 382
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 18-257 1.68e-15

Predicted acylesterase/phospholipase RssA, containd patatin domain [General function prediction only];


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 76.48  E-value: 1.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  18 FSGSGFLSFYQAGAVDALRDLAPRmletAHRFAGTSAGAVIAALAICGIEMDEYLR---------VLNVGVAEVKKSFLG 88
Cdd:COG1752    11 LSGGGARGAAHIGVLKALEEAGIP----PDVIAGTSAGAIVGALYAAGYSADELEElwrsldrrdLFDLSLPRRLLRLDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  89 PLSPSCKM-VQMMRQFLYRVLPEDSYKVTTGKLHVSLTRLTDGENVVVSEFtskeELIEALYCSCFVPvycGLIPP-TYR 166
Cdd:COG1752    87 GLSPGGLLdGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSG----PLADAVRASAAIP---GVFPPvEID 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 167 GVRYIDGGFTGMQP-------CAfwTDAITISTFSGQQDIcprdcPAIfhdFRMFNCSFQFSLENIARMTHALFPPDLVI 239
Cdd:COG1752   160 GRLYVDGGVVNNLPvdparalGA--DRVIAVDLNPPLRKL-----PSL---LDILGRALEIMFNSILRRELALEPADILI 229

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1757305629 240 --------LHDYYYR------GYEDAVLYLRR 257
Cdd:COG1752   230 epdlsgisLLDFSRAeelieaGYEAARRALDE 261
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 16-180 2.66e-15

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: 74.57  E-value: 2.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  16 ISFSGSGFLSFYQAGAVDALrdlaPRMLETAHRFAGTSAGAVIAALAICGIEMDE------------YLRVLNVGVAEVK 83
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKAL----GEAGIRFDVISGTSAGAINAALLALGRDPEEiedllleldlnlFLSLIRKRALSLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  84 KSFLGPLSPSCKM-VQMMRQFLYRVLPEDSYKVTTGKL-------------HVSLTRLTDGENVVVSEFTSKEELIEALY 149
Cdd:pfam01734  77 ALLRGLIGEGGLFdGDALRELLRKLLGDLTLEELAARLslllvvalralltVISTALGTRARILLPDDLDDDEDLADAVL 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1757305629 150 CSCFVPVYcgLIPPTYRGVRYIDGGFTGMQP 180
Cdd:pfam01734 157 ASSALPGV--FPPVRLDGELYVDGGLVDNVP 185
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 295-493 2.52e-06

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 50.54  E-value: 2.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 295 PSLRARQASLEGATQPHKEwvPKGDGRGSHGPPVSQPVQTLEFTCESPVSAPVSPLEQPPAqPLASSTPLSLSGMPPVSF 374
Cdd:pfam03154 310 PPGPSPAAPGQSQQRIHTP--PSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPN-PQSHKHPPHLSGPSPFQM 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 375 PA---------------VHKPPSSTP--------GSSLPTPPPGLSPLSPQQQVQPSGS---PARSLHSQAPTSPRPS-- 426
Cdd:pfam03154 387 NSnlppppalkplsslsTHHPPSAHPpplqlmpqSQQLPPPPAQPPVLTQSQSLPPPAAshpPTSGLHQVPSQSPFPQhp 466

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1757305629 427 ---LGPSTVGAPQTLPRSSLSAFPA-QPPveelgQEQPQAVALLVSSKPKSAVPLVHVK-ETVSKPYVTESP 493
Cdd:pfam03154 467 fvpGGPPPITPPSGPPTSTSSAMPGiQPP-----SSASVSSSGPVPAAVSCPLPPVQIKeEALDEAEEPESP 533
PHA03378 PHA03378
EBNA-3B; Provisional
 325-476 7.29e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 48.91  E-value: 7.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 325 GPPVSQPVQTLEFTCESPVSAPvSPLEQPPAQPLASSTPLSLSGM--PPVSFPAVHKPPSSTPGSSLPTPPPGLSPLSPQ 402
Cdd:PHA03378  680 GANTMLPIQWAPGTMQPPPRAP-TPMRPPAAPPGRAQRPAAATGRarPPAAAPGRARPPAAAPGRARPPAAAPGRARPPA 758

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 403 QQVQPSGSPARSLHSQAPTSP---------RPSLGPSTVGAPQTLPRSSLSAFPAQPpveelGQEQP--QAVALLVSSKP 471
Cdd:PHA03378  759 AAPGRARPPAAAPGAPTPQPPpqappapqqRPRGAPTPQPPPQAGPTSMQLMPRAAP-----GQQGPtkQILRQLLTGGV 833


                  ....*
gi 1757305629 472 KSAVP 476
Cdd:PHA03378  834 KRGRP 838
PHA03247 PHA03247
large tegument protein UL36; Provisional
 290-464 2.54e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 2.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  290 PERSQPSLRARQASLEGATQPhkeWVPKGDGRGSHGPPVSQPVQTLEFTCESPVSAPVSPLEQPPAQPLASSTPLSLSGM 369
Cdd:PHA03247  2781 RRLTRPAVASLSESRESLPSP---WDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA 2857

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  370 P-------PVSFPAVHKP--PSSTPGSSLPtppPGLSPLSPQQQVQPSGSPARSLHSQAPTSPRPSLGPSTVGAPQTLPR 440
Cdd:PHA03247  2858 PggdvrrrPPSRSPAAKPaaPARPPVRRLA---RPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPP 2934

                          170       180
                   ....*....|....*....|....*
gi 1757305629  441 S-SLSAFPAQPPVEELGQEQPQAVA 464
Cdd:PHA03247  2935 PpPRPQPPLAPTTDPAGAGEPSGAV 2959
 
Name Accession Description Interval E-value
Pat_PNPLA1 cd07219
Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin ...
 2-388 0e+00

Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin domain, initially discovered in potato tubers. Some members of PNPLA1 subfamily do not have the lipase consensus sequence Gly-X-Ser-X-Gly which is essential for hydrolase activity. This family includes PNPLA1 from Homo sapiens and Gallus gallus. Currently, there is no literature available on the physiological role, structure, or enzymatic activity of PNPLA1. It is expressed in various human tissues in low mRNA levels.


Pssm-ID: 132858  Cd Length: 382  Bit Score: 726.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629   2 EEQVFKGDPDTPHSISFSGSGFLSFYQAGAVDALRDLAPRMLETAHRFAGTSAGAVIAALAICGIEMDEYLRVLNVGVAE 81
Cdd:cd07219     1 MEQVFKGDPDTPHSISFSGSGFLSFYQAGVVDALRDLAPRMLETAHRVAGTSAGSVIAALVVCGISMDEYLRVLNVGVAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  82 VKKSFLGPLSPSCKMVQMMRQFLYRVLPEDSYKVTTGKLHVSLTRLTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLI 161
Cdd:cd07219    81 VRKSFLGPLSPSCKMVQMMRQFLYRVLPEDSYKVATGKLHVSLTRVTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 162 PPTYRGVRYIDGGFTGMQPCAFWTDAITISTFSGQQDICPRDCPAIFHDFRMFNCSFQFSLENIARMTHALFPPDLVILH 241
Cdd:cd07219   161 PPTYRGVRYIDGGFTGMQPCSFWTDSITISTFSGQQDICPRDCPAIFHDFRIFNCSFQFSLENIARMTHALFPPDLMVLH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 242 DYYYRGYEDAVLYLRRLNAVYLNSSSKRVIFPRVEVYCQielALGNECPERSQPSLRARQASLEGATQPHKEWVPKGDGR 321
Cdd:cd07219   241 DYYYRGYQDTVLYLRRLNAVYLNSPSKRVIFPRVEVYCQ---ALGKECPQRSQPSLQDGQASLEESWQPHLARAPKGDGR 317

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1757305629 322 GSHGPPVSQPVQ----TLEFTCESPVSAPVSPLEQPPAQplasstPLSLSGMPPVSFPAVHKPPSSTPGSS 388
Cdd:cd07219   318 GLHDPPLSPPLAapesTAEWVVESPVSSPASPLESSPSL------PGSLTDLSPASLPAVHSLPSSTPGLS 382
Pat_PNPLA_like cd07204
Patatin-like phospholipase domain containing protein family; Members of this family share a ...
 15-257 1.94e-142

Patatin-like phospholipase domain containing protein family; Members of this family share a patain domain, initially discovered in potato tubers. PNPLA protein members show non-specific hydrolase activity with a variety of substrates such as triacylglycerol, phospholipids, and retinylesters. It contains the lipase consensus sequence (Gly-X-Ser-X-Gly). Nomenclature of PNPLA family could be misleading as some of the mammalian members of this family show hydrolase, but no phospholipase activity.


Pssm-ID: 132843 [Multi-domain]  Cd Length: 243  Bit Score: 411.36  E-value: 1.94e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  15 SISFSGSGFLSFYQAGAVDALRDLAPRMLETAHRFAGTSAGAVIAALAICGIEMDEYLRVLNVGVAEVKKSFLGPLSPSC 94
Cdd:cd07204     1 NLSFSGCGFLGIYHVGVASALREHAPRLLQNARRIAGASAGAIVAAVVLCGVSMEEACSFILKVVSEARRRSLGPLHPSF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  95 KMVQMMRQFLYRVLPEDSYKVTTGKLHVSLTRLTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLIPPTYRGVRYIDGG 174
Cdd:cd07204    81 NLLKILRQGLEKILPDDAHELASGRLHISLTRVSDGENVLVSEFDSKEELIQALVCSCFIPFYCGLIPPKFRGVRYIDGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 175 FTGMQPCAFWTDAITISTFSGQQDICPRDCPAIFHDFRMFNCSFQFSLENIARMTHALFPPDLVILHDYYYRGYEDAVLY 254
Cdd:cd07204   161 LSDNLPILDDENTITVSPFSGESDICPQDKSSNLLEVNIANTSIQLSLENLYRLNRALFPPSLEILSRMCQQGYLDALRF 240


                  ...
gi 1757305629 255 LRR 257
Cdd:cd07204   241 LER 243
Pat_PNPLA2 cd07220
Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis ...
 11-257 8.61e-88

Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis of stored triacylglecerols and is also known as adipose triglyceride lipase (ATGL). Members of this family share a patain domain, initially discovered in potato tubers. ATGL is expressed in white and brown adipose tissue in high mRNA levels. Mutations in PNPLA2 encoding adipose triglyceride lipase (ATGL) leads to neutral lipid storage disease (NLSD) which is characterized by the accumulation of triglycerides in multiple tissues. ATGL mutations are also commonly associated with severe forms of skeletal- and cardio-myopathy. This family includes patatin-like proteins: TTS-2.2 (transport-secretion protein 2.2), PNPLA2 (Patatin-like phospholipase domain-containing protein 2), and iPLA2-zeta (Calcium-independent phospholipase A2) from Homo sapiens.


Pssm-ID: 132859  Cd Length: 249  Bit Score: 272.00  E-value: 8.61e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  11 DTPHSISFSGSGFLSFYQAGAVDALRDLAPRMLETAHRFAGTSAGAVIAALAICGIEMDEYL-RVLNVGvAEVKKSFLGP 89
Cdd:cd07220     2 DSGWNISFAGCGFLGVYHVGVASCLLEHAPFLVANARKIYGASAGALTATALVTGVCLGECGaSVIRVA-KEARKRFLGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  90 LSPSCKMVQMMRQFLYRVLPEDSYKVTTGKLHVSLTRLTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLIPPTYRGVR 169
Cdd:cd07220    81 LHPSFNLVKILRDGLLRTLPENAHELASGRLGISLTRVSDGENVLVSDFNSKEELIQALVCSCFIPVYCGLIPPTLRGVR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 170 YIDGGFTGMQPCAFWTDAITISTFSGQQDICPRDCPAIFHDFRMFNCSFQFSLENIARMTHALFPPDLVILHDYYYRGYE 249
Cdd:cd07220   161 YVDGGISDNLPQYELKNTITVSPFSGESDICPRDSSTNFHELRFTNTSIQFNLRNLYRLSKALFPPEPQVLAEMCKQGYR 240


                  ....*...
gi 1757305629 250 DAVLYLRR 257
Cdd:cd07220   241 DALRFLKE 248
Pat_iPLA2 cd07218
Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent ...
 14-261 4.08e-82

Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent phospholipase A2; otherwise known as Group IVA-1 PLA2. It contains the lipase consensus sequence (Gly-X-Ser-X-Gly);mutagenesis experiments confirm the role of this serine as a nucleophile. Some members of this group show triacylglycerol lipase activity (EC 3:1:1:3). Members include iPLA-1, iPLA-2, and iPLA-3 from Aedes aegypti and show acylglycerol transacylase/lipase activity. Also includes putative iPLA2-eta from Pediculus humanus corporis which shows patatin-like phospholipase activity.


Pssm-ID: 132857  Cd Length: 245  Bit Score: 256.89  E-value: 4.08e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  14 HSISFSGSGFLSFYQAGAVDALRDLAPRMLEtaHRFAGTSAGAVIAALAICGIEMDE----YLRVlnvgVAEVKKSFLGP 89
Cdd:cd07218     1 MNLSFAGCGFLGIYHVGVAVCLKKYAPHLLL--NKISGASAGALAACCLLCDLPLGEmtsdFLRV----VREARRHSLGP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  90 LSPSCKMVQMMRQFLYRVLPEDSYKVTTGKLHVSLTRLTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLIPPTYRGVR 169
Cdd:cd07218    75 FSPSFNIQTCLLEGLQKFLPDDAHERVSGRLHISLTRVSDGKNVIVSEFESREELLQALLCSCFIPVFSGLLPPKFRGVR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 170 YIDGGFTGMQPcAFWTDAITISTFSGQQDICPRDCPAIFHDFRMFNCSFQFSLENIARMTHALFPPDLVILHDYYYRGYE 249
Cdd:cd07218   155 YMDGGFSDNLP-TLDENTITVSPFCGESDICPRDNSSQLFHINWANTSIELSRQNIYRLVRILFPPRPEVLSSLCQQGFD 233

                         250
                  ....*....|..
gi 1757305629 250 DAVLYLRRLNAV 261
Cdd:cd07218   234 DALRFLHRNNLI 245
Pat_PNPLA3 cd07221
Patatin-like phospholipase domain containing protein 3; PNPLA3 is a triacylglycerol lipase ...
 15-255 3.80e-72

Patatin-like phospholipase domain containing protein 3; PNPLA3 is a triacylglycerol lipase that mediates triacylglycerol hydrolysis in adipocytes and is an indicator of the nutritional state. PNPLA3 is also known as adiponutrin (ADPN) or iPLA2-epsilon. Human adiponutrins are bound to the cell membrane of adipocytes and show transacylase, TG hydrolase, and PLA2 activity. This family includes patatin-like proteins: ADPN (adiponutrin) from mammals, PNPLA3 (Patatin-like phospholipase domain-containing protein 3), and iPLA2-epsilon (Calcium-independent phospholipase A2) from Homo sapiens.


Pssm-ID: 132860  Cd Length: 252  Bit Score: 231.59  E-value: 3.80e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  15 SISFSGSGFLSFYQAGAVDALRDLAPRMLETAHRFAGTSAGAVIAALAICGIEMDEYLRVLNVGVAEVKKSFLGPLSPSC 94
Cdd:cd07221     2 SLSFAGCGFLGFYHVGVTRCLSERAPHLLRDARMFFGASAGALHCVTFLSGLPLDQILQILMDLVRSARSRNIGILHPSF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  95 KMVQMMRQFLYRVLPEDSYKVTTGKLHVSLTRLTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLIPPTYRGVRYIDGG 174
Cdd:cd07221    82 NLSKHLRDGLQRHLPDNVHQLISGKMCISLTRVSDGENVLVSDFHSKDEVVDALVCSCFIPFFSGLIPPSFRGVRYVDGG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 175 FTGMQPCAFWTDAITISTFSGQQDICPRDCPAIFHDFRMFNCSFQFSLENIARMTHALFPPDLVILHDYYYRGYEDAVLY 254
Cdd:cd07221   162 VSDNVPFFDAKTTITVSPFYGEYDICPKVKSTNFLHVDFTKLSLRLCTENLYLLTRALFPPDVKVLGEICLRGYLDAFRF 241


                  .
gi 1757305629 255 L 255
Cdd:cd07221   242 L 242
Pat_PNPLA4 cd07222
Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene ...
 16-259 3.08e-67

Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene sequence-2), shows both lipase and transacylation activities. GS2 lipase is expressed in various tissues, predominantly in muscle and adipocytes tissue. It is also expressed in keratinocytes and shows retinyl ester hydrolase, acylglycerol, TG hydrolase, and PLA2 activity. This family includes patatin-like proteins: GS2 from mammals, PNPLA4 (Patatin-like phospholipase domain-containing protein 4), and iPLA2-eta (Calcium-independent phospholipase A2) from Homo sapiens.


Pssm-ID: 132861 [Multi-domain]  Cd Length: 246  Bit Score: 218.35  E-value: 3.08e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  16 ISFSGSGFLSFYQAGAVDALRDLAPRMLETAHRFAGTSAGAVIAALAICGIEMDEYLRVLNVGVA-EVKKSFLGPLSPSC 94
Cdd:cd07222     2 LSFAACGFLGIYHLGAAKALLRHGKKLLKRVKRFAGASAGSLVAAVLLTAPEKIEECKEFTYKFAeEVRKQRFGAMTPGY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  95 KMVQMMRQFLYRVLPEDSYKVTTGKLHVSLTRLTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLIPPTYRGVRYIDGG 174
Cdd:cd07222    82 DFMARLRKGIESILPTDAHELANDRLHVSITNLKTRKNYLVSNFTSREDLIKVLLASCYVPVYAGLKPVEYKGQKWIDGG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 175 FTGMQPCAFWTDAITISTFSGQQDICPRDCPAIFHDFRMFNCSFQFSLENIARMTHALFPPDLVILHDYYYRGYEDAVLY 254
Cdd:cd07222   162 FTNSLPVLPVGRTITVSPFSGRADICPQDKGQLDLYVRFANQDIMLSLANLVRLNQALFPPNRRKLESYYQMGFDDAVRF 241


                  ....*
gi 1757305629 255 LRRLN 259
Cdd:cd07222   242 LKKEN 246
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 16-191 3.76e-63

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: 204.88  E-value: 3.76e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  16 ISFSGSGFLSFYQAGAVDALRDLAPRmletAHRFAGTSAGAVIAALAICGIEMDEYLRVLNVGVAEVKKSFLGPLSPSCK 95
Cdd:cd07198     1 LVLSGGGALGIYHVGVAKALRERGPL----IDIIAGTSAGAIVAALLASGRDLEEALLLLLRLSREVRLRFDGAFPPTGR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  96 MVQMMRQFLYRVLPEDSYKVTTGKLHVSLTRLTDGENVVVSeFTSKEELIEALYCSCFVPVYCGLIPPTYRGVRYIDGGF 175
Cdd:cd07198    77 LLGILRQPLLSALPDDAHEDASGKLFISLTRLTDGENVLVS-DTSKGELWSAVRASSSIPGYFGPVPLSFRGRRYGDGGL 155

                         170
                  ....*....|....*.
gi 1757305629 176 TGMQPCAFWTDAITIS 191
Cdd:cd07198   156 SNNLPVAELGNTINVS 171
Pat_PNPLA5-mammals cd07223
Patatin-like phospholipase domain containing protein 5; PNPLA5, also known as GS2L (GS2-like), ...
 15-257 4.45e-59

Patatin-like phospholipase domain containing protein 5; PNPLA5, also known as GS2L (GS2-like), plays a role in regulation of adipocyte differentiation. PNPLA5 is expressed in brain tissue in high mRNA levels and low levels in liver tissue. There is no concrete evidence in support of the enzymatic activity of GS2L. This family includes patatin-like proteins: GS2L (GS2-like) and PNPLA5 (Patatin-like phospholipase domain-containing protein 5) reported exclusively in mammals.


Pssm-ID: 132862  Cd Length: 405  Bit Score: 202.06  E-value: 4.45e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  15 SISFSGSGFLSFYQAGAVDALRDLAPRMLETAHRFAGTSAGAVIAALAICGIEMDEYLRVLNVGVAEVKKSFLGPLSPSC 94
Cdd:cd07223    11 NLSFSGAGYLGLYHVGVTECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSADFCCSNLLGMVKHLERLSLGIFHPAY 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  95 KMVQMMRQFLYRVLPEDSYKVTTGKLHVSLTRLTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLIPPTYRGVRYIDGG 174
Cdd:cd07223    91 APIEHIRQQLQESLPPNIHILASQRLGISMTRWPDGRNFIVTDFATRDELIQALICTLYFPFYCGIIPPEFRGERYIDGA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 175 FTGMQPCAFWTDAITISTFSGQQDICPRDCPAIFHDFRMFNCSFQFSLENIARMTHALFPPDLVILHDYYYRGYEDAVLY 254
Cdd:cd07223   171 LSNNLPFSDCPSTITVSPFHGTVDICPQSTSANLHELNAFNASFQISTRNFFLGLKCLIPPKPEVVADNCRQGYLDALRF 250


                  ...
gi 1757305629 255 LRR 257
Cdd:cd07223   251 LER 253
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 16-192 1.53e-37

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: 136.01  E-value: 1.53e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  16 ISFSGSGFLSFYQAGAVDALRDLAPrmLETAHRFAGTSAGAVIAALAicgiemdeylrvlnvgvaevkksflgpLSPSCK 95
Cdd:cd01819     1 LSFSGGGFRGMYHAGVLSALAERGL--LDCVTYLAGTSGGAWVAATL---------------------------YPPSSS 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  96 MVQMMRQFLYrvlpedsyKVTTGKLHVSLTRLTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLIPP----------TY 165
Cdd:cd01819    52 LDNKPRQSLE--------EALSGKLWVSFTPVTAGENVLVSRFVSKEELIRALFASGSWPSYFGLIPPaelytsksnlKE 123

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1757305629 166 RGVRYIDGGFTGMQPCA-----FWTDAITIST 192
Cdd:cd01819   124 KGVRLVDGGVSNNLPAPvllrpGRGVTLTISP 155
Pat_like cd07224
Patatin-like phospholipase; Patatin-like phospholipase. This family consists of various ...
 16-257 3.83e-28

Patatin-like phospholipase; 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: 132863  Cd Length: 233  Bit Score: 112.43  E-value: 3.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  16 ISFSGSGFLSFYQAGAVDALRDLApRMLETAhRFAGTSAGAVIAALAICGIEMDEYLRVLnVGVAEVKKSF-----LGpl 90
Cdd:cd07224     2 FSFSAAGLLFPYHLGVLSLLIEAG-VINETT-PLAGASAGSLAAACSASGLSPEEALEAT-EELAEDCRSNgtafrLG-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  91 spsckmvQMMRQFLYRVLPEDSY-KVTTGKLHVSLTRL---TDGENVvvSEFTSKEELIEALYCSCFVPVYCGLIPPT-Y 165
Cdd:cd07224    77 -------GVLRDELDKTLPDDAHeRCNRGRIRVAVTQLfpvPRGLLV--SSFDSKSDLIDALLASCNIPGYLAPWPATmF 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 166 RGVRYIDGGFTGMQP-----------CAFWTDAITISTfsgqQDICPRDCPAifHDFRMFNCSFQfsleniarmthALFP 234
Cdd:cd07224   148 RGKLCVDGGFALFIPpttaadrtvrvCPFPASRSSIKG----QNLDNDDTED--VPYSRRQLLNW-----------ALEP 210

                         250       260
                  ....*....|....*....|...
gi 1757305629 235 PDLVILHDYYYRGYEDAVLYLRR 257
Cdd:cd07224   211 ADDAMLLELFNEGYKDANEWAKE 233
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 18-257 1.68e-15

Predicted acylesterase/phospholipase RssA, containd patatin domain [General function prediction only];


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 76.48  E-value: 1.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  18 FSGSGFLSFYQAGAVDALRDLAPRmletAHRFAGTSAGAVIAALAICGIEMDEYLR---------VLNVGVAEVKKSFLG 88
Cdd:COG1752    11 LSGGGARGAAHIGVLKALEEAGIP----PDVIAGTSAGAIVGALYAAGYSADELEElwrsldrrdLFDLSLPRRLLRLDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  89 PLSPSCKM-VQMMRQFLYRVLPEDSYKVTTGKLHVSLTRLTDGENVVVSEFtskeELIEALYCSCFVPvycGLIPP-TYR 166
Cdd:COG1752    87 GLSPGGLLdGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSG----PLADAVRASAAIP---GVFPPvEID 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 167 GVRYIDGGFTGMQP-------CAfwTDAITISTFSGQQDIcprdcPAIfhdFRMFNCSFQFSLENIARMTHALFPPDLVI 239
Cdd:COG1752   160 GRLYVDGGVVNNLPvdparalGA--DRVIAVDLNPPLRKL-----PSL---LDILGRALEIMFNSILRRELALEPADILI 229

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1757305629 240 --------LHDYYYR------GYEDAVLYLRR 257
Cdd:COG1752   230 epdlsgisLLDFSRAeelieaGYEAARRALDE 261
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 16-180 2.66e-15

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: 74.57  E-value: 2.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  16 ISFSGSGFLSFYQAGAVDALrdlaPRMLETAHRFAGTSAGAVIAALAICGIEMDE------------YLRVLNVGVAEVK 83
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKAL----GEAGIRFDVISGTSAGAINAALLALGRDPEEiedllleldlnlFLSLIRKRALSLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  84 KSFLGPLSPSCKM-VQMMRQFLYRVLPEDSYKVTTGKL-------------HVSLTRLTDGENVVVSEFTSKEELIEALY 149
Cdd:pfam01734  77 ALLRGLIGEGGLFdGDALRELLRKLLGDLTLEELAARLslllvvalralltVISTALGTRARILLPDDLDDDEDLADAVL 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1757305629 150 CSCFVPVYcgLIPPTYRGVRYIDGGFTGMQP 180
Cdd:pfam01734 157 ASSALPGV--FPPVRLDGELYVDGGLVDNVP 185
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 20-174 4.10e-13

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: 68.91  E-value: 4.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  20 GSGFLSFY-QAGAVDAL--RDLAPRmletahRFAGTSAGAVIAALAICGIEMDEYLRVLnvgVAEVKKSFLGPLSPSCKM 96
Cdd:cd07210     6 SSGFFGFYaHLGFLAALleMGLEPS------AISGTSAGALVGGLFASGISPDEMAELL---LSLERKDFWMFWDPPLRG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  97 ----VQMMRQFLYRVLPEDSYKVTTGKLHVSLTRLTDGENVVVSEftskEELIEALYCSCFVP-VYCgliPPTYRGVRYI 171
Cdd:cd07210    77 gllsGDRFAALLREHLPPDRFEELRIPLAVSVVDLTSRETLLLSE----GDLAEAVAASCAVPpLFQ---PVEIGGRPFV 149


                  ...
gi 1757305629 172 DGG 174
Cdd:cd07210   150 DGG 152
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 18-176 5.98e-09

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: 56.53  E-value: 5.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  18 FSGSGFLSFYQAGAVDALRDLAPRmletAHRFAGTSAGAVIAALAICGieMDEYLRVL-----NVGVAEVkksflgplsp 92
Cdd:cd07209     3 LSGGGALGAYQAGVLKALAEAGIE----PDIISGTSIGAINGALIAGG--DPEAVERLeklwrELSREDV---------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  93 sckmvqMMRQFLYRVLPEDS---YKVTTGKLHVSLTRLTDGENVVVSEfTSKEELIEALYCSCFVPVycGLIPPTYRGVR 169
Cdd:cd07209    67 ------FLRGLLDRALDFDTlrlLAILFAGLVIVAVNVLTGEPVYFDD-IPDGILPEHLLASAALPP--FFPPVEIDGRY 137


                  ....*..
gi 1757305629 170 YIDGGFT 176
Cdd:cd07209   138 YWDGGVV 144
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 16-174 6.42e-09

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


Pssm-ID: 132846  Cd Length: 194  Bit Score: 55.75  E-value: 6.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  16 ISFSGSGFLSFYQAGAVDALRDLAprMLETahRFAGTSAGAVIAALAICGIEMDEYLRVLN-----------VGVAEVKK 84
Cdd:cd07207     2 LVFEGGGAKGIAYIGALKALEEAG--ILKK--RVAGTSAGAITAALLALGYSAADIKDILKetdfaklldspVGLLFLLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  85 SFLGP--LSPSCKMVQMMRQ------------FLYRVLPEDSYKvttgKLHVSLTRLTDGENVVVSEFTSKEELI-EALY 149
Cdd:cd07207    78 SLFKEggLYKGDALEEWLREllkektgnsfatSLLRDLDDDLGK----DLKVVATDLTTGALVVFSAETTPDMPVaKAVR 153

                         170       180
                  ....*....|....*....|....*...
gi 1757305629 150 CSCFVPVY---CGLIpptyRGVRYIDGG 174
Cdd:cd07207   154 ASMSIPFVfkpVRLA----KGDVYVDGG 177
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
27-176 2.65e-07

Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 52.47  E-value: 2.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  27 YQAGAVDALrdlaprmLETAHRF---AGTSAGAVIAALAICGieMDEYLRVLNVGVAeVKKSFLGPLSP--SCKMVQMmr 101
Cdd:COG4667    19 FTAGVLDAL-------LEEGIPFdlvIGVSAGALNGASYLSR--QPGRARRVITDYA-TDPRFFSLRNFlrGGNLFDL-- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 102 QFLYRVLPE-------DSYKVTTGKLHVSLTRLTDGENVVVSEFTSKEELIEALYCSCFVPVYCGliPPTYRGVRYIDGG 174
Cdd:COG4667    87 DFLYDEIPNellpfdfETFKASPREFYVVATNADTGEAEYFSKKDDDYDLLDALRASSALPLLYP--PVEIDGKRYLDGG 164


                  ..
gi 1757305629 175 FT 176
Cdd:COG4667   165 VA 166
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 18-174 3.21e-07

Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase similar to yjju 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: 132847 [Multi-domain]  Cd Length: 266  Bit Score: 51.84  E-value: 3.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  18 FSGSGFLSFYQAGAVDALrdlaprMLETAHRF---AGTSAGAVIAALAICGieMDEYLRVLNVGVAEvKKSFLGPLS-PS 93
Cdd:cd07208     3 LEGGGMRGAYTAGVLDAF------LEAGIRPFdlvIGVSAGALNAASYLSG--QRGRALRINTKYAT-DPRYLGLRSlLR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  94 CKmvQMM-RQFLYRVLPE-------DSYKVTTGKLHVSLTRLTDGENVVVSEFTSKEELIEALYCSCFVPVYCGliPPTY 165
Cdd:cd07208    74 TG--NLFdLDFLYDELPDgldpfdfEAFAASPARFYVVATDADTGEAVYFDKPDILDDLLDALRASSALPGLFP--PVRI 149


                  ....*....
gi 1757305629 166 RGVRYIDGG 174
Cdd:cd07208   150 DGEPYVDGG 158
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 295-493 2.52e-06

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 50.54  E-value: 2.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 295 PSLRARQASLEGATQPHKEwvPKGDGRGSHGPPVSQPVQTLEFTCESPVSAPVSPLEQPPAqPLASSTPLSLSGMPPVSF 374
Cdd:pfam03154 310 PPGPSPAAPGQSQQRIHTP--PSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPN-PQSHKHPPHLSGPSPFQM 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 375 PA---------------VHKPPSSTP--------GSSLPTPPPGLSPLSPQQQVQPSGS---PARSLHSQAPTSPRPS-- 426
Cdd:pfam03154 387 NSnlppppalkplsslsTHHPPSAHPpplqlmpqSQQLPPPPAQPPVLTQSQSLPPPAAshpPTSGLHQVPSQSPFPQhp 466

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1757305629 427 ---LGPSTVGAPQTLPRSSLSAFPA-QPPveelgQEQPQAVALLVSSKPKSAVPLVHVK-ETVSKPYVTESP 493
Cdd:pfam03154 467 fvpGGPPPITPPSGPPTSTSSAMPGiQPP-----SSASVSSSGPVPAAVSCPLPPVQIKeEALDEAEEPESP 533
PHA03378 PHA03378
EBNA-3B; Provisional
 325-476 7.29e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 48.91  E-value: 7.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 325 GPPVSQPVQTLEFTCESPVSAPvSPLEQPPAQPLASSTPLSLSGM--PPVSFPAVHKPPSSTPGSSLPTPPPGLSPLSPQ 402
Cdd:PHA03378  680 GANTMLPIQWAPGTMQPPPRAP-TPMRPPAAPPGRAQRPAAATGRarPPAAAPGRARPPAAAPGRARPPAAAPGRARPPA 758

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 403 QQVQPSGSPARSLHSQAPTSP---------RPSLGPSTVGAPQTLPRSSLSAFPAQPpveelGQEQP--QAVALLVSSKP 471
Cdd:PHA03378  759 AAPGRARPPAAAPGAPTPQPPpqappapqqRPRGAPTPQPPPQAGPTSMQLMPRAAP-----GQQGPtkQILRQLLTGGV 833


                  ....*
gi 1757305629 472 KSAVP 476
Cdd:PHA03378  834 KRGRP 838
PHA03247 PHA03247
large tegument protein UL36; Provisional
 290-494 2.50e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 2.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  290 PERSQPSLRARQASLEGATQPHKEWVPKGDGRGSHGPPVSQPVQTlefTCESPVSAPVSPLEQP--PAQPLASSTPLSLS 367
Cdd:PHA03247  2623 APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRA---RRLGRAAQASSPPQRPrrRAARPTVGSLTSLA 2699

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  368 GMPPVSFPAVHKPPSSTPGSSLPTPPpglsplspqqQVQPSGSPARSLhsqAPTSPRPSLGPSTVGAPQTLPRSSLSAFP 447
Cdd:PHA03247  2700 DPPPPPPTPEPAPHALVSATPLPPGP----------AAARQASPALPA---APAPPAVPAGPATPGGPARPARPPTTAGP 2766

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1757305629  448 AQ--PPVEELGQEQPQAVALLVSSKPKSAVPLVHVKETVSKPYVTESPA 494
Cdd:PHA03247  2767 PApaPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPA 2815
PHA03247 PHA03247
large tegument protein UL36; Provisional
 290-464 2.54e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 2.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  290 PERSQPSLRARQASLEGATQPhkeWVPKGDGRGSHGPPVSQPVQTLEFTCESPVSAPVSPLEQPPAQPLASSTPLSLSGM 369
Cdd:PHA03247  2781 RRLTRPAVASLSESRESLPSP---WDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA 2857

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  370 P-------PVSFPAVHKP--PSSTPGSSLPtppPGLSPLSPQQQVQPSGSPARSLHSQAPTSPRPSLGPSTVGAPQTLPR 440
Cdd:PHA03247  2858 PggdvrrrPPSRSPAAKPaaPARPPVRRLA---RPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPP 2934

                          170       180
                   ....*....|....*....|....*
gi 1757305629  441 S-SLSAFPAQPPVEELGQEQPQAVA 464
Cdd:PHA03247  2935 PpPRPQPPLAPTTDPAGAGEPSGAV 2959
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 18-180 3.01e-05

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: 44.84  E-value: 3.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  18 FSGSGFLSFYQAGAVDAL--RDLAPrmletaHRFAGTSAGAVIAALAICGI---EMDEYLRVLNVGVAEVKKSFL--GPL 90
Cdd:cd07205     5 LSGGGARGLAHIGVLKALeeAGIPI------DIVSGTSAGAIVGALYAAGYspeEIEERAKLRSTDLKALSDLTIptAGL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  91 SPSCKMVQMMRQFLYRVLPEDSYKvttgKLHVSLTRLTDGENVVVSEftskEELIEALYCSCFVPvycGLIPP-TYRGVR 169
Cdd:cd07205    79 LRGDKFLELLDEYFGDRDIEDLWI----PFFIVATDLTSGKLVVFRS----GSLVRAVRASMSIP---GIFPPvKIDGQL 147

                         170
                  ....*....|.
gi 1757305629 170 YIDGGFTGMQP 180
Cdd:cd07205   148 LVDGGVLNNLP 158
PHA03247 PHA03247
large tegument protein UL36; Provisional
 290-494 4.53e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 4.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  290 PERSQPSLRARQASLEGATQPHKEWVPKGDGRGSHGPPVSQPvqtleftceSPVSAPvsPLEQPPAQPLASSTPLSLSGM 369
Cdd:PHA03247  2575 PRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSP---------LPPDTH--APDPPPPSPSPAANEPDPHPP 2643

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  370 PPVSFPAVHKPPSSTPGSSLPtpppglsplspqQQVQPSGSPARSlhSQAPTSPRPSLGPSTVGA-------------PQ 436
Cdd:PHA03247  2644 PTVPPPERPRDDPAPGRVSRP------------RRARRLGRAAQA--SSPPQRPRRRAARPTVGSltsladpppppptPE 2709

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1757305629  437 TLPRSSLSAFPAQPPVEELGQEQPQAVALLVSSKPKSAVPLVHVKETVSKPYVTESPA 494
Cdd:PHA03247  2710 PAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPP 2767
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 305-478 8.01e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.75  E-value: 8.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 305 EGATQPHKEWVPKGDGRGSHGPPVSQPVQTLEFTCESPVSAPVSPLEQPPAQPLASSTPlslsgmPPVSFPAVHKPPSST 384
Cdd:PRK07764  371 ERGLLARLERLERRLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAP------QPAPAPAPAPAPPSP 444

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 385 PGSSlptppPGLSPLSPQQQVQPSGSPARSLHSQAPTSPRPSLGPSTVGAPQTLPRSSLSAFPAQPP--VEELGQEQPQA 462
Cdd:PRK07764  445 AGNA-----PAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGAddAATLRERWPEI 519

                         170
                  ....*....|....*.
gi 1757305629 463 VALLVSSKPKSAVPLV 478
Cdd:PRK07764  520 LAAVPKRSRKTWAILL 535
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 18-61 1.24e-04

Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are involved in triacylglycerol mobilization and degradation; they are found in lipid particles. TGL4 is 30% homologus to TGL3, whereas TGL5 is 26% homologus to TGL3. Sugar-Dependent 1 (SDP1) lipase has a patatin-like acyl-hydrolase domain that initiates the breakdown of storage oil in germinating Arabidopsis seeds. This family includes subfamilies of proteins: TGL3, TGL4, TGL5, and SDP1.


Pssm-ID: 132845  Cd Length: 298  Bit Score: 44.12  E-value: 1.24e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1757305629  18 FSGSGFLSFYQAGAVDAL--RDLAPRMLetahrfAGTSAGAVIAAL 61
Cdd:cd07206    74 LSGGASLGLFHLGVVKALweQDLLPRVI------SGSSAGAIVAAL 113
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
322-461 1.28e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 44.77  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 322 GSHGPPVSQPVQTLEFTCESPVSAPvspleQPPAQPLASSTPLSLSGMPPVSFPavhkPPSSTPGSSLPTPPPGLSPlsp 401
Cdd:PRK14971  366 GDDASGGRGPKQHIKPVFTQPAAAP-----QPSAAAAASPSPSQSSAAAQPSAP----QSATQPAGTPPTVSVDPPA--- 433

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 402 QQQVQPSGSPARSLHSQ-------APTSPRPSLGPSTVGA---PQTLPRSSLSAFPAQPPVEELGQEQPQ 461
Cdd:PRK14971  434 AVPVNPPSTAPQAVRPAqfkeekkIPVSKVSSLGPSTLRPiqeKAEQATGNIKEAPTGTQKEIFTEEDLQ 503
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 16-86 2.07e-04

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: 43.43  E-value: 2.07e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1757305629  16 ISFSGSGFLSFYQAGAVDALRDLAPRMLETAHRFAGTSAGAVIAALAICGIEMDEylrVLNVGVAEVKKSF 86
Cdd:cd07213     5 LSLDGGGVKGIVQLVLLKRLAEEFPSFLDQIDLFAGTSAGSLIALGLALGYSPRQ---VLKLYEEVGLKVF 72
PHA03247 PHA03247
large tegument protein UL36; Provisional
 325-461 2.08e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 2.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  325 GPPVSQPVQtleftceSPVSAPVSPLEQPPAQPLASSTPlslsGMPPVSFPAVHKPPSSTPGSSLPTPPPGLSPLSPQQQ 404
Cdd:PHA03247  2765 GPPAPAPPA-------APAAGPPRRLTRPAVASLSESRE----SLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTS 2833

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1757305629  405 VQPSGSPARSLHSQAPTSPRPSLGPSTVGAPQTLPRSSLS--AFPAQPPVEELGQEQPQ 461
Cdd:PHA03247  2834 AQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAkpAAPARPPVRRLARPAVS 2892
PLN02217 PLN02217
probable pectinesterase/pectinesterase inhibitor
 354-485 3.29e-04

probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 215130 [Multi-domain]  Cd Length: 670  Bit Score: 43.54  E-value: 3.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 354 PAQPLASSTPLSLSGMP--PVSFPAVHKPPSSTPGSSLPTPPPGLSPLSPQQQVQPSGSPARSLHSQAPTSPRPSLGPST 431
Cdd:PLN02217  540 PAQYIQGDAWIPGKGVPyiPGLFAGNPGSTNSTPTGSAASSNTTFSSDSPSTVVAPSTSPPAGHLGSPPATPSKIVSPST 619

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1757305629 432 vgAPqtlPRSSLSAfpaqPPVEELGQEQPQAVALLVSSKPKSAVPLVHVKETVS 485
Cdd:PLN02217  620 --SP---PASHLGS----PSTTPSSPESSIKVASTETASPESSIKVASTESSVS 664
PHA03247 PHA03247
large tegument protein UL36; Provisional
 290-471 3.41e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 3.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  290 PERSQPSLRAR-QASLEGATQPHKEWVPKG------------DGRGSHGPPVSQPVQTLEFTCESPvsAPVSPLEQPPAQ 356
Cdd:PHA03247  2658 PGRVSRPRRARrLGRAAQASSPPQRPRRRAarptvgsltslaDPPPPPPTPEPAPHALVSATPLPP--GPAAARQASPAL 2735

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  357 PLASSTPLSLSGMPPVSFPAVHKPPSSTPGSSLPTPPPGLSPLSPQQQVQPSGSPARSLHSQAPTSPRPSLGPSTVGAPQ 436
Cdd:PHA03247  2736 PAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPA 2815

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1757305629  437 -TLPRSSLSAFPAQPPVEELGQEQPQAVALLVSSKP 471
Cdd:PHA03247  2816 aALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLP 2851
PHA03247 PHA03247
large tegument protein UL36; Provisional
 295-476 6.08e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 6.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  295 PSLRARQASLEGATQPHKEWVPKGdgrgshGPPVSQPVQTLEFTCESPVSAPVSPLEQPPAQPL--------ASSTPLSL 366
Cdd:PHA03247  2754 PARPARPPTTAGPPAPAPPAAPAA------GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVlapaaalpPAASPAGP 2827

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  367 SGMPPVSFPAVHKPPSSTP-------GSSLPTPPPGLSPLSPqqqvQPSGSPARSLHSQAPTSPRPSLGPSTvgAPQTLP 439
Cdd:PHA03247  2828 LPPPTSAQPTAPPPPPGPPppslplgGSVAPGGDVRRRPPSR----SPAAKPAAPARPPVRRLARPAVSRST--ESFALP 2901

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1757305629  440 RSSLSAFPA-QPPVEELGQEQPQAVALLVSSKPKSAVP 476
Cdd:PHA03247  2902 PDQPERPPQpQAPPPPQPQPQPPPPPQPQPPPPPPPRP 2939
PHA03247 PHA03247
large tegument protein UL36; Provisional
 290-497 8.99e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 8.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  290 PERSQPSLrarqaSLEGATQPHKEWVPKGDGRGSHGPPVSQPVQTLEFTCESPVSAPVSPLEQPPAQPLASSTPLSlsgm 369
Cdd:PHA03247  2843 PGPPPPSL-----PLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQA---- 2913

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  370 PPVSFPAVHKPPSSTPGSSLPTPPPGLSPLSPQQQVQPSGSParslhsqAPTSPRPSLG---PSTVGAPQTL---PRSSL 443
Cdd:PHA03247  2914 PPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEP-------SGAVPQPWLGalvPGRVAVPRFRvpqPAPSR 2986

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629  444 SAfPAQPPVEELGQEQPQ------AVALLVSSKPksavPLVHVKETVSKPYVTESPAEDS 497
Cdd:PHA03247  2987 EA-PASSTPPLTGHSLSRvsswasSLALHEETDP----PPVSLKQTLWPPDDTEDSDADS 3041
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 292-438 1.08e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 41.95  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 292 RSQPSLRARQASLEGATQPHKEWVPKGDGRGSHGPPVSQPVQTLEFTCESP----VSAPVSPLEQPPAQPLASSTPlsls 367
Cdd:pfam09770 204 RAQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQqhpgQGHPVTILQRPQSPQPDPAQP---- 279

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1757305629 368 GMPPVSFPAVHKPPsstPGSSLPT--------PPPGLSPLSPQQQVQPSGSPARSLHSQAPTSPRPslgPSTVGAPQTL 438
Cdd:pfam09770 280 SIQPQAQQFHQQPP---PVPVQPTqilqnpnrLSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQ---APIITHPQQL 352
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 341-496 1.41e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 41.39  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 341 SPVSAPVSPLEQPPAQPLASSTPLSLSGMPPVSFPAVHKPPSSTPgsslptpppglsplspQQQVQPSGSPARSLHSQAP 420
Cdd:PRK07994  363 APLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAP----------------QQAPAVPLPETTSQLLAAR 426

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 421 TSPRPSLGPSTVGAPQtlPRSSLSAFPAQPPVEELGQEQPQAVALLVSSKPKSAV------PLVHVKETVSKPYVTESPA 494
Cdd:PRK07994  427 QQLQRAQGATKAKKSE--PAAASRARPVNSALERLASVRPAPSALEKAPAKKEAYrwkatnPVEVKKEPVATPKALKKAL 504


                  ..
gi 1757305629 495 ED 496
Cdd:PRK07994  505 EH 506
PHA03378 PHA03378
EBNA-3B; Provisional
 352-462 4.79e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.05  E-value: 4.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 352 QPPAQPLASSTPLSLSGMPPVSFPAVHKPPSSTPGSSLPTPPPGLSPLSPQQQVQPSGSPARSLHSQAPTSPRPSLGPST 431
Cdd:PHA03378  668 QIGHIPYQPSPTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPP 747

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1757305629 432 VGAPQTLPRSSLSAFPAQPPVEELG----QEQPQA 462
Cdd:PHA03378  748 AAAPGRARPPAAAPGRARPPAAAPGaptpQPPPQA 782
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 333-450 8.28e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 39.37  E-value: 8.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757305629 333 QTLEFTCESPVSAPVSPLEQPPAQPLASSTPLSLSGMPPVSFPAVHKPPSSTPGSSLPTPPPglsplspqqQVQPSGSPA 412
Cdd:pfam03154 170 QPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLI---------QQTPTLHPQ 240

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1757305629 413 RSLHSQAPTSPRPSLGPSTVGAPQTLPRSSLSAfPAQP 450
Cdd:pfam03154 241 RLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHG-QMPP 277
 
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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