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Conserved domains on  [gi|1510371787|ref|XP_026848433|]
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neuropathy target esterase sws isoform X3 [Drosophila persimilis]

Protein Classification

CAP_ED and Pat_PNPLA6_PNPLA7 domain-containing protein( domain architecture ID 11503664)

CAP_ED and Pat_PNPLA6_PNPLA7 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 905-1210 0e+00

Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like phospholipase domain containing protein 6 (PNPLA6) and protein 7 (PNPLA7) are 60% identical to each other. 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 homologous 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 PNPLA6 and PNPLA7 from Homo sapiens, YMF9 from Yeast, and Swiss Cheese protein (sws) from Drosophila melanogaster.


:

Pssm-ID: 132864 [Multi-domain]  Cd Length: 306  Bit Score: 635.60  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  905 HSDFSRLARWLTGNSIGLVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNITTVTQKAREWSKKM 984
Cdd:cd07225      1 HSDFSRLARVLTGNSIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKDM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  985 TKWFLQLLDLTYPITSMFSGREFNKTIHETFGDVNIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPL 1064
Cdd:cd07225     81 TSIWKKLLDLTYPITSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPPL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787 1065 CDPKDGHLLLDGGYVNNLPADVMHNLGAAHIIAIDVGSQDDTDLTNYGDDLSGWWLLYKKWNPFTAPVKVPDLPDIQSRL 1144
Cdd:cd07225    161 CDPKDGHLLMDGGYINNLPADVARSMGAKTVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLAEKVKVPNMAEIQSRL 240

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1510371787 1145 AYVSCVRQLEEVKNSDYCEYIRPPIDKYKTLAFGSFDEIRDVGYVFGKNYFEGMAKAGRLGRFNQW 1210
Cdd:cd07225    241 AYVSCVRQLEEVKSSDYCEYLRPPIDKYKTLDFGKFDEICEVGYQHGKTVFDGWKRSGVLEKMLQD 306
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 590-689 1.68e-20

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


:

Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 88.15  E-value: 1.68e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  590 ALDWIFLESGRALYRQDESSDSTYIVLSGRMRSVITHPGGKKEIVGEYGKGDLVGIVEMITETSRTTTVMAVRDSELAKL 669
Cdd:cd00038     16 ALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRALTDSELLVL 95

                           90       100
                   ....*....|....*....|
gi 1510371787  670 PEGLFNAIKLRYPIVVTKLI 689
Cdd:cd00038     96 PRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 154-275 1.30e-17

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


:

Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 80.06  E-value: 1.30e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  154 IFGHFEKPIFLRLCKHTQLLELMGGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGESVtsllSFIDVLS 233
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLF----GELALLG 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1510371787  234 GNPSYYktvTAKAIEKSVVIRLPMAAFQEVFKDSPDVMIRVI 275
Cdd:cd00038     77 NGPRSA---TVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 454-580 9.33e-14

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


:

Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 71.56  E-value: 9.33e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  454 GLPEQDAHIIDPFVEVREMEPNVTLITEGNADDvCVWFVMTGTLAVYQGNADATRIkqdktdlLIHYVHPGEIVGGLAML 533
Cdd:COG0664      3 GLSDEELEALLAHLELRTLKKGEVLFREGDPAD-HLYFVLSGLVKLYRISEDGREQ-------ILGFLGPGDFFGELSLL 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1510371787  534 TGEASAYTIRSRNHSRVAFIRRAAIYQIMRQRPRIVLDLGNGVVRRL 580
Cdd:COG0664     75 GGEPSPATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRL 121
 
Name Accession Description Interval E-value
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 905-1210 0e+00

Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like phospholipase domain containing protein 6 (PNPLA6) and protein 7 (PNPLA7) are 60% identical to each other. 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 homologous 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 PNPLA6 and PNPLA7 from Homo sapiens, YMF9 from Yeast, and Swiss Cheese protein (sws) from Drosophila melanogaster.


Pssm-ID: 132864 [Multi-domain]  Cd Length: 306  Bit Score: 635.60  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  905 HSDFSRLARWLTGNSIGLVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNITTVTQKAREWSKKM 984
Cdd:cd07225      1 HSDFSRLARVLTGNSIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKDM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  985 TKWFLQLLDLTYPITSMFSGREFNKTIHETFGDVNIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPL 1064
Cdd:cd07225     81 TSIWKKLLDLTYPITSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPPL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787 1065 CDPKDGHLLLDGGYVNNLPADVMHNLGAAHIIAIDVGSQDDTDLTNYGDDLSGWWLLYKKWNPFTAPVKVPDLPDIQSRL 1144
Cdd:cd07225    161 CDPKDGHLLMDGGYINNLPADVARSMGAKTVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLAEKVKVPNMAEIQSRL 240

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1510371787 1145 AYVSCVRQLEEVKNSDYCEYIRPPIDKYKTLAFGSFDEIRDVGYVFGKNYFEGMAKAGRLGRFNQW 1210
Cdd:cd07225    241 AYVSCVRQLEEVKSSDYCEYLRPPIDKYKTLDFGKFDEICEVGYQHGKTVFDGWKRSGVLEKMLQD 306
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 932-1188 1.09e-46

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 168.54  E-value: 1.09e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  932 AAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNIttvtQKAREWSKKMTKW---------FLQLLDLTYPITSMF 1002
Cdd:COG1752     19 AAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSA----DELEELWRSLDRRdlfdlslprRLLRLDLGLSPGGLL 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787 1003 SGREFNKTIHETFGDVNIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPLcdPKDGHLLLDGGYVNNL 1082
Cdd:COG1752     95 DGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPV--EIDGRLYVDGGVVNNL 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787 1083 PADVMHNLGAAHIIAIDVGSQDDtdltnygddlsgwwllykkwnpftapvKVPDLPDIQSRLAYVSCVRQLEEVKNSDYC 1162
Cdd:COG1752    173 PVDPARALGADRVIAVDLNPPLR---------------------------KLPSLLDILGRALEIMFNSILRRELALEPA 225

                          250       260
                   ....*....|....*....|....*..
gi 1510371787 1163 -EYIRPPIDKYKTLAFGSFDEIRDVGY 1188
Cdd:COG1752    226 dILIEPDLSGISLLDFSRAEELIEAGY 252
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 590-689 1.68e-20

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 88.15  E-value: 1.68e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  590 ALDWIFLESGRALYRQDESSDSTYIVLSGRMRSVITHPGGKKEIVGEYGKGDLVGIVEMITETSRTTTVMAVRDSELAKL 669
Cdd:cd00038     16 ALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRALTDSELLVL 95

                           90       100
                   ....*....|....*....|
gi 1510371787  670 PEGLFNAIKLRYPIVVTKLI 689
Cdd:cd00038     96 PRSDFRRLLQEYPELARRLL 115
PRK10279 PRK10279
patatin-like phospholipase RssA;
920-1108 1.60e-19

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 90.93  E-value: 1.60e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  920 IGLVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERnittvTQKAREWSKKMTKW-FLQLLDLTYPI 998
Cdd:PRK10279     6 IGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDR-----LSALEDWVTSFSYWdVLRLMDLSWQR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  999 TSMFSG-REFNKtIHETFGDVNIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPLcdPKDGHLLLDGG 1077
Cdd:PRK10279    81 GGLLRGeRVFNQ-YREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPV--AHNGYWLVDGA 157

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1510371787 1078 YVNNLPADVMHNLGAAHIIAIDVgsQDDTDL 1108
Cdd:PRK10279   158 VVNPVPVSLTRALGADIVIAVDL--QHDAHL 186
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 922-1086 9.76e-18

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


Pssm-ID: 396341  Cd Length: 190  Bit Score: 82.66  E-value: 9.76e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  922 LVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERN--------ITTVTQKAREWSKKMTKWFLQLLD 993
Cdd:pfam01734    1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDpeeiedllLELDLNLFLSLIRKRALSLLALLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  994 LTYPITSMFSGREFNKTIHETFGDVNIEDLWIPYFTLTTDITASCHRI-----------------HTNGSLWRYVRSSMS 1056
Cdd:pfam01734   81 GLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVistalgtrarillpddlDDDEDLADAVLASSA 160

                          170       180       190
                   ....*....|....*....|....*....|
gi 1510371787 1057 LSGYMPPLcdPKDGHLLLDGGYVNNLPADV 1086
Cdd:pfam01734  161 LPGVFPPV--RLDGELYVDGGLVDNVPVEA 188
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 154-275 1.30e-17

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 80.06  E-value: 1.30e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  154 IFGHFEKPIFLRLCKHTQLLELMGGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGESVtsllSFIDVLS 233
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLF----GELALLG 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1510371787  234 GNPSYYktvTAKAIEKSVVIRLPMAAFQEVFKDSPDVMIRVI 275
Cdd:cd00038     77 NGPRSA---TVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 594-681 1.72e-17

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 78.81  E-value: 1.72e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  594 IFLESGRALYRQDESSDSTYIVLSGRMRSVITHPGGKKEIVGEYGKGDLVGIVEMITETSRTTTVMAVRDSELAKLPEGL 673
Cdd:pfam00027    2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRED 81


                   ....*...
gi 1510371787  674 FNAIKLRY 681
Cdd:pfam00027   82 FLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 596-702 4.13e-16

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 78.49  E-value: 4.13e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  596 LESGRALYRQDESSDSTYIVLSGRMRSVITHPGGKKEIVGEYGKGDLVGIVEMITETSRTTTVMAVRDSELAKLPEGLFN 675
Cdd:COG0664     21 LKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSPATAEALEDSELLRIPREDLE 100

                           90       100
                   ....*....|....*....|....*..
gi 1510371787  676 AIKLRYPIVVTKLISFLSHRFLGSMQT 702
Cdd:COG0664    101 ELLERNPELARALLRLLARRLRQLQER 127
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 155-284 1.10e-15

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 77.33  E-value: 1.10e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  155 FGHFEKPIFLRLCKHTQLLELMGGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGEsvtsLLSFIDVLSG 234
Cdd:COG0664      1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGD----FFGELSLLGG 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1510371787  235 NPSyykTVTAKAIEKSVVIRLPMAAFQEVFKDSPDVMIRVIQVIMIRLQR 284
Cdd:COG0664     77 EPS---PATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQ 123
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 454-580 9.33e-14

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 71.56  E-value: 9.33e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  454 GLPEQDAHIIDPFVEVREMEPNVTLITEGNADDvCVWFVMTGTLAVYQGNADATRIkqdktdlLIHYVHPGEIVGGLAML 533
Cdd:COG0664      3 GLSDEELEALLAHLELRTLKKGEVLFREGDPAD-HLYFVLSGLVKLYRISEDGREQ-------ILGFLGPGDFFGELSLL 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1510371787  534 TGEASAYTIRSRNHSRVAFIRRAAIYQIMRQRPRIVLDLGNGVVRRL 580
Cdd:COG0664     75 GGEPSPATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRL 121
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 454-572 1.77e-13

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 68.12  E-value: 1.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  454 GLPEQDAHIIDPFVEVREMEPNVTLITEGNADDvCVWFVMTGTLAVYQGNADATRIkqdktdlLIHYVHPGEIVGGLAML 533
Cdd:cd00038      4 GLDDEELEELADALEERRFPAGEVIIRQGDPAD-SLYIVLSGSVEVYKLDEDGREQ-------IVGFLGPGDLFGELALL 75

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1510371787  534 TGEASAYTIRSRNHSRVAFIRRAAIYQIMRQRPRIVLDL 572
Cdd:cd00038     76 GNGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 172-267 1.50e-12

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 64.55  E-value: 1.50e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  172 LLELMGGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGEsvtsLLSFIDVLSGNPSyykTVTAKAIEKSV 251
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGD----FFGELALLGGEPR---SATVVALTDSE 73

                           90
                   ....*....|....*.
gi 1510371787  252 VIRLPMAAFQEVFKDS 267
Cdd:pfam00027   74 LLVIPREDFLELLERD 89
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 469-564 4.14e-12

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 63.40  E-value: 4.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  469 VREMEPNVTLITEGNADDvCVWFVMTGTLAVYqgnadatRIKQDKTDLLIHYVHPGEIVGGLAMLTGEASAYTIRSRNHS 548
Cdd:pfam00027    1 LRSYKAGEVIFREGDPAD-SLYIVLSGKVKVY-------RTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDS 72

                           90
                   ....*....|....*.
gi 1510371787  549 RVAFIRRAAIYQIMRQ 564
Cdd:pfam00027   73 ELLVIPREDFLELLER 88
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 590-677 1.63e-10

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 59.72  E-value: 1.63e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787   590 ALDWIFLESGRALYRQDESSDSTYIVLSGRMRSVITHPGGKKEIVGEYGKGDLVGIVEMITETSRTTTVmAVRDSELAKL 669
Cdd:smart00100   16 ALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRRAASA-AAVALELATL 94


                    ....*...
gi 1510371787   670 PEGLFNAI 677
Cdd:smart00100   95 LRIDFRDF 102
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 154-276 2.88e-09

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 56.26  E-value: 2.88e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787   154 IFGHFEKPIFLRLCKHTQLLELMGGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGESVtsllSFIDVLS 233
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFF----GELALLT 76

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 1510371787   234 GNPSYYkTVTAKAIEKSVVIRLPMAAFQEVFKDSPDVMIRVIQ 276
Cdd:smart00100   77 NSRRAA-SAAAVALELATLLRIDFRDFLQLLPELPQLLLELLL 118
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 468-670 1.11e-07

bacteriocin-type transport-associated protein; Members of this protein family are uncharacterized and contain two copies of the cyclic nucleotide-binding domain pfam00027. Members are restricted to select cyanobacteria but are found regularly in association with a transport operon that, in turn, is associated with the production of putative bacteriocins. The models describing the transport operon are TIGR03794, TIGR03796, and TIGR03797.


Pssm-ID: 274839 [Multi-domain]  Cd Length: 317  Bit Score: 55.29  E-value: 1.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  468 EVREMEPNVTLITEGNADDVcVWFVMTGTLAVyqgnadatRIKQDKTDLLIHYVH-----PGEIVGGLAMLTGEASAYTI 542
Cdd:TIGR03896    9 HQREIAAGTTLIEEGKAADF-LFILLDGTFTV--------TTPQPEDNPLTRAFElarlsRGEIVGEMSLLETRPPVATI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  543 RSRNHSRVAFIRRAAI--------------YQIMRQRPRIVLDLGNGVVRRLS-----PLvRQC--------DYALDWIF 595
Cdd:TIGR03896   80 KAVPKSRVMSIPVGELaaklqsdvgfaahfYRAIAIKLALQIQNQNHQLHRRNgadsePL-RKVlfifgelhESDVAWMM 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  596 -------LESGRALYRQDESSDSTYIVLSGRMRSVIThPGGKKEIVGEYGKGDLVGIVEMI-TETSRTTTVMAVRDSELA 667
Cdd:TIGR03896  159 asgtpqkLPAGTILIHEGGTVDALYILLYGEASLSIS-PDGPGREVGSSRRGEILGETPFLnGSLPGTATVKAIENSVLL 237


                   ...
gi 1510371787  668 KLP 670
Cdd:TIGR03896  238 AID 240
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 454-570 4.68e-06

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 47.01  E-value: 4.68e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787   454 GLPEQDAHIIDPFVEVREMEPNVTLITEGN-ADDVCvwFVMTGTLAVYqgnadatRIKQDKTDLLIHYVHPGEIVGGLAM 532
Cdd:smart00100    4 NLDAEELRELADALEPVRYPAGEVIIRQGDvGDSFY--IIVSGEVEVY-------KVLEDGEEQIVGTLGPGDFFGELAL 74

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|
gi 1510371787   533 LTGEASAYTIRSRNHS--RVAFIRRAAIYQIMRQRPRIVL 570
Cdd:smart00100   75 LTNSRRAASAAAVALElaTLLRIDFRDFLQLLPELPQLLL 114
 
Name Accession Description Interval E-value
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 905-1210 0e+00

Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like phospholipase domain containing protein 6 (PNPLA6) and protein 7 (PNPLA7) are 60% identical to each other. 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 homologous 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 PNPLA6 and PNPLA7 from Homo sapiens, YMF9 from Yeast, and Swiss Cheese protein (sws) from Drosophila melanogaster.


Pssm-ID: 132864 [Multi-domain]  Cd Length: 306  Bit Score: 635.60  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  905 HSDFSRLARWLTGNSIGLVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNITTVTQKAREWSKKM 984
Cdd:cd07225      1 HSDFSRLARVLTGNSIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKDM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  985 TKWFLQLLDLTYPITSMFSGREFNKTIHETFGDVNIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPL 1064
Cdd:cd07225     81 TSIWKKLLDLTYPITSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPPL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787 1065 CDPKDGHLLLDGGYVNNLPADVMHNLGAAHIIAIDVGSQDDTDLTNYGDDLSGWWLLYKKWNPFTAPVKVPDLPDIQSRL 1144
Cdd:cd07225    161 CDPKDGHLLMDGGYINNLPADVARSMGAKTVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLAEKVKVPNMAEIQSRL 240

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1510371787 1145 AYVSCVRQLEEVKNSDYCEYIRPPIDKYKTLAFGSFDEIRDVGYVFGKNYFEGMAKAGRLGRFNQW 1210
Cdd:cd07225    241 AYVSCVRQLEEVKSSDYCEYLRPPIDKYKTLDFGKFDEICEVGYQHGKTVFDGWKRSGVLEKMLQD 306
Pat_Fungal_NTE1 cd07227
Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy ...
 910-1180 1.03e-101

Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy Target Esterase (NTE), commonly referred to as NTE1. Patatin-like phospholipase. 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 family includes NTE1 from fungi.


Pssm-ID: 132865 [Multi-domain]  Cd Length: 269  Bit Score: 325.60  E-value: 1.03e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  910 RLARWLTGNSIGLVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNITTVTQKAREWSKKMTKWFL 989
Cdd:cd07227      1 RLARRLCGQAIGLVLGGGGARGISHIGILQALEEAGIPIDAIGGTSIGSFVGGLYAREADLVPIFGRAKKFAGRMASMWR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  990 QLLDLTYPITSMFSGREFNKTIHETFGDVNIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPLCDpkD 1069
Cdd:cd07227     81 FLSDVTYPFASYTTGHEFNRGIWKTFGNTHIEDFWIPFYANSTNITHSRMEIHSSGYAWRYIRASMSLAGLLPPLSD--N 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787 1070 GHLLLDGGYVNNLPADVMHNLGAAHIIAIDVGSQDDTDLTNYGDDLSGWWLLYKKWNPFTAPVKVPDLPDIQSRLAYVSC 1149
Cdd:cd07227    159 GSMLLDGGYMDNLPVSPMRSLGIRDIFAVDVGSVDDRTPMDYGDSVSGVWIFFNRWNPFSSRPNVPSMAEIQSRLTYVSS 238

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1510371787 1150 VRQLEEVKNSDYCEYIRPPIDKYKTLAFGSF 1180
Cdd:cd07227    239 VKTLEKVKATPGCHYMRPPVQDFDTLDFGKF 269
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 920-1100 4.16e-58

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: 198.15  E-value: 4.16e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  920 IGLVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNIttvtQKAREWSKKMTKWFLQLLDLTYPIT 999
Cdd:cd07205      1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAGYSP----EEIEERAKLRSTDLKALSDLTIPTA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787 1000 SMFSGREFNKTIHETFGDVNIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPLCDpkDGHLLLDGGYV 1079
Cdd:cd07205     77 GLLRGDKFLELLDEYFGDRDIEDLWIPFFIVATDLTSGKLVVFRSGSLVRAVRASMSIPGIFPPVKI--DGQLLVDGGVL 154

                          170       180
                   ....*....|....*....|.
gi 1510371787 1080 NNLPADVMHNLGAAHIIAIDV 1100
Cdd:cd07205    155 NNLPVDVLRELGADIIIAVDL 175
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 932-1188 1.09e-46

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 168.54  E-value: 1.09e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  932 AAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNIttvtQKAREWSKKMTKW---------FLQLLDLTYPITSMF 1002
Cdd:COG1752     19 AAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSA----DELEELWRSLDRRdlfdlslprRLLRLDLGLSPGGLL 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787 1003 SGREFNKTIHETFGDVNIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPLcdPKDGHLLLDGGYVNNL 1082
Cdd:COG1752     95 DGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPV--EIDGRLYVDGGVVNNL 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787 1083 PADVMHNLGAAHIIAIDVGSQDDtdltnygddlsgwwllykkwnpftapvKVPDLPDIQSRLAYVSCVRQLEEVKNSDYC 1162
Cdd:COG1752    173 PVDPARALGADRVIAVDLNPPLR---------------------------KLPSLLDILGRALEIMFNSILRRELALEPA 225

                          250       260
                   ....*....|....*....|....*..
gi 1510371787 1163 -EYIRPPIDKYKTLAFGSFDEIRDVGY 1188
Cdd:COG1752    226 dILIEPDLSGISLLDFSRAEELIEAGY 252
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 920-1100 1.74e-35

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: 133.17  E-value: 1.74e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  920 IGLVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNITTVtqkarEWSKKMTKW-FLQLLDLTYPI 998
Cdd:cd07228      1 IGLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYAAGHLDALE-----EWVRSLSQRdVLRLLDLSASR 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  999 TSMFSGREFNKTIHETFGDVNIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPLCDpkDGHLLLDGGY 1078
Cdd:cd07228     76 SGLLKGEKVLEYLREIMGGVTIEELPIPFAAVATDLQTGKEVWFREGSLIDAIRASISIPGIFAPVEH--NGRLLVDGGV 153

                          170       180
                   ....*....|....*....|..
gi 1510371787 1079 VNNLPADVMHNLGAAHIIAIDV 1100
Cdd:cd07228    154 VNPIPVSVARALGADIVIAVDL 175
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 932-1087 1.39e-34

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: 130.54  E-value: 1.39e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  932 AAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNITTVTQKAREWSKKMTKWFlqllDLTYPITSMFSGREFNKTI 1011
Cdd:cd07198     11 IYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASGRDLEEALLLLLRLSREVRLRF----DGAFPPTGRLLGILRQPLL 86

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1510371787 1012 HETFGDVnIEDLWIPYFTLTTDITASCHRIH---TNGSLWRYVRSSMSLSGYMPPLCDPKDGHLLLDGGYVNNLPADVM 1087
Cdd:cd07198     87 SALPDDA-HEDASGKLFISLTRLTDGENVLVsdtSKGELWSAVRASSSIPGYFGPVPLSFRGRRYGDGGLSNNLPVAEL 164
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 590-689 1.68e-20

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 88.15  E-value: 1.68e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  590 ALDWIFLESGRALYRQDESSDSTYIVLSGRMRSVITHPGGKKEIVGEYGKGDLVGIVEMITETSRTTTVMAVRDSELAKL 669
Cdd:cd00038     16 ALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRALTDSELLVL 95

                           90       100
                   ....*....|....*....|
gi 1510371787  670 PEGLFNAIKLRYPIVVTKLI 689
Cdd:cd00038     96 PRSDFRRLLQEYPELARRLL 115
PRK10279 PRK10279
patatin-like phospholipase RssA;
920-1108 1.60e-19

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 90.93  E-value: 1.60e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  920 IGLVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERnittvTQKAREWSKKMTKW-FLQLLDLTYPI 998
Cdd:PRK10279     6 IGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDR-----LSALEDWVTSFSYWdVLRLMDLSWQR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  999 TSMFSG-REFNKtIHETFGDVNIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPLcdPKDGHLLLDGG 1077
Cdd:PRK10279    81 GGLLRGeRVFNQ-YREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPV--AHNGYWLVDGA 157

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1510371787 1078 YVNNLPADVMHNLGAAHIIAIDVgsQDDTDL 1108
Cdd:PRK10279   158 VVNPVPVSLTRALGADIVIAVDL--QHDAHL 186
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 920-1085 4.51e-18

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: 84.70  E-value: 4.51e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  920 IGLVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNITTVTQKArewSKKMTKWFLQLLDLTYPiT 999
Cdd:cd07210      1 FALVLSSGFFGFYAHLGFLAALLEMGLEPSAISGTSAGALVGGLFASGISPDEMAELL---LSLERKDFWMFWDPPLR-G 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787 1000 SMFSGREFNKTIHETFGDVNIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPLcdPKDGHLLLDGGYV 1079
Cdd:cd07210     77 GLLSGDRFAALLREHLPPDRFEELRIPLAVSVVDLTSRETLLLSEGDLAEAVAASCAVPPLFQPV--EIGGRPFVDGGVA 154


                   ....*.
gi 1510371787 1080 NNLPAD 1085
Cdd:cd07210    155 DRLPFD 160
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 922-1086 9.76e-18

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


Pssm-ID: 396341  Cd Length: 190  Bit Score: 82.66  E-value: 9.76e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  922 LVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERN--------ITTVTQKAREWSKKMTKWFLQLLD 993
Cdd:pfam01734    1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDpeeiedllLELDLNLFLSLIRKRALSLLALLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  994 LTYPITSMFSGREFNKTIHETFGDVNIEDLWIPYFTLTTDITASCHRI-----------------HTNGSLWRYVRSSMS 1056
Cdd:pfam01734   81 GLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVistalgtrarillpddlDDDEDLADAVLASSA 160

                          170       180       190
                   ....*....|....*....|....*....|
gi 1510371787 1057 LSGYMPPLcdPKDGHLLLDGGYVNNLPADV 1086
Cdd:pfam01734  161 LPGVFPPV--RLDGELYVDGGLVDNVPVEA 188
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 154-275 1.30e-17

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 80.06  E-value: 1.30e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  154 IFGHFEKPIFLRLCKHTQLLELMGGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGESVtsllSFIDVLS 233
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLF----GELALLG 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1510371787  234 GNPSYYktvTAKAIEKSVVIRLPMAAFQEVFKDSPDVMIRVI 275
Cdd:cd00038     77 NGPRSA---TVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 594-681 1.72e-17

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 78.81  E-value: 1.72e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  594 IFLESGRALYRQDESSDSTYIVLSGRMRSVITHPGGKKEIVGEYGKGDLVGIVEMITETSRTTTVMAVRDSELAKLPEGL 673
Cdd:pfam00027    2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRED 81


                   ....*...
gi 1510371787  674 FNAIKLRY 681
Cdd:pfam00027   82 FLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 596-702 4.13e-16

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 78.49  E-value: 4.13e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  596 LESGRALYRQDESSDSTYIVLSGRMRSVITHPGGKKEIVGEYGKGDLVGIVEMITETSRTTTVMAVRDSELAKLPEGLFN 675
Cdd:COG0664     21 LKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSPATAEALEDSELLRIPREDLE 100

                           90       100
                   ....*....|....*....|....*..
gi 1510371787  676 AIKLRYPIVVTKLISFLSHRFLGSMQT 702
Cdd:COG0664    101 ELLERNPELARALLRLLARRLRQLQER 127
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 155-284 1.10e-15

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 77.33  E-value: 1.10e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  155 FGHFEKPIFLRLCKHTQLLELMGGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGEsvtsLLSFIDVLSG 234
Cdd:COG0664      1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGD----FFGELSLLGG 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1510371787  235 NPSyykTVTAKAIEKSVVIRLPMAAFQEVFKDSPDVMIRVIQVIMIRLQR 284
Cdd:COG0664     77 EPS---PATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQ 123
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 934-1098 2.46e-14

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: 72.06  E-value: 2.46e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  934 HIGMLKAIQEAGI--PIDMVGGVSIGALMGALWcsernittvtqkarewskkmtkwflqlldltYPITSMFSGREFNKTI 1011
Cdd:cd01819     13 HAGVLSALAERGLldCVTYLAGTSGGAWVAATL-------------------------------YPPSSSLDNKPRQSLE 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787 1012 hetfgdvniEDLWIPYFTLTTDITAS----CHRIHTNGSLWRYVRSSMSLSGYMPPLCD----------PKDGHLLLDGG 1077
Cdd:cd01819     62 ---------EALSGKLWVSFTPVTAGenvlVSRFVSKEELIRALFASGSWPSYFGLIPPaelytsksnlKEKGVRLVDGG 132

                          170       180
                   ....*....|....*....|...
gi 1510371787 1078 YVNNLPADVMH--NLGAAHIIAI 1098
Cdd:cd01819    133 VSNNLPAPVLLrpGRGVTLTISP 155
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 454-580 9.33e-14

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 71.56  E-value: 9.33e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  454 GLPEQDAHIIDPFVEVREMEPNVTLITEGNADDvCVWFVMTGTLAVYQGNADATRIkqdktdlLIHYVHPGEIVGGLAML 533
Cdd:COG0664      3 GLSDEELEALLAHLELRTLKKGEVLFREGDPAD-HLYFVLSGLVKLYRISEDGREQ-------ILGFLGPGDFFGELSLL 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1510371787  534 TGEASAYTIRSRNHSRVAFIRRAAIYQIMRQRPRIVLDLGNGVVRRL 580
Cdd:COG0664     75 GGEPSPATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRL 121
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 454-572 1.77e-13

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 68.12  E-value: 1.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  454 GLPEQDAHIIDPFVEVREMEPNVTLITEGNADDvCVWFVMTGTLAVYQGNADATRIkqdktdlLIHYVHPGEIVGGLAML 533
Cdd:cd00038      4 GLDDEELEELADALEERRFPAGEVIIRQGDPAD-SLYIVLSGSVEVYKLDEDGREQ-------IVGFLGPGDLFGELALL 75

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1510371787  534 TGEASAYTIRSRNHSRVAFIRRAAIYQIMRQRPRIVLDL 572
Cdd:cd00038     76 GNGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 922-1102 2.70e-13

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: 70.40  E-value: 2.70e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  922 LVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSerNITTVTQKAREWskkmtkWflqlLDLTYPiTSM 1001
Cdd:cd07209      1 LVLSGGGALGAYQAGVLKALAEAGIEPDIISGTSIGAINGALIAG--GDPEAVERLEKL------W----RELSRE-DVF 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787 1002 FSGREFNKTIHETFGDVNIEDLWIPYFTLTTDiTASCHRI--HTNGSLWRYVRSSMSLsgymPPLCDPK--DGHLLLDGG 1077
Cdd:cd07209     68 LRGLLDRALDFDTLRLLAILFAGLVIVAVNVL-TGEPVYFddIPDGILPEHLLASAAL----PPFFPPVeiDGRYYWDGG 142

                          170       180
                   ....*....|....*....|....*
gi 1510371787 1078 YVNNLPADVMHNLGAAHIIAIDVGS 1102
Cdd:cd07209    143 VVDNTPLSPAIDLGADEIIVVSLSD 167
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 172-267 1.50e-12

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 64.55  E-value: 1.50e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  172 LLELMGGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGEsvtsLLSFIDVLSGNPSyykTVTAKAIEKSV 251
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGD----FFGELALLGGEPR---SATVVALTDSE 73

                           90
                   ....*....|....*.
gi 1510371787  252 VIRLPMAAFQEVFKDS 267
Cdd:pfam00027   74 LLVIPREDFLELLERD 89
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 469-564 4.14e-12

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 63.40  E-value: 4.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  469 VREMEPNVTLITEGNADDvCVWFVMTGTLAVYqgnadatRIKQDKTDLLIHYVHPGEIVGGLAMLTGEASAYTIRSRNHS 548
Cdd:pfam00027    1 LRSYKAGEVIFREGDPAD-SLYIVLSGKVKVY-------RTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDS 72

                           90
                   ....*....|....*.
gi 1510371787  549 RVAFIRRAAIYQIMRQ 564
Cdd:pfam00027   73 ELLVIPREDFLELLER 88
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 590-677 1.63e-10

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 59.72  E-value: 1.63e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787   590 ALDWIFLESGRALYRQDESSDSTYIVLSGRMRSVITHPGGKKEIVGEYGKGDLVGIVEMITETSRTTTVmAVRDSELAKL 669
Cdd:smart00100   16 ALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRRAASA-AAVALELATL 94


                    ....*...
gi 1510371787   670 PEGLFNAI 677
Cdd:smart00100   95 LRIDFRDF 102
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 934-1086 7.60e-10

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: 59.99  E-value: 7.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  934 HIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNITTVTQKARE--WSKKMTK--WFLQLLDLTYPITSMFSGREFNK 1009
Cdd:cd07207     14 YIGALKALEEAGILKKRVAGTSAGAITAALLALGYSAADIKDILKEtdFAKLLDSpvGLLFLLPSLFKEGGLYKGDALEE 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787 1010 TIHETFGDVNI------------EDLWIPYFTLTTDITAS----CHRIHT-NGSLWRYVRSSMSLSGYMPPLCDPKdGHL 1072
Cdd:cd07207     94 WLRELLKEKTGnsfatsllrdldDDLGKDLKVVATDLTTGalvvFSAETTpDMPVAKAVRASMSIPFVFKPVRLAK-GDV 172

                          170
                   ....*....|....
gi 1510371787 1073 LLDGGYVNNLPADV 1086
Cdd:cd07207    173 YVDGGVLDNYPVWL 186
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 154-276 2.88e-09

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 56.26  E-value: 2.88e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787   154 IFGHFEKPIFLRLCKHTQLLELMGGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGESVtsllSFIDVLS 233
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFF----GELALLT 76

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 1510371787   234 GNPSYYkTVTAKAIEKSVVIRLPMAAFQEVFKDSPDVMIRVIQ 276
Cdd:smart00100   77 NSRRAA-SAAAVALELATLLRIDFRDFLQLLPELPQLLLELLL 118
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 468-670 1.11e-07

bacteriocin-type transport-associated protein; Members of this protein family are uncharacterized and contain two copies of the cyclic nucleotide-binding domain pfam00027. Members are restricted to select cyanobacteria but are found regularly in association with a transport operon that, in turn, is associated with the production of putative bacteriocins. The models describing the transport operon are TIGR03794, TIGR03796, and TIGR03797.


Pssm-ID: 274839 [Multi-domain]  Cd Length: 317  Bit Score: 55.29  E-value: 1.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  468 EVREMEPNVTLITEGNADDVcVWFVMTGTLAVyqgnadatRIKQDKTDLLIHYVH-----PGEIVGGLAMLTGEASAYTI 542
Cdd:TIGR03896    9 HQREIAAGTTLIEEGKAADF-LFILLDGTFTV--------TTPQPEDNPLTRAFElarlsRGEIVGEMSLLETRPPVATI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  543 RSRNHSRVAFIRRAAI--------------YQIMRQRPRIVLDLGNGVVRRLS-----PLvRQC--------DYALDWIF 595
Cdd:TIGR03896   80 KAVPKSRVMSIPVGELaaklqsdvgfaahfYRAIAIKLALQIQNQNHQLHRRNgadsePL-RKVlfifgelhESDVAWMM 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  596 -------LESGRALYRQDESSDSTYIVLSGRMRSVIThPGGKKEIVGEYGKGDLVGIVEMI-TETSRTTTVMAVRDSELA 667
Cdd:TIGR03896  159 asgtpqkLPAGTILIHEGGTVDALYILLYGEASLSIS-PDGPGREVGSSRRGEILGETPFLnGSLPGTATVKAIENSVLL 237


                   ...
gi 1510371787  668 KLP 670
Cdd:TIGR03896  238 AID 240
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 454-570 4.68e-06

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 47.01  E-value: 4.68e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787   454 GLPEQDAHIIDPFVEVREMEPNVTLITEGN-ADDVCvwFVMTGTLAVYqgnadatRIKQDKTDLLIHYVHPGEIVGGLAM 532
Cdd:smart00100    4 NLDAEELRELADALEPVRYPAGEVIIRQGDvGDSFY--IIVSGEVEVY-------KVLEDGEEQIVGTLGPGDFFGELAL 74

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|
gi 1510371787   533 LTGEASAYTIRSRNHS--RVAFIRRAAIYQIMRQRPRIVL 570
Cdd:smart00100   75 LTNSRRAASAAAVALElaTLLRIDFRDFLQLLPELPQLLL 114
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
936-1098 2.69e-05

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 47.47  E-value: 2.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787  936 GMLKAIQEAGIPIDMVGGVSIGALMGALWCS---ERN---ITTVTQKARewskkmtkwFLQLLdltypitSMFSGRE-FN 1008
Cdd:COG4667     22 GVLDALLEEGIPFDLVIGVSAGALNGASYLSrqpGRArrvITDYATDPR---------FFSLR-------NFLRGGNlFD 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510371787 1009 K--TIHETFGDVNIEDlWIPYFTLTTDITASCHRIHTN-----------GSLWRYVRSSMSlsgyMPPLCDP--KDGHLL 1073
Cdd:COG4667     86 LdfLYDEIPNELLPFD-FETFKASPREFYVVATNADTGeaeyfskkdddYDLLDALRASSA----LPLLYPPveIDGKRY 160

                          170       180
                   ....*....|....*....|....*
gi 1510371787 1074 LDGGYVNNLPADVMHNLGAAHIIAI 1098
Cdd:COG4667    161 LDGGVADSIPVREAIRDGADKIVVI 185
 
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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