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Conserved domains on  [gi|269969676|sp|B4H3U8|]
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RecName: Full=Neuropathy target esterase sws; AltName: Full=Swiss cheese

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 ...
 927-1236 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: 554.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  927 HSDFSRLARWLTGNSIGLVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNITTVTQKAREWSKKM 1006
Cdd:cd07225     1 HSDFSRLARVLTGNSIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKDM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676 1007 TKWFLQLLDLTYPITSMFSGREFNKTIHETFGDVNIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPL 1086
Cdd:cd07225    81 TSIWKKLLDLTYPITSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676 1087 CDPKDGHLLLDGGYVNNLpghlwrycrasmsiagvfppfcdyrdghllldgcytnnvPADVMHNLGAAHIIAIDVGSQDD 1166
Cdd:cd07225   161 CDPKDGHLLMDGGYINNL---------------------------------------PADVARSMGAKTVIAIDVGSQDE 201

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676 1167 TDLTNYGDDLSGWWLLYKKWNPFTAPVKVPDLPDIQSRLAYVSCVRQLEEVKNSDYCEYIRPLINKYQTL 1236
Cdd:cd07225   202 TDLTNYGDALSGWWLLWKRWNPLAEKVKVPNMAEIQSRLAYVSCVRQLEEVKSSDYCEYLRPPIDKYKTL 271
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 612-711 1.27e-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: 88.54  E-value: 1.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  612 ALDWIFLESGRALYRQDESSDSTYIVLSGRMRSVITHPGGKKEIVGEYGKGDLVGIVEMITETSRTTTVMAVRDSELAKL 691
Cdd:cd00038    16 ALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRALTDSELLVL 95

                          90       100
                  ....*....|....*....|
gi 269969676  692 PEGLFNAIKLRYPIVVTKLI 711
Cdd:cd00038    96 PRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 176-297 9.74e-18

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: 80.45  E-value: 9.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  176 IFGHFEKPIFLRLCKHTQLLELMGGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGESVtsllSFIDVLS 255
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLF----GELALLG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 269969676  256 GNPSYYktvTAKAIEKSVVIRLPMAAFQEVFKDSPDVMIRVI 297
Cdd:cd00038    77 NGPRSA---TVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 476-602 7.16e-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: 71.94  E-value: 7.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  476 GLPEQDAHIIDPFVEVREMEPNVTLITEGNADDvCVWFVMTGTLAVYQGNADATRIkqdktdlLIHYVHPGEIVGGLAML 555
Cdd:COG0664     3 GLSDEELEALLAHLELRTLKKGEVLFREGDPAD-HLYFVLSGLVKLYRISEDGREQ-------ILGFLGPGDFFGELSLL 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 269969676  556 TGEASAYTIRSRNHSRVAFIRRAAIYQIMRQRPRIVLDLGNGVVRRL 602
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 ...
 927-1236 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: 554.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  927 HSDFSRLARWLTGNSIGLVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNITTVTQKAREWSKKM 1006
Cdd:cd07225     1 HSDFSRLARVLTGNSIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKDM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676 1007 TKWFLQLLDLTYPITSMFSGREFNKTIHETFGDVNIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPL 1086
Cdd:cd07225    81 TSIWKKLLDLTYPITSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676 1087 CDPKDGHLLLDGGYVNNLpghlwrycrasmsiagvfppfcdyrdghllldgcytnnvPADVMHNLGAAHIIAIDVGSQDD 1166
Cdd:cd07225   161 CDPKDGHLLMDGGYINNL---------------------------------------PADVARSMGAKTVIAIDVGSQDE 201

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676 1167 TDLTNYGDDLSGWWLLYKKWNPFTAPVKVPDLPDIQSRLAYVSCVRQLEEVKNSDYCEYIRPLINKYQTL 1236
Cdd:cd07225   202 TDLTNYGDALSGWWLLWKRWNPLAEKVKVPNMAEIQSRLAYVSCVRQLEEVKSSDYCEYLRPPIDKYKTL 271
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 956-1166 1.68e-37

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 142.35  E-value: 1.68e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  956 HIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNIttvtQKAREWSKKMTKW---------FLQLLDLTYPITSMFSG 1026
Cdd:COG1752    21 HIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSA----DELEELWRSLDRRdlfdlslprRLLRLDLGLSPGGLLDG 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676 1027 REFNKTIHETFGDVNIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRssmslsgympplcdpkdghllldggyvnnlpg 1106
Cdd:COG1752    97 DPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVR-------------------------------- 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676 1107 hlwrycrASMSIAGVFPPFcdYRDGHLLLDGCYTNNVPADVMHNLGAAHIIAIDVGSQDD 1166
Cdd:COG1752   145 -------ASAAIPGVFPPV--EIDGRLYVDGGVVNNLPVDPARALGADRVIAVDLNPPLR 195
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 612-711 1.27e-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: 88.54  E-value: 1.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  612 ALDWIFLESGRALYRQDESSDSTYIVLSGRMRSVITHPGGKKEIVGEYGKGDLVGIVEMITETSRTTTVMAVRDSELAKL 691
Cdd:cd00038    16 ALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRALTDSELLVL 95

                          90       100
                  ....*....|....*....|
gi 269969676  692 PEGLFNAIKLRYPIVVTKLI 711
Cdd:cd00038    96 PRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 176-297 9.74e-18

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: 80.45  E-value: 9.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  176 IFGHFEKPIFLRLCKHTQLLELMGGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGESVtsllSFIDVLS 255
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLF----GELALLG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 269969676  256 GNPSYYktvTAKAIEKSVVIRLPMAAFQEVFKDSPDVMIRVI 297
Cdd:cd00038    77 NGPRSA---TVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 616-703 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 269969676   616 IFLESGRALYRQDESSDSTYIVLSGRMRSVITHPGGKKEIVGEYGKGDLVGIVEMITETSRTTTVMAVRDSELAKLPEGL 695
Cdd:pfam00027    2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRED 81


                   ....*...
gi 269969676   696 FNAIKLRY 703
Cdd:pfam00027   82 FLELLERD 89
PRK10279 PRK10279
patatin-like phospholipase RssA;
942-1119 3.26e-17

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 83.99  E-value: 3.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  942 IGLVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERnittvTQKAREWSKKMTKW-FLQLLDLTYPI 1020
Cdd:PRK10279    6 IGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDR-----LSALEDWVTSFSYWdVLRLMDLSWQR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676 1021 TSMFSG-REFNKtIHETFGDVNIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPLcdPKDGHLLLDGG 1099
Cdd:PRK10279   81 GGLLRGeRVFNQ-YREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPV--AHNGYWLVDGA 157

                         170       180
                  ....*....|....*....|
gi 269969676 1100 YVNNLPGHLWRYCRASMSIA 1119
Cdd:PRK10279  158 VVNPVPVSLTRALGADIVIA 177
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 944-1105 6.91e-17

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: 80.35  E-value: 6.91e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676   944 LVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERN--------ITTVTQKAREWSKKMTKWFLQLLD 1015
Cdd:pfam01734    1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDpeeiedllLELDLNLFLSLIRKRALSLLALLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  1016 LTYPITSMFSGREFNKTIHETFGDVNIEDLWIPYFTLTTDITASCHRI-----------------HTNGSLWRYVRSSMS 1078
Cdd:pfam01734   81 GLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVistalgtrarillpddlDDDEDLADAVLASSA 160

                          170       180
                   ....*....|....*....|....*..
gi 269969676  1079 LSGYMPPLcdPKDGHLLLDGGYVNNLP 1105
Cdd:pfam01734  161 LPGVFPPV--RLDGELYVDGGLVDNVP 185
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 618-724 3.02e-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: 78.88  E-value: 3.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  618 LESGRALYRQDESSDSTYIVLSGRMRSVITHPGGKKEIVGEYGKGDLVGIVEMITETSRTTTVMAVRDSELAKLPEGLFN 697
Cdd:COG0664    21 LKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSPATAEALEDSELLRIPREDLE 100

                          90       100
                  ....*....|....*....|....*..
gi 269969676  698 AIKLRYPIVVTKLISFLSHRFLGSMQT 724
Cdd:COG0664   101 ELLERNPELARALLRLLARRLRQLQER 127
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 177-306 8.54e-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: 77.72  E-value: 8.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  177 FGHFEKPIFLRLCKHTQLLELMGGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGEsvtsLLSFIDVLSG 256
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGD----FFGELSLLGG 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 269969676  257 NPSyykTVTAKAIEKSVVIRLPMAAFQEVFKDSPDVMIRVIQVIMIRLQR 306
Cdd:COG0664    77 EPS---PATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQ 123
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 476-602 7.16e-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: 71.94  E-value: 7.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  476 GLPEQDAHIIDPFVEVREMEPNVTLITEGNADDvCVWFVMTGTLAVYQGNADATRIkqdktdlLIHYVHPGEIVGGLAML 555
Cdd:COG0664     3 GLSDEELEALLAHLELRTLKKGEVLFREGDPAD-HLYFVLSGLVKLYRISEDGREQ-------ILGFLGPGDFFGELSLL 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 269969676  556 TGEASAYTIRSRNHSRVAFIRRAAIYQIMRQRPRIVLDLGNGVVRRL 602
Cdd:COG0664    75 GGEPSPATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRL 121
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 476-594 1.43e-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: 68.51  E-value: 1.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  476 GLPEQDAHIIDPFVEVREMEPNVTLITEGNADDvCVWFVMTGTLAVYQGNADATRIkqdktdlLIHYVHPGEIVGGLAML 555
Cdd:cd00038     4 GLDDEELEELADALEERRFPAGEVIIRQGDPAD-SLYIVLSGSVEVYKLDEDGREQ-------IVGFLGPGDLFGELALL 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 269969676  556 TGEASAYTIRSRNHSRVAFIRRAAIYQIMRQRPRIVLDL 594
Cdd:cd00038    76 GNGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 194-289 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 269969676   194 LLELMGGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGEsvtsLLSFIDVLSGNPSyykTVTAKAIEKSV 273
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGD----FFGELALLGGEPR---SATVVALTDSE 73

                           90
                   ....*....|....*.
gi 269969676   274 VIRLPMAAFQEVFKDS 289
Cdd:pfam00027   74 LLVIPREDFLELLERD 89
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 491-586 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 269969676   491 VREMEPNVTLITEGNADDvCVWFVMTGTLAVYqgnadatRIKQDKTDLLIHYVHPGEIVGGLAMLTGEASAYTIRSRNHS 570
Cdd:pfam00027    1 LRSYKAGEVIFREGDPAD-SLYIVLSGKVKVY-------RTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDS 72

                           90
                   ....*....|....*.
gi 269969676   571 RVAFIRRAAIYQIMRQ 586
Cdd:pfam00027   73 ELLVIPREDFLELLER 88
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 612-699 1.32e-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: 60.11  E-value: 1.32e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676    612 ALDWIFLESGRALYRQDESSDSTYIVLSGRMRSVITHPGGKKEIVGEYGKGDLVGIVEMITETSRTTTVmAVRDSELAKL 691
Cdd:smart00100   16 ALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRRAASA-AAVALELATL 94


                    ....*...
gi 269969676    692 PEGLFNAI 699
Cdd:smart00100   95 LRIDFRDF 102
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 176-298 2.33e-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: 56.64  E-value: 2.33e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676    176 IFGHFEKPIFLRLCKHTQLLELMGGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGESVtsllSFIDVLS 255
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFF----GELALLT 76

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 269969676    256 GNPSYYkTVTAKAIEKSVVIRLPMAAFQEVFKDSPDVMIRVIQ 298
Cdd:smart00100   77 NSRRAA-SAAAVALELATLLRIDFRDFLQLLPELPQLLLELLL 118
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 490-692 8.21e-08

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: 55.67  E-value: 8.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676   490 EVREMEPNVTLITEGNADDVcVWFVMTGTLAVyqgnadatRIKQDKTDLLIHYVH-----PGEIVGGLAMLTGEASAYTI 564
Cdd:TIGR03896    9 HQREIAAGTTLIEEGKAADF-LFILLDGTFTV--------TTPQPEDNPLTRAFElarlsRGEIVGEMSLLETRPPVATI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676   565 RSRNHSRVAFIRRAAI--------------YQIMRQRPRIVLDLGNGVVRRLS-----PLvRQC--------DYALDWIF 617
Cdd:TIGR03896   80 KAVPKSRVMSIPVGELaaklqsdvgfaahfYRAIAIKLALQIQNQNHQLHRRNgadsePL-RKVlfifgelhESDVAWMM 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676   618 -------LESGRALYRQDESSDSTYIVLSGRMRSVIThPGGKKEIVGEYGKGDLVGIVEMI-TETSRTTTVMAVRDSELA 689
Cdd:TIGR03896  159 asgtpqkLPAGTILIHEGGTVDALYILLYGEASLSIS-PDGPGREVGSSRRGEILGETPFLnGSLPGTATVKAIENSVLL 237


                   ...
gi 269969676   690 KLP 692
Cdd:TIGR03896  238 AID 240
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 476-592 3.61e-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: 47.40  E-value: 3.61e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676    476 GLPEQDAHIIDPFVEVREMEPNVTLITEGN-ADDVCvwFVMTGTLAVYqgnadatRIKQDKTDLLIHYVHPGEIVGGLAM 554
Cdd:smart00100    4 NLDAEELRELADALEPVRYPAGEVIIRQGDvGDSFY--IIVSGEVEVY-------KVLEDGEEQIVGTLGPGDFFGELAL 74

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|
gi 269969676    555 LTGEASAYTIRSRNHS--RVAFIRRAAIYQIMRQRPRIVL 592
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 ...
 927-1236 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: 554.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  927 HSDFSRLARWLTGNSIGLVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNITTVTQKAREWSKKM 1006
Cdd:cd07225     1 HSDFSRLARVLTGNSIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKDM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676 1007 TKWFLQLLDLTYPITSMFSGREFNKTIHETFGDVNIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPL 1086
Cdd:cd07225    81 TSIWKKLLDLTYPITSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676 1087 CDPKDGHLLLDGGYVNNLpghlwrycrasmsiagvfppfcdyrdghllldgcytnnvPADVMHNLGAAHIIAIDVGSQDD 1166
Cdd:cd07225   161 CDPKDGHLLMDGGYINNL---------------------------------------PADVARSMGAKTVIAIDVGSQDE 201

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676 1167 TDLTNYGDDLSGWWLLYKKWNPFTAPVKVPDLPDIQSRLAYVSCVRQLEEVKNSDYCEYIRPLINKYQTL 1236
Cdd:cd07225   202 TDLTNYGDALSGWWLLWKRWNPLAEKVKVPNMAEIQSRLAYVSCVRQLEEVKSSDYCEYLRPPIDKYKTL 271
Pat_Fungal_NTE1 cd07227
Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy ...
 932-1236 4.00e-90

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: 293.25  E-value: 4.00e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  932 RLARWLTGNSIGLVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNITTVTQKAREWSKKMTKWFL 1011
Cdd:cd07227     1 RLARRLCGQAIGLVLGGGGARGISHIGILQALEEAGIPIDAIGGTSIGSFVGGLYAREADLVPIFGRAKKFAGRMASMWR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676 1012 QLLDLTYPITSMFSGREFNKTIHETFGDVNIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPLCDpkD 1091
Cdd:cd07227    81 FLSDVTYPFASYTTGHEFNRGIWKTFGNTHIEDFWIPFYANSTNITHSRMEIHSSGYAWRYIRASMSLAGLLPPLSD--N 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676 1092 GHLLLDGGYVNNLPghlwrycrasmsiagVFPpfcdyrdghllldgcytnnvpadvMHNLGAAHIIAIDVGSQDDTDLTN 1171
Cdd:cd07227   159 GSMLLDGGYMDNLP---------------VSP------------------------MRSLGIRDIFAVDVGSVDDRTPMD 199

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269969676 1172 YGDDLSGWWLLYKKWNPFTAPVKVPDLPDIQSRLAYVSCVRQLEEVKNSDYCEYIRPLINKYQTL 1236
Cdd:cd07227   200 YGDSVSGVWIFFNRWNPFSSRPNVPSMAEIQSRLTYVSSVKTLEKVKATPGCHYMRPPVQDFDTL 264
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 942-1161 7.47e-53

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: 183.13  E-value: 7.47e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  942 IGLVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNIttvtQKAREWSKKMTKWFLQLLDLTYPIT 1021
Cdd:cd07205     1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAGYSP----EEIEERAKLRSTDLKALSDLTIPTA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676 1022 SMFSGREFNKTIHETFGDVNIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVrssmslsgympplcdpkdghllldggyv 1101
Cdd:cd07205    77 GLLRGDKFLELLDEYFGDRDIEDLWIPFFIVATDLTSGKLVVFRSGSLVRAV---------------------------- 128

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676 1102 nnlpghlwrycRASMSIAGVFPPFCDyrDGHLLLDGCYTNNVPADVMHNLGAAHIIAIDV 1161
Cdd:cd07205   129 -----------RASMSIPGIFPPVKI--DGQLLVDGGVLNNLPVDVLRELGADIIIAVDL 175
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 956-1166 1.68e-37

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 142.35  E-value: 1.68e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  956 HIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNIttvtQKAREWSKKMTKW---------FLQLLDLTYPITSMFSG 1026
Cdd:COG1752    21 HIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSA----DELEELWRSLDRRdlfdlslprRLLRLDLGLSPGGLLDG 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676 1027 REFNKTIHETFGDVNIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRssmslsgympplcdpkdghllldggyvnnlpg 1106
Cdd:COG1752    97 DPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVR-------------------------------- 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676 1107 hlwrycrASMSIAGVFPPFcdYRDGHLLLDGCYTNNVPADVMHNLGAAHIIAIDVGSQDD 1166
Cdd:COG1752   145 -------ASAAIPGVFPPV--EIDGRLYVDGGVVNNLPVDPARALGADRVIAVDLNPPLR 195
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 954-1105 1.01e-33

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: 128.23  E-value: 1.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  954 AAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNITTVTQKAREWSKKMTKWFlqllDLTYPITSMFSGREFNKTI 1033
Cdd:cd07198    11 IYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASGRDLEEALLLLLRLSREVRLRF----DGAFPPTGRLLGILRQPLL 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269969676 1034 HETFGDVnIEDLWIPYFTLTTDITASCHRIH---TNGSLWRYVRSSMSLSGYMPPLCDPKDGHLLLDGGYVNNLP 1105
Cdd:cd07198    87 SALPDDA-HEDASGKLFISLTRLTDGENVLVsdtSKGELWSAVRASSSIPGYFGPVPLSFRGRRYGDGGLSNNLP 160
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 942-1119 1.77e-30

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: 118.92  E-value: 1.77e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  942 IGLVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNITTVtqkarEWSKKMTKW-FLQLLDLTYPI 1020
Cdd:cd07228     1 IGLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYAAGHLDALE-----EWVRSLSQRdVLRLLDLSASR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676 1021 TSMFSGREFNKTIHETFGDVNIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPLCDpkDGHLLLDGGY 1100
Cdd:cd07228    76 SGLLKGEKVLEYLREIMGGVTIEELPIPFAAVATDLQTGKEVWFREGSLIDAIRASISIPGIFAPVEH--NGRLLVDGGV 153

                         170
                  ....*....|....*....
gi 269969676 1101 VNNLPGHLWRYCRASMSIA 1119
Cdd:cd07228   154 VNPIPVSVARALGADIVIA 172
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 956-1148 1.68e-27

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: 110.12  E-value: 1.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  956 HIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNITTVTQKAREWSKKMTKWFlqllDLTYPITSMFSGREFNKTIHE 1035
Cdd:cd07198    13 HVGVAKALRERGPLIDIIAGTSAGAIVAALLASGRDLEEALLLLLRLSREVRLRF----DGAFPPTGRLLGILRQPLLSA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676 1036 TFGDVnIEDLWIPYFTLTTDITAschrihtngslwryvrssmslsGYMPPLCDPKDGHLlldggyvnnlpghlWRYCRAS 1115
Cdd:cd07198    89 LPDDA-HEDASGKLFISLTRLTD----------------------GENVLVSDTSKGEL--------------WSAVRAS 131

                         170       180       190
                  ....*....|....*....|....*....|...
gi 269969676 1116 MSIAGVFPPFCDYRDGHLLLDGCYTNNVPADVM 1148
Cdd:cd07198   132 SSIPGYFGPVPLSFRGRRYGDGGLSNNLPVAEL 164
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 612-711 1.27e-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: 88.54  E-value: 1.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  612 ALDWIFLESGRALYRQDESSDSTYIVLSGRMRSVITHPGGKKEIVGEYGKGDLVGIVEMITETSRTTTVMAVRDSELAKL 691
Cdd:cd00038    16 ALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRALTDSELLVL 95

                          90       100
                  ....*....|....*....|
gi 269969676  692 PEGLFNAIKLRYPIVVTKLI 711
Cdd:cd00038    96 PRSDFRRLLQEYPELARRLL 115
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 942-1111 3.18e-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: 85.09  E-value: 3.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  942 IGLVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNITTVTQKArewSKKMTKWFLQLLDLTYPiT 1021
Cdd:cd07210     1 FALVLSSGFFGFYAHLGFLAALLEMGLEPSAISGTSAGALVGGLFASGISPDEMAELL---LSLERKDFWMFWDPPLR-G 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676 1022 SMFSGREFNKTIHETFGDVNIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPLcdPKDGHLLLDGGYV 1101
Cdd:cd07210    77 GLLSGDRFAALLREHLPPDRFEELRIPLAVSVVDLTSRETLLLSEGDLAEAVAASCAVPPLFQPV--EIGGRPFVDGGVA 154

                         170
                  ....*....|
gi 269969676 1102 NNLPGHLWRY 1111
Cdd:cd07210   155 DRLPFDALRP 164
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 176-297 9.74e-18

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: 80.45  E-value: 9.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  176 IFGHFEKPIFLRLCKHTQLLELMGGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGESVtsllSFIDVLS 255
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLF----GELALLG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 269969676  256 GNPSYYktvTAKAIEKSVVIRLPMAAFQEVFKDSPDVMIRVI 297
Cdd:cd00038    77 NGPRSA---TVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 616-703 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 269969676   616 IFLESGRALYRQDESSDSTYIVLSGRMRSVITHPGGKKEIVGEYGKGDLVGIVEMITETSRTTTVMAVRDSELAKLPEGL 695
Cdd:pfam00027    2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRED 81


                   ....*...
gi 269969676   696 FNAIKLRY 703
Cdd:pfam00027   82 FLELLERD 89
PRK10279 PRK10279
patatin-like phospholipase RssA;
942-1119 3.26e-17

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 83.99  E-value: 3.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  942 IGLVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERnittvTQKAREWSKKMTKW-FLQLLDLTYPI 1020
Cdd:PRK10279    6 IGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDR-----LSALEDWVTSFSYWdVLRLMDLSWQR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676 1021 TSMFSG-REFNKtIHETFGDVNIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPLcdPKDGHLLLDGG 1099
Cdd:PRK10279   81 GGLLRGeRVFNQ-YREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPV--AHNGYWLVDGA 157

                         170       180
                  ....*....|....*....|
gi 269969676 1100 YVNNLPGHLWRYCRASMSIA 1119
Cdd:PRK10279  158 VVNPVPVSLTRALGADIVIA 177
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 944-1105 6.91e-17

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: 80.35  E-value: 6.91e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676   944 LVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERN--------ITTVTQKAREWSKKMTKWFLQLLD 1015
Cdd:pfam01734    1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDpeeiedllLELDLNLFLSLIRKRALSLLALLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  1016 LTYPITSMFSGREFNKTIHETFGDVNIEDLWIPYFTLTTDITASCHRI-----------------HTNGSLWRYVRSSMS 1078
Cdd:pfam01734   81 GLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVistalgtrarillpddlDDDEDLADAVLASSA 160

                          170       180
                   ....*....|....*....|....*..
gi 269969676  1079 LSGYMPPLcdPKDGHLLLDGGYVNNLP 1105
Cdd:pfam01734  161 LPGVFPPV--RLDGELYVDGGLVDNVP 185
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 618-724 3.02e-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: 78.88  E-value: 3.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  618 LESGRALYRQDESSDSTYIVLSGRMRSVITHPGGKKEIVGEYGKGDLVGIVEMITETSRTTTVMAVRDSELAKLPEGLFN 697
Cdd:COG0664    21 LKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSPATAEALEDSELLRIPREDLE 100

                          90       100
                  ....*....|....*....|....*..
gi 269969676  698 AIKLRYPIVVTKLISFLSHRFLGSMQT 724
Cdd:COG0664   101 ELLERNPELARALLRLLARRLRQLQER 127
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 177-306 8.54e-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: 77.72  E-value: 8.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  177 FGHFEKPIFLRLCKHTQLLELMGGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGEsvtsLLSFIDVLSG 256
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGD----FFGELSLLGG 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 269969676  257 NPSyykTVTAKAIEKSVVIRLPMAAFQEVFKDSPDVMIRVIQVIMIRLQR 306
Cdd:COG0664    77 EPS---PATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQ 123
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 476-602 7.16e-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: 71.94  E-value: 7.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  476 GLPEQDAHIIDPFVEVREMEPNVTLITEGNADDvCVWFVMTGTLAVYQGNADATRIkqdktdlLIHYVHPGEIVGGLAML 555
Cdd:COG0664     3 GLSDEELEALLAHLELRTLKKGEVLFREGDPAD-HLYFVLSGLVKLYRISEDGREQ-------ILGFLGPGDFFGELSLL 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 269969676  556 TGEASAYTIRSRNHSRVAFIRRAAIYQIMRQRPRIVLDLGNGVVRRL 602
Cdd:COG0664    75 GGEPSPATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRL 121
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 476-594 1.43e-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: 68.51  E-value: 1.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  476 GLPEQDAHIIDPFVEVREMEPNVTLITEGNADDvCVWFVMTGTLAVYQGNADATRIkqdktdlLIHYVHPGEIVGGLAML 555
Cdd:cd00038     4 GLDDEELEELADALEERRFPAGEVIIRQGDPAD-SLYIVLSGSVEVYKLDEDGREQ-------IVGFLGPGDLFGELALL 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 269969676  556 TGEASAYTIRSRNHSRVAFIRRAAIYQIMRQRPRIVLDL 594
Cdd:cd00038    76 GNGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 956-1163 1.76e-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: 71.17  E-value: 1.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  956 HIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSerNITTVTQKAREWSKKMTK---WFLQLLDlTYPItsmfsgreFNKt 1032
Cdd:cd07209    13 QAGVLKALAEAGIEPDIISGTSIGAINGALIAG--GDPEAVERLEKLWRELSRedvFLRGLLD-RALD--------FDT- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676 1033 ihetfgdvnIEDLWIPYFTLTtdITAschrihTNGSLWRYVRSSMSLSGYMPPlcdpkdgHLLldggyvnnlpghlwryc 1112
Cdd:cd07209    81 ---------LRLLAILFAGLV--IVA------VNVLTGEPVYFDDIPDGILPE-------HLL----------------- 119

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 269969676 1113 rASMSIAGVFPPfcDYRDGHLLLDGCYTNNVPADVMHNLGAAHIIAIDVGS 1163
Cdd:cd07209   120 -ASAALPPFFPP--VEIDGRYYWDGGVVDNTPLSPAIDLGADEIIVVSLSD 167
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 194-289 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 269969676   194 LLELMGGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGEsvtsLLSFIDVLSGNPSyykTVTAKAIEKSV 273
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGD----FFGELALLGGEPR---SATVVALTDSE 73

                           90
                   ....*....|....*.
gi 269969676   274 VIRLPMAAFQEVFKDS 289
Cdd:pfam00027   74 LLVIPREDFLELLERD 89
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 491-586 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 269969676   491 VREMEPNVTLITEGNADDvCVWFVMTGTLAVYqgnadatRIKQDKTDLLIHYVHPGEIVGGLAMLTGEASAYTIRSRNHS 570
Cdd:pfam00027    1 LRSYKAGEVIFREGDPAD-SLYIVLSGKVKVY-------RTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDS 72

                           90
                   ....*....|....*.
gi 269969676   571 RVAFIRRAAIYQIMRQ 586
Cdd:pfam00027   73 ELLVIPREDFLELLER 88
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 956-1105 6.58e-12

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: 65.13  E-value: 6.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  956 HIGMLKAIQEAGI--PIDMVGGVSIGALMGALWcsernittvtqkarewskkmtkwflqlldltYPITSMFSGREFNKTI 1033
Cdd:cd01819    13 HAGVLSALAERGLldCVTYLAGTSGGAWVAATL-------------------------------YPPSSSLDNKPRQSLE 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676 1034 hetfgdvniEDLWIPYFTLTTDITAS----CHRIHTNGSLWRYVRSSMSLSGYMPPLCD----------PKDGHLLLDGG 1099
Cdd:cd01819    62 ---------EALSGKLWVSFTPVTAGenvlVSRFVSKEELIRALFASGSWPSYFGLIPPaelytsksnlKEKGVRLVDGG 132


                  ....*.
gi 269969676 1100 YVNNLP 1105
Cdd:cd01819   133 VSNNLP 138
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 612-699 1.32e-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: 60.11  E-value: 1.32e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676    612 ALDWIFLESGRALYRQDESSDSTYIVLSGRMRSVITHPGGKKEIVGEYGKGDLVGIVEMITETSRTTTVmAVRDSELAKL 691
Cdd:smart00100   16 ALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRRAASA-AAVALELATL 94


                    ....*...
gi 269969676    692 PEGLFNAI 699
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 ...
 956-1109 2.00e-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: 61.53  E-value: 2.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  956 HIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNITTVTQKARE--WSKKMTK--WFLQLLDLTYPITSMFSGREFNK 1031
Cdd:cd07207    14 YIGALKALEEAGILKKRVAGTSAGAITAALLALGYSAADIKDILKEtdFAKLLDSpvGLLFLLPSLFKEGGLYKGDALEE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676 1032 TIHETFGDVNI------------EDLWIPYFTLTTDITAS----CHRIHT-NGSLWRYVRSSMSLSGYMPPLCDPKdGHL 1094
Cdd:cd07207    94 WLRELLKEKTGnsfatsllrdldDDLGKDLKVVATDLTTGalvvFSAETTpDMPVAKAVRASMSIPFVFKPVRLAK-GDV 172

                         170
                  ....*....|....*
gi 269969676 1095 LLDGGYVNNLPGHLW 1109
Cdd:cd07207   173 YVDGGVLDNYPVWLF 187
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 176-298 2.33e-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: 56.64  E-value: 2.33e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676    176 IFGHFEKPIFLRLCKHTQLLELMGGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGESVtsllSFIDVLS 255
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFF----GELALLT 76

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 269969676    256 GNPSYYkTVTAKAIEKSVVIRLPMAAFQEVFKDSPDVMIRVIQ 298
Cdd:smart00100   77 NSRRAA-SAAAVALELATLLRIDFRDFLQLLPELPQLLLELLL 118
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 490-692 8.21e-08

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: 55.67  E-value: 8.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676   490 EVREMEPNVTLITEGNADDVcVWFVMTGTLAVyqgnadatRIKQDKTDLLIHYVH-----PGEIVGGLAMLTGEASAYTI 564
Cdd:TIGR03896    9 HQREIAAGTTLIEEGKAADF-LFILLDGTFTV--------TTPQPEDNPLTRAFElarlsRGEIVGEMSLLETRPPVATI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676   565 RSRNHSRVAFIRRAAI--------------YQIMRQRPRIVLDLGNGVVRRLS-----PLvRQC--------DYALDWIF 617
Cdd:TIGR03896   80 KAVPKSRVMSIPVGELaaklqsdvgfaahfYRAIAIKLALQIQNQNHQLHRRNgadsePL-RKVlfifgelhESDVAWMM 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676   618 -------LESGRALYRQDESSDSTYIVLSGRMRSVIThPGGKKEIVGEYGKGDLVGIVEMI-TETSRTTTVMAVRDSELA 689
Cdd:TIGR03896  159 asgtpqkLPAGTILIHEGGTVDALYILLYGEASLSIS-PDGPGREVGSSRRGEILGETPFLnGSLPGTATVKAIENSVLL 237


                   ...
gi 269969676   690 KLP 692
Cdd:TIGR03896  238 AID 240
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 476-592 3.61e-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: 47.40  E-value: 3.61e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676    476 GLPEQDAHIIDPFVEVREMEPNVTLITEGN-ADDVCvwFVMTGTLAVYqgnadatRIKQDKTDLLIHYVHPGEIVGGLAM 554
Cdd:smart00100    4 NLDAEELRELADALEPVRYPAGEVIIRQGDvGDSFY--IIVSGEVEVY-------KVLEDGEEQIVGTLGPGDFFGELAL 74

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|
gi 269969676    555 LTGEASAYTIRSRNHS--RVAFIRRAAIYQIMRQRPRIVL 592
Cdd:smart00100   75 LTNSRRAASAAAVALElaTLLRIDFRDFLQLLPELPQLLL 114
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
958-1159 5.16e-03

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 40.53  E-value: 5.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676  958 GMLKAIQEAGIPIDMVGGVSIGALMGALWCS---ERN---ITTVTQKARewskkmtkwFLQLLdltypitSMFSGRE-FN 1030
Cdd:COG4667    22 GVLDALLEEGIPFDLVIGVSAGALNGASYLSrqpGRArrvITDYATDPR---------FFSLR-------NFLRGGNlFD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269969676 1031 K--TIHETFGDVNIEDlWIPYFTLTTDITASCHRIHTNgslwryvrssmsLSGYMPPLCDPKDghllldggyvnnlpghL 1108
Cdd:COG4667    86 LdfLYDEIPNELLPFD-FETFKASPREFYVVATNADTG------------EAEYFSKKDDDYD----------------L 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 269969676 1109 WRYCRASMSIAGVFPPFcdYRDGHLLLDGCYTNNVPADVMHNLGAAHIIAI 1159
Cdd:COG4667   137 LDALRASSALPLLYPPV--EIDGKRYLDGGVADSIPVREAIRDGADKIVVI 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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