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Conserved domains on  [gi|1239920273|ref|XP_022279214|]
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patatin-like phospholipase domain-containing protein 7 isoform X2 [Canis lupus familiaris]

Protein Classification

cyclic nucleotide-binding domain-containing protein( domain architecture ID 10186569)

cyclic nucleotide-binding domain-containing protein binds cyclic nucleotides (cAMP or cGMP) where binding of the effector leads to conformational changes; may be involved in regulating transcription, be present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK), or be part of vertebrate cyclic nucleotide-gated ion-channels.

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 ...
 946-1251 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: 691.07  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  946 HSDFSRLARVLTGNAIALVLGGGGARGCAQVGIIRALAECGIPVDMVGGTSIGAFMGALYSEERNYSQIRIRAKEWAEDM 1025
Cdd:cd07225      1 HSDFSRLARVLTGNSIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKDM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273 1026 TSMVKTVLDLTYPITSMFSGAGFNSSICNVFKDRQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPL 1105
Cdd:cd07225     81 TSIWKKLLDLTYPITSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPPL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273 1106 CDPKDGHLLMDGGYINNLPADVARSMGAKVVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLATKVKVLNMAEIQTRL 1185
Cdd:cd07225    161 CDPKDGHLLMDGGYINNLPADVARSMGAKTVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLAEKVKVPNMAEIQSRL 240

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239920273 1186 AYVCCVRQLEMVKNSEYCEYLRPPIDSYRTLDFGKFNEICEVGYQHGRTVFDIWGRSGVLEKMLQD 1251
Cdd:cd07225    241 AYVSCVRQLEEVKSSDYCEYLRPPIDKYKTLDFGKFDEICEVGYQHGKTVFDGWKRSGVLEKMLQD 306
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 620-728 1.96e-21

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: 90.85  E-value: 1.96e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  620 SSFVRQIDFALDWMEVEAGRAVYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLIGVVETLTHQARATTVHA 699
Cdd:cd00038      7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRA 86

                           90       100
                   ....*....|....*....|....*....
gi 1239920273  700 VRDSELAKLPAGALTSIKRRYPQVVTRLI 728
Cdd:cd00038     87 LTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 183-304 1.64e-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: 79.68  E-value: 1.64e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  183 VLGHFEKPLFLELCKHMVFVQLLEGEHVFQPGEPDTSIYVVQDGRLEVCIQDADGSEVAVKEVLAGDSVhSLLSILDVIT 262
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLF-GELALLGNGP 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1239920273  263 gHTApyktvSARAAVPSTVLRLPAVAFQGVFEKYPETLVRVV 304
Cdd:cd00038     80 -RSA-----TVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 497-605 2.77e-16

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: 76.21  E-value: 2.77e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  497 LLTLMKLDDPSLLDGRVTLLHVPGGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEdTCLFVVRPGEIVGQLAVLTGEP 576
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGRE-QIVGFLGPGDLFGELALLGNGP 79

                           90       100
                   ....*....|....*....|....*....
gi 1239920273  577 LIFTIKANRDCSFLSISKAHFYEIMRKQP 605
Cdd:cd00038     80 RSATVRALTDSELLVLPRSDFRRLLQEYP 108
TM_EGFR-like cd12087
Transmembrane domain of the Epidermal Growth Factor Receptor family of Protein Tyrosine ...
 42-79 1.46e-04

Transmembrane domain of the Epidermal Growth Factor Receptor family of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane (TM) helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. They are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. The TM domain not only serves as a membrane anchor, but also plays an important role in receptor dimerization and optimal activation. Mutations in the TM domain of EGFR family RTKs have been associated with increased breast cancer risk.


:

Pssm-ID: 213052  Cd Length: 38  Bit Score: 40.21  E-value: 1.46e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1239920273   42 RHSQSTMLLGIVIGALLALALVGITVFFVYRRVNRFRQ 79
Cdd:cd12087      1 RTSKTTSIAAGVVGGLLVLVILGLIVFLFRRRRHIKRK 38
 
Name Accession Description Interval E-value
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 946-1251 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: 691.07  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  946 HSDFSRLARVLTGNAIALVLGGGGARGCAQVGIIRALAECGIPVDMVGGTSIGAFMGALYSEERNYSQIRIRAKEWAEDM 1025
Cdd:cd07225      1 HSDFSRLARVLTGNSIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKDM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273 1026 TSMVKTVLDLTYPITSMFSGAGFNSSICNVFKDRQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPL 1105
Cdd:cd07225     81 TSIWKKLLDLTYPITSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPPL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273 1106 CDPKDGHLLMDGGYINNLPADVARSMGAKVVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLATKVKVLNMAEIQTRL 1185
Cdd:cd07225    161 CDPKDGHLLMDGGYINNLPADVARSMGAKTVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLAEKVKVPNMAEIQSRL 240

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239920273 1186 AYVCCVRQLEMVKNSEYCEYLRPPIDSYRTLDFGKFNEICEVGYQHGRTVFDIWGRSGVLEKMLQD 1251
Cdd:cd07225    241 AYVSCVRQLEEVKSSDYCEYLRPPIDKYKTLDFGKFDEICEVGYQHGKTVFDGWKRSGVLEKMLQD 306
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 961-1237 9.94e-58

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 200.51  E-value: 9.94e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  961 IALVLGGGGARGCAQVGIIRALAECGIPVDMVGGTSIGAFMGALYSEERNYSQIR-----IRAKEWAEDMTSMVKTVLDL 1035
Cdd:COG1752      7 IGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADELEelwrsLDRRDLFDLSLPRRLLRLDL 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273 1036 TYPITSMFSGAGFNSSICNVFKDRQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLcdPKDGHLLM 1115
Cdd:COG1752     87 GLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPV--EIDGRLYV 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273 1116 DGGYINNLPADVARSMGAKVVIAIDVGSQDEtdltnygdalsgwwllwkrwnplatkvKVLNMAEIQTRLAYVCCVRQLE 1195
Cdd:COG1752    165 DGGVVNNLPVDPARALGADRVIAVDLNPPLR---------------------------KLPSLLDILGRALEIMFNSILR 217

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1239920273 1196 MVKNSEYC-EYLRPPIDSYRTLDFGKFNEICEVGYQHGRTVFD 1237
Cdd:COG1752    218 RELALEPAdILIEPDLSGISLLDFSRAEELIEAGYEAARRALD 260
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 963-1128 1.53e-25

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: 105.38  E-value: 1.53e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  963 LVLGGGGARGCAQVGIIRALAECGIPVDMVGGTSIGAFMGALYS--------EERNYSQIRIRAKEWAEDMTSMVKTVLD 1034
Cdd:pfam01734    1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLAlgrdpeeiEDLLLELDLNLFLSLIRKRALSLLALLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273 1035 LTYPITSMFSGAGFNSSICNVFKDRQIEDLWIPYFTI-----------------TTDITASAMRVHTDGSLWRYVRASMS 1097
Cdd:pfam01734   81 GLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLlvvalralltvistalgTRARILLPDDLDDDEDLADAVLASSA 160

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1239920273 1098 LSGYMPPLcdPKDGHLLMDGGYINNLPADVA 1128
Cdd:pfam01734  161 LPGVFPPV--RLDGELYVDGGLVDNVPVEAA 189
PRK10279 PRK10279
patatin-like phospholipase RssA;
961-1140 2.40e-24

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 105.18  E-value: 2.40e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  961 IALVLGGGGARGCAQVGIIRALAECGIPVDMVGGTSIGAFMGALYSEERNYSQiriraKEWAEDMTSM-VKTVLDLTYPI 1039
Cdd:PRK10279     6 IGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRLSAL-----EDWVTSFSYWdVLRLMDLSWQR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273 1040 TSMFSGAGFNSSICNVFKDRQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLcdPKDGHLLMDGGY 1119
Cdd:PRK10279    81 GGLLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPV--AHNGYWLVDGAV 158

                          170       180
                   ....*....|....*....|.
gi 1239920273 1120 INNLPADVARSMGAKVVIAID 1140
Cdd:PRK10279   159 VNPVPVSLTRALGADIVIAVD 179
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 620-728 1.96e-21

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: 90.85  E-value: 1.96e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  620 SSFVRQIDFALDWMEVEAGRAVYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLIGVVETLTHQARATTVHA 699
Cdd:cd00038      7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRA 86

                           90       100
                   ....*....|....*....|....*....
gi 1239920273  700 VRDSELAKLPAGALTSIKRRYPQVVTRLI 728
Cdd:cd00038     87 LTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 633-720 4.57e-18

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: 80.35  E-value: 4.57e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  633 MEVEAGRAVYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLIGVVETLTHQARATTVHAVRDSELAKLPAGA 712
Cdd:pfam00027    2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRED 81


                   ....*...
gi 1239920273  713 LTSIKRRY 720
Cdd:pfam00027   82 FLELLERD 89
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 183-304 1.64e-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: 79.68  E-value: 1.64e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  183 VLGHFEKPLFLELCKHMVFVQLLEGEHVFQPGEPDTSIYVVQDGRLEVCIQDADGSEVAVKEVLAGDSVhSLLSILDVIT 262
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLF-GELALLGNGP 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1239920273  263 gHTApyktvSARAAVPSTVLRLPAVAFQGVFEKYPETLVRVV 304
Cdd:cd00038     80 -RSA-----TVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 633-741 2.38e-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: 79.26  E-value: 2.38e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  633 MEVEAGRAVYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLIGVVETLTHQARATTVHAVRDSELAKLPAGA 712
Cdd:COG0664     19 RTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSPATAEALEDSELLRIPRED 98

                           90       100
                   ....*....|....*....|....*....
gi 1239920273  713 LTSIKRRYPQVVTRLIHLLGEKILGSLQQ 741
Cdd:COG0664     99 LEELLERNPELARALLRLLARRLRQLQER 127
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 497-605 2.77e-16

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: 76.21  E-value: 2.77e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  497 LLTLMKLDDPSLLDGRVTLLHVPGGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEdTCLFVVRPGEIVGQLAVLTGEP 576
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGRE-QIVGFLGPGDLFGELALLGNGP 79

                           90       100
                   ....*....|....*....|....*....
gi 1239920273  577 LIFTIKANRDCSFLSISKAHFYEIMRKQP 605
Cdd:cd00038     80 RSATVRALTDSELLVLPRSDFRRLLQEYP 108
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 184-321 1.17e-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: 1.17e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  184 LGHFEKPLFLELCKHMVFVQLLEGEHVFQPGEPDTSIYVVQDGRLEVCIQDADGSEVAVKEVLAGDsvhsLLSILDVITG 263
Cdd:COG0664      1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGD----FFGELSLLGG 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239920273  264 HTAPYktvSARAAVPSTVLRLPAVAFQGVFEKYPETLVRVVQIIMVRL----QRVTFLALHN 321
Cdd:COG0664     77 EPSPA---TAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLrqlqERLVSLAFLS 135
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 515-603 4.47e-15

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: 71.87  E-value: 4.47e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  515 LLHVPGGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEDTcLFVVRPGEIVGQLAVLTGEPLIFTIKANRDCSFLSISK 594
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQI-LAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPR 79


                   ....*....
gi 1239920273  595 AHFYEIMRK 603
Cdd:pfam00027   80 EDFLELLER 88
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 201-296 2.93e-14

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: 69.56  E-value: 2.93e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  201 FVQLLEGEHVFQPGEPDTSIYVVQDGRLEVCIQDADGSEVAVKEVLAGDSVHsLLSILdvitgHTAPYkTVSARAAVPST 280
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFG-ELALL-----GGEPR-SATVVALTDSE 73

                           90
                   ....*....|....*.
gi 1239920273  281 VLRLPAVAFQGVFEKY 296
Cdd:pfam00027   74 LLVIPREDFLELLERD 89
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 183-306 4.15e-14

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: 70.12  E-value: 4.15e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273   183 VLGHFEKPLFLELCKHMVFVQLLEGEHVFQPGEPDTSIYVVQDGRLEVCIQDADGSEVAVKEVLAGDSVhSLLSILdviT 262
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFF-GELALL---T 76

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 1239920273   263 GHTAPYkTVSARAAVPSTVLRLPAVAFQGVFEKYPETLVRVVQI 306
Cdd:smart00100   77 NSRRAA-SAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 504-627 5.19e-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: 72.33  E-value: 5.19e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  504 DDPSLLDGRVTLLHVPGGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEdTCLFVVRPGEIVGQLAVLTGEPLIFTIKA 583
Cdd:COG0664      7 EELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGRE-QILGFLGPGDFFGELSLLGGEPSPATAEA 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1239920273  584 NRDCSFLSISKAHFYEIMRKQPTVVLGVAHTVVKRVSSFVRQID 627
Cdd:COG0664     86 LEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLV 129
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 621-728 1.99e-11

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: 62.42  E-value: 1.99e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273   621 SFVRQIDFALDWMEVEAGRAVYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLIGVVETLTHQARATTVHAV 700
Cdd:smart00100    8 EELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRRAASAAAV 87

                            90       100       110
                    ....*....|....*....|....*....|
gi 1239920273   701 --RDSELAKLPAGALTSIKRRYPQVVTRLI 728
Cdd:smart00100   88 alELATLLRIDFRDFLQLLPELPQLLLELL 117
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 489-605 2.38e-08

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: 53.56  E-value: 2.38e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273   489 IFRAAKKDLLtlmklddpSLLDGRVTLLHVPGGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEDTcLFVVRPGEIVGQ 568
Cdd:smart00100    1 LFKNLDAEEL--------RELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQI-VGTLGPGDFFGE 71

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 1239920273   569 LAVLTGEPLI--FTIKANRDCSFLSISKAHFYEIMRKQP 605
Cdd:smart00100   72 LALLTNSRRAasAAAVALELATLLRIDFRDFLQLLPELP 110
TM_EGFR-like cd12087
Transmembrane domain of the Epidermal Growth Factor Receptor family of Protein Tyrosine ...
 42-79 1.46e-04

Transmembrane domain of the Epidermal Growth Factor Receptor family of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane (TM) helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. They are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. The TM domain not only serves as a membrane anchor, but also plays an important role in receptor dimerization and optimal activation. Mutations in the TM domain of EGFR family RTKs have been associated with increased breast cancer risk.


Pssm-ID: 213052  Cd Length: 38  Bit Score: 40.21  E-value: 1.46e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1239920273   42 RHSQSTMLLGIVIGALLALALVGITVFFVYRRVNRFRQ 79
Cdd:cd12087      1 RTSKTTSIAAGVVGGLLVLVILGLIVFLFRRRRHIKRK 38
 
Name Accession Description Interval E-value
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 946-1251 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: 691.07  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  946 HSDFSRLARVLTGNAIALVLGGGGARGCAQVGIIRALAECGIPVDMVGGTSIGAFMGALYSEERNYSQIRIRAKEWAEDM 1025
Cdd:cd07225      1 HSDFSRLARVLTGNSIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKDM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273 1026 TSMVKTVLDLTYPITSMFSGAGFNSSICNVFKDRQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPL 1105
Cdd:cd07225     81 TSIWKKLLDLTYPITSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPPL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273 1106 CDPKDGHLLMDGGYINNLPADVARSMGAKVVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLATKVKVLNMAEIQTRL 1185
Cdd:cd07225    161 CDPKDGHLLMDGGYINNLPADVARSMGAKTVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLAEKVKVPNMAEIQSRL 240

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239920273 1186 AYVCCVRQLEMVKNSEYCEYLRPPIDSYRTLDFGKFNEICEVGYQHGRTVFDIWGRSGVLEKMLQD 1251
Cdd:cd07225    241 AYVSCVRQLEEVKSSDYCEYLRPPIDKYKTLDFGKFDEICEVGYQHGKTVFDGWKRSGVLEKMLQD 306
Pat_Fungal_NTE1 cd07227
Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy ...
 951-1221 1.76e-112

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: 354.11  E-value: 1.76e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  951 RLARVLTGNAIALVLGGGGARGCAQVGIIRALAECGIPVDMVGGTSIGAFMGALYSEERNYSQIRIRAKEWAEDMTSMVK 1030
Cdd:cd07227      1 RLARRLCGQAIGLVLGGGGARGISHIGILQALEEAGIPIDAIGGTSIGSFVGGLYAREADLVPIFGRAKKFAGRMASMWR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273 1031 TVLDLTYPITSMFSGAGFNSSICNVFKDRQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLCDpkD 1110
Cdd:cd07227     81 FLSDVTYPFASYTTGHEFNRGIWKTFGNTHIEDFWIPFYANSTNITHSRMEIHSSGYAWRYIRASMSLAGLLPPLSD--N 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273 1111 GHLLMDGGYINNLPADVARSMGAKVVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLATKVKVLNMAEIQTRLAYVCC 1190
Cdd:cd07227    159 GSMLLDGGYMDNLPVSPMRSLGIRDIFAVDVGSVDDRTPMDYGDSVSGVWIFFNRWNPFSSRPNVPSMAEIQSRLTYVSS 238

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1239920273 1191 VRQLEMVKNSEYCEYLRPPIDSYRTLDFGKF 1221
Cdd:cd07227    239 VKTLEKVKATPGCHYMRPPVQDFDTLDFGKF 269
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 961-1141 6.18e-73

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: 240.53  E-value: 6.18e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  961 IALVLGGGGARGCAQVGIIRALAECGIPVDMVGGTSIGAFMGALYSEERNYSQIRIRAKEwaedMTSMVKTVLDLTYPIT 1040
Cdd:cd07205      1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAGYSPEEIEERAKL----RSTDLKALSDLTIPTA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273 1041 SMFSGAGFNSSICNVFKDRQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLCDpkDGHLLMDGGYI 1120
Cdd:cd07205     77 GLLRGDKFLELLDEYFGDRDIEDLWIPFFIVATDLTSGKLVVFRSGSLVRAVRASMSIPGIFPPVKI--DGQLLVDGGVL 154

                          170       180
                   ....*....|....*....|.
gi 1239920273 1121 NNLPADVARSMGAKVVIAIDV 1141
Cdd:cd07205    155 NNLPVDVLRELGADIIIAVDL 175
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 961-1237 9.94e-58

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 200.51  E-value: 9.94e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  961 IALVLGGGGARGCAQVGIIRALAECGIPVDMVGGTSIGAFMGALYSEERNYSQIR-----IRAKEWAEDMTSMVKTVLDL 1035
Cdd:COG1752      7 IGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADELEelwrsLDRRDLFDLSLPRRLLRLDL 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273 1036 TYPITSMFSGAGFNSSICNVFKDRQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLcdPKDGHLLM 1115
Cdd:COG1752     87 GLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPV--EIDGRLYV 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273 1116 DGGYINNLPADVARSMGAKVVIAIDVGSQDEtdltnygdalsgwwllwkrwnplatkvKVLNMAEIQTRLAYVCCVRQLE 1195
Cdd:COG1752    165 DGGVVNNLPVDPARALGADRVIAVDLNPPLR---------------------------KLPSLLDILGRALEIMFNSILR 217

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1239920273 1196 MVKNSEYC-EYLRPPIDSYRTLDFGKFNEICEVGYQHGRTVFD 1237
Cdd:COG1752    218 RELALEPAdILIEPDLSGISLLDFSRAEELIEAGYEAARRALD 260
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 963-1139 6.52e-49

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: 171.76  E-value: 6.52e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  963 LVLGGGGARGCAQVGIIRALAECGIPVDMVGGTSIGAFMGALYSEERNYSQIRIRAKEWAEDmtsmVKTVLDLTYPITSM 1042
Cdd:cd07198      1 LVLSGGGALGIYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASGRDLEEALLLLLRLSRE----VRLRFDGAFPPTGR 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273 1043 FSGAGFNSSICNVFKDRqIEDLWIPYFTITTDITASAMRVH---TDGSLWRYVRASMSLSGYMPPLCDPKDGHLLMDGGY 1119
Cdd:cd07198     77 LLGILRQPLLSALPDDA-HEDASGKLFISLTRLTDGENVLVsdtSKGELWSAVRASSSIPGYFGPVPLSFRGRRYGDGGL 155

                          170       180
                   ....*....|....*....|
gi 1239920273 1120 INNLPADVarsMGAKVVIAI 1139
Cdd:cd07198    156 SNNLPVAE---LGNTINVSP 172
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 961-1141 1.09e-37

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: 139.72  E-value: 1.09e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  961 IALVLGGGGARGCAQVGIIRALAECGIPVDMVGGTSIGAFMGALYSEERN-YSQIRIRAKEWAEdmtsmVKTVLDLTYPI 1039
Cdd:cd07228      1 IGLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYAAGHLdALEEWVRSLSQRD-----VLRLLDLSASR 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273 1040 TSMFSGAGFNSSICNVFKDRQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLCDpkDGHLLMDGGY 1119
Cdd:cd07228     76 SGLLKGEKVLEYLREIMGGVTIEELPIPFAAVATDLQTGKEVWFREGSLIDAIRASISIPGIFAPVEH--NGRLLVDGGV 153

                          170       180
                   ....*....|....*....|..
gi 1239920273 1120 INNLPADVARSMGAKVVIAIDV 1141
Cdd:cd07228    154 VNPIPVSVARALGADIVIAVDL 175
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 963-1140 3.59e-27

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: 108.66  E-value: 3.59e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  963 LVLGGGGARGCAQVGIIRALAECGI--PVDMVGGTSIGAFMGALYseernysqirirakewaedmtsmvktvldltYPIT 1040
Cdd:cd01819      1 LSFSGGGFRGMYHAGVLSALAERGLldCVTYLAGTSGGAWVAATL-------------------------------YPPS 49

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273 1041 SMFSGAGFNSSIcnvfkdrqiEDLWIPYFTITTDITASAM----RVHTDGSLWRYVRASMSLSGYMPPLCD--------- 1107
Cdd:cd01819     50 SSLDNKPRQSLE---------EALSGKLWVSFTPVTAGENvlvsRFVSKEELIRALFASGSWPSYFGLIPPaelytsksn 120

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1239920273 1108 -PKDGHLLMDGGYINNLPADVARSMGAKVVIAID 1140
Cdd:cd01819    121 lKEKGVRLVDGGVSNNLPAPVLLRPGRGVTLTIS 154
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 963-1128 1.53e-25

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: 105.38  E-value: 1.53e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  963 LVLGGGGARGCAQVGIIRALAECGIPVDMVGGTSIGAFMGALYS--------EERNYSQIRIRAKEWAEDMTSMVKTVLD 1034
Cdd:pfam01734    1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLAlgrdpeeiEDLLLELDLNLFLSLIRKRALSLLALLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273 1035 LTYPITSMFSGAGFNSSICNVFKDRQIEDLWIPYFTI-----------------TTDITASAMRVHTDGSLWRYVRASMS 1097
Cdd:pfam01734   81 GLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLlvvalralltvistalgTRARILLPDDLDDDEDLADAVLASSA 160

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1239920273 1098 LSGYMPPLcdPKDGHLLMDGGYINNLPADVA 1128
Cdd:pfam01734  161 LPGVFPPV--RLDGELYVDGGLVDNVPVEAA 189
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 963-1143 1.51e-24

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: 103.14  E-value: 1.51e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  963 LVLGGGGARGCAQVGIIRALAECGIPVDMVGGTSIGAFMGALYseernysqirirakewAEDMTSMVKTV----LDLTYP 1038
Cdd:cd07209      1 LVLSGGGALGAYQAGVLKALAEAGIEPDIISGTSIGAINGALI----------------AGGDPEAVERLeklwRELSRE 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273 1039 iTSMFsgAGFNSSICNVFKDRQIEDLWIPYFTITTDITASAMRVHTDGSLWR---YVRASMSLsgymPPLCDPK--DGHL 1113
Cdd:cd07209     65 -DVFL--RGLLDRALDFDTLRLLAILFAGLVIVAVNVLTGEPVYFDDIPDGIlpeHLLASAAL----PPFFPPVeiDGRY 137

                          170       180       190
                   ....*....|....*....|....*....|
gi 1239920273 1114 LMDGGYINNLPADVARSMGAKVVIAIDVGS 1143
Cdd:cd07209    138 YWDGGVVDNTPLSPAIDLGADEIIVVSLSD 167
PRK10279 PRK10279
patatin-like phospholipase RssA;
961-1140 2.40e-24

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 105.18  E-value: 2.40e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  961 IALVLGGGGARGCAQVGIIRALAECGIPVDMVGGTSIGAFMGALYSEERNYSQiriraKEWAEDMTSM-VKTVLDLTYPI 1039
Cdd:PRK10279     6 IGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRLSAL-----EDWVTSFSYWdVLRLMDLSWQR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273 1040 TSMFSGAGFNSSICNVFKDRQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLcdPKDGHLLMDGGY 1119
Cdd:PRK10279    81 GGLLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPV--AHNGYWLVDGAV 158

                          170       180
                   ....*....|....*....|.
gi 1239920273 1120 INNLPADVARSMGAKVVIAID 1140
Cdd:PRK10279   159 VNPVPVSLTRALGADIVIAVD 179
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 620-728 1.96e-21

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: 90.85  E-value: 1.96e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  620 SSFVRQIDFALDWMEVEAGRAVYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLIGVVETLTHQARATTVHA 699
Cdd:cd00038      7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRA 86

                           90       100
                   ....*....|....*....|....*....
gi 1239920273  700 VRDSELAKLPAGALTSIKRRYPQVVTRLI 728
Cdd:cd00038     87 LTDSELLVLPRSDFRRLLQEYPELARRLL 115
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 961-1137 2.71e-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: 2.71e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  961 IALVLGGGGARGCAQVGIIRALAECGIPVDMVGGTSIGAFMGALYseernysQIRIRAKEWAEDMTSM----VKTVLDLT 1036
Cdd:cd07210      1 FALVLSSGFFGFYAHLGFLAALLEMGLEPSAISGTSAGALVGGLF-------ASGISPDEMAELLLSLerkdFWMFWDPP 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273 1037 YPiTSMFSGAGFNSSICNVFKDRQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLcdPKDGHLLMD 1116
Cdd:cd07210     74 LR-GGLLSGDRFAALLREHLPPDRFEELRIPLAVSVVDLTSRETLLLSEGDLAEAVAASCAVPPLFQPV--EIGGRPFVD 150

                          170       180
                   ....*....|....*....|.
gi 1239920273 1117 GGYINNLPADVARSMGAKVVI 1137
Cdd:cd07210    151 GGVADRLPFDALRPEIERILY 171
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 633-720 4.57e-18

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: 80.35  E-value: 4.57e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  633 MEVEAGRAVYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLIGVVETLTHQARATTVHAVRDSELAKLPAGA 712
Cdd:pfam00027    2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRED 81


                   ....*...
gi 1239920273  713 LTSIKRRY 720
Cdd:pfam00027   82 FLELLERD 89
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 183-304 1.64e-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: 79.68  E-value: 1.64e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  183 VLGHFEKPLFLELCKHMVFVQLLEGEHVFQPGEPDTSIYVVQDGRLEVCIQDADGSEVAVKEVLAGDSVhSLLSILDVIT 262
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLF-GELALLGNGP 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1239920273  263 gHTApyktvSARAAVPSTVLRLPAVAFQGVFEKYPETLVRVV 304
Cdd:cd00038     80 -RSA-----TVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 633-741 2.38e-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: 79.26  E-value: 2.38e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  633 MEVEAGRAVYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLIGVVETLTHQARATTVHAVRDSELAKLPAGA 712
Cdd:COG0664     19 RTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSPATAEALEDSELLRIPRED 98

                           90       100
                   ....*....|....*....|....*....
gi 1239920273  713 LTSIKRRYPQVVTRLIHLLGEKILGSLQQ 741
Cdd:COG0664     99 LEELLERNPELARALLRLLARRLRQLQER 127
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 497-605 2.77e-16

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: 76.21  E-value: 2.77e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  497 LLTLMKLDDPSLLDGRVTLLHVPGGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEdTCLFVVRPGEIVGQLAVLTGEP 576
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGRE-QIVGFLGPGDLFGELALLGNGP 79

                           90       100
                   ....*....|....*....|....*....
gi 1239920273  577 LIFTIKANRDCSFLSISKAHFYEIMRKQP 605
Cdd:cd00038     80 RSATVRALTDSELLVLPRSDFRRLLQEYP 108
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 184-321 1.17e-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: 1.17e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  184 LGHFEKPLFLELCKHMVFVQLLEGEHVFQPGEPDTSIYVVQDGRLEVCIQDADGSEVAVKEVLAGDsvhsLLSILDVITG 263
Cdd:COG0664      1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGD----FFGELSLLGG 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239920273  264 HTAPYktvSARAAVPSTVLRLPAVAFQGVFEKYPETLVRVVQIIMVRL----QRVTFLALHN 321
Cdd:COG0664     77 EPSPA---TAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLrqlqERLVSLAFLS 135
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 515-603 4.47e-15

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: 71.87  E-value: 4.47e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  515 LLHVPGGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEDTcLFVVRPGEIVGQLAVLTGEPLIFTIKANRDCSFLSISK 594
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQI-LAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPR 79


                   ....*....
gi 1239920273  595 AHFYEIMRK 603
Cdd:pfam00027   80 EDFLELLER 88
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 963-1127 4.88e-15

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: 75.01  E-value: 4.88e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  963 LVLGGGGARGCAQVGIIRALAECGIPVDMVGGTSIGAFMGALYSEERNYSQIRIRAKE--WAEDMTS----MVKTVLDLT 1036
Cdd:cd07207      2 LVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLALGYSAADIKDILKEtdFAKLLDSpvglLFLLPSLFK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273 1037 YPITS-----------MFSGAGFNSSICNVFKDRQiEDLWIPYFTITTDITASAMRV----HT-DGSLWRYVRASMSLSG 1100
Cdd:cd07207     82 EGGLYkgdaleewlreLLKEKTGNSFATSLLRDLD-DDLGKDLKVVATDLTTGALVVfsaeTTpDMPVAKAVRASMSIPF 160

                          170       180
                   ....*....|....*....|....*..
gi 1239920273 1101 YMPPLCDPKdGHLLMDGGYINNLPADV 1127
Cdd:cd07207    161 VFKPVRLAK-GDVYVDGGVLDNYPVWL 186
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 201-296 2.93e-14

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: 69.56  E-value: 2.93e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  201 FVQLLEGEHVFQPGEPDTSIYVVQDGRLEVCIQDADGSEVAVKEVLAGDSVHsLLSILdvitgHTAPYkTVSARAAVPST 280
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFG-ELALL-----GGEPR-SATVVALTDSE 73

                           90
                   ....*....|....*.
gi 1239920273  281 VLRLPAVAFQGVFEKY 296
Cdd:pfam00027   74 LLVIPREDFLELLERD 89
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 183-306 4.15e-14

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: 70.12  E-value: 4.15e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273   183 VLGHFEKPLFLELCKHMVFVQLLEGEHVFQPGEPDTSIYVVQDGRLEVCIQDADGSEVAVKEVLAGDSVhSLLSILdviT 262
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFF-GELALL---T 76

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 1239920273   263 GHTAPYkTVSARAAVPSTVLRLPAVAFQGVFEKYPETLVRVVQI 306
Cdd:smart00100   77 NSRRAA-SAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 504-627 5.19e-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: 72.33  E-value: 5.19e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  504 DDPSLLDGRVTLLHVPGGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEdTCLFVVRPGEIVGQLAVLTGEPLIFTIKA 583
Cdd:COG0664      7 EELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGRE-QILGFLGPGDFFGELSLLGGEPSPATAEA 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1239920273  584 NRDCSFLSISKAHFYEIMRKQPTVVLGVAHTVVKRVSSFVRQID 627
Cdd:COG0664     86 LEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLV 129
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 621-728 1.99e-11

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: 62.42  E-value: 1.99e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273   621 SFVRQIDFALDWMEVEAGRAVYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLIGVVETLTHQARATTVHAV 700
Cdd:smart00100    8 EELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRRAASAAAV 87

                            90       100       110
                    ....*....|....*....|....*....|
gi 1239920273   701 --RDSELAKLPAGALTSIKRRYPQVVTRLI 728
Cdd:smart00100   88 alELATLLRIDFRDFLQLLPELPQLLLELL 117
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
961-1139 2.68e-10

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 62.87  E-value: 2.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  961 IALVLGGGGARGCAQVGIIRALAECGIPVDMVGGTSIGAFMGALY---------------SEERNYSQIR--IRAKEWAe 1023
Cdd:COG4667      6 TALVLEGGGMRGIFTAGVLDALLEEGIPFDLVIGVSAGALNGASYlsrqpgrarrvitdyATDPRFFSLRnfLRGGNLF- 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273 1024 DMTSMVKTVLDLTYPI---TSMFSGAGFNSSICNVfKDRQIEdlwipYFTITtditasamrvHTDGSLWRYVRASMSlsg 1100
Cdd:COG4667     85 DLDFLYDEIPNELLPFdfeTFKASPREFYVVATNA-DTGEAE-----YFSKK----------DDDYDLLDALRASSA--- 145

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1239920273 1101 yMPPLCDP--KDGHLLMDGGYINNLPADVARSMGAKVVIAI 1139
Cdd:COG4667    146 -LPLLYPPveIDGKRYLDGGVADSIPVREAIRDGADKIVVI 185
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 963-1139 1.28e-09

Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase similar to yjju protein of Escherichia coli. This family predominantly consists of bacterial patatin glycoproteins, and some representatives from eukaryotes and archaea. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates.


Pssm-ID: 132847 [Multi-domain]  Cd Length: 266  Bit Score: 60.70  E-value: 1.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  963 LVLGGGGARGCAQVGIIRALAECGI-PVDMVGGTSIGAFMGALY-SEERNYSQIRI----RAKEWAeDMTSMVKT----V 1032
Cdd:cd07208      1 LVLEGGGMRGAYTAGVLDAFLEAGIrPFDLVIGVSAGALNAASYlSGQRGRALRINtkyaTDPRYL-GLRSLLRTgnlfD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273 1033 LDLTYPITSMFSgagfnssicNVFKDRQIEDLWIPYFTITTDI-TASAM--RVHTDGSLW-RYVRASMSLSGYMPPlcDP 1108
Cdd:cd07208     80 LDFLYDELPDGL---------DPFDFEAFAASPARFYVVATDAdTGEAVyfDKPDILDDLlDALRASSALPGLFPP--VR 148

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1239920273 1109 KDGHLLMDGGYINNLPADVARSMGAKVVIAI 1139
Cdd:cd07208    149 IDGEPYVDGGLSDSIPVDKAIEDGADKIVVI 179
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 489-605 2.38e-08

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: 53.56  E-value: 2.38e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273   489 IFRAAKKDLLtlmklddpSLLDGRVTLLHVPGGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEDTcLFVVRPGEIVGQ 568
Cdd:smart00100    1 LFKNLDAEEL--------RELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQI-VGTLGPGDFFGE 71

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 1239920273   569 LAVLTGEPLI--FTIKANRDCSFLSISKAHFYEIMRKQP 605
Cdd:smart00100   72 LALLTNSRRAasAAAVALELATLLRIDFRDFLQLLPELP 110
TM_EGFR-like cd12087
Transmembrane domain of the Epidermal Growth Factor Receptor family of Protein Tyrosine ...
 42-79 1.46e-04

Transmembrane domain of the Epidermal Growth Factor Receptor family of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane (TM) helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. They are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. The TM domain not only serves as a membrane anchor, but also plays an important role in receptor dimerization and optimal activation. Mutations in the TM domain of EGFR family RTKs have been associated with increased breast cancer risk.


Pssm-ID: 213052  Cd Length: 38  Bit Score: 40.21  E-value: 1.46e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1239920273   42 RHSQSTMLLGIVIGALLALALVGITVFFVYRRVNRFRQ 79
Cdd:cd12087      1 RTSKTTSIAAGVVGGLLVLVILGLIVFLFRRRRHIKRK 38
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 963-1128 2.01e-03

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


Pssm-ID: 132852 [Multi-domain]  Cd Length: 288  Bit Score: 41.89  E-value: 2.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273  963 LVLGGGGARGCAQVGIIRALAECGiP-----VDMVGGTSIGAFMGALYSEERNYSQIRiraKEWAEdmtsMVKTVLDLTY 1037
Cdd:cd07213      5 LSLDGGGVKGIVQLVLLKRLAEEF-PsfldqIDLFAGTSAGSLIALGLALGYSPRQVL---KLYEE----VGLKVFSKSS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239920273 1038 PITSMFSGAGFNSSICNVFKDRQIEDL---------WIPYFTITTDI-----TASAMRVHT-------DGSLWRYVRASM 1096
Cdd:cd07213     77 AGGGAGNNQYFAAGFLKAFAEVFFGDLtlgdlkrkvLVPSFQLDSGKddpnrRWKPKLFHNfpgepdlDELLVDVCLRSS 156

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1239920273 1097 SLSGYMPPLcdpkDGHLlmDGG-YINNlPADVA 1128
Cdd:cd07213    157 AAPTYFPSY----QGYV--DGGvFANN-PSLCA 182
 
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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