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Conserved domains on  [gi|2124414728|ref|XP_044634177|]
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patatin-like phospholipase domain-containing protein 7 isoform X1 [Equus asinus]

Protein Classification

patatin-like phospholipase domain-containing protein( domain architecture ID 10035150)

patatin-like phospholipase domain-containing protein with CAP family effector domains, similar to human patatin-like phospholipase domain-containing protein 7 (PNPLA7), a lysophospholipase which preferentially deacylates unsaturated lysophosphatidylcholine (C18:1), generating glycerophosphocholine

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 ...
 893-1198 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: 681.44  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  893 HSDFSRLARVLTGNAIALVLGGGGARGCAQVGIIRALVECGIPVDMVGGTSIGAFMGALYSEERSCSQMRIRAKQWAEGM 972
Cdd:cd07225      1 HSDFSRLARVLTGNSIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKDM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  973 TSVVRTMLDLTYPITSMFSGAGFNNSICSVFKDRQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPL 1052
Cdd:cd07225     81 TSIWKKLLDLTYPITSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPPL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728 1053 CDPKDGHLLMDGGYINNLPADVARSMGAKVVIAIDVGSQDEVDLTNYGDALSGWWLLWKRWNPLATKVKVLNMAEIQTRL 1132
Cdd:cd07225    161 CDPKDGHLLMDGGYINNLPADVARSMGAKTVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLAEKVKVPNMAEIQSRL 240

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124414728 1133 AYVCCVRQLEMVKSSDYCECLRPPIDRYRTLDFGKFDEICEVGYQHGRTVFDIWGRSGVLEKMLQD 1198
Cdd:cd07225    241 AYVSCVRQLEEVKSSDYCEYLRPPIDKYKTLDFGKFDEICEVGYQHGKTVFDGWKRSGVLEKMLQD 306
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 564-672 1.18e-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: 91.23  E-value: 1.18e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  564 SSFVRQIDFALDWMEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLIGVVETLTHQARATTVHA 643
Cdd:cd00038      7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRA 86

                           90       100
                   ....*....|....*....|....*....
gi 2124414728  644 VRDSELAKLPAGALTSIKRRYPQVVTRLI 672
Cdd:cd00038     87 LTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 441-549 1.52e-15

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: 73.90  E-value: 1.52e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  441 LLTLMKLDDPSLLDGRVTLLHVPGGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEdTCLFVTRPGEMVGQLAVLTGEP 520
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGRE-QIVGFLGPGDLFGELALLGNGP 79

                           90       100
                   ....*....|....*....|....*....
gi 2124414728  521 LIFTIKANRDCSFLSISKAHFYEIMRKQP 549
Cdd:cd00038     80 RSATVRALTDSELLVLPRSDFRRLLQEYP 108
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 169-262 1.09e-11

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: 63.11  E-value: 1.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  169 VLGHFEKPLFLELCKHMVFVQLLEGEHVFRPGEPDTSIYVVQDGRLEVCIQDTDGTEVAVKEVLAGDSVHSLLSILD--- 245
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNgpr 80

                           90       100
                   ....*....|....*....|...
gi 2124414728  246 ---VITI---IMVRLQRVTFLAL 262
Cdd:cd00038     81 satVRALtdsELLVLPRSDFRRL 103
 
Name Accession Description Interval E-value
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 893-1198 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: 681.44  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  893 HSDFSRLARVLTGNAIALVLGGGGARGCAQVGIIRALVECGIPVDMVGGTSIGAFMGALYSEERSCSQMRIRAKQWAEGM 972
Cdd:cd07225      1 HSDFSRLARVLTGNSIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKDM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  973 TSVVRTMLDLTYPITSMFSGAGFNNSICSVFKDRQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPL 1052
Cdd:cd07225     81 TSIWKKLLDLTYPITSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPPL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728 1053 CDPKDGHLLMDGGYINNLPADVARSMGAKVVIAIDVGSQDEVDLTNYGDALSGWWLLWKRWNPLATKVKVLNMAEIQTRL 1132
Cdd:cd07225    161 CDPKDGHLLMDGGYINNLPADVARSMGAKTVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLAEKVKVPNMAEIQSRL 240

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124414728 1133 AYVCCVRQLEMVKSSDYCECLRPPIDRYRTLDFGKFDEICEVGYQHGRTVFDIWGRSGVLEKMLQD 1198
Cdd:cd07225    241 AYVSCVRQLEEVKSSDYCEYLRPPIDKYKTLDFGKFDEICEVGYQHGKTVFDGWKRSGVLEKMLQD 306
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 908-1184 6.03e-58

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 200.90  E-value: 6.03e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  908 IALVLGGGGARGCAQVGIIRALVECGIPVDMVGGTSIGAFMGALYSEERSCSQMR-----IRAKQWAEGMTSVVRTMLDL 982
Cdd:COG1752      7 IGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADELEelwrsLDRRDLFDLSLPRRLLRLDL 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  983 TYPITSMFSGAGFNNSICSVFKDRQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLcdPKDGHLLM 1062
Cdd:COG1752     87 GLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPV--EIDGRLYV 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728 1063 DGGYINNLPADVARSMGAKVVIAIDVGSQDEvdltnygdalsgwwllwkrwnplatkvKVLNMAEIQTRLAYVCCVRQLE 1142
Cdd:COG1752    165 DGGVVNNLPVDPARALGADRVIAVDLNPPLR---------------------------KLPSLLDILGRALEIMFNSILR 217

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2124414728 1143 MVKSSDYCECL-RPPIDRYRTLDFGKFDEICEVGYQHGRTVFD 1184
Cdd:COG1752    218 RELALEPADILiEPDLSGISLLDFSRAEELIEAGYEAARRALD 260
PRK10279 PRK10279
patatin-like phospholipase RssA;
908-1087 6.92e-27

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 112.50  E-value: 6.92e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  908 IALVLGGGGARGCAQVGIIRALVECGIPVDMVGGTSIGAFMGALYSEERsCSQMriraKQWAEGMT--SVVRTMlDLTYP 985
Cdd:PRK10279     6 IGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDR-LSAL----EDWVTSFSywDVLRLM-DLSWQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  986 ITSMFSGAGFNNSICSVFKDRQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLcdPKDGHLLMDGG 1065
Cdd:PRK10279    80 RGGLLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPV--AHNGYWLVDGA 157

                          170       180
                   ....*....|....*....|..
gi 2124414728 1066 YINNLPADVARSMGAKVVIAID 1087
Cdd:PRK10279   158 VVNPVPVSLTRALGADIVIAVD 179
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 910-1075 7.72e-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: 103.07  E-value: 7.72e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  910 LVLGGGGARGCAQVGIIRALVECGIPVDMVGGTSIGAFMGALYS--------EERSCSQMRIRAKQWAEGMTSVVRTMLD 981
Cdd:pfam01734    1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLAlgrdpeeiEDLLLELDLNLFLSLIRKRALSLLALLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  982 LTYPITSMFSGAGFNNSICSVFKDRQIEDLWIPYFTI-----------------TTDITASAMRVHTDGSLWRYVRASMS 1044
Cdd:pfam01734   81 GLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLlvvalralltvistalgTRARILLPDDLDDDEDLADAVLASSA 160

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2124414728 1045 LSGYMPPLcdPKDGHLLMDGGYINNLPADVA 1075
Cdd:pfam01734  161 LPGVFPPV--RLDGELYVDGGLVDNVPVEAA 189
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 564-672 1.18e-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: 91.23  E-value: 1.18e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  564 SSFVRQIDFALDWMEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLIGVVETLTHQARATTVHA 643
Cdd:cd00038      7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRA 86

                           90       100
                   ....*....|....*....|....*....
gi 2124414728  644 VRDSELAKLPAGALTSIKRRYPQVVTRLI 672
Cdd:cd00038     87 LTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 577-664 2.16e-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: 81.12  E-value: 2.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  577 MEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLIGVVETLTHQARATTVHAVRDSELAKLPAGA 656
Cdd:pfam00027    2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRED 81


                   ....*...
gi 2124414728  657 LTSIKRRY 664
Cdd:pfam00027   82 FLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 577-685 8.23e-17

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: 80.42  E-value: 8.23e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  577 MEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLIGVVETLTHQARATTVHAVRDSELAKLPAGA 656
Cdd:COG0664     19 RTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSPATAEALEDSELLRIPRED 98

                           90       100
                   ....*....|....*....|....*....
gi 2124414728  657 LTSIKRRYPQVVTRLIHLLGEKILGSLQQ 685
Cdd:COG0664     99 LEELLERNPELARALLRLLARRLRQLQER 127
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 441-549 1.52e-15

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: 73.90  E-value: 1.52e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  441 LLTLMKLDDPSLLDGRVTLLHVPGGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEdTCLFVTRPGEMVGQLAVLTGEP 520
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGRE-QIVGFLGPGDLFGELALLGNGP 79

                           90       100
                   ....*....|....*....|....*....
gi 2124414728  521 LIFTIKANRDCSFLSISKAHFYEIMRKQP 549
Cdd:cd00038     80 RSATVRALTDSELLVLPRSDFRRLLQEYP 108
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 459-547 2.43e-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: 2.43e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  459 LLHVPGGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEDTcLFVTRPGEMVGQLAVLTGEPLIFTIKANRDCSFLSISK 538
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQI-LAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPR 79


                   ....*....
gi 2124414728  539 AHFYEIMRK 547
Cdd:pfam00027   80 EDFLELLER 88
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 448-571 3.09e-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: 73.10  E-value: 3.09e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  448 DDPSLLDGRVTLLHVPGGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEdTCLFVTRPGEMVGQLAVLTGEPLIFTIKA 527
Cdd:COG0664      7 EELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGRE-QILGFLGPGDFFGELSLLGGEPSPATAEA 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2124414728  528 NRDCSFLSISKAHFYEIMRKQPTVVLGVAHTLVKRMSSFVRQID 571
Cdd:COG0664     86 LEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLV 129
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 169-262 1.09e-11

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: 63.11  E-value: 1.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  169 VLGHFEKPLFLELCKHMVFVQLLEGEHVFRPGEPDTSIYVVQDGRLEVCIQDTDGTEVAVKEVLAGDSVHSLLSILD--- 245
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNgpr 80

                           90       100
                   ....*....|....*....|...
gi 2124414728  246 ---VITI---IMVRLQRVTFLAL 262
Cdd:cd00038     81 satVRALtdsELLVLPRSDFRRL 103
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 565-672 1.41e-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: 62.80  E-value: 1.41e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728   565 SFVRQIDFALDWMEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLIGVVETLTHQARATTVHAV 644
Cdd:smart00100    8 EELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRRAASAAAV 87

                            90       100       110
                    ....*....|....*....|....*....|
gi 2124414728   645 --RDSELAKLPAGALTSIKRRYPQVVTRLI 672
Cdd:smart00100   88 alELATLLRIDFRDFLQLLPELPQLLLELL 117
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 169-268 5.53e-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: 58.18  E-value: 5.53e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728   169 VLGHFEKPLFLELCKHMVFVQLLEGEHVFRPGEPDTSIYVVQDGRLEVCIQDTDGTEVAVKEVLAGDSVhSLLSILD--- 245
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFF-GELALLTnsr 79

                            90       100
                    ....*....|....*....|....*.
gi 2124414728   246 ---VITIIMVRLQRVTFLALHNYLGL 268
Cdd:smart00100   80 raaSAAAVALELATLLRIDFRDFLQL 105
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 433-549 6.46e-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: 52.40  E-value: 6.46e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728   433 IFRAAKKDLLtlmklddpSLLDGRVTLLHVPGGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEDTcLFVTRPGEMVGQ 512
Cdd:smart00100    1 LFKNLDAEEL--------RELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQI-VGTLGPGDFFGE 71

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 2124414728   513 LAVLTGEPLI--FTIKANRDCSFLSISKAHFYEIMRKQP 549
Cdd:smart00100   72 LALLTNSRRAasAAAVALELATLLRIDFRDFLQLLPELP 110
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 187-237 1.26e-07

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: 50.69  E-value: 1.26e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2124414728  187 FVQLLEGEHVFRPGEPDTSIYVVQDGRLEVCIQDTDGTEVAVKEVLAGDSV 237
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFF 51
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 170-245 4.95e-07

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: 51.91  E-value: 4.95e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124414728  170 LGHFEKPLFLELCKHMVFVQLLEGEHVFRPGEPDTSIYVVQDGRLEVCIQDTDGTEVAVKEVLAGDSVhSLLSILD 245
Cdd:COG0664      1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFF-GELSLLG 75
 
Name Accession Description Interval E-value
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 893-1198 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: 681.44  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  893 HSDFSRLARVLTGNAIALVLGGGGARGCAQVGIIRALVECGIPVDMVGGTSIGAFMGALYSEERSCSQMRIRAKQWAEGM 972
Cdd:cd07225      1 HSDFSRLARVLTGNSIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKDM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  973 TSVVRTMLDLTYPITSMFSGAGFNNSICSVFKDRQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPL 1052
Cdd:cd07225     81 TSIWKKLLDLTYPITSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPPL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728 1053 CDPKDGHLLMDGGYINNLPADVARSMGAKVVIAIDVGSQDEVDLTNYGDALSGWWLLWKRWNPLATKVKVLNMAEIQTRL 1132
Cdd:cd07225    161 CDPKDGHLLMDGGYINNLPADVARSMGAKTVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLAEKVKVPNMAEIQSRL 240

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124414728 1133 AYVCCVRQLEMVKSSDYCECLRPPIDRYRTLDFGKFDEICEVGYQHGRTVFDIWGRSGVLEKMLQD 1198
Cdd:cd07225    241 AYVSCVRQLEEVKSSDYCEYLRPPIDKYKTLDFGKFDEICEVGYQHGKTVFDGWKRSGVLEKMLQD 306
Pat_Fungal_NTE1 cd07227
Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy ...
 898-1168 7.66e-110

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: 346.40  E-value: 7.66e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  898 RLARVLTGNAIALVLGGGGARGCAQVGIIRALVECGIPVDMVGGTSIGAFMGALYSEERSCSQMRIRAKQWAEGMTSVVR 977
Cdd:cd07227      1 RLARRLCGQAIGLVLGGGGARGISHIGILQALEEAGIPIDAIGGTSIGSFVGGLYAREADLVPIFGRAKKFAGRMASMWR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  978 TMLDLTYPITSMFSGAGFNNSICSVFKDRQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLCDpkD 1057
Cdd:cd07227     81 FLSDVTYPFASYTTGHEFNRGIWKTFGNTHIEDFWIPFYANSTNITHSRMEIHSSGYAWRYIRASMSLAGLLPPLSD--N 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728 1058 GHLLMDGGYINNLPADVARSMGAKVVIAIDVGSQDEVDLTNYGDALSGWWLLWKRWNPLATKVKVLNMAEIQTRLAYVCC 1137
Cdd:cd07227    159 GSMLLDGGYMDNLPVSPMRSLGIRDIFAVDVGSVDDRTPMDYGDSVSGVWIFFNRWNPFSSRPNVPSMAEIQSRLTYVSS 238

                          250       260       270
                   ....*....|....*....|....*....|.
gi 2124414728 1138 VRQLEMVKSSDYCECLRPPIDRYRTLDFGKF 1168
Cdd:cd07227    239 VKTLEKVKATPGCHYMRPPVQDFDTLDFGKF 269
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 908-1088 1.27e-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: 242.07  E-value: 1.27e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  908 IALVLGGGGARGCAQVGIIRALVECGIPVDMVGGTSIGAFMGALYSEERSCSQMRIRAKQwaegMTSVVRTMLDLTYPIT 987
Cdd:cd07205      1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAGYSPEEIEERAKL----RSTDLKALSDLTIPTA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  988 SMFSGAGFNNSICSVFKDRQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLCDpkDGHLLMDGGYI 1067
Cdd:cd07205     77 GLLRGDKFLELLDEYFGDRDIEDLWIPFFIVATDLTSGKLVVFRSGSLVRAVRASMSIPGIFPPVKI--DGQLLVDGGVL 154

                          170       180
                   ....*....|....*....|.
gi 2124414728 1068 NNLPADVARSMGAKVVIAIDV 1088
Cdd:cd07205    155 NNLPVDVLRELGADIIIAVDL 175
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 908-1184 6.03e-58

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 200.90  E-value: 6.03e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  908 IALVLGGGGARGCAQVGIIRALVECGIPVDMVGGTSIGAFMGALYSEERSCSQMR-----IRAKQWAEGMTSVVRTMLDL 982
Cdd:COG1752      7 IGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADELEelwrsLDRRDLFDLSLPRRLLRLDL 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  983 TYPITSMFSGAGFNNSICSVFKDRQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLcdPKDGHLLM 1062
Cdd:COG1752     87 GLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPV--EIDGRLYV 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728 1063 DGGYINNLPADVARSMGAKVVIAIDVGSQDEvdltnygdalsgwwllwkrwnplatkvKVLNMAEIQTRLAYVCCVRQLE 1142
Cdd:COG1752    165 DGGVVNNLPVDPARALGADRVIAVDLNPPLR---------------------------KLPSLLDILGRALEIMFNSILR 217

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2124414728 1143 MVKSSDYCECL-RPPIDRYRTLDFGKFDEICEVGYQHGRTVFD 1184
Cdd:COG1752    218 RELALEPADILiEPDLSGISLLDFSRAEELIEAGYEAARRALD 260
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 910-1086 6.76e-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: 171.37  E-value: 6.76e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  910 LVLGGGGARGCAQVGIIRALVECGIPVDMVGGTSIGAFMGALYSEERSCSQMRIRAKqwaeGMTSVVRTMLDLTYPITSM 989
Cdd:cd07198      1 LVLSGGGALGIYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASGRDLEEALLLLL----RLSREVRLRFDGAFPPTGR 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  990 FSGAGFnNSICSVFKDRQIEDLWIPYFTITTDITASAMRVH---TDGSLWRYVRASMSLSGYMPPLCDPKDGHLLMDGGY 1066
Cdd:cd07198     77 LLGILR-QPLLSALPDDAHEDASGKLFISLTRLTDGENVLVsdtSKGELWSAVRASSSIPGYFGPVPLSFRGRRYGDGGL 155

                          170       180
                   ....*....|....*....|
gi 2124414728 1067 INNLPADVarsMGAKVVIAI 1086
Cdd:cd07198    156 SNNLPVAE---LGNTINVSP 172
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 908-1088 1.62e-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: 138.95  E-value: 1.62e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  908 IALVLGGGGARGCAQVGIIRALVECGIPVDMVGGTSIGAFMGALYseersCSQMRIRAKQWAEGMTSV-VRTMLDLTYPI 986
Cdd:cd07228      1 IGLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALY-----AAGHLDALEEWVRSLSQRdVLRLLDLSASR 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  987 TSMFSGAGFNNSICSVFKDRQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLCDpkDGHLLMDGGY 1066
Cdd:cd07228     76 SGLLKGEKVLEYLREIMGGVTIEELPIPFAAVATDLQTGKEVWFREGSLIDAIRASISIPGIFAPVEH--NGRLLVDGGV 153

                          170       180
                   ....*....|....*....|..
gi 2124414728 1067 INNLPADVARSMGAKVVIAIDV 1088
Cdd:cd07228    154 VNPIPVSVARALGADIVIAVDL 175
PRK10279 PRK10279
patatin-like phospholipase RssA;
908-1087 6.92e-27

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 112.50  E-value: 6.92e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  908 IALVLGGGGARGCAQVGIIRALVECGIPVDMVGGTSIGAFMGALYSEERsCSQMriraKQWAEGMT--SVVRTMlDLTYP 985
Cdd:PRK10279     6 IGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDR-LSAL----EDWVTSFSywDVLRLM-DLSWQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  986 ITSMFSGAGFNNSICSVFKDRQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLcdPKDGHLLMDGG 1065
Cdd:PRK10279    80 RGGLLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPV--AHNGYWLVDGA 157

                          170       180
                   ....*....|....*....|..
gi 2124414728 1066 YINNLPADVARSMGAKVVIAID 1087
Cdd:PRK10279   158 VVNPVPVSLTRALGADIVIAVD 179
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 910-1087 3.04e-26

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: 105.96  E-value: 3.04e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  910 LVLGGGGARGCAQVGIIRALVECGI--PVDMVGGTSIGAFMGALYseerscsqmrirakqwaegmtsvvrtmldltYPIT 987
Cdd:cd01819      1 LSFSGGGFRGMYHAGVLSALAERGLldCVTYLAGTSGGAWVAATL-------------------------------YPPS 49

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  988 SMFSGAGFNnsicsvfkdRQIEDLWIPYFTITTDITASAM----RVHTDGSLWRYVRASMSLSGYMPPLCD--------- 1054
Cdd:cd01819     50 SSLDNKPRQ---------SLEEALSGKLWVSFTPVTAGENvlvsRFVSKEELIRALFASGSWPSYFGLIPPaelytsksn 120

                          170       180       190
                   ....*....|....*....|....*....|....
gi 2124414728 1055 -PKDGHLLMDGGYINNLPADVARSMGAKVVIAID 1087
Cdd:cd01819    121 lKEKGVRLVDGGVSNNLPAPVLLRPGRGVTLTIS 154
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 910-1075 7.72e-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: 103.07  E-value: 7.72e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  910 LVLGGGGARGCAQVGIIRALVECGIPVDMVGGTSIGAFMGALYS--------EERSCSQMRIRAKQWAEGMTSVVRTMLD 981
Cdd:pfam01734    1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLAlgrdpeeiEDLLLELDLNLFLSLIRKRALSLLALLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  982 LTYPITSMFSGAGFNNSICSVFKDRQIEDLWIPYFTI-----------------TTDITASAMRVHTDGSLWRYVRASMS 1044
Cdd:pfam01734   81 GLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLlvvalralltvistalgTRARILLPDDLDDDEDLADAVLASSA 160

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2124414728 1045 LSGYMPPLcdPKDGHLLMDGGYINNLPADVA 1075
Cdd:pfam01734  161 LPGVFPPV--RLDGELYVDGGLVDNVPVEAA 189
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 910-1095 1.31e-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: 1.31e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  910 LVLGGGGARGCAQVGIIRALVECGIPVDMVGGTSIGAFMGALYseerscsqmrirakqwAEGMTSVVRTM----LDLTYP 985
Cdd:cd07209      1 LVLSGGGALGAYQAGVLKALAEAGIEPDIISGTSIGAINGALI----------------AGGDPEAVERLeklwRELSRE 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  986 iTSMFSGAGFNNsicSVFKDRQIEDLWIPYFTITTDITASAMRV----HTDGSLWRYVRASMSLsgymPPLCDPK--DGH 1059
Cdd:cd07209     65 -DVFLRGLLDRA---LDFDTLRLLAILFAGLVIVAVNVLTGEPVyfddIPDGILPEHLLASAAL----PPFFPPVeiDGR 136

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2124414728 1060 LLMDGGYINNLPADVARSMGAKVVIAIDVGSQDEVD 1095
Cdd:cd07209    137 YYWDGGVVDNTPLSPAIDLGADEIIVVSLSDKGRDD 172
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 564-672 1.18e-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: 91.23  E-value: 1.18e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  564 SSFVRQIDFALDWMEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLIGVVETLTHQARATTVHA 643
Cdd:cd00038      7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRA 86

                           90       100
                   ....*....|....*....|....*....
gi 2124414728  644 VRDSELAKLPAGALTSIKRRYPQVVTRLI 672
Cdd:cd00038     87 LTDSELLVLPRSDFRRLLQEYPELARRLL 115
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 908-1084 1.13e-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: 86.25  E-value: 1.13e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  908 IALVLGGGGARGCAQVGIIRALVECGIPVDMVGGTSIGAFMGALYSEERSCSQMR-IRAKQWAEGMTSVVRTMLDltypi 986
Cdd:cd07210      1 FALVLSSGFFGFYAHLGFLAALLEMGLEPSAISGTSAGALVGGLFASGISPDEMAeLLLSLERKDFWMFWDPPLR----- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  987 TSMFSGAGFNNSICSVFKDRQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLcdPKDGHLLMDGGY 1066
Cdd:cd07210     76 GGLLSGDRFAALLREHLPPDRFEELRIPLAVSVVDLTSRETLLLSEGDLAEAVAASCAVPPLFQPV--EIGGRPFVDGGV 153

                          170
                   ....*....|....*...
gi 2124414728 1067 INNLPADVARSMGAKVVI 1084
Cdd:cd07210    154 ADRLPFDALRPEIERILY 171
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 577-664 2.16e-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: 81.12  E-value: 2.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  577 MEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLIGVVETLTHQARATTVHAVRDSELAKLPAGA 656
Cdd:pfam00027    2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRED 81


                   ....*...
gi 2124414728  657 LTSIKRRY 664
Cdd:pfam00027   82 FLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 577-685 8.23e-17

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: 80.42  E-value: 8.23e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  577 MEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLIGVVETLTHQARATTVHAVRDSELAKLPAGA 656
Cdd:COG0664     19 RTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSPATAEALEDSELLRIPRED 98

                           90       100
                   ....*....|....*....|....*....
gi 2124414728  657 LTSIKRRYPQVVTRLIHLLGEKILGSLQQ 685
Cdd:COG0664     99 LEELLERNPELARALLRLLARRLRQLQER 127
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 910-1074 1.20e-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: 76.55  E-value: 1.20e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  910 LVLGGGGARGCAQVGIIRALVECGIPVDMVGGTSIGAFMGALYSEERSCSQMRIRAKQ--WAEGMTSVVRTMLDLTYPIT 987
Cdd:cd07207      2 LVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLALGYSAADIKDILKEtdFAKLLDSPVGLLFLLPSLFK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  988 SMF---------------SGAGFNNSICSVFKDRQiEDLWIPYFTITTDITASAMRV----HT-DGSLWRYVRASMSLSG 1047
Cdd:cd07207     82 EGGlykgdaleewlrellKEKTGNSFATSLLRDLD-DDLGKDLKVVATDLTTGALVVfsaeTTpDMPVAKAVRASMSIPF 160

                          170       180
                   ....*....|....*....|....*..
gi 2124414728 1048 YMPPLCDPKdGHLLMDGGYINNLPADV 1074
Cdd:cd07207    161 VFKPVRLAK-GDVYVDGGVLDNYPVWL 186
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 441-549 1.52e-15

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: 73.90  E-value: 1.52e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  441 LLTLMKLDDPSLLDGRVTLLHVPGGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEdTCLFVTRPGEMVGQLAVLTGEP 520
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGRE-QIVGFLGPGDLFGELALLGNGP 79

                           90       100
                   ....*....|....*....|....*....
gi 2124414728  521 LIFTIKANRDCSFLSISKAHFYEIMRKQP 549
Cdd:cd00038     80 RSATVRALTDSELLVLPRSDFRRLLQEYP 108
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 459-547 2.43e-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: 2.43e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  459 LLHVPGGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEDTcLFVTRPGEMVGQLAVLTGEPLIFTIKANRDCSFLSISK 538
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQI-LAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPR 79


                   ....*....
gi 2124414728  539 AHFYEIMRK 547
Cdd:pfam00027   80 EDFLELLER 88
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 448-571 3.09e-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: 73.10  E-value: 3.09e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  448 DDPSLLDGRVTLLHVPGGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEdTCLFVTRPGEMVGQLAVLTGEPLIFTIKA 527
Cdd:COG0664      7 EELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGRE-QILGFLGPGDFFGELSLLGGEPSPATAEA 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2124414728  528 NRDCSFLSISKAHFYEIMRKQPTVVLGVAHTLVKRMSSFVRQID 571
Cdd:COG0664     86 LEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLV 129
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 169-262 1.09e-11

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: 63.11  E-value: 1.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  169 VLGHFEKPLFLELCKHMVFVQLLEGEHVFRPGEPDTSIYVVQDGRLEVCIQDTDGTEVAVKEVLAGDSVHSLLSILD--- 245
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNgpr 80

                           90       100
                   ....*....|....*....|...
gi 2124414728  246 ---VITI---IMVRLQRVTFLAL 262
Cdd:cd00038     81 satVRALtdsELLVLPRSDFRRL 103
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 565-672 1.41e-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: 62.80  E-value: 1.41e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728   565 SFVRQIDFALDWMEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLIGVVETLTHQARATTVHAV 644
Cdd:smart00100    8 EELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRRAASAAAV 87

                            90       100       110
                    ....*....|....*....|....*....|
gi 2124414728   645 --RDSELAKLPAGALTSIKRRYPQVVTRLI 672
Cdd:smart00100   88 alELATLLRIDFRDFLQLLPELPQLLLELL 117
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 169-268 5.53e-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: 58.18  E-value: 5.53e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728   169 VLGHFEKPLFLELCKHMVFVQLLEGEHVFRPGEPDTSIYVVQDGRLEVCIQDTDGTEVAVKEVLAGDSVhSLLSILD--- 245
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFF-GELALLTnsr 79

                            90       100
                    ....*....|....*....|....*.
gi 2124414728   246 ---VITIIMVRLQRVTFLALHNYLGL 268
Cdd:smart00100   80 raaSAAAVALELATLLRIDFRDFLQL 105
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
908-1086 9.69e-10

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 60.95  E-value: 9.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  908 IALVLGGGGARGCAQVGIIRALVECGIPVDMVGGTSIGAFMGALYseersCSQMRIRAKqwaegmtsvvRTMLDLTypit 987
Cdd:COG4667      6 TALVLEGGGMRGIFTAGVLDALLEEGIPFDLVIGVSAGALNGASY-----LSRQPGRAR----------RVITDYA---- 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  988 smfSGAGFnNSICSVFKDRQIEDL-WIpYFTIT---------------TDITASAMRVHT-----------DGSLWRYVR 1040
Cdd:COG4667     67 ---TDPRF-FSLRNFLRGGNLFDLdFL-YDEIPnellpfdfetfkaspREFYVVATNADTgeaeyfskkddDYDLLDALR 141

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2124414728 1041 ASMSlsgyMPPLCDP--KDGHLLMDGGYINNLPADVARSMGAKVVIAI 1086
Cdd:COG4667    142 ASSA----LPLLYPPveIDGKRYLDGGVADSIPVREAIRDGADKIVVI 185
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 910-1086 2.48e-08

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: 56.85  E-value: 2.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  910 LVLGGGGARGCAQVGIIRALVECGI-PVDMVGGTSIGAFMGALYSeerscSQMRIRA----------KQWAeGMTSVVRT 978
Cdd:cd07208      1 LVLEGGGMRGAYTAGVLDAFLEAGIrPFDLVIGVSAGALNAASYL-----SGQRGRAlrintkyatdPRYL-GLRSLLRT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  979 ----MLDLTYPITSMFSgagfnnsicSVFKDRQIEDLWIPYFTITTDI-TASAM--RVHTDGSLW-RYVRASMSLSGYMP 1050
Cdd:cd07208     75 gnlfDLDFLYDELPDGL---------DPFDFEAFAASPARFYVVATDAdTGEAVyfDKPDILDDLlDALRASSALPGLFP 145

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2124414728 1051 PlcDPKDGHLLMDGGYINNLPADVARSMGAKVVIAI 1086
Cdd:cd07208    146 P--VRIDGEPYVDGGLSDSIPVDKAIEDGADKIVVI 179
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 433-549 6.46e-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: 52.40  E-value: 6.46e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728   433 IFRAAKKDLLtlmklddpSLLDGRVTLLHVPGGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEDTcLFVTRPGEMVGQ 512
Cdd:smart00100    1 LFKNLDAEEL--------RELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQI-VGTLGPGDFFGE 71

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 2124414728   513 LAVLTGEPLI--FTIKANRDCSFLSISKAHFYEIMRKQP 549
Cdd:smart00100   72 LALLTNSRRAasAAAVALELATLLRIDFRDFLQLLPELP 110
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 187-237 1.26e-07

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: 50.69  E-value: 1.26e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2124414728  187 FVQLLEGEHVFRPGEPDTSIYVVQDGRLEVCIQDTDGTEVAVKEVLAGDSV 237
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFF 51
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 170-245 4.95e-07

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: 51.91  E-value: 4.95e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124414728  170 LGHFEKPLFLELCKHMVFVQLLEGEHVFRPGEPDTSIYVVQDGRLEVCIQDTDGTEVAVKEVLAGDSVhSLLSILD 245
Cdd:COG0664      1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFF-GELSLLG 75
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 910-1075 3.91e-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: 40.73  E-value: 3.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  910 LVLGGGGARGCAQVGIIRALVECGiP-----VDMVGGTSIGAFMGALYSEERSCSQMRiraKQWAEGMTSVvrtmLDLTY 984
Cdd:cd07213      5 LSLDGGGVKGIVQLVLLKRLAEEF-PsfldqIDLFAGTSAGSLIALGLALGYSPRQVL---KLYEEVGLKV----FSKSS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124414728  985 PITSMFSGAGFNNSICSVFKDRQIEDL---------WIPYFTITTDI-----TASAMRVHT-------DGSLWRYVRASM 1043
Cdd:cd07213     77 AGGGAGNNQYFAAGFLKAFAEVFFGDLtlgdlkrkvLVPSFQLDSGKddpnrRWKPKLFHNfpgepdlDELLVDVCLRSS 156

                          170       180       190
                   ....*....|....*....|....*....|...
gi 2124414728 1044 SLSGYMPPLcdpkDGHLlmDGG-YINNlPADVA 1075
Cdd:cd07213    157 AAPTYFPSY----QGYV--DGGvFANN-PSLCA 182
Pat_PLPL cd07232
Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin ...
 909-951 8.06e-03

Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants and fungi. 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 been found also in vertebrates.


Pssm-ID: 132870  Cd Length: 407  Bit Score: 40.33  E-value: 8.06e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2124414728  909 ALVLGGGGARGCAQVGIIRALVECGIPVDMVGGTSIGAFMGAL 951
Cdd:cd07232     69 ALCLSGGAAFAYYHFGVVKALLDADLLPNVISGTSGGSLVAAL 111
 
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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