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Conserved domains on  [gi|560992324|ref|XP_006218298|]
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patatin-like phospholipase domain-containing protein 7 isoform X4 [Vicugna pacos]

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 ...
 937-1242 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: 682.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  937 HSDFSRLARVLTGNAIALVLGGGGARGCAQVGVIRALTECGIPVDMVGGTSIGAFMGALYSEERNYSQIRIRAKQWAEDM 1016
Cdd:cd07225     1 HSDFSRLARVLTGNSIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKDM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324 1017 TSVVKTMLDLTYPITSVFSGAGFNSSLCSVFRDKQIEDLWVPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPL 1096
Cdd:cd07225    81 TSIWKKLLDLTYPITSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324 1097 CDPKDGHLLMDGGYINNLPADVARSMGAKVVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLATKVKVLNMAEIQTRL 1176
Cdd:cd07225   161 CDPKDGHLLMDGGYINNLPADVARSMGAKTVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLAEKVKVPNMAEIQSRL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 560992324 1177 AYVCCVRQLEMVKSSDYCEYLRPPIDGYGTLDFGKFDEICEVGYQHGRTVFDIWGRSGVLEKMLQD 1242
Cdd:cd07225   241 AYVSCVRQLEEVKSSDYCEYLRPPIDKYKTLDFGKFDEICEVGYQHGKTVFDGWKRSGVLEKMLQD 306
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 608-716 3.82e-22

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: 92.77  E-value: 3.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  608 SSFVRQIDFALDWVEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLVGVVETLTHQARATTVHA 687
Cdd:cd00038     7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRA 86

                          90       100
                  ....*....|....*....|....*....
gi 560992324  688 VRDSELAKLPAGALTSIKRRYPQVVTRLI 716
Cdd:cd00038    87 LTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 170-291 3.42e-18

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


:

Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 81.60  E-value: 3.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  170 VLGHFEKPLFLELCKHMVFVQLLEGEYVFRPGEPDTSVYVVQDGRLEVCTQDTDGTEVVVKEVLAGDSVhSLLSVLDVIT 249
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLF-GELALLGNGP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 560992324  250 gHTApyktvSARAAVQSTILRLPAVAFRGVFEKYPETLVRVV 291
Cdd:cd00038    80 -RSA-----TVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 485-595 9.57e-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: 77.37  E-value: 9.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  485 LLTLMKLDDPSLLDGRVTLLHVPAGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEdTCLFVTRPGEMVGQLAVLTGEP 564
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGRE-QIVGFLGPGDLFGELALLGNGP 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 560992324  565 LIFTIKANRDCSFLSISKAHFYDIMRRQPDV 595
Cdd:cd00038    80 RSATVRALTDSELLVLPRSDFRRLLQEYPEL 110
TM_EGFR-like cd12087
Transmembrane domain of the Epidermal Growth Factor Receptor family of Protein Tyrosine ...
 29-66 2.11e-03

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: 37.12  E-value: 2.11e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 560992324   29 QHSQSTMLVGVAIGVLLALTLVGITIFFVYRRVSRFRQ 66
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 ...
 937-1242 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: 682.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  937 HSDFSRLARVLTGNAIALVLGGGGARGCAQVGVIRALTECGIPVDMVGGTSIGAFMGALYSEERNYSQIRIRAKQWAEDM 1016
Cdd:cd07225     1 HSDFSRLARVLTGNSIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKDM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324 1017 TSVVKTMLDLTYPITSVFSGAGFNSSLCSVFRDKQIEDLWVPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPL 1096
Cdd:cd07225    81 TSIWKKLLDLTYPITSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324 1097 CDPKDGHLLMDGGYINNLPADVARSMGAKVVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLATKVKVLNMAEIQTRL 1176
Cdd:cd07225   161 CDPKDGHLLMDGGYINNLPADVARSMGAKTVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLAEKVKVPNMAEIQSRL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 560992324 1177 AYVCCVRQLEMVKSSDYCEYLRPPIDGYGTLDFGKFDEICEVGYQHGRTVFDIWGRSGVLEKMLQD 1242
Cdd:cd07225   241 AYVSCVRQLEEVKSSDYCEYLRPPIDKYKTLDFGKFDEICEVGYQHGKTVFDGWKRSGVLEKMLQD 306
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 952-1228 4.93e-59

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 203.98  E-value: 4.93e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  952 IALVLGGGGARGCAQVGVIRALTECGIPVDMVGGTSIGAFMGALYSEERNYSQIR-----IRAKQWAEDMTSVVKTMLDL 1026
Cdd:COG1752     7 IGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADELEelwrsLDRRDLFDLSLPRRLLRLDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324 1027 TYPITSVFSGAGFNSSLCSVFRDKQIEDLWVPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLcdPKDGHLLM 1106
Cdd:COG1752    87 GLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPV--EIDGRLYV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324 1107 DGGYINNLPADVARSMGAKVVIAIDVGSQDEtdltnygdalsgwwllwkrwnplatkvKVLNMAEIQTRLAYVCCVRQLE 1186
Cdd:COG1752   165 DGGVVNNLPVDPARALGADRVIAVDLNPPLR---------------------------KLPSLLDILGRALEIMFNSILR 217

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 560992324 1187 MVKSSDYC-EYLRPPIDGYGTLDFGKFDEICEVGYQHGRTVFD 1228
Cdd:COG1752   218 RELALEPAdILIEPDLSGISLLDFSRAEELIEAGYEAARRALD 260
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 954-1119 3.05e-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: 104.23  E-value: 3.05e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324   954 LVLGGGGARGCAQVGVIRALTECGIPVDMVGGTSIGAFMGALYSEERNYSQIR-IRAKQWAEDMTSVVKTM-------LD 1025
Cdd:pfam01734    1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPEEIEdLLLELDLNLFLSLIRKRalsllalLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  1026 LTYPITSVFSGAGFNSSLCSVFRDKQIEDL------------WVPYFTITTDITASAMRV-----HTDGSLWRYVRASMS 1088
Cdd:pfam01734   81 GLIGEGGLFDGDALRELLRKLLGDLTLEELaarlslllvvalRALLTVISTALGTRARILlpddlDDDEDLADAVLASSA 160

                          170       180       190
                   ....*....|....*....|....*....|.
gi 560992324  1089 LSGYMPPLcdPKDGHLLMDGGYINNLPADVA 1119
Cdd:pfam01734  161 LPGVFPPV--RLDGELYVDGGLVDNVPVEAA 189
PRK10279 PRK10279
patatin-like phospholipase RssA;
952-1131 4.01e-25

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 107.49  E-value: 4.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  952 IALVLGGGGARGCAQVGVIRALTECGIPVDMVGGTSIGAFMGALYSEERNYSQiriraKQWAEDMT--SVVKTMlDLTYP 1029
Cdd:PRK10279    6 IGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRLSAL-----EDWVTSFSywDVLRLM-DLSWQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324 1030 ITSVFSGAGFNSSLCSVFRDKQIEDLWVPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLcdPKDGHLLMDGG 1109
Cdd:PRK10279   80 RGGLLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPV--AHNGYWLVDGA 157

                         170       180
                  ....*....|....*....|..
gi 560992324 1110 YINNLPADVARSMGAKVVIAID 1131
Cdd:PRK10279  158 VVNPVPVSLTRALGADIVIAVD 179
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 608-716 3.82e-22

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: 92.77  E-value: 3.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  608 SSFVRQIDFALDWVEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLVGVVETLTHQARATTVHA 687
Cdd:cd00038     7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRA 86

                          90       100
                  ....*....|....*....|....*....
gi 560992324  688 VRDSELAKLPAGALTSIKRRYPQVVTRLI 716
Cdd:cd00038    87 LTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 621-708 1.36e-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: 81.89  E-value: 1.36e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324   621 VEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLVGVVETLTHQARATTVHAVRDSELAKLPAGA 700
Cdd:pfam00027    2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRED 81


                   ....*...
gi 560992324   701 LTSIKRRY 708
Cdd:pfam00027   82 FLELLERD 89
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 170-291 3.42e-18

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


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 81.60  E-value: 3.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  170 VLGHFEKPLFLELCKHMVFVQLLEGEYVFRPGEPDTSVYVVQDGRLEVCTQDTDGTEVVVKEVLAGDSVhSLLSVLDVIT 249
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLF-GELALLGNGP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 560992324  250 gHTApyktvSARAAVQSTILRLPAVAFRGVFEKYPETLVRVV 291
Cdd:cd00038    80 -RSA-----TVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 621-729 5.83e-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: 80.80  E-value: 5.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  621 VEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLVGVVETLTHQARATTVHAVRDSELAKLPAGA 700
Cdd:COG0664    19 RTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSPATAEALEDSELLRIPRED 98

                          90       100
                  ....*....|....*....|....*....
gi 560992324  701 LTSIKRRYPQVVTRLIHLLGEKILGSLQQ 729
Cdd:COG0664    99 LEELLERNPELARALLRLLARRLRQLQER 127
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 485-595 9.57e-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: 77.37  E-value: 9.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  485 LLTLMKLDDPSLLDGRVTLLHVPAGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEdTCLFVTRPGEMVGQLAVLTGEP 564
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGRE-QIVGFLGPGDLFGELALLGNGP 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 560992324  565 LIFTIKANRDCSFLSISKAHFYDIMRRQPDV 595
Cdd:cd00038    80 RSATVRALTDSELLVLPRSDFRRLLQEYPEL 110
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 171-308 2.33e-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: 2.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  171 LGHFEKPLFLELCKHMVFVQLLEGEYVFRPGEPDTSVYVVQDGRLEVCTQDTDGTEVVVKEVLAGDsvhsLLSVLDVITG 250
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGD----FFGELSLLGG 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 560992324  251 HTAPYktvSARAAVQSTILRLPAVAFRGVFEKYPETLVRVVQIIMVRL----QRVTFLALHN 308
Cdd:COG0664    77 EPSPA---TAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLrqlqERLVSLAFLS 135
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 170-293 6.54e-16

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: 75.13  E-value: 6.54e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324    170 VLGHFEKPLFLELCKHMVFVQLLEGEYVFRPGEPDTSVYVVQDGRLEVCTQDTDGTEVVVKEVLAGDSVhsllSVLDVIT 249
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFF----GELALLT 76

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 560992324    250 GHTAPYkTVSARAAVQSTILRLPAVAFRGVFEKYPETLVRVVQI 293
Cdd:smart00100   77 NSRRAA-SAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 503-591 3.52e-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: 3.52e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324   503 LLHVPAGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEDTcLFVTRPGEMVGQLAVLTGEPLIFTIKANRDCSFLSISK 582
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQI-LAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPR 79


                   ....*....
gi 560992324   583 AHFYDIMRR 591
Cdd:pfam00027   80 EDFLELLER 88
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 492-615 1.11e-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: 74.25  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  492 DDPSLLDGRVTLLHVPAGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEdTCLFVTRPGEMVGQLAVLTGEPLIFTIKA 571
Cdd:COG0664     7 EELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGRE-QILGFLGPGDFFGELSLLGGEPSPATAEA 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 560992324  572 NRDCSFLSISKAHFYDIMRRQPDVVLGVAHTVVKRVSSFVRQID 615
Cdd:COG0664    86 LEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLV 129
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 188-283 2.01e-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: 69.95  E-value: 2.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324   188 FVQLLEGEYVFRPGEPDTSVYVVQDGRLEVCTQDTDGTEVVVKEVLAGDSVHsLLSVLdvitgHTAPYkTVSARAAVQST 267
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFG-ELALL-----GGEPR-SATVVALTDSE 73

                           90
                   ....*....|....*.
gi 560992324   268 ILRLPAVAFRGVFEKY 283
Cdd:pfam00027   74 LLVIPREDFLELLERD 89
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 609-716 5.61e-13

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: 67.04  E-value: 5.61e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324    609 SFVRQIDFALDWVEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLVGVVETLTHQARATTVHAV 688
Cdd:smart00100    8 EELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRRAASAAAV 87

                            90       100       110
                    ....*....|....*....|....*....|
gi 560992324    689 --RDSELAKLPAGALTSIKRRYPQVVTRLI 716
Cdd:smart00100   88 alELATLLRIDFRDFLQLLPELPQLLLELL 117
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 485-594 1.83e-09

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


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 56.64  E-value: 1.83e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324    485 LLTLMKLDDPSLLDGRVTLLHVPAGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEDTcLFVTRPGEMVGQLAVLTGEP 564
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQI-VGTLGPGDFFGELALLTNSR 79

                            90       100       110
                    ....*....|....*....|....*....|..
gi 560992324    565 LI--FTIKANRDCSFLSISKAHFYDIMRRQPD 594
Cdd:smart00100   80 RAasAAAVALELATLLRIDFRDFLQLLPELPQ 111
TM_EGFR-like cd12087
Transmembrane domain of the Epidermal Growth Factor Receptor family of Protein Tyrosine ...
 29-66 2.11e-03

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: 37.12  E-value: 2.11e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 560992324   29 QHSQSTMLVGVAIGVLLALTLVGITIFFVYRRVSRFRQ 66
Cdd:cd12087     1 RTSKTTSIAAGVVGGLLVLVILGLIVFLFRRRRHIKRK 38
ftrB PRK09392
transcriptional activator FtrB; Provisional
 177-292 2.29e-03

transcriptional activator FtrB; Provisional


Pssm-ID: 181817 [Multi-domain]  Cd Length: 236  Bit Score: 41.16  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  177 PLFLELCKHmVFVQLLEGEYV---------FRPGEPDTSVYVVQDGRLEVCT--QDTDGTEVVVKEVlagdSVHSLLSVL 245
Cdd:PRK09392   13 PLFADMADA-TFERLMRGAFLqrfppgtmlITEGEPADFLFVVLDGLVELSAssQDRETTLAILRPV----STFILAAVV 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 560992324  246 DvitghTAPYkTVSARAAVQSTILRLPAVAFRGVFEKYPETLVRVVQ 292
Cdd:PRK09392   88 L-----DAPY-LMSARTLTRSRVLMIPAELVREAMSEDPGFMRAVVF 128
 
Name Accession Description Interval E-value
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 937-1242 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: 682.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  937 HSDFSRLARVLTGNAIALVLGGGGARGCAQVGVIRALTECGIPVDMVGGTSIGAFMGALYSEERNYSQIRIRAKQWAEDM 1016
Cdd:cd07225     1 HSDFSRLARVLTGNSIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKDM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324 1017 TSVVKTMLDLTYPITSVFSGAGFNSSLCSVFRDKQIEDLWVPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPL 1096
Cdd:cd07225    81 TSIWKKLLDLTYPITSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324 1097 CDPKDGHLLMDGGYINNLPADVARSMGAKVVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLATKVKVLNMAEIQTRL 1176
Cdd:cd07225   161 CDPKDGHLLMDGGYINNLPADVARSMGAKTVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLAEKVKVPNMAEIQSRL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 560992324 1177 AYVCCVRQLEMVKSSDYCEYLRPPIDGYGTLDFGKFDEICEVGYQHGRTVFDIWGRSGVLEKMLQD 1242
Cdd:cd07225   241 AYVSCVRQLEEVKSSDYCEYLRPPIDKYKTLDFGKFDEICEVGYQHGKTVFDGWKRSGVLEKMLQD 306
Pat_Fungal_NTE1 cd07227
Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy ...
 942-1212 5.37e-111

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: 350.25  E-value: 5.37e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  942 RLARVLTGNAIALVLGGGGARGCAQVGVIRALTECGIPVDMVGGTSIGAFMGALYSEERNYSQIRIRAKQWAEDMTSVVK 1021
Cdd:cd07227     1 RLARRLCGQAIGLVLGGGGARGISHIGILQALEEAGIPIDAIGGTSIGSFVGGLYAREADLVPIFGRAKKFAGRMASMWR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324 1022 TMLDLTYPITSVFSGAGFNSSLCSVFRDKQIEDLWVPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLCDpkD 1101
Cdd:cd07227    81 FLSDVTYPFASYTTGHEFNRGIWKTFGNTHIEDFWIPFYANSTNITHSRMEIHSSGYAWRYIRASMSLAGLLPPLSD--N 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324 1102 GHLLMDGGYINNLPADVARSMGAKVVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLATKVKVLNMAEIQTRLAYVCC 1181
Cdd:cd07227   159 GSMLLDGGYMDNLPVSPMRSLGIRDIFAVDVGSVDDRTPMDYGDSVSGVWIFFNRWNPFSSRPNVPSMAEIQSRLTYVSS 238

                         250       260       270
                  ....*....|....*....|....*....|.
gi 560992324 1182 VRQLEMVKSSDYCEYLRPPIDGYGTLDFGKF 1212
Cdd:cd07227   239 VKTLEKVKATPGCHYMRPPVQDFDTLDFGKF 269
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 952-1132 6.67e-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: 240.14  E-value: 6.67e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  952 IALVLGGGGARGCAQVGVIRALTECGIPVDMVGGTSIGAFMGALYSEERNYSQIRIRAKQWAEDMtsvvKTMLDLTYPIT 1031
Cdd:cd07205     1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAGYSPEEIEERAKLRSTDL----KALSDLTIPTA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324 1032 SVFSGAGFNSSLCSVFRDKQIEDLWVPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLCDpkDGHLLMDGGYI 1111
Cdd:cd07205    77 GLLRGDKFLELLDEYFGDRDIEDLWIPFFIVATDLTSGKLVVFRSGSLVRAVRASMSIPGIFPPVKI--DGQLLVDGGVL 154

                         170       180
                  ....*....|....*....|.
gi 560992324 1112 NNLPADVARSMGAKVVIAIDV 1132
Cdd:cd07205   155 NNLPVDVLRELGADIIIAVDL 175
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 952-1228 4.93e-59

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 203.98  E-value: 4.93e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  952 IALVLGGGGARGCAQVGVIRALTECGIPVDMVGGTSIGAFMGALYSEERNYSQIR-----IRAKQWAEDMTSVVKTMLDL 1026
Cdd:COG1752     7 IGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADELEelwrsLDRRDLFDLSLPRRLLRLDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324 1027 TYPITSVFSGAGFNSSLCSVFRDKQIEDLWVPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLcdPKDGHLLM 1106
Cdd:COG1752    87 GLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPV--EIDGRLYV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324 1107 DGGYINNLPADVARSMGAKVVIAIDVGSQDEtdltnygdalsgwwllwkrwnplatkvKVLNMAEIQTRLAYVCCVRQLE 1186
Cdd:COG1752   165 DGGVVNNLPVDPARALGADRVIAVDLNPPLR---------------------------KLPSLLDILGRALEIMFNSILR 217

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 560992324 1187 MVKSSDYC-EYLRPPIDGYGTLDFGKFDEICEVGYQHGRTVFD 1228
Cdd:COG1752   218 RELALEPAdILIEPDLSGISLLDFSRAEELIEAGYEAARRALD 260
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 954-1130 4.90e-48

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: 169.06  E-value: 4.90e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  954 LVLGGGGARGCAQVGVIRALTECGIPVDMVGGTSIGAFMGALYSEERNYSQIRIRAKqwaeDMTSVVKTMLDLTYPITSV 1033
Cdd:cd07198     1 LVLSGGGALGIYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASGRDLEEALLLLL----RLSREVRLRFDGAFPPTGR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324 1034 FSGAGFNsSLCSVFRDKQIEDLWVPYFTITTDITASAMRVH---TDGSLWRYVRASMSLSGYMPPLCDPKDGHLLMDGGY 1110
Cdd:cd07198    77 LLGILRQ-PLLSALPDDAHEDASGKLFISLTRLTDGENVLVsdtSKGELWSAVRASSSIPGYFGPVPLSFRGRRYGDGGL 155

                         170       180
                  ....*....|....*....|
gi 560992324 1111 INNLPADVarsMGAKVVIAI 1130
Cdd:cd07198   156 SNNLPVAE---LGNTINVSP 172
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 952-1132 1.12e-38

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: 142.41  E-value: 1.12e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  952 IALVLGGGGARGCAQVGVIRALTECGIPVDMVGGTSIGAFMGALYSEERN-YSQIRIRAKQWAEdmtsvVKTMLDLTYPI 1030
Cdd:cd07228     1 IGLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYAAGHLdALEEWVRSLSQRD-----VLRLLDLSASR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324 1031 TSVFSGAGFNSSLCSVFRDKQIEDLWVPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLCDpkDGHLLMDGGY 1110
Cdd:cd07228    76 SGLLKGEKVLEYLREIMGGVTIEELPIPFAAVATDLQTGKEVWFREGSLIDAIRASISIPGIFAPVEH--NGRLLVDGGV 153

                         170       180
                  ....*....|....*....|..
gi 560992324 1111 INNLPADVARSMGAKVVIAIDV 1132
Cdd:cd07228   154 VNPIPVSVARALGADIVIAVDL 175
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 954-1131 8.62e-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: 104.80  E-value: 8.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  954 LVLGGGGARGCAQVGVIRALTECGI--PVDMVGGTSIGAFMGALYseernysqirirakqwaedmtsvvktmldltYPIT 1031
Cdd:cd01819     1 LSFSGGGFRGMYHAGVLSALAERGLldCVTYLAGTSGGAWVAATL-------------------------------YPPS 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324 1032 SVFSGAGFNSSlcsvfrdkqIEDLWVPYFTITTDITASAM----RVHTDGSLWRYVRASMSLSGYMPPLCD--------- 1098
Cdd:cd01819    50 SSLDNKPRQSL---------EEALSGKLWVSFTPVTAGENvlvsRFVSKEELIRALFASGSWPSYFGLIPPaelytsksn 120

                         170       180       190
                  ....*....|....*....|....*....|....
gi 560992324 1099 -PKDGHLLMDGGYINNLPADVARSMGAKVVIAID 1131
Cdd:cd01819   121 lKEKGVRLVDGGVSNNLPAPVLLRPGRGVTLTIS 154
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 954-1119 3.05e-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: 104.23  E-value: 3.05e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324   954 LVLGGGGARGCAQVGVIRALTECGIPVDMVGGTSIGAFMGALYSEERNYSQIR-IRAKQWAEDMTSVVKTM-------LD 1025
Cdd:pfam01734    1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPEEIEdLLLELDLNLFLSLIRKRalsllalLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  1026 LTYPITSVFSGAGFNSSLCSVFRDKQIEDL------------WVPYFTITTDITASAMRV-----HTDGSLWRYVRASMS 1088
Cdd:pfam01734   81 GLIGEGGLFDGDALRELLRKLLGDLTLEELaarlslllvvalRALLTVISTALGTRARILlpddlDDDEDLADAVLASSA 160

                          170       180       190
                   ....*....|....*....|....*....|.
gi 560992324  1089 LSGYMPPLcdPKDGHLLMDGGYINNLPADVA 1119
Cdd:pfam01734  161 LPGVFPPV--RLDGELYVDGGLVDNVPVEAA 189
PRK10279 PRK10279
patatin-like phospholipase RssA;
952-1131 4.01e-25

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 107.49  E-value: 4.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  952 IALVLGGGGARGCAQVGVIRALTECGIPVDMVGGTSIGAFMGALYSEERNYSQiriraKQWAEDMT--SVVKTMlDLTYP 1029
Cdd:PRK10279    6 IGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRLSAL-----EDWVTSFSywDVLRLM-DLSWQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324 1030 ITSVFSGAGFNSSLCSVFRDKQIEDLWVPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLcdPKDGHLLMDGG 1109
Cdd:PRK10279   80 RGGLLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPV--AHNGYWLVDGA 157

                         170       180
                  ....*....|....*....|..
gi 560992324 1110 YINNLPADVARSMGAKVVIAID 1131
Cdd:PRK10279  158 VVNPVPVSLTRALGADIVIAVD 179
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 954-1134 1.65e-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: 1.65e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  954 LVLGGGGARGCAQVGVIRALTECGIPVDMVGGTSIGAFMGALYseernysqirirakqwAEDMTSVVKTM----LDLTYP 1029
Cdd:cd07209     1 LVLSGGGALGAYQAGVLKALAEAGIEPDIISGTSIGAINGALI----------------AGGDPEAVERLeklwRELSRE 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324 1030 iTSVFSGAGFNSSLCSVFRDKQIEDlwvPYFTITTDITASAMRV----HTDGSLWRYVRASMSLsgymPPLCDPK--DGH 1103
Cdd:cd07209    65 -DVFLRGLLDRALDFDTLRLLAILF---AGLVIVAVNVLTGEPVyfddIPDGILPEHLLASAAL----PPFFPPVeiDGR 136

                         170       180       190
                  ....*....|....*....|....*....|.
gi 560992324 1104 LLMDGGYINNLPADVARSMGAKVVIAIDVGS 1134
Cdd:cd07209   137 YYWDGGVVDNTPLSPAIDLGADEIIVVSLSD 167
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 608-716 3.82e-22

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: 92.77  E-value: 3.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  608 SSFVRQIDFALDWVEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLVGVVETLTHQARATTVHA 687
Cdd:cd00038     7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRA 86

                          90       100
                  ....*....|....*....|....*....
gi 560992324  688 VRDSELAKLPAGALTSIKRRYPQVVTRLI 716
Cdd:cd00038    87 LTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 621-708 1.36e-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: 81.89  E-value: 1.36e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324   621 VEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLVGVVETLTHQARATTVHAVRDSELAKLPAGA 700
Cdd:pfam00027    2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRED 81


                   ....*...
gi 560992324   701 LTSIKRRY 708
Cdd:pfam00027   82 FLELLERD 89
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 952-1128 2.16e-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: 85.48  E-value: 2.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  952 IALVLGGGGARGCAQVGVIRALTECGIPVDMVGGTSIGAFMGALYSEERNYSQIR-IRAKQWAEDMTSVVKTMLDltypi 1030
Cdd:cd07210     1 FALVLSSGFFGFYAHLGFLAALLEMGLEPSAISGTSAGALVGGLFASGISPDEMAeLLLSLERKDFWMFWDPPLR----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324 1031 TSVFSGAGFNSSLCSVFRDKQIEDLWVPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLcdPKDGHLLMDGGY 1110
Cdd:cd07210    76 GGLLSGDRFAALLREHLPPDRFEELRIPLAVSVVDLTSRETLLLSEGDLAEAVAASCAVPPLFQPV--EIGGRPFVDGGV 153

                         170
                  ....*....|....*...
gi 560992324 1111 INNLPADVARSMGAKVVI 1128
Cdd:cd07210   154 ADRLPFDALRPEIERILY 171
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 170-291 3.42e-18

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


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 81.60  E-value: 3.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  170 VLGHFEKPLFLELCKHMVFVQLLEGEYVFRPGEPDTSVYVVQDGRLEVCTQDTDGTEVVVKEVLAGDSVhSLLSVLDVIT 249
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLF-GELALLGNGP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 560992324  250 gHTApyktvSARAAVQSTILRLPAVAFRGVFEKYPETLVRVV 291
Cdd:cd00038    80 -RSA-----TVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 621-729 5.83e-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: 80.80  E-value: 5.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  621 VEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLVGVVETLTHQARATTVHAVRDSELAKLPAGA 700
Cdd:COG0664    19 RTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSPATAEALEDSELLRIPRED 98

                          90       100
                  ....*....|....*....|....*....
gi 560992324  701 LTSIKRRYPQVVTRLIHLLGEKILGSLQQ 729
Cdd:COG0664    99 LEELLERNPELARALLRLLARRLRQLQER 127
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 485-595 9.57e-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: 77.37  E-value: 9.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  485 LLTLMKLDDPSLLDGRVTLLHVPAGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEdTCLFVTRPGEMVGQLAVLTGEP 564
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGRE-QIVGFLGPGDLFGELALLGNGP 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 560992324  565 LIFTIKANRDCSFLSISKAHFYDIMRRQPDV 595
Cdd:cd00038    80 RSATVRALTDSELLVLPRSDFRRLLQEYPEL 110
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 171-308 2.33e-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: 2.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  171 LGHFEKPLFLELCKHMVFVQLLEGEYVFRPGEPDTSVYVVQDGRLEVCTQDTDGTEVVVKEVLAGDsvhsLLSVLDVITG 250
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGD----FFGELSLLGG 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 560992324  251 HTAPYktvSARAAVQSTILRLPAVAFRGVFEKYPETLVRVVQIIMVRL----QRVTFLALHN 308
Cdd:COG0664    77 EPSPA---TAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLrqlqERLVSLAFLS 135
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 170-293 6.54e-16

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: 75.13  E-value: 6.54e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324    170 VLGHFEKPLFLELCKHMVFVQLLEGEYVFRPGEPDTSVYVVQDGRLEVCTQDTDGTEVVVKEVLAGDSVhsllSVLDVIT 249
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFF----GELALLT 76

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 560992324    250 GHTAPYkTVSARAAVQSTILRLPAVAFRGVFEKYPETLVRVVQI 293
Cdd:smart00100   77 NSRRAA-SAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 954-1118 1.15e-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: 76.93  E-value: 1.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  954 LVLGGGGARGCAQVGVIRALTECGIPVDMVGGTSIGAFMGALYSEerNYSQIRIRAKQWAEDMTSVVKTMLDLTYPITSV 1033
Cdd:cd07207     2 LVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLAL--GYSAADIKDILKETDFAKLLDSPVGLLFLLPSL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324 1034 FSGAG----------------------FNSSLCSVFRDKQIEDLwvpyFTITTDITASAMRV----HT-DGSLWRYVRAS 1086
Cdd:cd07207    80 FKEGGlykgdaleewlrellkektgnsFATSLLRDLDDDLGKDL----KVVATDLTTGALVVfsaeTTpDMPVAKAVRAS 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 560992324 1087 MSLSGYMPPLCDPKdGHLLMDGGYINNLPADV 1118
Cdd:cd07207   156 MSIPFVFKPVRLAK-GDVYVDGGVLDNYPVWL 186
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 503-591 3.52e-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: 3.52e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324   503 LLHVPAGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEDTcLFVTRPGEMVGQLAVLTGEPLIFTIKANRDCSFLSISK 582
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQI-LAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPR 79


                   ....*....
gi 560992324   583 AHFYDIMRR 591
Cdd:pfam00027   80 EDFLELLER 88
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 492-615 1.11e-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: 74.25  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  492 DDPSLLDGRVTLLHVPAGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEdTCLFVTRPGEMVGQLAVLTGEPLIFTIKA 571
Cdd:COG0664     7 EELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGRE-QILGFLGPGDFFGELSLLGGEPSPATAEA 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 560992324  572 NRDCSFLSISKAHFYDIMRRQPDVVLGVAHTVVKRVSSFVRQID 615
Cdd:COG0664    86 LEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLV 129
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 188-283 2.01e-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: 69.95  E-value: 2.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324   188 FVQLLEGEYVFRPGEPDTSVYVVQDGRLEVCTQDTDGTEVVVKEVLAGDSVHsLLSVLdvitgHTAPYkTVSARAAVQST 267
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFG-ELALL-----GGEPR-SATVVALTDSE 73

                           90
                   ....*....|....*.
gi 560992324   268 ILRLPAVAFRGVFEKY 283
Cdd:pfam00027   74 LLVIPREDFLELLERD 89
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 609-716 5.61e-13

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: 67.04  E-value: 5.61e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324    609 SFVRQIDFALDWVEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLVGVVETLTHQARATTVHAV 688
Cdd:smart00100    8 EELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRRAASAAAV 87

                            90       100       110
                    ....*....|....*....|....*....|
gi 560992324    689 --RDSELAKLPAGALTSIKRRYPQVVTRLI 716
Cdd:smart00100   88 alELATLLRIDFRDFLQLLPELPQLLLELL 117
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
952-1130 7.94e-10

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 61.33  E-value: 7.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  952 IALVLGGGGARGCAQVGVIRALTECGIPVDMVGGTSIGAFMGALY-SEERNYSqIRIrakqwaedmtsvvktmldltypI 1030
Cdd:COG4667     6 TALVLEGGGMRGIFTAGVLDALLEEGIPFDLVIGVSAGALNGASYlSRQPGRA-RRV----------------------I 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324 1031 TSVFSGAGFNsSLCSVFRDKQIEDL----------WVP-----YFTITTDITASAMRVHT-----------DGSLWRYVR 1084
Cdd:COG4667    63 TDYATDPRFF-SLRNFLRGGNLFDLdflydeipneLLPfdfetFKASPREFYVVATNADTgeaeyfskkddDYDLLDALR 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 560992324 1085 ASMSlsgyMPPLCDP--KDGHLLMDGGYINNLPADVARSMGAKVVIAI 1130
Cdd:COG4667   142 ASSA----LPLLYPPveIDGKRYLDGGVADSIPVREAIRDGADKIVVI 185
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 954-1130 8.10e-10

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: 61.09  E-value: 8.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  954 LVLGGGGARGCAQVGVIRALTECGI-PVDMVGGTSIGAFMGALY-SEERNYSQIRI----RAKQWAeDMTSVVKT--MLD 1025
Cdd:cd07208     1 LVLEGGGMRGAYTAGVLDAFLEAGIrPFDLVIGVSAGALNAASYlSGQRGRALRINtkyaTDPRYL-GLRSLLRTgnLFD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324 1026 LTYPITSVFSGAgfnsslcSVFRDKQIEDLWVPYFTITTDI-TASAM--RVHTDGSLW-RYVRASMSLSGYMPPlcDPKD 1101
Cdd:cd07208    80 LDFLYDELPDGL-------DPFDFEAFAASPARFYVVATDAdTGEAVyfDKPDILDDLlDALRASSALPGLFPP--VRID 150

                         170       180
                  ....*....|....*....|....*....
gi 560992324 1102 GHLLMDGGYINNLPADVARSMGAKVVIAI 1130
Cdd:cd07208   151 GEPYVDGGLSDSIPVDKAIEDGADKIVVI 179
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 485-594 1.83e-09

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


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 56.64  E-value: 1.83e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324    485 LLTLMKLDDPSLLDGRVTLLHVPAGTVVSRQGDQDVNILFVVSGLLHVYQRKIDSEEDTcLFVTRPGEMVGQLAVLTGEP 564
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQI-VGTLGPGDFFGELALLTNSR 79

                            90       100       110
                    ....*....|....*....|....*....|..
gi 560992324    565 LI--FTIKANRDCSFLSISKAHFYDIMRRQPD 594
Cdd:smart00100   80 RAasAAAVALELATLLRIDFRDFLQLLPELPQ 111
TM_EGFR-like cd12087
Transmembrane domain of the Epidermal Growth Factor Receptor family of Protein Tyrosine ...
 29-66 2.11e-03

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: 37.12  E-value: 2.11e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 560992324   29 QHSQSTMLVGVAIGVLLALTLVGITIFFVYRRVSRFRQ 66
Cdd:cd12087     1 RTSKTTSIAAGVVGGLLVLVILGLIVFLFRRRRHIKRK 38
ftrB PRK09392
transcriptional activator FtrB; Provisional
 177-292 2.29e-03

transcriptional activator FtrB; Provisional


Pssm-ID: 181817 [Multi-domain]  Cd Length: 236  Bit Score: 41.16  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560992324  177 PLFLELCKHmVFVQLLEGEYV---------FRPGEPDTSVYVVQDGRLEVCT--QDTDGTEVVVKEVlagdSVHSLLSVL 245
Cdd:PRK09392   13 PLFADMADA-TFERLMRGAFLqrfppgtmlITEGEPADFLFVVLDGLVELSAssQDRETTLAILRPV----STFILAAVV 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 560992324  246 DvitghTAPYkTVSARAAVQSTILRLPAVAFRGVFEKYPETLVRVVQ 292
Cdd:PRK09392   88 L-----DAPY-LMSARTLTRSRVLMIPAELVREAMSEDPGFMRAVVF 128
 
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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