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Conserved domains on  [gi|1841932993|ref|XP_034293701|]
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patatin-like phospholipase domain-containing protein 6 isoform X8 [Pantherophis guttatus]

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 ...
 957-1301 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: 657.17  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  957 HSDFSRLARILTGNTIALVLGGGGARGCSHIGVIKAMEEASLPIDLIGGTSIGSFIGALYAEERSAVRTKQRAREWAKSM 1036
Cdd:cd07225      1 HSDFSRLARVLTGNSIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKDM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1037 NSVFATVLDLTYPITSMFSGSAFNTSIHKVFQDKQIEDLWLPYFNVTTDITASAMRVHKDGSvwryvrasasytpylppl 1116
Cdd:cd07225     81 TSIWKKLLDLTYPITSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGS------------------ 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1117 cdpkdshllvdgcyvnnvpgsLWRYVRASMTLSGYLPPLCDPKDGNLLMDGGYINNLPADIARNMGAKTVIAIDVGSQDE 1196
Cdd:cd07225    143 ---------------------LWRYVRASMSLSGYLPPLCDPKDGHLLMDGGYINNLPADVARSMGAKTVIAIDVGSQDE 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1197 TDLCNYGDSLSGWWLLWKRLNPWAEKVKVPDMAEIQSRLAYVSCVRQLEVVKSSSYCEYIRPPIDRFKTMDFGKFDEIYD 1276
Cdd:cd07225    202 TDLTNYGDALSGWWLLWKRWNPLAEKVKVPNMAEIQSRLAYVSCVRQLEEVKSSDYCEYLRPPIDKYKTLDFGKFDEICE 281

                          330       340
                   ....*....|....*....|....*
gi 1841932993 1277 VGYQHGKVVFGGWCRGDIIEKMVQD 1301
Cdd:cd07225    282 VGYQHGKTVFDGWKRSGVLEKMLQD 306
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 629-737 1.90e-21

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


:

Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 90.85  E-value: 1.90e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  629 SPFVRQMDFAIDWMAVEAGRALYRQGDKSDCTYIVLNGRLRSVIQKANGKKELVGEYGRGDLIGVVEALTHQVRATTVHA 708
Cdd:cd00038      7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRA 86

                           90       100
                   ....*....|....*....|....*....
gi 1841932993  709 VRDTELAKLPEGTLNNIKRRYPQVVTRLI 737
Cdd:cd00038     87 LTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 187-308 2.26e-21

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


:

Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 90.85  E-value: 2.26e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  187 VLGHFEKPLFLELCKHMTFQQCQQGEYVFRPGQPDTSIYVVQDGKLELFLSEQDGKETLVKEVFPGDSVhSLLSILDVIT 266
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLF-GELALLGNGP 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1841932993  267 ghqrpyRTVSARVAEDSTVLRLPVEAFSAVFEKYPESLVRVV 308
Cdd:cd00038     80 ------RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 506-616 1.12e-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: 83.14  E-value: 1.12e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  506 LIKLMKIEDSSLLNNRVLLHHAKAGTVIARQGDQDVSLHFVLWGCLHVYQRMIDKAEdVCLFLVQPGEMVGQLAVLTGEP 585
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGRE-QIVGFLGPGDLFGELALLGNGP 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1841932993  586 LIFTIKANRDCTFLKISKSDFYEIMREQPSV 616
Cdd:cd00038     80 RSATVRALTDSELLVLPRSDFRRLLQEYPEL 110
 
Name Accession Description Interval E-value
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 957-1301 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: 657.17  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  957 HSDFSRLARILTGNTIALVLGGGGARGCSHIGVIKAMEEASLPIDLIGGTSIGSFIGALYAEERSAVRTKQRAREWAKSM 1036
Cdd:cd07225      1 HSDFSRLARVLTGNSIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKDM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1037 NSVFATVLDLTYPITSMFSGSAFNTSIHKVFQDKQIEDLWLPYFNVTTDITASAMRVHKDGSvwryvrasasytpylppl 1116
Cdd:cd07225     81 TSIWKKLLDLTYPITSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGS------------------ 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1117 cdpkdshllvdgcyvnnvpgsLWRYVRASMTLSGYLPPLCDPKDGNLLMDGGYINNLPADIARNMGAKTVIAIDVGSQDE 1196
Cdd:cd07225    143 ---------------------LWRYVRASMSLSGYLPPLCDPKDGHLLMDGGYINNLPADVARSMGAKTVIAIDVGSQDE 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1197 TDLCNYGDSLSGWWLLWKRLNPWAEKVKVPDMAEIQSRLAYVSCVRQLEVVKSSSYCEYIRPPIDRFKTMDFGKFDEIYD 1276
Cdd:cd07225    202 TDLTNYGDALSGWWLLWKRWNPLAEKVKVPNMAEIQSRLAYVSCVRQLEEVKSSDYCEYLRPPIDKYKTLDFGKFDEICE 281

                          330       340
                   ....*....|....*....|....*
gi 1841932993 1277 VGYQHGKVVFGGWCRGDIIEKMVQD 1301
Cdd:cd07225    282 VGYQHGKTVFDGWKRSGVLEKMLQD 306
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 968-1283 5.88e-53

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 186.65  E-value: 5.88e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  968 TGNTIALVLGGGGARGCSHIGVIKAMEEASLPIDLIGGTSIGSFIGALYAEERSAvrtkQRAREWAKSMN---------S 1038
Cdd:COG1752      3 ARPKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSA----DELEELWRSLDrrdlfdlslP 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1039 VFATVLDLTYPITSMFSGSAFNTSIHKVFQDKQIEDLWLPYFNVTTDITASAMRVHKDGSVWRYVRASASytpyLPPLCD 1118
Cdd:COG1752     79 RRLLRLDLGLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAA----IPGVFP 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1119 PkdshllvdgcyvnnvpgslwryVRasmtlsgylpplcdpKDGNLLMDGGYINNLPADIARNMGAKTVIAIDVGSQDEtd 1198
Cdd:COG1752    155 P----------------------VE---------------IDGRLYVDGGVVNNLPVDPARALGADRVIAVDLNPPLR-- 195

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1199 lcnygdslsgwwllwkrlnpwaekvKVPDMAEIQSRLAYVSCVRQLEVVKSSSYC-EYIRPPIDRFKTMDFGKFDEIYDV 1277
Cdd:COG1752    196 -------------------------KLPSLLDILGRALEIMFNSILRRELALEPAdILIEPDLSGISLLDFSRAEELIEA 250


                   ....*.
gi 1841932993 1278 GYQHGK 1283
Cdd:COG1752    251 GYEAAR 256
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 974-1178 5.84e-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: 103.46  E-value: 5.84e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  974 LVLGGGGARGCSHIGVIKAMEEASLPIDLIGGTSIGSFIGALYA---------EERSAVRTKQRAREWAKSMNSVFATvL 1044
Cdd:pfam01734    1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLAlgrdpeeieDLLLELDLNLFLSLIRKRALSLLAL-L 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1045 DLTYPITSMFSGSAFNTSIHKVFQDKQIEDLWLPYFnvttditasamRVHKDGSVWRYVRASASYTPYLPPLCDPKDSHl 1124
Cdd:pfam01734   80 RGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLS-----------LLLVVALRALLTVISTALGTRARILLPDDLDD- 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1841932993 1125 lvdgcyvnnvPGSLWRYVRASMTLSGYLPPLcdPKDGNLLMDGGYINNLPADIA 1178
Cdd:pfam01734  148 ----------DEDLADAVLASSALPGVFPPV--RLDGELYVDGGLVDNVPVEAA 189
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 629-737 1.90e-21

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


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 90.85  E-value: 1.90e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  629 SPFVRQMDFAIDWMAVEAGRALYRQGDKSDCTYIVLNGRLRSVIQKANGKKELVGEYGRGDLIGVVEALTHQVRATTVHA 708
Cdd:cd00038      7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRA 86

                           90       100
                   ....*....|....*....|....*....
gi 1841932993  709 VRDTELAKLPEGTLNNIKRRYPQVVTRLI 737
Cdd:cd00038     87 LTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 187-308 2.26e-21

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


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 90.85  E-value: 2.26e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  187 VLGHFEKPLFLELCKHMTFQQCQQGEYVFRPGQPDTSIYVVQDGKLELFLSEQDGKETLVKEVFPGDSVhSLLSILDVIT 266
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLF-GELALLGNGP 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1841932993  267 ghqrpyRTVSARVAEDSTVLRLPVEAFSAVFEKYPESLVRVV 308
Cdd:cd00038     80 ------RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 188-325 1.26e-19

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: 88.89  E-value: 1.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  188 LGHFEKPLFLELCKHMTFQQCQQGEYVFRPGQPDTSIYVVQDGKLELFLSEQDGKETLVKEVFPGDSVhSLLSILDvitg 267
Cdd:COG0664      1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFF-GELSLLG---- 75

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1841932993  268 hqRPYRTVSARVAEDSTVLRLPVEAFSAVFEKYPESLVRVVQIIMVRL----QRVTFLALHN 325
Cdd:COG0664     76 --GEPSPATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLrqlqERLVSLAFLS 135
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 506-616 1.12e-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: 83.14  E-value: 1.12e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  506 LIKLMKIEDSSLLNNRVLLHHAKAGTVIARQGDQDVSLHFVLWGCLHVYQRMIDKAEdVCLFLVQPGEMVGQLAVLTGEP 585
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGRE-QIVGFLGPGDLFGELALLGNGP 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1841932993  586 LIFTIKANRDCTFLKISKSDFYEIMREQPSV 616
Cdd:cd00038     80 RSATVRALTDSELLVLPRSDFRRLLQEYPEL 110
PRK10279 PRK10279
patatin-like phospholipase RssA;
972-1140 4.56e-18

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 86.69  E-value: 4.56e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  972 IALVLGGGGARGCSHIGVIKAMEEASLPIDLIGGTSIGSFIGALYAEERSAVRTKqrareWAKSMNsvFATVL---DLTY 1048
Cdd:PRK10279     6 IGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRLSALED-----WVTSFS--YWDVLrlmDLSW 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1049 PITSMFSGSAFNTSIHKVFQDKQIEDLWLPYFNVTTDITASAMRVHKDGSVWRYVRASASYTPYLPPLcdPKDSHLLVDG 1128
Cdd:PRK10279    79 QRGGLLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPV--AHNGYWLVDG 156

                          170
                   ....*....|..
gi 1841932993 1129 CYVNNVPGSLWR 1140
Cdd:PRK10279   157 AVVNPVPVSLTR 168
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 524-612 2.29e-17

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


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 78.42  E-value: 2.29e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  524 LHHAKAGTVIARQGDQDVSLHFVLWGCLHVYQRMIDKAEdVCLFLVQPGEMVGQLAVLTGEPLIFTIKANRDCTFLKISK 603
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGRE-QILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPR 79


                   ....*....
gi 1841932993  604 SDFYEIMRE 612
Cdd:pfam00027   80 EDFLELLER 88
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 644-729 4.89e-17

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


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 77.26  E-value: 4.89e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  644 VEAGRALYRQGDKSDCTYIVLNGRLRSVIQKANGKKELVGEYGRGDLIGVVEALTHQVRATTVHAVRDTELAKLPEGTLN 723
Cdd:pfam00027    4 YKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPREDFL 83


                   ....*.
gi 1841932993  724 NIKRRY 729
Cdd:pfam00027   84 ELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 644-752 1.59e-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: 79.65  E-value: 1.59e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  644 VEAGRALYRQGDKSDCTYIVLNGRLRSVIQKANGKKELVGEYGRGDLIGVVEALTHQVRATTVHAVRDTELAKLPEGTLN 723
Cdd:COG0664     21 LKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSPATAEALEDSELLRIPREDLE 100

                           90       100
                   ....*....|....*....|....*....
gi 1841932993  724 NIKRRYPQVVTRLIHLLSQKILGNLQQLR 752
Cdd:COG0664    101 ELLERNPELARALLRLLARRLRQLQERLV 129
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 209-300 3.93e-16

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: 74.95  E-value: 3.93e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  209 QQGEYVFRPGQPDTSIYVVQDGKLELFLSEQDGKETLVKEVFPGDSVHsLLSILDvitGHQRPYrtvSARVAEDSTVLRL 288
Cdd:pfam00027    5 KAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFG-ELALLG---GEPRSA---TVVALTDSELLVI 77

                           90
                   ....*....|..
gi 1841932993  289 PVEAFSAVFEKY 300
Cdd:pfam00027   78 PREDFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 513-628 1.35e-15

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


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 76.95  E-value: 1.35e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  513 EDSSLLNNRVLLHHAKAGTVIARQGDQDVSLHFVLWGCLHVYQRMIDkAEDVCLFLVQPGEMVGQLAVLTGEPLIFTIKA 592
Cdd:COG0664      7 EELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISED-GREQILGFLGPGDFFGELSLLGGEPSPATAEA 85

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1841932993  593 NRDCTFLKISKSDFYEIMREQPSVVLSVAHTVAARM 628
Cdd:COG0664     86 LEDSELLRIPREDLEELLERNPELARALLRLLARRL 121
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 187-310 4.46e-14

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


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 70.12  E-value: 4.46e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993   187 VLGHFEKPLFLELCKHMTFQQCQQGEYVFRPGQPDTSIYVVQDGKLELFLSEQDGKETLVKEVFPGDSVhSLLSILDvit 266
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFF-GELALLT--- 76

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 1841932993   267 gHQRPYRTVSARVAEDSTVLRLPVEAFSAVFEKYPESLVRVVQI 310
Cdd:smart00100   77 -NSRRAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 644-742 6.64e-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: 60.88  E-value: 6.64e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993   644 VEAGRALYRQGDKSDCTYIVLNGRLRSVIQKANGKKELVGEYGRGDLIGVVEALTHQVRATTVhAVRDTELAKLPEGTLN 723
Cdd:smart00100   22 YPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRRAASA-AAVALELATLLRIDFR 100

                            90
                    ....*....|....*....
gi 1841932993   724 NIKRRYPQVVTRLIHLLSQ 742
Cdd:smart00100  101 DFLQLLPELPQLLLELLLE 119
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 513-614 3.45e-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: 58.95  E-value: 3.45e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993   513 EDSSLLNNRVLLHHAKAGTVIARQGDQDVSLHFVLWGCLHVYQRMIDKAEDVcLFLVQPGEMVGQLAVLTGEPLI--FTI 590
Cdd:smart00100    8 EELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQI-VGTLGPGDFFGELALLTNSRRAasAAA 86

                            90       100
                    ....*....|....*....|....
gi 1841932993   591 KANRDCTFLKISKSDFYEIMREQP 614
Cdd:smart00100   87 VALELATLLRIDFRDFLQLLPELP 110
ftrB PRK09392
transcriptional activator FtrB; Provisional
 194-309 1.11e-04

transcriptional activator FtrB; Provisional


Pssm-ID: 181817 [Multi-domain]  Cd Length: 236  Bit Score: 45.40  E-value: 1.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  194 PLFLELCKHmTFQQCQQGEYV---------FRPGQPDTSIYVVQDGKLELFlSEQDGKETLVKEVFPGDSVhsllsILDV 264
Cdd:PRK09392    13 PLFADMADA-TFERLMRGAFLqrfppgtmlITEGEPADFLFVVLDGLVELS-ASSQDRETTLAILRPVSTF-----ILAA 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1841932993  265 ITGHQrPYrTVSARVAEDSTVLRLPVEAFSAVFEKYPESLVRVVQ 309
Cdd:PRK09392    86 VVLDA-PY-LMSARTLTRSRVLMIPAELVREAMSEDPGFMRAVVF 128
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
974-1084 3.48e-04

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 44.41  E-value: 3.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  974 LVLGGGGARGCSHIGVIKAMEE-ASLPI----DLIGGTSIGSFIgAL-YAEERSAVRTKQ----------RAREWAKSMn 1037
Cdd:NF041079     4 LSLSGGGYRGLYTASVLAELEEqFGRPIadhfDLICGTSIGGIL-ALaLALEIPARELVElfeehgkdifPKRKWPRRL- 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1841932993 1038 svfatvldLTYPITSMFSGSAFNTSIHKVFQDKQIEDL----WLPYFNVTT 1084
Cdd:NF041079    82 --------LGLLKKPKYSSEPLREVLEEIFGDKTIGDLkhrvLIPAVNYTT 124
 
Name Accession Description Interval E-value
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 957-1301 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: 657.17  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  957 HSDFSRLARILTGNTIALVLGGGGARGCSHIGVIKAMEEASLPIDLIGGTSIGSFIGALYAEERSAVRTKQRAREWAKSM 1036
Cdd:cd07225      1 HSDFSRLARVLTGNSIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKDM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1037 NSVFATVLDLTYPITSMFSGSAFNTSIHKVFQDKQIEDLWLPYFNVTTDITASAMRVHKDGSvwryvrasasytpylppl 1116
Cdd:cd07225     81 TSIWKKLLDLTYPITSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGS------------------ 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1117 cdpkdshllvdgcyvnnvpgsLWRYVRASMTLSGYLPPLCDPKDGNLLMDGGYINNLPADIARNMGAKTVIAIDVGSQDE 1196
Cdd:cd07225    143 ---------------------LWRYVRASMSLSGYLPPLCDPKDGHLLMDGGYINNLPADVARSMGAKTVIAIDVGSQDE 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1197 TDLCNYGDSLSGWWLLWKRLNPWAEKVKVPDMAEIQSRLAYVSCVRQLEVVKSSSYCEYIRPPIDRFKTMDFGKFDEIYD 1276
Cdd:cd07225    202 TDLTNYGDALSGWWLLWKRWNPLAEKVKVPNMAEIQSRLAYVSCVRQLEEVKSSDYCEYLRPPIDKYKTLDFGKFDEICE 281

                          330       340
                   ....*....|....*....|....*
gi 1841932993 1277 VGYQHGKVVFGGWCRGDIIEKMVQD 1301
Cdd:cd07225    282 VGYQHGKTVFDGWKRSGVLEKMLQD 306
Pat_Fungal_NTE1 cd07227
Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy ...
 962-1271 3.11e-108

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: 343.32  E-value: 3.11e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  962 RLARILTGNTIALVLGGGGARGCSHIGVIKAMEEASLPIDLIGGTSIGSFIGALYAEERSAVRTKQRAREWAKSMNSVFA 1041
Cdd:cd07227      1 RLARRLCGQAIGLVLGGGGARGISHIGILQALEEAGIPIDAIGGTSIGSFVGGLYAREADLVPIFGRAKKFAGRMASMWR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1042 TVLDLTYPITSMFSGSAFNTSIHKVFQDKQIEDLWLPYFNVTTDITASAMRVHKDGSVwryvrasasytpylpplcdpkd 1121
Cdd:cd07227     81 FLSDVTYPFASYTTGHEFNRGIWKTFGNTHIEDFWIPFYANSTNITHSRMEIHSSGYA---------------------- 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1122 shllvdgcyvnnvpgslWRYVRASMTLSGYLPPLCDpkDGNLLMDGGYINNLPADIARNMGAKTVIAIDVGSQDETDLCN 1201
Cdd:cd07227    139 -----------------WRYIRASMSLAGLLPPLSD--NGSMLLDGGYMDNLPVSPMRSLGIRDIFAVDVGSVDDRTPMD 199

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1202 YGDSLSGWWLLWKRLNPWAEKVKVPDMAEIQSRLAYVSCVRQLEVVKSSSYCEYIRPPIDRFKTMDFGKF 1271
Cdd:cd07227    200 YGDSVSGVWIFFNRWNPFSSRPNVPSMAEIQSRLTYVSSVKTLEKVKATPGCHYMRPPVQDFDTLDFGKF 269
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 972-1191 6.98e-64

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: 214.72  E-value: 6.98e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  972 IALVLGGGGARGCSHIGVIKAMEEASLPIDLIGGTSIGSFIGALYAEERSAVRTKQRAREwaksMNSVFATVLDLTYPIT 1051
Cdd:cd07205      1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAGYSPEEIEERAKL----RSTDLKALSDLTIPTA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1052 SMFSGSAFNTSIHKVFQDKQIEDLWLPYFNVTTDITASAMRVHKDGSVWRYVRASASytpylpplcdpkdshllvdgcyv 1131
Cdd:cd07205     77 GLLRGDKFLELLDEYFGDRDIEDLWIPFFIVATDLTSGKLVVFRSGSLVRAVRASMS----------------------- 133

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1132 nnvpgslwryvrasmtLSGYLPPLCDpkDGNLLMDGGYINNLPADIARNMGAKTVIAIDV 1191
Cdd:cd07205    134 ----------------IPGIFPPVKI--DGQLLVDGGVLNNLPVDVLRELGADIIIAVDL 175
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 968-1283 5.88e-53

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 186.65  E-value: 5.88e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  968 TGNTIALVLGGGGARGCSHIGVIKAMEEASLPIDLIGGTSIGSFIGALYAEERSAvrtkQRAREWAKSMN---------S 1038
Cdd:COG1752      3 ARPKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSA----DELEELWRSLDrrdlfdlslP 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1039 VFATVLDLTYPITSMFSGSAFNTSIHKVFQDKQIEDLWLPYFNVTTDITASAMRVHKDGSVWRYVRASASytpyLPPLCD 1118
Cdd:COG1752     79 RRLLRLDLGLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAA----IPGVFP 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1119 PkdshllvdgcyvnnvpgslwryVRasmtlsgylpplcdpKDGNLLMDGGYINNLPADIARNMGAKTVIAIDVGSQDEtd 1198
Cdd:COG1752    155 P----------------------VE---------------IDGRLYVDGGVVNNLPVDPARALGADRVIAVDLNPPLR-- 195

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1199 lcnygdslsgwwllwkrlnpwaekvKVPDMAEIQSRLAYVSCVRQLEVVKSSSYC-EYIRPPIDRFKTMDFGKFDEIYDV 1277
Cdd:COG1752    196 -------------------------KLPSLLDILGRALEIMFNSILRRELALEPAdILIEPDLSGISLLDFSRAEELIEA 250


                   ....*.
gi 1841932993 1278 GYQHGK 1283
Cdd:COG1752    251 GYEAAR 256
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 974-1135 1.65e-38

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: 141.71  E-value: 1.65e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  974 LVLGGGGARGCSHIGVIKAMEEASLPIDLIGGTSIGSFIGALYAEERSAVRTKQRAREWAKSMNSVFatvlDLTYPITSM 1053
Cdd:cd07198      1 LVLSGGGALGIYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASGRDLEEALLLLLRLSREVRLRF----DGAFPPTGR 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1054 FSGSAFNTSIhKVFQDKQIEDLWLPYFNVTTDITASAMRVHKD---GSVWRYVRASASYTPYLPPLCDPKDSHLLVDGCY 1130
Cdd:cd07198     77 LLGILRQPLL-SALPDDAHEDASGKLFISLTRLTDGENVLVSDtskGELWSAVRASSSIPGYFGPVPLSFRGRRYGDGGL 155


                   ....*
gi 1841932993 1131 VNNVP 1135
Cdd:cd07198    156 SNNLP 160
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 972-1191 3.11e-34

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: 129.70  E-value: 3.11e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  972 IALVLGGGGARGCSHIGVIKAMEEASLPIDLIGGTSIGSFIGALYAEERsavrtKQRAREWAKSMNSV-FATVLDLTYPI 1050
Cdd:cd07228      1 IGLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYAAGH-----LDALEEWVRSLSQRdVLRLLDLSASR 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1051 TSMFSGSAFNTSIHKVFQDKQIEDLWLPYFNVTTDITASAMRVHKDGSVwryvrASAsytpylpplcdpkdshllvdgcy 1130
Cdd:cd07228     76 SGLLKGEKVLEYLREIMGGVTIEELPIPFAAVATDLQTGKEVWFREGSL-----IDA----------------------- 127

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1841932993 1131 vnnvpgslwryVRASMTLSGYLPPLCDpkDGNLLMDGGYINNLPADIARNMGAKTVIAIDV 1191
Cdd:cd07228    128 -----------IRASISIPGIFAPVEH--NGRLLVDGGVVNPIPVSVARALGADIVIAVDL 175
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 974-1178 5.84e-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: 103.46  E-value: 5.84e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  974 LVLGGGGARGCSHIGVIKAMEEASLPIDLIGGTSIGSFIGALYA---------EERSAVRTKQRAREWAKSMNSVFATvL 1044
Cdd:pfam01734    1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLAlgrdpeeieDLLLELDLNLFLSLIRKRALSLLAL-L 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1045 DLTYPITSMFSGSAFNTSIHKVFQDKQIEDLWLPYFnvttditasamRVHKDGSVWRYVRASASYTPYLPPLCDPKDSHl 1124
Cdd:pfam01734   80 RGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLS-----------LLLVVALRALLTVISTALGTRARILLPDDLDD- 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1841932993 1125 lvdgcyvnnvPGSLWRYVRASMTLSGYLPPLcdPKDGNLLMDGGYINNLPADIA 1178
Cdd:pfam01734  148 ----------DEDLADAVLASSALPGVFPPV--RLDGELYVDGGLVDNVPVEAA 189
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 629-737 1.90e-21

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


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 90.85  E-value: 1.90e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  629 SPFVRQMDFAIDWMAVEAGRALYRQGDKSDCTYIVLNGRLRSVIQKANGKKELVGEYGRGDLIGVVEALTHQVRATTVHA 708
Cdd:cd00038      7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRA 86

                           90       100
                   ....*....|....*....|....*....
gi 1841932993  709 VRDTELAKLPEGTLNNIKRRYPQVVTRLI 737
Cdd:cd00038     87 LTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 187-308 2.26e-21

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


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 90.85  E-value: 2.26e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  187 VLGHFEKPLFLELCKHMTFQQCQQGEYVFRPGQPDTSIYVVQDGKLELFLSEQDGKETLVKEVFPGDSVhSLLSILDVIT 266
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLF-GELALLGNGP 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1841932993  267 ghqrpyRTVSARVAEDSTVLRLPVEAFSAVFEKYPESLVRVV 308
Cdd:cd00038     80 ------RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 974-1193 2.62e-20

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: 90.81  E-value: 2.62e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  974 LVLGGGGARGCSHIGVIKAMEEASLPIDLIGGTSIGSFIGALYA-EERSAVrtkQRAREWAKSM--NSVFATVLDLTYPI 1050
Cdd:cd07209      1 LVLSGGGALGAYQAGVLKALAEAGIEPDIISGTSIGAINGALIAgGDPEAV---ERLEKLWRELsrEDVFLRGLLDRALD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1051 TSMFSGSAfntsihkvfqdkqieDLWLPYFNVTTDITASAMRVHKDGSVWR---YVRASASYTPYLPPlcdpkdshllvd 1127
Cdd:cd07209     78 FDTLRLLA---------------ILFAGLVIVAVNVLTGEPVYFDDIPDGIlpeHLLASAALPPFFPP------------ 130

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1841932993 1128 gcyvnnvpgslwRYVrasmtlsgylpplcdpkDGNLLMDGGYINNLPADIARNMGAKTVIAIDVGS 1193
Cdd:cd07209    131 ------------VEI-----------------DGRYYWDGGVVDNTPLSPAIDLGADEIIVVSLSD 167
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 188-325 1.26e-19

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: 88.89  E-value: 1.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  188 LGHFEKPLFLELCKHMTFQQCQQGEYVFRPGQPDTSIYVVQDGKLELFLSEQDGKETLVKEVFPGDSVhSLLSILDvitg 267
Cdd:COG0664      1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFF-GELSLLG---- 75

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1841932993  268 hqRPYRTVSARVAEDSTVLRLPVEAFSAVFEKYPESLVRVVQIIMVRL----QRVTFLALHN 325
Cdd:COG0664     76 --GEPSPATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLrqlqERLVSLAFLS 135
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 506-616 1.12e-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: 83.14  E-value: 1.12e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  506 LIKLMKIEDSSLLNNRVLLHHAKAGTVIARQGDQDVSLHFVLWGCLHVYQRMIDKAEdVCLFLVQPGEMVGQLAVLTGEP 585
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGRE-QIVGFLGPGDLFGELALLGNGP 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1841932993  586 LIFTIKANRDCTFLKISKSDFYEIMREQPSV 616
Cdd:cd00038     80 RSATVRALTDSELLVLPRSDFRRLLQEYPEL 110
PRK10279 PRK10279
patatin-like phospholipase RssA;
972-1140 4.56e-18

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 86.69  E-value: 4.56e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  972 IALVLGGGGARGCSHIGVIKAMEEASLPIDLIGGTSIGSFIGALYAEERSAVRTKqrareWAKSMNsvFATVL---DLTY 1048
Cdd:PRK10279     6 IGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRLSALED-----WVTSFS--YWDVLrlmDLSW 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1049 PITSMFSGSAFNTSIHKVFQDKQIEDLWLPYFNVTTDITASAMRVHKDGSVWRYVRASASYTPYLPPLcdPKDSHLLVDG 1128
Cdd:PRK10279    79 QRGGLLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPV--AHNGYWLVDG 156

                          170
                   ....*....|..
gi 1841932993 1129 CYVNNVPGSLWR 1140
Cdd:PRK10279   157 AVVNPVPVSLTR 168
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 524-612 2.29e-17

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


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 78.42  E-value: 2.29e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  524 LHHAKAGTVIARQGDQDVSLHFVLWGCLHVYQRMIDKAEdVCLFLVQPGEMVGQLAVLTGEPLIFTIKANRDCTFLKISK 603
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGRE-QILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPR 79


                   ....*....
gi 1841932993  604 SDFYEIMRE 612
Cdd:pfam00027   80 EDFLELLER 88
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 644-729 4.89e-17

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


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 77.26  E-value: 4.89e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  644 VEAGRALYRQGDKSDCTYIVLNGRLRSVIQKANGKKELVGEYGRGDLIGVVEALTHQVRATTVHAVRDTELAKLPEGTLN 723
Cdd:pfam00027    4 YKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPREDFL 83


                   ....*.
gi 1841932993  724 NIKRRY 729
Cdd:pfam00027   84 ELLERD 89
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 972-1141 1.01e-16

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: 80.85  E-value: 1.01e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  972 IALVLGGGGARGCSHIGVIKAMEEASLPIDLIGGTSIGSFIGALYA------EERSAVRTKQRAREWAKSMNSVFatvld 1045
Cdd:cd07210      1 FALVLSSGFFGFYAHLGFLAALLEMGLEPSAISGTSAGALVGGLFAsgispdEMAELLLSLERKDFWMFWDPPLR----- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1046 ltypiTSMFSGSAFNTSIHKVFQDKQIEDLWLPYFNVTTDITASAMRVHKDGSVWRYVRASASytpyLPPLCDPK--DSH 1123
Cdd:cd07210     76 -----GGLLSGDRFAALLREHLPPDRFEELRIPLAVSVVDLTSRETLLLSEGDLAEAVAASCA----VPPLFQPVeiGGR 146

                          170
                   ....*....|....*...
gi 1841932993 1124 LLVDGCYVNNVPGSLWRY 1141
Cdd:cd07210    147 PFVDGGVADRLPFDALRP 164
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 644-752 1.59e-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: 79.65  E-value: 1.59e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  644 VEAGRALYRQGDKSDCTYIVLNGRLRSVIQKANGKKELVGEYGRGDLIGVVEALTHQVRATTVHAVRDTELAKLPEGTLN 723
Cdd:COG0664     21 LKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSPATAEALEDSELLRIPREDLE 100

                           90       100
                   ....*....|....*....|....*....
gi 1841932993  724 NIKRRYPQVVTRLIHLLSQKILGNLQQLR 752
Cdd:COG0664    101 ELLERNPELARALLRLLARRLRQLQERLV 129
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 209-300 3.93e-16

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: 74.95  E-value: 3.93e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  209 QQGEYVFRPGQPDTSIYVVQDGKLELFLSEQDGKETLVKEVFPGDSVHsLLSILDvitGHQRPYrtvSARVAEDSTVLRL 288
Cdd:pfam00027    5 KAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFG-ELALLG---GEPRSA---TVVALTDSELLVI 77

                           90
                   ....*....|..
gi 1841932993  289 PVEAFSAVFEKY 300
Cdd:pfam00027   78 PREDFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 513-628 1.35e-15

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


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 76.95  E-value: 1.35e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  513 EDSSLLNNRVLLHHAKAGTVIARQGDQDVSLHFVLWGCLHVYQRMIDkAEDVCLFLVQPGEMVGQLAVLTGEPLIFTIKA 592
Cdd:COG0664      7 EELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISED-GREQILGFLGPGDFFGELSLLGGEPSPATAEA 85

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1841932993  593 NRDCTFLKISKSDFYEIMREQPSVVLSVAHTVAARM 628
Cdd:COG0664     86 LEDSELLRIPREDLEELLERNPELARALLRLLARRL 121
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 974-1190 7.82e-15

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: 73.22  E-value: 7.82e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  974 LVLGGGGARGCSHIGVIKAMEEASL--PIDLIGGTSIGSFIGALYaeersavrtkqrarewaksmnsvfatvldltYPIT 1051
Cdd:cd01819      1 LSFSGGGFRGMYHAGVLSALAERGLldCVTYLAGTSGGAWVAATL-------------------------------YPPS 49

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1052 SMFSGSAFNTSihkvfqdkqIEDLWLPYFNVTTDITASAMRVhkdgsVWRYVRasasytpylpplcdpkdshllvdgcyv 1131
Cdd:cd01819     50 SSLDNKPRQSL---------EEALSGKLWVSFTPVTAGENVL-----VSRFVS--------------------------- 88

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1841932993 1132 nnvPGSLWRYVRASMTLSGYLPPLCD----------PKDGNLLMDGGYINNLPADIARNMGAKTVIAID 1190
Cdd:cd01819     89 ---KEELIRALFASGSWPSYFGLIPPaelytsksnlKEKGVRLVDGGVSNNLPAPVLLRPGRGVTLTIS 154
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 974-1139 1.39e-14

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: 73.85  E-value: 1.39e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  974 LVLGGGGARGCSHIGVIKAMEEASLPIDLIGGTSIGSFIGALYAEERSAVRTKQRARE--WAKSMNS----VFATVLDLT 1047
Cdd:cd07207      2 LVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLALGYSAADIKDILKEtdFAKLLDSpvglLFLLPSLFK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1048 YPITS--------------MFSGSAFNTSIHKVFQDKQIEDLWLpyfnVTTDITASAMRVHK-----DGSVWRYVRASAS 1108
Cdd:cd07207     82 EGGLYkgdaleewlrellkEKTGNSFATSLLRDLDDDLGKDLKV----VATDLTTGALVVFSaettpDMPVAKAVRASMS 157

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1841932993 1109 YTPYLPPLCDPKdSHLLVDGCYVNNVPGSLW 1139
Cdd:cd07207    158 IPFVFKPVRLAK-GDVYVDGGVLDNYPVWLF 187
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 187-310 4.46e-14

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


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 70.12  E-value: 4.46e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993   187 VLGHFEKPLFLELCKHMTFQQCQQGEYVFRPGQPDTSIYVVQDGKLELFLSEQDGKETLVKEVFPGDSVhSLLSILDvit 266
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFF-GELALLT--- 76

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 1841932993   267 gHQRPYRTVSARVAEDSTVLRLPVEAFSAVFEKYPESLVRVVQI 310
Cdd:smart00100   77 -NSRRAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 644-742 6.64e-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: 60.88  E-value: 6.64e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993   644 VEAGRALYRQGDKSDCTYIVLNGRLRSVIQKANGKKELVGEYGRGDLIGVVEALTHQVRATTVhAVRDTELAKLPEGTLN 723
Cdd:smart00100   22 YPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRRAASA-AAVALELATLLRIDFR 100

                            90
                    ....*....|....*....
gi 1841932993   724 NIKRRYPQVVTRLIHLLSQ 742
Cdd:smart00100  101 DFLQLLPELPQLLLELLLE 119
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 513-614 3.45e-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: 58.95  E-value: 3.45e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993   513 EDSSLLNNRVLLHHAKAGTVIARQGDQDVSLHFVLWGCLHVYQRMIDKAEDVcLFLVQPGEMVGQLAVLTGEPLI--FTI 590
Cdd:smart00100    8 EELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQI-VGTLGPGDFFGELALLTNSRRAasAAA 86

                            90       100
                    ....*....|....*....|....
gi 1841932993   591 KANRDCTFLKISKSDFYEIMREQP 614
Cdd:smart00100   87 VALELATLLRIDFRDFLQLLPELP 110
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 965-1133 8.40e-09

Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function prediction only];


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 58.76  E-value: 8.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  965 RILTgntialvLGGGGARGCSHIGVIKAMEEA-SLPI----DLIGGTSIGSFIGALYAEERSA--VRT--KQRARE-WAK 1034
Cdd:COG3621      8 RILS-------LDGGGIRGLIPARILAELEERlGKPLaeyfDLIAGTSTGGIIALGLAAGYSAeeILDlyEEEGKEiFPK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1035 SMNSVFATVLDLTYPItsmFSGSAFNTSIHKVFQDKQIEDLWLPYFNVTTDITASAMRVHK----------DGSVWRYVR 1104
Cdd:COG3621     81 SRWRKLLSLRGLFGPK---YDSEGLEKVLKEYFGDTTLGDLKTPVLIPSYDLDNGKPVFFKsphakfdrdrDFLLVDVAR 157

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1841932993 1105 ASASYTPYLPPLC---DPKDSHLLVDGC-YVNN 1133
Cdd:COG3621    158 ATSAAPTYFPPAQiknLTGEGYALIDGGvFANN 190
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
968-1283 1.28e-08

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 57.87  E-value: 1.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  968 TGNTIALVLGGGGARGcshI---GVIKAMEEASLPIDLIGGTSIGSFIGALYAeersavrTKQRARewAKSMNSVFAT-- 1042
Cdd:COG4667      2 NMMKTALVLEGGGMRG---IftaGVLDALLEEGIPFDLVIGVSAGALNGASYL-------SRQPGR--ARRVITDYATdp 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1043 -VLDLTYPITsmfSGSAFNTsiHKVFQdkQIEDLWLPyFNVTTdITASAMRVhkdgsvwrYVRAS--ASYTP-YLPPLCD 1118
Cdd:COG4667     70 rFFSLRNFLR---GGNLFDL--DFLYD--EIPNELLP-FDFET-FKASPREF--------YVVATnaDTGEAeYFSKKDD 132

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1119 PKDshllvdgcyvnnvpgsLWRYVRASMTlsgyLPPLCDP--KDGNLLMDGGYINNLPADIARNMGAKTVIAIdvGSQDE 1196
Cdd:COG4667    133 DYD----------------LLDALRASSA----LPLLYPPveIDGKRYLDGGVADSIPVREAIRDGADKIVVI--LTRPR 190

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1197 tdlcNYGDSLSgwWLlwKRLNPWAEKvKVPDMAE-IQSR-LAYVSCVRQLE--------VVksssyceyIRPP----IDR 1262
Cdd:COG4667    191 ----GYRKKPS--KF--KRLLRRLYR-KYPKLVEaLLNRhERYNETLEFIEqlekegkiFV--------IRPPkpltVSR 253

                          330       340
                   ....*....|....*....|.
gi 1841932993 1263 FkTMDFGKFDEIYDVGYQHGK 1283
Cdd:COG4667    254 L-ERDPEKLRALYELGYEDAR 273
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 974-1280 3.10e-07

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: 53.38  E-value: 3.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  974 LVLGGGGARGCSHIGVIKAMEEASL-PIDLIGGTSIGSFIGALYAeersavrTKQRAR------------EWAkSMNSVF 1040
Cdd:cd07208      1 LVLEGGGMRGAYTAGVLDAFLEAGIrPFDLVIGVSAGALNAASYL-------SGQRGRalrintkyatdpRYL-GLRSLL 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1041 AT----VLDLTYPITSMfsgsafntsIHKVFQDKQIEDLWLPYFNVTTDI-TASAM--RVHKDGSVW-RYVRASASytpy 1112
Cdd:cd07208     73 RTgnlfDLDFLYDELPD---------GLDPFDFEAFAASPARFYVVATDAdTGEAVyfDKPDILDDLlDALRASSA---- 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1113 LPPLCDPkdshllvdgCYVNNVPgslwrYVrasmtlsgylpplcdpkdgnllmDGGYINNLPADIARNMGAKTVIAIDvg 1192
Cdd:cd07208    140 LPGLFPP---------VRIDGEP-----YV-----------------------DGGLSDSIPVDKAIEDGADKIVVIL-- 180

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1193 SQDETDlcNYGDSLSGWwlLWKRLnpwaeKVKVPDMAE--IQSRLAYVSC---VRQLEVVKSSSyceYIRPP----IDRF 1263
Cdd:cd07208    181 TRPRGY--RKKPSKSSP--LAKLL-----YRKYPNLVEalLRRHSRYNETlefIRRLEAEGKIF---VIAPEkplkVSRL 248

                          330
                   ....*....|....*..
gi 1841932993 1264 kTMDFGKFDEIYDVGYQ 1280
Cdd:cd07208    249 -ERDPEKLEALYDLGYE 264
Pat_PLPL cd07232
Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin ...
 935-1017 7.31e-07

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: 53.42  E-value: 7.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  935 SRRSPNKLREMYgKVFEKNadrhsdfsrlarilTGNTiALVLGGGGARGCSHIGVIKAMEEASLPIDLIGGTSIGSFIGA 1014
Cdd:cd07232     47 SQLDLEEKRRLF-KRLSTN--------------YGRT-ALCLSGGAAFAYYHFGVVKALLDADLLPNVISGTSGGSLVAA 110


                   ...
gi 1841932993 1015 LYA 1017
Cdd:cd07232    111 LLC 113
Pat_TGL4-5_like cd07230
Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in ...
 964-1014 5.49e-06

Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in triacylglycerol mobilization and degradation; they are found in lipid particles. Tgl4 is a functional ortholog of mammalian adipose TG lipase (ATGL) and is phosphorylated and activated by cyclin-dependent kinase 1 (Cdk1/Cdc28). TGL4 is 30% homologus to TGL3, whereas TGL5 is 26% homologus to TGL3. This family includes TGL4 (STC1) and TGL5 (STC2) from Saccharomyces cerevisiae.


Pssm-ID: 132868  Cd Length: 421  Bit Score: 50.68  E-value: 5.49e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1841932993  964 ARILTGNTiALVLGGGGARGCSHIGVIKAMEEASLPIDLIGGTSIGSFIGA 1014
Cdd:cd07230     67 TRKNFGRT-ALLLSGGGTFGMFHIGVLKALFEANLLPRIISGSSAGSIVAA 116
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 959-1015 1.72e-05

Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are involved in triacylglycerol mobilization and degradation; they are found in lipid particles. TGL4 is 30% homologus to TGL3, whereas TGL5 is 26% homologus to TGL3. Sugar-Dependent 1 (SDP1) lipase has a patatin-like acyl-hydrolase domain that initiates the breakdown of storage oil in germinating Arabidopsis seeds. This family includes subfamilies of proteins: TGL3, TGL4, TGL5, and SDP1.


Pssm-ID: 132845  Cd Length: 298  Bit Score: 48.36  E-value: 1.72e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1841932993  959 DFSRLARILTGNTiALVLGGGGARGCSHIGVIKAMEEASLPIDLIGGTSIGSFIGAL 1015
Cdd:cd07206     58 DFFRRARHAFGRT-ALMLSGGASLGLFHLGVVKALWEQDLLPRVISGSSAGAIVAAL 113
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
 974-1133 1.80e-05

Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; 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: 132838 [Multi-domain]  Cd Length: 258  Bit Score: 48.10  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  974 LVLGGGGARGCSHIGVIKAMEEA---SLPI----DLIGGTSIGSFIG-ALYAEERSAvrtKQRAREWAKSMNSVFATVL- 1044
Cdd:cd07199      2 LSLDGGGIRGIIPAEILAELEKRlgkPSRIadlfDLIAGTSTGGIIAlGLALGRYSA---EELVELYEELGRKIFPRVLv 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1045 ---DLTYPITSMFSgsafntSIHkvfqdkqiEDLWLPYFNVttditasamrvhkdgSVWRYVRASASYTPYLPP--LCDP 1119
Cdd:cd07199     79 tayDLSTGKPVVFS------NYD--------AEEPDDDDDF---------------KLWDVARATSAAPTYFPPavIESG 129

                          170
                   ....*....|....*
gi 1841932993 1120 KDSHLLVDG-CYVNN 1133
Cdd:cd07199    130 GDEGAFVDGgVAANN 144
Pat_SDP1-like cd07231
Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like ...
 916-1029 3.23e-05

Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like acyl-hydrolase domain that initiates the breakdown of storage oil in germinating Arabidopsis seeds. This acyl-hydrolase domain is homologus to yeast triacylglycerol lipase 3 and human adipose triglyceride lipase. This family includes SDP1 from Arabidopsis thaliana.


Pssm-ID: 132869  Cd Length: 323  Bit Score: 47.83  E-value: 3.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  916 NMRSWCSGHLH---IKCPRRVfsRRSPNKLREMYGKVFEKNADRHSDFSRLA-----RILTGNTiALVLGGGGARGCSHI 987
Cdd:cd07231      8 NLGNMCNPELHkgrLEVPRLI--RDYIAEVKAQLRAVVESDEDELSLEEKLAffqetRHAFGRT-ALLLSGGAALGTFHV 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1841932993  988 GVIKAMEEASLPIDLIGGTSIGSFIGALYAEERSA-VRTKQRA 1029
Cdd:cd07231     85 GVVRTLVEHQLLPRVIAGSSVGSIVCAIIATRTDEeLQSFFRA 127
Pat_TGL3_like cd07229
Triacylglycerol lipase 3; Triacylglycerol lipase 3 (TGL3) are responsible for all the TAG ...
 959-1015 1.08e-04

Triacylglycerol lipase 3; Triacylglycerol lipase 3 (TGL3) are responsible for all the TAG lipase activity of the lipid particle. Triacylglycerol (TAG) lipases are also necessary for the mobilization of TAG stored in lipid particles. TGL3 contains the consensus sequence motif GXSXG, which is found in lipolytic enzymes. This family includes Tgl3p from Saccharomyces cerevisiae.


Pssm-ID: 132867  Cd Length: 391  Bit Score: 46.14  E-value: 1.08e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1841932993  959 DFSRLARILTGNTiALVLGGGGARGCSHIGVIKAMEEASLPIDLIGGTSIGSFIGAL 1015
Cdd:cd07229     72 DFFHDTRQSFGRT-ALVLQGGSIFGLCHLGVVKALWLRGLLPRIITGTATGALIAAL 127
ftrB PRK09392
transcriptional activator FtrB; Provisional
 194-309 1.11e-04

transcriptional activator FtrB; Provisional


Pssm-ID: 181817 [Multi-domain]  Cd Length: 236  Bit Score: 45.40  E-value: 1.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  194 PLFLELCKHmTFQQCQQGEYV---------FRPGQPDTSIYVVQDGKLELFlSEQDGKETLVKEVFPGDSVhsllsILDV 264
Cdd:PRK09392    13 PLFADMADA-TFERLMRGAFLqrfppgtmlITEGEPADFLFVVLDGLVELS-ASSQDRETTLAILRPVSTF-----ILAA 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1841932993  265 ITGHQrPYrTVSARVAEDSTVLRLPVEAFSAVFEKYPESLVRVVQ 309
Cdd:PRK09392    86 VVLDA-PY-LMSARTLTRSRVLMIPAELVREAMSEDPGFMRAVVF 128
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
974-1084 3.48e-04

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 44.41  E-value: 3.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  974 LVLGGGGARGCSHIGVIKAMEE-ASLPI----DLIGGTSIGSFIgAL-YAEERSAVRTKQ----------RAREWAKSMn 1037
Cdd:NF041079     4 LSLSGGGYRGLYTASVLAELEEqFGRPIadhfDLICGTSIGGIL-ALaLALEIPARELVElfeehgkdifPKRKWPRRL- 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1841932993 1038 svfatvldLTYPITSMFSGSAFNTSIHKVFQDKQIEDL----WLPYFNVTT 1084
Cdd:NF041079    82 --------LGLLKKPKYSSEPLREVLEEIFGDKTIGDLkhrvLIPAVNYTT 124
Pat17_PNPLA8_PNPLA9_like4 cd07217
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 974-1154 8.82e-04

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: 132856 [Multi-domain]  Cd Length: 344  Bit Score: 43.25  E-value: 8.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993  974 LVLGGGGARGCSHIGVIKAMEEA-----SLP-------IDLIGGTSIGSFIGALYAEERSAVRTKQRAREWAKSM----- 1036
Cdd:cd07217      4 LALDGGGIRGLLSVEILGRIEKDlrthlDDPefrlgdyFDFVGGTSTGSIIAACIALGMSVTDLLSFYTLNGVNMfdkaw 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841932993 1037 --NSVFATVLDLTYPITSMfsGSAFNTsihkVFQDKQIEDlwlPYFNVTTDITasaMRVHKDGSVWryvrasasytpylp 1114
Cdd:cd07217     84 laQRLFLNKLYNQYDPTNL--GKKLNT----VFPETTLGD---DTLRTLLMIV---TRNATTGSPW-------------- 137

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1841932993 1115 PLCDPKDSHLLVDGCYVNNVPGSLWRYVRASMTLSGYLPP 1154
Cdd:cd07217    138 PVCNNPEAKYNDSDRSDCNLDLPLWQLVRASTAAPTFFPP 177
 
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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