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Conserved domains on  [gi|679140551|gb|KFW68727|]
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Patatin-like phospholipase domain-containing protein 7, partial [Pygoscelis adeliae]

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 ...
 899-1204 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: 692.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  899 HSDFSRLARVLTGNAIALVLGGGGARGCSQVGVIRALIEAGIPVDMIGGTSIGAFMSALYAEERSYNQMRIKARQWAMVM 978
Cdd:cd07225     1 HSDFSRLARVLTGNSIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKDM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  979 NSVFKTILDLTYPITSMFSGAAFNNSINSIFKDKQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPL 1058
Cdd:cd07225    81 TSIWKKLLDLTYPITSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551 1059 CDPKDGHLLMDGGYINNLPADVARSMGAKVVIAIDVGSRDETDLTNYGDCLSGWWLLWKRWNPLAEKIKVLNMAEIQTRL 1138
Cdd:cd07225   161 CDPKDGHLLMDGGYINNLPADVARSMGAKTVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLAEKVKVPNMAEIQSRL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 679140551 1139 AYVCCVRQLEMVKNSDYCEYIRPPIDRYRTLDFGKFDEICEVGYQHGKTVFNVWCRSGVLDKMLRD 1204
Cdd:cd07225   241 AYVSCVRQLEEVKSSDYCEYLRPPIDKYKTLDFGKFDEICEVGYQHGKTVFDGWKRSGVLEKMLQD 306
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 573-681 2.04e-22

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


:

Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 93.54  E-value: 2.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  573 SPFVRQIDFALDWMEVEAGRAVYRQGDKSDCTYIVLNGRLRSVIRMDDGKKHLTGEYGRGDLIGVVEALTHQPRATTVHA 652
Cdd:cd00038     7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRA 86

                          90       100
                  ....*....|....*....|....*....
gi 679140551  653 VRDSELAKLPEGALTSIKRKFPQVVTRLI 681
Cdd:cd00038    87 LTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 137-258 5.75e-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: 89.31  E-value: 5.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  137 VLGHFEKPLFLELCKHMFFVQLHEGEYIFRPGQLDNSIYVVQDGKLEVCIQESDGTEVVVKEVLAGDSVhSLLSILdviT 216
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLF-GELALL---G 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 679140551  217 GHPAPYktvSARAAIPSTILRLPASAFQDVFQKYPETLVRVV 258
Cdd:cd00038    77 NGPRSA---TVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 456-560 6.89e-16

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


:

Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 75.05  E-value: 6.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  456 LDDPSL--LNGKVTLHQVTAGTVLSRQGDQDVNVCFVVSGMLHVYQRKIDSEEdTCLFITHPGELVGQLAVLTGEPLIFT 533
Cdd:cd00038     5 LDDEELeeLADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGRE-QIVGFLGPGDLFGELALLGNGPRSAT 83

                          90       100
                  ....*....|....*....|....*..
gi 679140551  534 IKANRDCSFLSISKSHFYEIMREQPSV 560
Cdd:cd00038    84 VRALTDSELLVLPRSDFRRLLQEYPEL 110
 
Name Accession Description Interval E-value
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 899-1204 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: 692.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  899 HSDFSRLARVLTGNAIALVLGGGGARGCSQVGVIRALIEAGIPVDMIGGTSIGAFMSALYAEERSYNQMRIKARQWAMVM 978
Cdd:cd07225     1 HSDFSRLARVLTGNSIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKDM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  979 NSVFKTILDLTYPITSMFSGAAFNNSINSIFKDKQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPL 1058
Cdd:cd07225    81 TSIWKKLLDLTYPITSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551 1059 CDPKDGHLLMDGGYINNLPADVARSMGAKVVIAIDVGSRDETDLTNYGDCLSGWWLLWKRWNPLAEKIKVLNMAEIQTRL 1138
Cdd:cd07225   161 CDPKDGHLLMDGGYINNLPADVARSMGAKTVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLAEKVKVPNMAEIQSRL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 679140551 1139 AYVCCVRQLEMVKNSDYCEYIRPPIDRYRTLDFGKFDEICEVGYQHGKTVFNVWCRSGVLDKMLRD 1204
Cdd:cd07225   241 AYVSCVRQLEEVKSSDYCEYLRPPIDKYKTLDFGKFDEICEVGYQHGKTVFDGWKRSGVLEKMLQD 306
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 914-1189 9.09e-61

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 208.99  E-value: 9.09e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  914 IALVLGGGGARGCSQVGVIRALIEAGIPVDMIGGTSIGAFMSALYAEERSYNQMR-----IKARQWAMVMNSVFKTILDL 988
Cdd:COG1752     7 IGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADELEelwrsLDRRDLFDLSLPRRLLRLDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  989 TYPITSMFSGAAFNNSINSIFKDKQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLcdPKDGHLLM 1068
Cdd:COG1752    87 GLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPV--EIDGRLYV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551 1069 DGGYINNLPADVARSMGAKVVIAIDVGSRDEtdltnygdclsgwwllwkrwnplaekiKVLNMAEIQTRLAYVCCVRQLE 1148
Cdd:COG1752   165 DGGVVNNLPVDPARALGADRVIAVDLNPPLR---------------------------KLPSLLDILGRALEIMFNSILR 217

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 679140551 1149 MVKNSDYC-EYIRPPIDRYRTLDFGKFDEICEVGYQHGKTVF 1189
Cdd:COG1752   218 RELALEPAdILIEPDLSGISLLDFSRAEELIEAGYEAARRAL 259
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 916-1081 5.91e-29

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: 115.01  E-value: 5.91e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551   916 LVLGGGGARGCSQVGVIRALIEAGIPVDMIGGTSIGAFMSALYA--------EERSYNQMRIKARQWAMVMNSVFKTILD 987
Cdd:pfam01734    1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLAlgrdpeeiEDLLLELDLNLFLSLIRKRALSLLALLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551   988 LTYPITSMFSGAAFNNSINSIFKDKQIEDLWIPYFTI-----------------TTDITASAMRVHTDGSLWRYVRASMS 1050
Cdd:pfam01734   81 GLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLlvvalralltvistalgTRARILLPDDLDDDEDLADAVLASSA 160

                          170       180       190
                   ....*....|....*....|....*....|.
gi 679140551  1051 LSGYMPPLcdPKDGHLLMDGGYINNLPADVA 1081
Cdd:pfam01734  161 LPGVFPPV--RLDGELYVDGGLVDNVPVEAA 189
PRK10279 PRK10279
patatin-like phospholipase RssA;
914-1093 1.71e-26

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 111.34  E-value: 1.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  914 IALVLGGGGARGCSQVGVIRALIEAGIPVDMIGGTSIGAFMSALYAEER--SYNQMRIKARQWAMVmnsvfkTILDLTYP 991
Cdd:PRK10279    6 IGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRlsALEDWVTSFSYWDVL------RLMDLSWQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  992 ITSMFSGAAFNNSINSIFKDKQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLcdPKDGHLLMDGG 1071
Cdd:PRK10279   80 RGGLLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPV--AHNGYWLVDGA 157

                         170       180
                  ....*....|....*....|..
gi 679140551 1072 YINNLPADVARSMGAKVVIAID 1093
Cdd:PRK10279  158 VVNPVPVSLTRALGADIVIAVD 179
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 573-681 2.04e-22

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


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 93.54  E-value: 2.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  573 SPFVRQIDFALDWMEVEAGRAVYRQGDKSDCTYIVLNGRLRSVIRMDDGKKHLTGEYGRGDLIGVVEALTHQPRATTVHA 652
Cdd:cd00038     7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRA 86

                          90       100
                  ....*....|....*....|....*....
gi 679140551  653 VRDSELAKLPEGALTSIKRKFPQVVTRLI 681
Cdd:cd00038    87 LTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 137-258 5.75e-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: 89.31  E-value: 5.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  137 VLGHFEKPLFLELCKHMFFVQLHEGEYIFRPGQLDNSIYVVQDGKLEVCIQESDGTEVVVKEVLAGDSVhSLLSILdviT 216
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLF-GELALL---G 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 679140551  217 GHPAPYktvSARAAIPSTILRLPASAFQDVFQKYPETLVRVV 258
Cdd:cd00038    77 NGPRSA---TVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 138-293 1.14e-18

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: 85.81  E-value: 1.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  138 LGHFEKPLFLELCKHMFFVQLHEGEYIFRPGQLDNSIYVVQDGKLEVCIQESDGTEVVVKEVLAGDsvhsLLSILDVITG 217
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGD----FFGELSLLGG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  218 HPAPYktvSARAAIPSTILRLPASAFQDVFQKYPETLVRVVQIIMVRL----QRVTFLALHN----YLGLTTELFNCQSQ 289
Cdd:COG0664    77 EPSPA---TAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLrqlqERLVSLAFLSaeerLARFLLELADRLDG 153


                  ....
gi 679140551  290 AIPL 293
Cdd:COG0664   154 RIDL 157
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 586-669 2.24e-18

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


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 81.12  E-value: 2.24e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551   586 MEVEAGRAVYRQGDKSDCTYIVLNGRLRSVIRMDDGKKHLTGEYGRGDLIGVVEALTHQPRATTVHAVRDSELAKLPEGA 665
Cdd:pfam00027    2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRED 81


                   ....
gi 679140551   666 LTSI 669
Cdd:pfam00027   82 FLEL 85
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 586-694 2.90e-17

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


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 81.96  E-value: 2.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  586 MEVEAGRAVYRQGDKSDCTYIVLNGRLRSVIRMDDGKKHLTGEYGRGDLIGVVEALTHQPRATTVHAVRDSELAKLPEGA 665
Cdd:COG0664    19 RTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSPATAEALEDSELLRIPRED 98

                          90       100
                  ....*....|....*....|....*....
gi 679140551  666 LTSIKRKFPQVVTRLIHLLGEKILGSLQQ 694
Cdd:COG0664    99 LEELLERNPELARALLRLLARRLRQLQER 127
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 456-560 6.89e-16

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


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 75.05  E-value: 6.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  456 LDDPSL--LNGKVTLHQVTAGTVLSRQGDQDVNVCFVVSGMLHVYQRKIDSEEdTCLFITHPGELVGQLAVLTGEPLIFT 533
Cdd:cd00038     5 LDDEELeeLADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGRE-QIVGFLGPGDLFGELALLGNGPRSAT 83

                          90       100
                  ....*....|....*....|....*..
gi 679140551  534 IKANRDCSFLSISKSHFYEIMREQPSV 560
Cdd:cd00038    84 VRALTDSELLVLPRSDFRRLLQEYPEL 110
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 155-250 1.07e-15

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


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 73.41  E-value: 1.07e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551   155 FVQLHEGEYIFRPGQLDNSIYVVQDGKLEVCIQESDGTEVVVKEVLAGDSVHsLLSILDvitGHPAPYktvSARAAIPST 234
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFG-ELALLG---GEPRSA---TVVALTDSE 73

                           90
                   ....*....|....*.
gi 679140551   235 ILRLPASAFQDVFQKY 250
Cdd:pfam00027   74 LLVIPREDFLELLERD 89
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 137-260 2.04e-15

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: 73.59  E-value: 2.04e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551    137 VLGHFEKPLFLELCKHMFFVQLHEGEYIFRPGQLDNSIYVVQDGKLEVCIQESDGTEVVVKEVLAGDSVhSLLSILdviT 216
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFF-GELALL---T 76

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 679140551    217 GHPAPYkTVSARAAIPSTILRLPASAFQDVFQKYPETLVRVVQI 260
Cdd:smart00100   77 NSRRAA-SAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 468-556 1.11e-14

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


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 70.72  E-value: 1.11e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551   468 LHQVTAGTVLSRQGDQDVNVCFVVSGMLHVYQRKIDSEEDTcLFITHPGELVGQLAVLTGEPLIFTIKANRDCSFLSISK 547
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQI-LAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPR 79


                   ....*....
gi 679140551   548 SHFYEIMRE 556
Cdd:pfam00027   80 EDFLELLER 88
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 457-572 1.50e-14

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


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 73.87  E-value: 1.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  457 DDPSLLNGKVTLHQVTAGTVLSRQGDQDVNVCFVVSGMLHVYQRKIDSEEdTCLFITHPGELVGQLAVLTGEPLIFTIKA 536
Cdd:COG0664     7 EELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGRE-QILGFLGPGDFFGELSLLGGEPSPATAEA 85

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 679140551  537 NRDCSFLSISKSHFYEIMREQPSVVLGVAHTVVKRM 572
Cdd:COG0664    86 LEDSELLRIPREDLEELLERNPELARALLRLLARRL 121
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 577-675 7.15e-12

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: 63.57  E-value: 7.15e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551    577 RQIDFALDWMEVEAGRAVYRQGDKSDCTYIVLNGRLRSVIRMDDGKKHLTGEYGRGDLIGVVEALTHQPRATTVhAVRDS 656
Cdd:smart00100   11 RELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRRAASA-AAVAL 89

                            90
                    ....*....|....*....
gi 679140551    657 ELAKLPEGALTSIKRKFPQ 675
Cdd:smart00100   90 ELATLLRIDFRDFLQLLPE 108
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 456-558 3.88e-09

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


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 55.87  E-value: 3.88e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551    456 LDDPSL--LNGKVTLHQVTAGTVLSRQGDQDVNVCFVVSGMLHVYQRKIDSEEDTcLFITHPGELVGQLAVLTGEPLI-- 531
Cdd:smart00100    5 LDAEELreLADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQI-VGTLGPGDFFGELALLTNSRRAas 83

                            90       100
                    ....*....|....*....|....*..
gi 679140551    532 FTIKANRDCSFLSISKSHFYEIMREQP 558
Cdd:smart00100   84 AAAVALELATLLRIDFRDFLQLLPELP 110
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 470-666 2.21e-05

bacteriocin-type transport-associated protein; Members of this protein family are uncharacterized and contain two copies of the cyclic nucleotide-binding domain pfam00027. Members are restricted to select cyanobacteria but are found regularly in association with a transport operon that, in turn, is associated with the production of putative bacteriocins. The models describing the transport operon are TIGR03794, TIGR03796, and TIGR03797.


Pssm-ID: 274839 [Multi-domain]  Cd Length: 317  Bit Score: 47.97  E-value: 2.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551   470 QVTAGTVLSRQGDQDVNVCFVVSGMLHVyqrKIDSEEDTCLFIT------HPGELVGQLAVLTGEPLIFTIKANRDCSFL 543
Cdd:TIGR03896   12 EIAAGTTLIEEGKAADFLFILLDGTFTV---TTPQPEDNPLTRAfelarlSRGEIVGEMSLLETRPPVATIKAVPKSRVM 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551   544 SISK--------------SHFYEIMREQPSVVLGVAHTVVKRM----SPFVRQIDFAL--------DWME-------VEA 590
Cdd:TIGR03896   89 SIPVgelaaklqsdvgfaAHFYRAIAIKLALQIQNQNHQLHRRngadSEPLRKVLFIFgelhesdvAWMMasgtpqkLPA 168

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 679140551   591 GRAVYRQGDKSDCTYIVLNGRLRSVIRmDDGKKHLTGEYGRGDLIGVVEALTHQPRAT-TVHAVRDSELAKLPEGAL 666
Cdd:TIGR03896  169 GTILIHEGGTVDALYILLYGEASLSIS-PDGPGREVGSSRRGEILGETPFLNGSLPGTaTVKAIENSVLLAIDKQQL 244
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
916-1026 8.50e-04

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 42.87  E-value: 8.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  916 LVLGGGGARGCSQVGVIRALIE-AGIPV----DMIGGTSIG-------------AFMSALYAEERSynqmRI-KARQWAM 976
Cdd:NF041079    4 LSLSGGGYRGLYTASVLAELEEqFGRPIadhfDLICGTSIGgilalalaleipaRELVELFEEHGK----DIfPKRKWPR 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 679140551  977 VMNSVFKtildltypiTSMFSGAAFNNSINSIFKDKQIEDL----WIPYFTITT 1026
Cdd:NF041079   80 RLLGLLK---------KPKYSSEPLREVLEEIFGDKTIGDLkhrvLIPAVNYTT 124
 
Name Accession Description Interval E-value
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 899-1204 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: 692.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  899 HSDFSRLARVLTGNAIALVLGGGGARGCSQVGVIRALIEAGIPVDMIGGTSIGAFMSALYAEERSYNQMRIKARQWAMVM 978
Cdd:cd07225     1 HSDFSRLARVLTGNSIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKDM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  979 NSVFKTILDLTYPITSMFSGAAFNNSINSIFKDKQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPL 1058
Cdd:cd07225    81 TSIWKKLLDLTYPITSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551 1059 CDPKDGHLLMDGGYINNLPADVARSMGAKVVIAIDVGSRDETDLTNYGDCLSGWWLLWKRWNPLAEKIKVLNMAEIQTRL 1138
Cdd:cd07225   161 CDPKDGHLLMDGGYINNLPADVARSMGAKTVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLAEKVKVPNMAEIQSRL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 679140551 1139 AYVCCVRQLEMVKNSDYCEYIRPPIDRYRTLDFGKFDEICEVGYQHGKTVFNVWCRSGVLDKMLRD 1204
Cdd:cd07225   241 AYVSCVRQLEEVKSSDYCEYLRPPIDKYKTLDFGKFDEICEVGYQHGKTVFDGWKRSGVLEKMLQD 306
Pat_Fungal_NTE1 cd07227
Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy ...
 904-1174 2.11e-111

Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy Target Esterase (NTE), commonly referred to as NTE1. Patatin-like phospholipase. NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. This family includes NTE1 from fungi.


Pssm-ID: 132865 [Multi-domain]  Cd Length: 269  Bit Score: 350.64  E-value: 2.11e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  904 RLARVLTGNAIALVLGGGGARGCSQVGVIRALIEAGIPVDMIGGTSIGAFMSALYAEERSYNQMRIKARQWAMVMNSVFK 983
Cdd:cd07227     1 RLARRLCGQAIGLVLGGGGARGISHIGILQALEEAGIPIDAIGGTSIGSFVGGLYAREADLVPIFGRAKKFAGRMASMWR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  984 TILDLTYPITSMFSGAAFNNSINSIFKDKQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLCDpkD 1063
Cdd:cd07227    81 FLSDVTYPFASYTTGHEFNRGIWKTFGNTHIEDFWIPFYANSTNITHSRMEIHSSGYAWRYIRASMSLAGLLPPLSD--N 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551 1064 GHLLMDGGYINNLPADVARSMGAKVVIAIDVGSRDETDLTNYGDCLSGWWLLWKRWNPLAEKIKVLNMAEIQTRLAYVCC 1143
Cdd:cd07227   159 GSMLLDGGYMDNLPVSPMRSLGIRDIFAVDVGSVDDRTPMDYGDSVSGVWIFFNRWNPFSSRPNVPSMAEIQSRLTYVSS 238

                         250       260       270
                  ....*....|....*....|....*....|.
gi 679140551 1144 VRQLEMVKNSDYCEYIRPPIDRYRTLDFGKF 1174
Cdd:cd07227   239 VKTLEKVKATPGCHYMRPPVQDFDTLDFGKF 269
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 914-1094 4.58e-73

Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; Patatin-like phospholipase domain containing protein 6 (PNPLA6) and protein 7 (PNPLA7) are included in this family. PNPLA6 is commonly known as Neuropathy Target Esterase (NTE). NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. PNPLA7 is an insulin-regulated phospholipase that is homologus to Neuropathy Target Esterase (NTE or PNPLA6) and is also known as NTE-related esterase (NRE). Human NRE is predominantly expressed in prostate, white adipose, and pancreatic tissue. NRE hydrolyzes sn-1 esters in lysophosphatidylcholine and lysophosphatidic acid, but shows no lipase activity with substrates like triacylglycerols (TG), cholesteryl esters, retinyl esters (RE), phosphatidylcholine (PC), or monoacylglycerol (MG). This family includes subfamily of PNPLA6 (NTE) and PNPLA7 (NRE)-like phospholipases.


Pssm-ID: 132844 [Multi-domain]  Cd Length: 175  Bit Score: 240.53  E-value: 4.58e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  914 IALVLGGGGARGCSQVGVIRALIEAGIPVDMIGGTSIGAFMSALYAEERSYNQMRIKARQwamvMNSVFKTILDLTYPIT 993
Cdd:cd07205     1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAGYSPEEIEERAKL----RSTDLKALSDLTIPTA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  994 SMFSGAAFNNSINSIFKDKQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLCDpkDGHLLMDGGYI 1073
Cdd:cd07205    77 GLLRGDKFLELLDEYFGDRDIEDLWIPFFIVATDLTSGKLVVFRSGSLVRAVRASMSIPGIFPPVKI--DGQLLVDGGVL 154

                         170       180
                  ....*....|....*....|.
gi 679140551 1074 NNLPADVARSMGAKVVIAIDV 1094
Cdd:cd07205   155 NNLPVDVLRELGADIIIAVDL 175
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 914-1189 9.09e-61

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 208.99  E-value: 9.09e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  914 IALVLGGGGARGCSQVGVIRALIEAGIPVDMIGGTSIGAFMSALYAEERSYNQMR-----IKARQWAMVMNSVFKTILDL 988
Cdd:COG1752     7 IGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADELEelwrsLDRRDLFDLSLPRRLLRLDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  989 TYPITSMFSGAAFNNSINSIFKDKQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLcdPKDGHLLM 1068
Cdd:COG1752    87 GLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPV--EIDGRLYV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551 1069 DGGYINNLPADVARSMGAKVVIAIDVGSRDEtdltnygdclsgwwllwkrwnplaekiKVLNMAEIQTRLAYVCCVRQLE 1148
Cdd:COG1752   165 DGGVVNNLPVDPARALGADRVIAVDLNPPLR---------------------------KLPSLLDILGRALEIMFNSILR 217

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 679140551 1149 MVKNSDYC-EYIRPPIDRYRTLDFGKFDEICEVGYQHGKTVF 1189
Cdd:COG1752   218 RELALEPAdILIEPDLSGISLLDFSRAEELIEAGYEAARRAL 259
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 916-1092 5.84e-48

Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes PNPLA (1-9), TGL (3-5), ExoU-like, and SDP1-like subfamilies. There are some additional hypothetical proteins included in this family.


Pssm-ID: 132837 [Multi-domain]  Cd Length: 172  Bit Score: 168.67  E-value: 5.84e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  916 LVLGGGGARGCSQVGVIRALIEAGIPVDMIGGTSIGAFMSALYAEERSYNQMRIKARQWAMVMNSVFktilDLTYPITSM 995
Cdd:cd07198     1 LVLSGGGALGIYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASGRDLEEALLLLLRLSREVRLRF----DGAFPPTGR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  996 FSGAAFNNSInSIFKDKQIEDLWIPYFTITTDITASAMRVH---TDGSLWRYVRASMSLSGYMPPLCDPKDGHLLMDGGY 1072
Cdd:cd07198    77 LLGILRQPLL-SALPDDAHEDASGKLFISLTRLTDGENVLVsdtSKGELWSAVRASSSIPGYFGPVPLSFRGRRYGDGGL 155

                         170       180
                  ....*....|....*....|
gi 679140551 1073 INNLPADVarsMGAKVVIAI 1092
Cdd:cd07198   156 SNNLPVAE---LGNTINVSP 172
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 914-1094 1.70e-39

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: 144.72  E-value: 1.70e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  914 IALVLGGGGARGCSQVGVIRALIEAGIPVDMIGGTSIGAFMSALYAEERSYNQMrikarQWAMVMNSV-FKTILDLTYPI 992
Cdd:cd07228     1 IGLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYAAGHLDALE-----EWVRSLSQRdVLRLLDLSASR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  993 TSMFSGAAFNNSINSIFKDKQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLCDpkDGHLLMDGGY 1072
Cdd:cd07228    76 SGLLKGEKVLEYLREIMGGVTIEELPIPFAAVATDLQTGKEVWFREGSLIDAIRASISIPGIFAPVEH--NGRLLVDGGV 153

                         170       180
                  ....*....|....*....|..
gi 679140551 1073 INNLPADVARSMGAKVVIAIDV 1094
Cdd:cd07228   154 VNPIPVSVARALGADIVIAVDL 175
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 916-1081 5.91e-29

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: 115.01  E-value: 5.91e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551   916 LVLGGGGARGCSQVGVIRALIEAGIPVDMIGGTSIGAFMSALYA--------EERSYNQMRIKARQWAMVMNSVFKTILD 987
Cdd:pfam01734    1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLAlgrdpeeiEDLLLELDLNLFLSLIRKRALSLLALLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551   988 LTYPITSMFSGAAFNNSINSIFKDKQIEDLWIPYFTI-----------------TTDITASAMRVHTDGSLWRYVRASMS 1050
Cdd:pfam01734   81 GLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLlvvalralltvistalgTRARILLPDDLDDDEDLADAVLASSA 160

                          170       180       190
                   ....*....|....*....|....*....|.
gi 679140551  1051 LSGYMPPLcdPKDGHLLMDGGYINNLPADVA 1081
Cdd:pfam01734  161 LPGVFPPV--RLDGELYVDGGLVDNVPVEAA 189
PRK10279 PRK10279
patatin-like phospholipase RssA;
914-1093 1.71e-26

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 111.34  E-value: 1.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  914 IALVLGGGGARGCSQVGVIRALIEAGIPVDMIGGTSIGAFMSALYAEER--SYNQMRIKARQWAMVmnsvfkTILDLTYP 991
Cdd:PRK10279    6 IGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRlsALEDWVTSFSYWDVL------RLMDLSWQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  992 ITSMFSGAAFNNSINSIFKDKQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLcdPKDGHLLMDGG 1071
Cdd:PRK10279   80 RGGLLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPV--AHNGYWLVDGA 157

                         170       180
                  ....*....|....*....|..
gi 679140551 1072 YINNLPADVARSMGAKVVIAID 1093
Cdd:PRK10279  158 VVNPVPVSLTRALGADIVIAVD 179
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 916-1096 2.00e-25

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: 105.84  E-value: 2.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  916 LVLGGGGARGCSQVGVIRALIEAGIPVDMIGGTSIGAFMSALYA--EERSYNQMRikaRQWamvmnsvfktiLDLTYPiT 993
Cdd:cd07209     1 LVLSGGGALGAYQAGVLKALAEAGIEPDIISGTSIGAINGALIAggDPEAVERLE---KLW-----------RELSRE-D 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  994 SMFSGAAFNNSINSIFKDKQIEdlwIPYFTITTDITASAMRV----HTDGSLWRYVRASMSLsgymPPLCDPK--DGHLL 1067
Cdd:cd07209    66 VFLRGLLDRALDFDTLRLLAIL---FAGLVIVAVNVLTGEPVyfddIPDGILPEHLLASAAL----PPFFPPVeiDGRYY 138

                         170       180
                  ....*....|....*....|....*....
gi 679140551 1068 MDGGYINNLPADVARSMGAKVVIAIDVGS 1096
Cdd:cd07209   139 WDGGVVDNTPLSPAIDLGADEIIVVSLSD 167
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 916-1093 7.53e-25

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: 102.11  E-value: 7.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  916 LVLGGGGARGCSQVGVIRALIEAGI--PVDMIGGTSIGAFMSALYaeersynqmrikarqwamvmnsvfktildltYPIT 993
Cdd:cd01819     1 LSFSGGGFRGMYHAGVLSALAERGLldCVTYLAGTSGGAWVAATL-------------------------------YPPS 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  994 SMFSGAAFNNSInsifkdkqiEDLWIPYFTITTDITASAM----RVHTDGSLWRYVRASMSLSGYMPPLCD--------- 1060
Cdd:cd01819    50 SSLDNKPRQSLE---------EALSGKLWVSFTPVTAGENvlvsRFVSKEELIRALFASGSWPSYFGLIPPaelytsksn 120

                         170       180       190
                  ....*....|....*....|....*....|....
gi 679140551 1061 -PKDGHLLMDGGYINNLPADVARSMGAKVVIAID 1093
Cdd:cd01819   121 lKEKGVRLVDGGVSNNLPAPVLLRPGRGVTLTIS 154
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 573-681 2.04e-22

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


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 93.54  E-value: 2.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  573 SPFVRQIDFALDWMEVEAGRAVYRQGDKSDCTYIVLNGRLRSVIRMDDGKKHLTGEYGRGDLIGVVEALTHQPRATTVHA 652
Cdd:cd00038     7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRA 86

                          90       100
                  ....*....|....*....|....*....
gi 679140551  653 VRDSELAKLPEGALTSIKRKFPQVVTRLI 681
Cdd:cd00038    87 LTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 137-258 5.75e-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: 89.31  E-value: 5.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  137 VLGHFEKPLFLELCKHMFFVQLHEGEYIFRPGQLDNSIYVVQDGKLEVCIQESDGTEVVVKEVLAGDSVhSLLSILdviT 216
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLF-GELALL---G 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 679140551  217 GHPAPYktvSARAAIPSTILRLPASAFQDVFQKYPETLVRVV 258
Cdd:cd00038    77 NGPRSA---TVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 914-1100 1.25e-20

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: 92.02  E-value: 1.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  914 IALVLGGGGARGCSQVGVIRALIEAGIPVDMIGGTSIGAFMSALYAEERSYNQMRikarqwAMVMNSVFKTILDLTYPI- 992
Cdd:cd07210     1 FALVLSSGFFGFYAHLGFLAALLEMGLEPSAISGTSAGALVGGLFASGISPDEMA------ELLLSLERKDFWMFWDPPl 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  993 -TSMFSGAAFNNSINSIFKDKQIEDLWIPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLcdPKDGHLLMDGG 1071
Cdd:cd07210    75 rGGLLSGDRFAALLREHLPPDRFEELRIPLAVSVVDLTSRETLLLSEGDLAEAVAASCAVPPLFQPV--EIGGRPFVDGG 152

                         170       180
                  ....*....|....*....|....*....
gi 679140551 1072 YINNLPADVARSMGAKVVIaIDVGSRDET 1100
Cdd:cd07210   153 VADRLPFDALRPEIERILY-HHVAPRRPW 180
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 138-293 1.14e-18

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: 85.81  E-value: 1.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  138 LGHFEKPLFLELCKHMFFVQLHEGEYIFRPGQLDNSIYVVQDGKLEVCIQESDGTEVVVKEVLAGDsvhsLLSILDVITG 217
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGD----FFGELSLLGG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  218 HPAPYktvSARAAIPSTILRLPASAFQDVFQKYPETLVRVVQIIMVRL----QRVTFLALHN----YLGLTTELFNCQSQ 289
Cdd:COG0664    77 EPSPA---TAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLrqlqERLVSLAFLSaeerLARFLLELADRLDG 153


                  ....
gi 679140551  290 AIPL 293
Cdd:COG0664   154 RIDL 157
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 586-669 2.24e-18

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


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 81.12  E-value: 2.24e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551   586 MEVEAGRAVYRQGDKSDCTYIVLNGRLRSVIRMDDGKKHLTGEYGRGDLIGVVEALTHQPRATTVHAVRDSELAKLPEGA 665
Cdd:pfam00027    2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRED 81


                   ....
gi 679140551   666 LTSI 669
Cdd:pfam00027   82 FLEL 85
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 916-1080 4.11e-18

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: 83.87  E-value: 4.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  916 LVLGGGGARGCSQVGVIRALIEAGIPVDMIGGTSIGAFMSALYAEERSYNQMR--IKARQWAMVMNS----VFKTILDLT 989
Cdd:cd07207     2 LVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLALGYSAADIKdiLKETDFAKLLDSpvglLFLLPSLFK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  990 YPItsMFSGAAFNNSINSIFKDKQI------------EDLWIPYFTITTDITASAMRV----HT-DGSLWRYVRASMSLS 1052
Cdd:cd07207    82 EGG--LYKGDALEEWLRELLKEKTGnsfatsllrdldDDLGKDLKVVATDLTTGALVVfsaeTTpDMPVAKAVRASMSIP 159

                         170       180
                  ....*....|....*....|....*...
gi 679140551 1053 GYMPPLCDPKdGHLLMDGGYINNLPADV 1080
Cdd:cd07207   160 FVFKPVRLAK-GDVYVDGGVLDNYPVWL 186
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 586-694 2.90e-17

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


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 81.96  E-value: 2.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  586 MEVEAGRAVYRQGDKSDCTYIVLNGRLRSVIRMDDGKKHLTGEYGRGDLIGVVEALTHQPRATTVHAVRDSELAKLPEGA 665
Cdd:COG0664    19 RTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSPATAEALEDSELLRIPRED 98

                          90       100
                  ....*....|....*....|....*....
gi 679140551  666 LTSIKRKFPQVVTRLIHLLGEKILGSLQQ 694
Cdd:COG0664    99 LEELLERNPELARALLRLLARRLRQLQER 127
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 456-560 6.89e-16

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


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 75.05  E-value: 6.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  456 LDDPSL--LNGKVTLHQVTAGTVLSRQGDQDVNVCFVVSGMLHVYQRKIDSEEdTCLFITHPGELVGQLAVLTGEPLIFT 533
Cdd:cd00038     5 LDDEELeeLADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGRE-QIVGFLGPGDLFGELALLGNGPRSAT 83

                          90       100
                  ....*....|....*....|....*..
gi 679140551  534 IKANRDCSFLSISKSHFYEIMREQPSV 560
Cdd:cd00038    84 VRALTDSELLVLPRSDFRRLLQEYPEL 110
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 155-250 1.07e-15

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


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 73.41  E-value: 1.07e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551   155 FVQLHEGEYIFRPGQLDNSIYVVQDGKLEVCIQESDGTEVVVKEVLAGDSVHsLLSILDvitGHPAPYktvSARAAIPST 234
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFG-ELALLG---GEPRSA---TVVALTDSE 73

                           90
                   ....*....|....*.
gi 679140551   235 ILRLPASAFQDVFQKY 250
Cdd:pfam00027   74 LLVIPREDFLELLERD 89
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 137-260 2.04e-15

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: 73.59  E-value: 2.04e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551    137 VLGHFEKPLFLELCKHMFFVQLHEGEYIFRPGQLDNSIYVVQDGKLEVCIQESDGTEVVVKEVLAGDSVhSLLSILdviT 216
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFF-GELALL---T 76

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 679140551    217 GHPAPYkTVSARAAIPSTILRLPASAFQDVFQKYPETLVRVVQI 260
Cdd:smart00100   77 NSRRAA-SAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 468-556 1.11e-14

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


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 70.72  E-value: 1.11e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551   468 LHQVTAGTVLSRQGDQDVNVCFVVSGMLHVYQRKIDSEEDTcLFITHPGELVGQLAVLTGEPLIFTIKANRDCSFLSISK 547
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQI-LAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPR 79


                   ....*....
gi 679140551   548 SHFYEIMRE 556
Cdd:pfam00027   80 EDFLELLER 88
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 457-572 1.50e-14

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


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 73.87  E-value: 1.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  457 DDPSLLNGKVTLHQVTAGTVLSRQGDQDVNVCFVVSGMLHVYQRKIDSEEdTCLFITHPGELVGQLAVLTGEPLIFTIKA 536
Cdd:COG0664     7 EELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGRE-QILGFLGPGDFFGELSLLGGEPSPATAEA 85

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 679140551  537 NRDCSFLSISKSHFYEIMREQPSVVLGVAHTVVKRM 572
Cdd:COG0664    86 LEDSELLRIPREDLEELLERNPELARALLRLLARRL 121
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 916-1092 1.47e-12

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: 69.18  E-value: 1.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  916 LVLGGGGARGCSQVGVIRALIEAGI-PVDMIGGTSIGA-FMSALYAEERSYNQMRIKARQWA---MVMNSVFKT----IL 986
Cdd:cd07208     1 LVLEGGGMRGAYTAGVLDAFLEAGIrPFDLVIGVSAGAlNAASYLSGQRGRALRINTKYATDpryLGLRSLLRTgnlfDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  987 DLTYPITSMfsgaafnnsINSIFKDKQIEDLWIPYFTITTDI-TASAM--RVHTDGSLW-RYVRASMSLSGYMPPlcDPK 1062
Cdd:cd07208    81 DFLYDELPD---------GLDPFDFEAFAASPARFYVVATDAdTGEAVyfDKPDILDDLlDALRASSALPGLFPP--VRI 149

                         170       180       190
                  ....*....|....*....|....*....|
gi 679140551 1063 DGHLLMDGGYINNLPADVARSMGAKVVIAI 1092
Cdd:cd07208   150 DGEPYVDGGLSDSIPVDKAIEDGADKIVVI 179
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 577-675 7.15e-12

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: 63.57  E-value: 7.15e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551    577 RQIDFALDWMEVEAGRAVYRQGDKSDCTYIVLNGRLRSVIRMDDGKKHLTGEYGRGDLIGVVEALTHQPRATTVhAVRDS 656
Cdd:smart00100   11 RELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRRAASA-AAVAL 89

                            90
                    ....*....|....*....
gi 679140551    657 ELAKLPEGALTSIKRKFPQ 675
Cdd:smart00100   90 ELATLLRIDFRDFLQLLPE 108
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
914-1092 2.37e-11

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 65.96  E-value: 2.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  914 IALVLGGGGARGCSQVGVIRALIEAGIPVDMIGGTSIGAFMSALYAeersynqmrikARQwamvMNSVFKTILDLTypit 993
Cdd:COG4667     6 TALVLEGGGMRGIFTAGVLDALLEEGIPFDLVIGVSAGALNGASYL-----------SRQ----PGRARRVITDYA---- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  994 smfSGAAFnNSINSIFKDKQIEDL-WIpYFTIT---------------TDITASAMRVHT-----------DGSLWRYVR 1046
Cdd:COG4667    67 ---TDPRF-FSLRNFLRGGNLFDLdFL-YDEIPnellpfdfetfkaspREFYVVATNADTgeaeyfskkddDYDLLDALR 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 679140551 1047 ASMSlsgyMPPLCDP--KDGHLLMDGGYINNLPADVARSMGAKVVIAI 1092
Cdd:COG4667   142 ASSA----LPLLYPPveIDGKRYLDGGVADSIPVREAIRDGADKIVVI 185
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 456-558 3.88e-09

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


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 55.87  E-value: 3.88e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551    456 LDDPSL--LNGKVTLHQVTAGTVLSRQGDQDVNVCFVVSGMLHVYQRKIDSEEDTcLFITHPGELVGQLAVLTGEPLI-- 531
Cdd:smart00100    5 LDAEELreLADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQI-VGTLGPGDFFGELALLTNSRRAas 83

                            90       100
                    ....*....|....*....|....*..
gi 679140551    532 FTIKANRDCSFLSISKSHFYEIMREQP 558
Cdd:smart00100   84 AAAVALELATLLRIDFRDFLQLLPELP 110
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 916-1081 1.03e-05

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


Pssm-ID: 132852 [Multi-domain]  Cd Length: 288  Bit Score: 48.82  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  916 LVLGGGGARGCSQVGVIRALIEAGiP-----VDMIGGTSIGAFMSALYAEERSYNQMRikaRQWAMVMNSVFKtildLTY 990
Cdd:cd07213     5 LSLDGGGVKGIVQLVLLKRLAEEF-PsfldqIDLFAGTSAGSLIALGLALGYSPRQVL---KLYEEVGLKVFS----KSS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  991 PITSMFSGAAFNNSI-----NSIFKDKQIEDL----WIPYFTITTDI-----TASAMRVHT-------DGSLWRYVRASM 1049
Cdd:cd07213    77 AGGGAGNNQYFAAGFlkafaEVFFGDLTLGDLkrkvLVPSFQLDSGKddpnrRWKPKLFHNfpgepdlDELLVDVCLRSS 156

                         170       180       190
                  ....*....|....*....|....*....|...
gi 679140551 1050 SLSGYMPPLcdpkDGHLlmDGG-YINNlPADVA 1081
Cdd:cd07213   157 AAPTYFPSY----QGYV--DGGvFANN-PSLCA 182
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 470-666 2.21e-05

bacteriocin-type transport-associated protein; Members of this protein family are uncharacterized and contain two copies of the cyclic nucleotide-binding domain pfam00027. Members are restricted to select cyanobacteria but are found regularly in association with a transport operon that, in turn, is associated with the production of putative bacteriocins. The models describing the transport operon are TIGR03794, TIGR03796, and TIGR03797.


Pssm-ID: 274839 [Multi-domain]  Cd Length: 317  Bit Score: 47.97  E-value: 2.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551   470 QVTAGTVLSRQGDQDVNVCFVVSGMLHVyqrKIDSEEDTCLFIT------HPGELVGQLAVLTGEPLIFTIKANRDCSFL 543
Cdd:TIGR03896   12 EIAAGTTLIEEGKAADFLFILLDGTFTV---TTPQPEDNPLTRAfelarlSRGEIVGEMSLLETRPPVATIKAVPKSRVM 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551   544 SISK--------------SHFYEIMREQPSVVLGVAHTVVKRM----SPFVRQIDFAL--------DWME-------VEA 590
Cdd:TIGR03896   89 SIPVgelaaklqsdvgfaAHFYRAIAIKLALQIQNQNHQLHRRngadSEPLRKVLFIFgelhesdvAWMMasgtpqkLPA 168

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 679140551   591 GRAVYRQGDKSDCTYIVLNGRLRSVIRmDDGKKHLTGEYGRGDLIGVVEALTHQPRAT-TVHAVRDSELAKLPEGAL 666
Cdd:TIGR03896  169 GTILIHEGGTVDALYILLYGEASLSIS-PDGPGREVGSSRRGEILGETPFLNGSLPGTaTVKAIENSVLLAIDKQQL 244
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 916-1081 4.97e-05

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 46.82  E-value: 4.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  916 LVLGGGGARGcsqvgVIRALI------EAGIP----VDMIGGTSIGAFMSALYAEERSYNQM---------RIKARQWam 976
Cdd:COG3621    10 LSLDGGGIRG-----LIPARIlaeleeRLGKPlaeyFDLIAGTSTGGIIALGLAAGYSAEEIldlyeeegkEIFPKSR-- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  977 vmNSVFKTILDLTYPItsmFSGAAFNNSINSIFKDKQIEDLWIPYFTITTDITASAMRVHT----------DGSLWRYVR 1046
Cdd:COG3621    83 --WRKLLSLRGLFGPK---YDSEGLEKVLKEYFGDTTLGDLKTPVLIPSYDLDNGKPVFFKsphakfdrdrDFLLVDVAR 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 679140551 1047 ASMSLSGYMPPLC---DPKDGHLLMDGG-YINNlPADVA 1081
Cdd:COG3621   158 ATSAAPTYFPPAQiknLTGEGYALIDGGvFANN-PALCA 195
Pat_PLPL cd07232
Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin ...
 915-959 2.31e-04

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: 45.33  E-value: 2.31e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 679140551  915 ALVLGGGGARGCSQVGVIRALIEAGIPVDMIGGTSIGAFMSALYA 959
Cdd:cd07232    69 ALCLSGGAAFAYYHFGVVKALLDADLLPNVISGTSGGSLVAALLC 113
Pat_SDP1-like cd07231
Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like ...
 858-989 6.85e-04

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: 43.21  E-value: 6.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  858 NMRSWCSAHLHLHcprrvfsKRSLPKLIEMY--------ERVFQKPPDRHSDFSRLA-----RVLTGNAiALVLGGGGAR 924
Cdd:cd07231     8 NLGNMCNPELHKG-------RLEVPRLIRDYiaevkaqlRAVVESDEDELSLEEKLAffqetRHAFGRT-ALLLSGGAAL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 679140551  925 GCSQVGVIRALIEAGIPVDMIGGTSIGAFMSALYAeERSYNQMRIKARqwAMVMNSVFKTILDLT 989
Cdd:cd07231    80 GTFHVGVVRTLVEHQLLPRVIAGSSVGSIVCAIIA-TRTDEELQSFFR--ALLGDLTFQEAYDRT 141
CBASS_lipase NF041079
CBASS cGAMP-activated phospholipase;
916-1026 8.50e-04

CBASS cGAMP-activated phospholipase;


Pssm-ID: 469006 [Multi-domain]  Cd Length: 317  Bit Score: 42.87  E-value: 8.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  916 LVLGGGGARGCSQVGVIRALIE-AGIPV----DMIGGTSIG-------------AFMSALYAEERSynqmRI-KARQWAM 976
Cdd:NF041079    4 LSLSGGGYRGLYTASVLAELEEqFGRPIadhfDLICGTSIGgilalalaleipaRELVELFEEHGK----DIfPKRKWPR 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 679140551  977 VMNSVFKtildltypiTSMFSGAAFNNSINSIFKDKQIEDL----WIPYFTITT 1026
Cdd:NF041079   80 RLLGLLK---------KPKYSSEPLREVLEEIFGDKTIGDLkhrvLIPAVNYTT 124
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 858-957 1.68e-03

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: 42.20  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679140551  858 NMRSWCSAHLHLHCprRVFSKrslpKLIEMY-------------ERVFQKPPDRHSDFSRLARVLTGNAiALVLGGGGAR 924
Cdd:cd07206     8 NLGNMGNPSLYRHA--YFGTK----HLIEDYieevdlsleylalLDTKELSVEEKLDFFRRARHAFGRT-ALMLSGGASL 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 679140551  925 GCSQVGVIRALIEAGIPVDMIGGTSIGAFMSAL 957
Cdd:cd07206    81 GLFHLGVVKALWEQDLLPRVISGSSAGAIVAAL 113
Pat_TGL4-5_like cd07230
Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in ...
 906-956 7.00e-03

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: 40.28  E-value: 7.00e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 679140551  906 ARVLTGNAiALVLGGGGARGCSQVGVIRALIEAGIPVDMIGGTSIGAFMSA 956
Cdd:cd07230    67 TRKNFGRT-ALLLSGGGTFGMFHIGVLKALFEANLLPRIISGSSAGSIVAA 116
 
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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