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Conserved domains on  [gi|568913635|ref|XP_006498078|]
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patatin-like phospholipase domain-containing protein 7 isoform X5 [Mus musculus]

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 ...
 933-1238 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: 685.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  933 HSDFSRLARMLTGNAIALVLGGGGARGCAQVGILRALAECGVPVDIIGGTSIGAFMGALFAEERSYSQTRIRAKQWAEGM 1012
Cdd:cd07225     1 HSDFSRLARVLTGNSIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKDM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635 1013 TSMMKTILDLTYPITSMFSGTGFNSSISNIFKDRQIEDLWLPYFAITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPL 1092
Cdd:cd07225    81 TSIWKKLLDLTYPITSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635 1093 CDPKDGHLLMDGGYINNLPADVARSMGAKVVIAIDVGSRDETDLTNYGDALSGWWLLWKRWNPLATKVKVLNMAEIQTRL 1172
Cdd:cd07225   161 CDPKDGHLLMDGGYINNLPADVARSMGAKTVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLAEKVKVPNMAEIQSRL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568913635 1173 AYVCCVRQLEMVKNSDYCEYLRPPIDSYRTLDFGKFDEICEVGYQHGRTVFDIWVRSGVLEKMLQD 1238
Cdd:cd07225   241 AYVSCVRQLEEVKSSDYCEYLRPPIDKYKTLDFGKFDEICEVGYQHGKTVFDGWKRSGVLEKMLQD 306
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 604-712 9.89e-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: 91.62  E-value: 9.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  604 SSFVRQIDFALDWMEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLVGVVETLTHQARATTVHA 683
Cdd:cd00038     7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRA 86

                          90       100
                  ....*....|....*....|....*....
gi 568913635  684 VRDSELAKLPAGALTSIKRRYPQVVTRLI 712
Cdd:cd00038    87 LTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 170-291 7.66e-18

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


:

Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 80.45  E-value: 7.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  170 VLGHFEKPLFLELCKHMVFVQLQEGEHVFQPGEPDISIYVVQDGRLEVCIQDADGTEVVVKEVLPGDSVhSLLSILDVIT 249
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLF-GELALLGNGP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568913635  250 gHTApyktvSARAAVSSTVLWLPAAAFQGVFEKYPETLVRVV 291
Cdd:cd00038    80 -RSA-----TVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 481-591 2.57e-15

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


:

Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 73.51  E-value: 2.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  481 LLTLMKLDDPSLLDGRVAFLHVPAGTLVSKQGDQDVNILFVVSGMLHVYQQKIDSlEDTCLFLTHPGEMVGQLAVLTGEP 560
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDG-REQIVGFLGPGDLFGELALLGNGP 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568913635  561 LMFTIRANRDCSFLSISKAHFYEIMRKRPDV 591
Cdd:cd00038    80 RSATVRALTDSELLVLPRSDFRRLLQEYPEL 110
 
Name Accession Description Interval E-value
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 933-1238 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: 685.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  933 HSDFSRLARMLTGNAIALVLGGGGARGCAQVGILRALAECGVPVDIIGGTSIGAFMGALFAEERSYSQTRIRAKQWAEGM 1012
Cdd:cd07225     1 HSDFSRLARVLTGNSIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKDM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635 1013 TSMMKTILDLTYPITSMFSGTGFNSSISNIFKDRQIEDLWLPYFAITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPL 1092
Cdd:cd07225    81 TSIWKKLLDLTYPITSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635 1093 CDPKDGHLLMDGGYINNLPADVARSMGAKVVIAIDVGSRDETDLTNYGDALSGWWLLWKRWNPLATKVKVLNMAEIQTRL 1172
Cdd:cd07225   161 CDPKDGHLLMDGGYINNLPADVARSMGAKTVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLAEKVKVPNMAEIQSRL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568913635 1173 AYVCCVRQLEMVKNSDYCEYLRPPIDSYRTLDFGKFDEICEVGYQHGRTVFDIWVRSGVLEKMLQD 1238
Cdd:cd07225   241 AYVSCVRQLEEVKSSDYCEYLRPPIDKYKTLDFGKFDEICEVGYQHGKTVFDGWKRSGVLEKMLQD 306
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 948-1224 1.66e-59

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 205.52  E-value: 1.66e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  948 IALVLGGGGARGCAQVGILRALAECGVPVDIIGGTSIGAFMGALFAEERSYSQ-----TRIRAKQWAEGMTSMMKTILDL 1022
Cdd:COG1752     7 IGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADEleelwRSLDRRDLFDLSLPRRLLRLDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635 1023 TYPITSMFSGTGFNSSISNIFKDRQIEDLWLPYFAITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLcdPKDGHLLM 1102
Cdd:COG1752    87 GLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPV--EIDGRLYV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635 1103 DGGYINNLPADVARSMGAKVVIAIDVGSRDEtdltnygdalsgwwllwkrwnplatkvKVLNMAEIQTRLAYVCCVRQLE 1182
Cdd:COG1752   165 DGGVVNNLPVDPARALGADRVIAVDLNPPLR---------------------------KLPSLLDILGRALEIMFNSILR 217

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 568913635 1183 MVKNSDYC-EYLRPPIDSYRTLDFGKFDEICEVGYQHGRTVFD 1224
Cdd:COG1752   218 RELALEPAdILIEPDLSGISLLDFSRAEELIEAGYEAARRALD 260
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 950-1115 9.08e-26

Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein but it also has the enzymatic activity of lipid acyl hydrolase, catalysing the cleavage of fatty acids from membrane lipids. Members of this family have been found also in vertebrates.


Pssm-ID: 396341  Cd Length: 190  Bit Score: 105.77  E-value: 9.08e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635   950 LVLGGGGARGCAQVGILRALAECGVPVDIIGGTSIGAFMGALFA--------EERSYSQTRIRAKQWAEGMTSMMKTILD 1021
Cdd:pfam01734    1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLAlgrdpeeiEDLLLELDLNLFLSLIRKRALSLLALLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  1022 LTYPITSMFSGTGFNSSISNIFKDRQIEDLWLPYFAI-----------------TTDITASAMRVHTDGSLWRYVRASMS 1084
Cdd:pfam01734   81 GLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLlvvalralltvistalgTRARILLPDDLDDDEDLADAVLASSA 160

                          170       180       190
                   ....*....|....*....|....*....|.
gi 568913635  1085 LSGYMPPLcdPKDGHLLMDGGYINNLPADVA 1115
Cdd:pfam01734  161 LPGVFPPV--RLDGELYVDGGLVDNVPVEAA 189
PRK10279 PRK10279
patatin-like phospholipase RssA;
948-1127 3.73e-25

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 107.49  E-value: 3.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  948 IALVLGGGGARGCAQVGILRALAECGVPVDIIGGTSIGAFMGALFAEERSYSQTR-IRAKQWAEGMTSMmktilDLTYPI 1026
Cdd:PRK10279    6 IGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRLSALEDwVTSFSYWDVLRLM-----DLSWQR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635 1027 TSMFSGTGFNSSISNIFKDRQIEDLWLPYFAITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLcdPKDGHLLMDGGY 1106
Cdd:PRK10279   81 GGLLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPV--AHNGYWLVDGAV 158

                         170       180
                  ....*....|....*....|.
gi 568913635 1107 INNLPADVARSMGAKVVIAID 1127
Cdd:PRK10279  159 VNPVPVSLTRALGADIVIAVD 179
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 604-712 9.89e-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: 91.62  E-value: 9.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  604 SSFVRQIDFALDWMEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLVGVVETLTHQARATTVHA 683
Cdd:cd00038     7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRA 86

                          90       100
                  ....*....|....*....|....*....
gi 568913635  684 VRDSELAKLPAGALTSIKRRYPQVVTRLI 712
Cdd:cd00038    87 LTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 617-704 1.89e-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: 81.50  E-value: 1.89e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635   617 MEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLVGVVETLTHQARATTVHAVRDSELAKLPAGA 696
Cdd:pfam00027    2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRED 81


                   ....*...
gi 568913635   697 LTSIKRRY 704
Cdd:pfam00027   82 FLELLERD 89
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 170-291 7.66e-18

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


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 80.45  E-value: 7.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  170 VLGHFEKPLFLELCKHMVFVQLQEGEHVFQPGEPDISIYVVQDGRLEVCIQDADGTEVVVKEVLPGDSVhSLLSILDVIT 249
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLF-GELALLGNGP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568913635  250 gHTApyktvSARAAVSSTVLWLPAAAFQGVFEKYPETLVRVV 291
Cdd:cd00038    80 -RSA-----TVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 171-308 4.30e-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: 81.19  E-value: 4.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  171 LGHFEKPLFLELCKHMVFVQLQEGEHVFQPGEPDISIYVVQDGRLEVCIQDADGTEVVVKEVLPGDsvhsLLSILDVITG 250
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGD----FFGELSLLGG 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568913635  251 HTAPYktvSARAAVSSTVLWLPAAAFQGVFEKYPETLVRVVQIIMVRL----QRVTFLALHN 308
Cdd:COG0664    77 EPSPA---TAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLrqlqERLVSLAFLS 135
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 617-738 5.51e-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: 81.19  E-value: 5.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  617 MEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLVGVVETLTHQARATTVHAVRDSELAKLPAGA 696
Cdd:COG0664    19 RTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSPATAEALEDSELLRIPRED 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568913635  697 LTSIKRRYPQVVTRLIHLLGEKilgsLQQGSATGHQLGFNTA 738
Cdd:COG0664    99 LEELLERNPELARALLRLLARR----LRQLQERLVSLAFLSA 136
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 481-591 2.57e-15

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


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 73.51  E-value: 2.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  481 LLTLMKLDDPSLLDGRVAFLHVPAGTLVSKQGDQDVNILFVVSGMLHVYQQKIDSlEDTCLFLTHPGEMVGQLAVLTGEP 560
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDG-REQIVGFLGPGDLFGELALLGNGP 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568913635  561 LMFTIRANRDCSFLSISKAHFYEIMRKRPDV 591
Cdd:cd00038    80 RSATVRALTDSELLVLPRSDFRRLLQEYPEL 110
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 501-611 2.39e-13

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: 70.40  E-value: 2.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  501 HVPAGTLVSKQGDQDVNILFVVSGMLHVYQQKIDSlEDTCLFLTHPGEMVGQLAVLTGEPLMFTIRANRDCSFLSISKAH 580
Cdd:COG0664    20 TLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDG-REQILGFLGPGDFFGELSLLGGEPSPATAEALEDSELLRIPRED 98

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568913635  581 FYEIMRKRPDVVLGVAHTVVKRMSSFVRQID 611
Cdd:COG0664    99 LEELLERNPELARALLRLLARRLRQLQERLV 129
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 499-587 2.53e-13

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: 66.86  E-value: 2.53e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635   499 FLHVPAGTLVSKQGDQDVNILFVVSGMLHVYQQKIDSLEDTcLFLTHPGEMVGQLAVLTGEPLMFTIRANRDCSFLSISK 578
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQI-LAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPR 79


                   ....*....
gi 568913635   579 AHFYEIMRK 587
Cdd:pfam00027   80 EDFLELLER 88
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 188-283 6.52e-13

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: 65.71  E-value: 6.52e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635   188 FVQLQEGEHVFQPGEPDISIYVVQDGRLEVCIQDADGTEVVVKEVLPGDSVHsLLSILdvitgHTAPYkTVSARAAVSST 267
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFG-ELALL-----GGEPR-SATVVALTDSE 73

                           90
                   ....*....|....*.
gi 568913635   268 VLWLPAAAFQGVFEKY 283
Cdd:pfam00027   74 LLVIPREDFLELLERD 89
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 170-293 1.98e-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: 65.50  E-value: 1.98e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635    170 VLGHFEKPLFLELCKHMVFVQLQEGEHVFQPGEPDISIYVVQDGRLEVCIQDADGTEVVVKEVLPGDSVhSLLSILdviT 249
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFF-GELALL---T 76

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 568913635    250 GHTAPYkTVSARAAVSSTVLWLPAAAFQGVFEKYPETLVRVVQI 293
Cdd:smart00100   77 NSRRAA-SAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 605-712 8.17e-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: 8.17e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635    605 SFVRQIDFALDWMEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLVGVVETLTHQARATTVHAV 684
Cdd:smart00100    8 EELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRRAASAAAV 87

                            90       100       110
                    ....*....|....*....|....*....|
gi 568913635    685 --RDSELAKLPAGALTSIKRRYPQVVTRLI 712
Cdd:smart00100   88 alELATLLRIDFRDFLQLLPELPQLLLELL 117
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 473-590 5.32e-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: 55.48  E-value: 5.32e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635    473 IFRAATKDLLtlmklddpSLLDGRVAFLHVPAGTLVSKQGDQDVNILFVVSGMLHVYQQKIDSLEDTcLFLTHPGEMVGQ 552
Cdd:smart00100    1 LFKNLDAEEL--------RELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQI-VGTLGPGDFFGE 71

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|
gi 568913635    553 LAVLTGEPL--MFTIRANRDCSFLSISKAHFYEIMRKRPD 590
Cdd:smart00100   72 LALLTNSRRaaSAAAVALELATLLRIDFRDFLQLLPELPQ 111
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 546-693 6.37e-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: 46.81  E-value: 6.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635   546 PGEMVGQLAVLTGEPLMFTIRANRDCSFLSISK--------------AHFYE-IMRKRPDVVLGVAHTVVKRM---SSFV 607
Cdd:TIGR03896   60 RGEIVGEMSLLETRPPVATIKAVPKSRVMSIPVgelaaklqsdvgfaAHFYRaIAIKLALQIQNQNHQLHRRNgadSEPL 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635   608 RQIDFAL--------DWME-------VEAGRAIYRQGDKSDCTYIVLSGRLRSVIrKDDGKKRLAGEYGRGDLVGVVETL 672
Cdd:TIGR03896  140 RKVLFIFgelhesdvAWMMasgtpqkLPAGTILIHEGGTVDALYILLYGEASLSI-SPDGPGREVGSSRRGEILGETPFL 218

                          170       180
                   ....*....|....*....|..
gi 568913635   673 THQARAT-TVHAVRDSELAKLP 693
Cdd:TIGR03896  219 NGSLPGTaTVKAIENSVLLAID 240
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
625-735 4.97e-03

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 39.96  E-value: 4.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  625 IYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLVGVVETL-THQARATTVHAVRDSELAKLPAGALTSIKRR 703
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFeEGQERSAWVRAKTACEVAEISYKKFRQLIQV 110

                          90       100       110
                  ....*....|....*....|....*....|..
gi 568913635  704 YPqvvtRLIHLLGEKILGSLQQGSATGHQLGF 735
Cdd:PRK11753  111 NP----DILMALSAQMARRLQNTSRKVGDLAF 138
 
Name Accession Description Interval E-value
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 933-1238 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: 685.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  933 HSDFSRLARMLTGNAIALVLGGGGARGCAQVGILRALAECGVPVDIIGGTSIGAFMGALFAEERSYSQTRIRAKQWAEGM 1012
Cdd:cd07225     1 HSDFSRLARVLTGNSIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKDM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635 1013 TSMMKTILDLTYPITSMFSGTGFNSSISNIFKDRQIEDLWLPYFAITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPL 1092
Cdd:cd07225    81 TSIWKKLLDLTYPITSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635 1093 CDPKDGHLLMDGGYINNLPADVARSMGAKVVIAIDVGSRDETDLTNYGDALSGWWLLWKRWNPLATKVKVLNMAEIQTRL 1172
Cdd:cd07225   161 CDPKDGHLLMDGGYINNLPADVARSMGAKTVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLAEKVKVPNMAEIQSRL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568913635 1173 AYVCCVRQLEMVKNSDYCEYLRPPIDSYRTLDFGKFDEICEVGYQHGRTVFDIWVRSGVLEKMLQD 1238
Cdd:cd07225   241 AYVSCVRQLEEVKSSDYCEYLRPPIDKYKTLDFGKFDEICEVGYQHGKTVFDGWKRSGVLEKMLQD 306
Pat_Fungal_NTE1 cd07227
Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy ...
 938-1208 7.69e-112

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


Pssm-ID: 132865 [Multi-domain]  Cd Length: 269  Bit Score: 352.57  E-value: 7.69e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  938 RLARMLTGNAIALVLGGGGARGCAQVGILRALAECGVPVDIIGGTSIGAFMGALFAEERSYSQTRIRAKQWAEGMTSMMK 1017
Cdd:cd07227     1 RLARRLCGQAIGLVLGGGGARGISHIGILQALEEAGIPIDAIGGTSIGSFVGGLYAREADLVPIFGRAKKFAGRMASMWR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635 1018 TILDLTYPITSMFSGTGFNSSISNIFKDRQIEDLWLPYFAITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLCDpkD 1097
Cdd:cd07227    81 FLSDVTYPFASYTTGHEFNRGIWKTFGNTHIEDFWIPFYANSTNITHSRMEIHSSGYAWRYIRASMSLAGLLPPLSD--N 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635 1098 GHLLMDGGYINNLPADVARSMGAKVVIAIDVGSRDETDLTNYGDALSGWWLLWKRWNPLATKVKVLNMAEIQTRLAYVCC 1177
Cdd:cd07227   159 GSMLLDGGYMDNLPVSPMRSLGIRDIFAVDVGSVDDRTPMDYGDSVSGVWIFFNRWNPFSSRPNVPSMAEIQSRLTYVSS 238

                         250       260       270
                  ....*....|....*....|....*....|.
gi 568913635 1178 VRQLEMVKNSDYCEYLRPPIDSYRTLDFGKF 1208
Cdd:cd07227   239 VKTLEKVKATPGCHYMRPPVQDFDTLDFGKF 269
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 948-1128 1.13e-72

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: 239.76  E-value: 1.13e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  948 IALVLGGGGARGCAQVGILRALAECGVPVDIIGGTSIGAFMGALFAEERSYSQTRIRAKQwaegMTSMMKTILDLTYPIT 1027
Cdd:cd07205     1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAGYSPEEIEERAKL----RSTDLKALSDLTIPTA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635 1028 SMFSGTGFNSSISNIFKDRQIEDLWLPYFAITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLCDpkDGHLLMDGGYI 1107
Cdd:cd07205    77 GLLRGDKFLELLDEYFGDRDIEDLWIPFFIVATDLTSGKLVVFRSGSLVRAVRASMSIPGIFPPVKI--DGQLLVDGGVL 154

                         170       180
                  ....*....|....*....|.
gi 568913635 1108 NNLPADVARSMGAKVVIAIDV 1128
Cdd:cd07205   155 NNLPVDVLRELGADIIIAVDL 175
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 948-1224 1.66e-59

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 205.52  E-value: 1.66e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  948 IALVLGGGGARGCAQVGILRALAECGVPVDIIGGTSIGAFMGALFAEERSYSQ-----TRIRAKQWAEGMTSMMKTILDL 1022
Cdd:COG1752     7 IGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADEleelwRSLDRRDLFDLSLPRRLLRLDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635 1023 TYPITSMFSGTGFNSSISNIFKDRQIEDLWLPYFAITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLcdPKDGHLLM 1102
Cdd:COG1752    87 GLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPV--EIDGRLYV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635 1103 DGGYINNLPADVARSMGAKVVIAIDVGSRDEtdltnygdalsgwwllwkrwnplatkvKVLNMAEIQTRLAYVCCVRQLE 1182
Cdd:COG1752   165 DGGVVNNLPVDPARALGADRVIAVDLNPPLR---------------------------KLPSLLDILGRALEIMFNSILR 217

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 568913635 1183 MVKNSDYC-EYLRPPIDSYRTLDFGKFDEICEVGYQHGRTVFD 1224
Cdd:COG1752   218 RELALEPAdILIEPDLSGISLLDFSRAEELIEAGYEAARRALD 260
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 950-1126 4.28e-48

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


Pssm-ID: 132837 [Multi-domain]  Cd Length: 172  Bit Score: 169.44  E-value: 4.28e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  950 LVLGGGGARGCAQVGILRALAECGVPVDIIGGTSIGAFMGALFAEERSYSQTRIRAKqwaeGMTSMMKTILDLTYPITSM 1029
Cdd:cd07198     1 LVLSGGGALGIYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASGRDLEEALLLLL----RLSREVRLRFDGAFPPTGR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635 1030 FSGTGFNSSISNIFKDRqIEDLWLPYFAITTDITASAMRVH---TDGSLWRYVRASMSLSGYMPPLCDPKDGHLLMDGGY 1106
Cdd:cd07198    77 LLGILRQPLLSALPDDA-HEDASGKLFISLTRLTDGENVLVsdtSKGELWSAVRASSSIPGYFGPVPLSFRGRRYGDGGL 155

                         170       180
                  ....*....|....*....|
gi 568913635 1107 INNLPADVarsMGAKVVIAI 1126
Cdd:cd07198   156 SNNLPVAE---LGNTINVSP 172
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 948-1128 5.58e-38

Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like phospholipase domain containing protein 6. PNPLA6 is commonly known as Neuropathy Target Esterase (NTE). NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. This group includes YCHK and rssA from Escherichia coli as well as Ylbk from Bacillus amyloliquefaciens.


Pssm-ID: 132866 [Multi-domain]  Cd Length: 175  Bit Score: 140.49  E-value: 5.58e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  948 IALVLGGGGARGCAQVGILRALAECGVPVDIIGGTSIGAFMGALFAEERS-YSQTRIRAKQWAEgmtsmMKTILDLTYPI 1026
Cdd:cd07228     1 IGLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYAAGHLdALEEWVRSLSQRD-----VLRLLDLSASR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635 1027 TSMFSGTGFNSSISNIFKDRQIEDLWLPYFAITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLCDpkDGHLLMDGGY 1106
Cdd:cd07228    76 SGLLKGEKVLEYLREIMGGVTIEELPIPFAAVATDLQTGKEVWFREGSLIDAIRASISIPGIFAPVEH--NGRLLVDGGV 153

                         170       180
                  ....*....|....*....|..
gi 568913635 1107 INNLPADVARSMGAKVVIAIDV 1128
Cdd:cd07228   154 VNPIPVSVARALGADIVIAVDL 175
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 950-1127 5.21e-26

Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates. This family also includes the catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms.


Pssm-ID: 132836 [Multi-domain]  Cd Length: 155  Bit Score: 105.19  E-value: 5.21e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  950 LVLGGGGARGCAQVGILRALAECGV--PVDIIGGTSIGAFMGALFaeersysqtrirakqwaegmtsmmktildltYPIT 1027
Cdd:cd01819     1 LSFSGGGFRGMYHAGVLSALAERGLldCVTYLAGTSGGAWVAATL-------------------------------YPPS 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635 1028 SMFSGTGFNSSIsnifkdrqiEDLWLPYFAITTDITASAM----RVHTDGSLWRYVRASMSLSGYMPPLCD--------- 1094
Cdd:cd01819    50 SSLDNKPRQSLE---------EALSGKLWVSFTPVTAGENvlvsRFVSKEELIRALFASGSWPSYFGLIPPaelytsksn 120

                         170       180       190
                  ....*....|....*....|....*....|....
gi 568913635 1095 -PKDGHLLMDGGYINNLPADVARSMGAKVVIAID 1127
Cdd:cd01819   121 lKEKGVRLVDGGVSNNLPAPVLLRPGRGVTLTIS 154
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 950-1115 9.08e-26

Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein but it also has the enzymatic activity of lipid acyl hydrolase, catalysing the cleavage of fatty acids from membrane lipids. Members of this family have been found also in vertebrates.


Pssm-ID: 396341  Cd Length: 190  Bit Score: 105.77  E-value: 9.08e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635   950 LVLGGGGARGCAQVGILRALAECGVPVDIIGGTSIGAFMGALFA--------EERSYSQTRIRAKQWAEGMTSMMKTILD 1021
Cdd:pfam01734    1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLAlgrdpeeiEDLLLELDLNLFLSLIRKRALSLLALLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  1022 LTYPITSMFSGTGFNSSISNIFKDRQIEDLWLPYFAI-----------------TTDITASAMRVHTDGSLWRYVRASMS 1084
Cdd:pfam01734   81 GLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLlvvalralltvistalgTRARILLPDDLDDDEDLADAVLASSA 160

                          170       180       190
                   ....*....|....*....|....*....|.
gi 568913635  1085 LSGYMPPLcdPKDGHLLMDGGYINNLPADVA 1115
Cdd:pfam01734  161 LPGVFPPV--RLDGELYVDGGLVDNVPVEAA 189
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 950-1130 1.24e-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: 106.22  E-value: 1.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  950 LVLGGGGARGCAQVGILRALAECGVPVDIIGGTSIGAFMGALFAEersysqtrirakqwaeGMTSMMKTI----LDLTYP 1025
Cdd:cd07209     1 LVLSGGGALGAYQAGVLKALAEAGIEPDIISGTSIGAINGALIAG----------------GDPEAVERLeklwRELSRE 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635 1026 iTSMFsgTGFNSSISNIFKDRQIEDLWLPYFAITTDITASAMRVHTDGSLWR---YVRASMSLsgymPPLCDPK--DGHL 1100
Cdd:cd07209    65 -DVFL--RGLLDRALDFDTLRLLAILFAGLVIVAVNVLTGEPVYFDDIPDGIlpeHLLASAAL----PPFFPPVeiDGRY 137

                         170       180       190
                  ....*....|....*....|....*....|
gi 568913635 1101 LMDGGYINNLPADVARSMGAKVVIAIDVGS 1130
Cdd:cd07209   138 YWDGGVVDNTPLSPAIDLGADEIIVVSLSD 167
PRK10279 PRK10279
patatin-like phospholipase RssA;
948-1127 3.73e-25

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 107.49  E-value: 3.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  948 IALVLGGGGARGCAQVGILRALAECGVPVDIIGGTSIGAFMGALFAEERSYSQTR-IRAKQWAEGMTSMmktilDLTYPI 1026
Cdd:PRK10279    6 IGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRLSALEDwVTSFSYWDVLRLM-----DLSWQR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635 1027 TSMFSGTGFNSSISNIFKDRQIEDLWLPYFAITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLcdPKDGHLLMDGGY 1106
Cdd:PRK10279   81 GGLLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPV--AHNGYWLVDGAV 158

                         170       180
                  ....*....|....*....|.
gi 568913635 1107 INNLPADVARSMGAKVVIAID 1127
Cdd:PRK10279  159 VNPVPVSLTRALGADIVIAVD 179
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 604-712 9.89e-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: 91.62  E-value: 9.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  604 SSFVRQIDFALDWMEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLVGVVETLTHQARATTVHA 683
Cdd:cd00038     7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRA 86

                          90       100
                  ....*....|....*....|....*....
gi 568913635  684 VRDSELAKLPAGALTSIKRRYPQVVTRLI 712
Cdd:cd00038    87 LTDSELLVLPRSDFRRLLQEYPELARRLL 115
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 948-1134 4.72e-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: 90.48  E-value: 4.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  948 IALVLGGGGARGCAQVGILRALAECGVPVDIIGGTSIGAFMGALFAeersysqTRIRAKQWAEGMTSMMK----TILDLT 1023
Cdd:cd07210     1 FALVLSSGFFGFYAHLGFLAALLEMGLEPSAISGTSAGALVGGLFA-------SGISPDEMAELLLSLERkdfwMFWDPP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635 1024 YPiTSMFSGTGFNSSISNIFKDRQIEDLWLPYFAITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLcdPKDGHLLMD 1103
Cdd:cd07210    74 LR-GGLLSGDRFAALLREHLPPDRFEELRIPLAVSVVDLTSRETLLLSEGDLAEAVAASCAVPPLFQPV--EIGGRPFVD 150

                         170       180       190
                  ....*....|....*....|....*....|.
gi 568913635 1104 GGYINNLPADVARSMGAKVVIaIDVGSRDET 1134
Cdd:cd07210   151 GGVADRLPFDALRPEIERILY-HHVAPRRPW 180
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 617-704 1.89e-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: 81.50  E-value: 1.89e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635   617 MEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLVGVVETLTHQARATTVHAVRDSELAKLPAGA 696
Cdd:pfam00027    2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRED 81


                   ....*...
gi 568913635   697 LTSIKRRY 704
Cdd:pfam00027   82 FLELLERD 89
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 170-291 7.66e-18

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


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 80.45  E-value: 7.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  170 VLGHFEKPLFLELCKHMVFVQLQEGEHVFQPGEPDISIYVVQDGRLEVCIQDADGTEVVVKEVLPGDSVhSLLSILDVIT 249
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLF-GELALLGNGP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568913635  250 gHTApyktvSARAAVSSTVLWLPAAAFQGVFEKYPETLVRVV 291
Cdd:cd00038    80 -RSA-----TVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 171-308 4.30e-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: 81.19  E-value: 4.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  171 LGHFEKPLFLELCKHMVFVQLQEGEHVFQPGEPDISIYVVQDGRLEVCIQDADGTEVVVKEVLPGDsvhsLLSILDVITG 250
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGD----FFGELSLLGG 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568913635  251 HTAPYktvSARAAVSSTVLWLPAAAFQGVFEKYPETLVRVVQIIMVRL----QRVTFLALHN 308
Cdd:COG0664    77 EPSPA---TAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLrqlqERLVSLAFLS 135
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 617-738 5.51e-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: 81.19  E-value: 5.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  617 MEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLVGVVETLTHQARATTVHAVRDSELAKLPAGA 696
Cdd:COG0664    19 RTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSPATAEALEDSELLRIPRED 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568913635  697 LTSIKRRYPQVVTRLIHLLGEKilgsLQQGSATGHQLGFNTA 738
Cdd:COG0664    99 LEELLERNPELARALLRLLARR----LRQLQERLVSLAFLSA 136
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 481-591 2.57e-15

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


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 73.51  E-value: 2.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  481 LLTLMKLDDPSLLDGRVAFLHVPAGTLVSKQGDQDVNILFVVSGMLHVYQQKIDSlEDTCLFLTHPGEMVGQLAVLTGEP 560
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDG-REQIVGFLGPGDLFGELALLGNGP 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568913635  561 LMFTIRANRDCSFLSISKAHFYEIMRKRPDV 591
Cdd:cd00038    80 RSATVRALTDSELLVLPRSDFRRLLQEYPEL 110
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 950-1114 1.18e-14

ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is a potent virulence factor of Pseudomonas aeruginosa. One of the pathogenic mechanisms of P. aeruginosa is to induce cytotoxicity by the injection of effector proteins (e.g. ExoU) using the type III secretion (T3S) system. ExoU is homologus to patatin and also has the conserved catalytic residues of mammalian calcium-independent (iPLA2) and cytosolic (cPLA2) PLA2. In vitro, ExoU cytotoxity is blocked by the inhibitor of cytosolic and Ca2-independent phospholipase A2 (cPLA2 and iPLA2) enzymes, suggesting that phospholipase A2 inhibitors may represent a novel mode of treatment for acute P. aeruginosa infections. ExoU requires eukaryotic superoxide dismutase as a cofactor and cleaves phosphatidylcholine and phosphatidylethanolamine in vitro. VipD, a 69-kDa cytosolic protein, belongs to the members of Legionella pneumophila family and is homologus to ExoU from Pseudomonas. Even though VipD shows high sequence similarity with several functional regions of ExoU (e.g. oxyanion hole, active site serine, active site aspartate), it has been shown to have no phospholipase activity. This family includes ExoU from Pseudomonas aeruginosa and VipD of Legionella pneumophila.


Pssm-ID: 132846  Cd Length: 194  Bit Score: 73.85  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  950 LVLGGGGARGCAQVGILRALAECGVPVDIIGGTSIGAFMGALFAEerSYSQTRIRAKQWAEGMTSMM--------KTILD 1021
Cdd:cd07207     2 LVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLAL--GYSAADIKDILKETDFAKLLdspvgllfLLPSL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635 1022 LTYPITS-----------MFSGTGFNSSISNIFKDRQiEDLWLPYFAITTDITASAMRV----HT-DGSLWRYVRASMSL 1085
Cdd:cd07207    80 FKEGGLYkgdaleewlreLLKEKTGNSFATSLLRDLD-DDLGKDLKVVATDLTTGALVVfsaeTTpDMPVAKAVRASMSI 158

                         170       180
                  ....*....|....*....|....*....
gi 568913635 1086 SGYMPPLCDPKdGHLLMDGGYINNLPADV 1114
Cdd:cd07207   159 PFVFKPVRLAK-GDVYVDGGVLDNYPVWL 186
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 501-611 2.39e-13

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: 70.40  E-value: 2.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  501 HVPAGTLVSKQGDQDVNILFVVSGMLHVYQQKIDSlEDTCLFLTHPGEMVGQLAVLTGEPLMFTIRANRDCSFLSISKAH 580
Cdd:COG0664    20 TLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDG-REQILGFLGPGDFFGELSLLGGEPSPATAEALEDSELLRIPRED 98

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568913635  581 FYEIMRKRPDVVLGVAHTVVKRMSSFVRQID 611
Cdd:COG0664    99 LEELLERNPELARALLRLLARRLRQLQERLV 129
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 499-587 2.53e-13

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: 66.86  E-value: 2.53e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635   499 FLHVPAGTLVSKQGDQDVNILFVVSGMLHVYQQKIDSLEDTcLFLTHPGEMVGQLAVLTGEPLMFTIRANRDCSFLSISK 578
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQI-LAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPR 79


                   ....*....
gi 568913635   579 AHFYEIMRK 587
Cdd:pfam00027   80 EDFLELLER 88
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 188-283 6.52e-13

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: 65.71  E-value: 6.52e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635   188 FVQLQEGEHVFQPGEPDISIYVVQDGRLEVCIQDADGTEVVVKEVLPGDSVHsLLSILdvitgHTAPYkTVSARAAVSST 267
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFG-ELALL-----GGEPR-SATVVALTDSE 73

                           90
                   ....*....|....*.
gi 568913635   268 VLWLPAAAFQGVFEKY 283
Cdd:pfam00027   74 LLVIPREDFLELLERD 89
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 170-293 1.98e-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: 65.50  E-value: 1.98e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635    170 VLGHFEKPLFLELCKHMVFVQLQEGEHVFQPGEPDISIYVVQDGRLEVCIQDADGTEVVVKEVLPGDSVhSLLSILdviT 249
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFF-GELALL---T 76

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 568913635    250 GHTAPYkTVSARAAVSSTVLWLPAAAFQGVFEKYPETLVRVVQI 293
Cdd:smart00100   77 NSRRAA-SAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 605-712 8.17e-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: 8.17e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635    605 SFVRQIDFALDWMEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLVGVVETLTHQARATTVHAV 684
Cdd:smart00100    8 EELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRRAASAAAV 87

                            90       100       110
                    ....*....|....*....|....*....|
gi 568913635    685 --RDSELAKLPAGALTSIKRRYPQVVTRLI 712
Cdd:smart00100   88 alELATLLRIDFRDFLQLLPELPQLLLELL 117
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
948-1126 2.60e-10

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 62.87  E-value: 2.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  948 IALVLGGGGARGCAQVGILRALAECGVPVDIIGGTSIGAFMGALFAeersysqtrirAKQWAEGMTSMMKTILDLTYpit 1027
Cdd:COG4667     6 TALVLEGGGMRGIFTAGVLDALLEEGIPFDLVIGVSAGALNGASYL-----------SRQPGRARRVITDYATDPRF--- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635 1028 smfsgtgfnSSISNIFKDRQIEDL-WL---------P-----YFAITTDITASAMRVHT-----------DGSLWRYVRA 1081
Cdd:COG4667    72 ---------FSLRNFLRGGNLFDLdFLydeipnellPfdfetFKASPREFYVVATNADTgeaeyfskkddDYDLLDALRA 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568913635 1082 SMSlsgyMPPLCDP--KDGHLLMDGGYINNLPADVARSMGAKVVIAI 1126
Cdd:COG4667   143 SSA----LPLLYPPveIDGKRYLDGGVADSIPVREAIRDGADKIVVI 185
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 950-1126 2.25e-09

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


Pssm-ID: 132847 [Multi-domain]  Cd Length: 266  Bit Score: 59.93  E-value: 2.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  950 LVLGGGGARGCAQVGILRALAECGV-PVDIIGGTSIGAFMGA-LFAEERSYSQTRI----RAKQWAeGMTSMMKT----I 1019
Cdd:cd07208     1 LVLEGGGMRGAYTAGVLDAFLEAGIrPFDLVIGVSAGALNAAsYLSGQRGRALRINtkyaTDPRYL-GLRSLLRTgnlfD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635 1020 LDLTYPITSMfsgtgfnssISNIFKDRQIEDLWLPYFAITTDI-TASAM--RVHTDGSLW-RYVRASMSLSGYMPPlcDP 1095
Cdd:cd07208    80 LDFLYDELPD---------GLDPFDFEAFAASPARFYVVATDAdTGEAVyfDKPDILDDLlDALRASSALPGLFPP--VR 148

                         170       180       190
                  ....*....|....*....|....*....|.
gi 568913635 1096 KDGHLLMDGGYINNLPADVARSMGAKVVIAI 1126
Cdd:cd07208   149 IDGEPYVDGGLSDSIPVDKAIEDGADKIVVI 179
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 473-590 5.32e-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: 55.48  E-value: 5.32e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635    473 IFRAATKDLLtlmklddpSLLDGRVAFLHVPAGTLVSKQGDQDVNILFVVSGMLHVYQQKIDSLEDTcLFLTHPGEMVGQ 552
Cdd:smart00100    1 LFKNLDAEEL--------RELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQI-VGTLGPGDFFGE 71

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|
gi 568913635    553 LAVLTGEPL--MFTIRANRDCSFLSISKAHFYEIMRKRPD 590
Cdd:smart00100   72 LALLTNSRRaaSAAAVALELATLLRIDFRDFLQLLPELPQ 111
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 546-693 6.37e-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: 46.81  E-value: 6.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635   546 PGEMVGQLAVLTGEPLMFTIRANRDCSFLSISK--------------AHFYE-IMRKRPDVVLGVAHTVVKRM---SSFV 607
Cdd:TIGR03896   60 RGEIVGEMSLLETRPPVATIKAVPKSRVMSIPVgelaaklqsdvgfaAHFYRaIAIKLALQIQNQNHQLHRRNgadSEPL 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635   608 RQIDFAL--------DWME-------VEAGRAIYRQGDKSDCTYIVLSGRLRSVIrKDDGKKRLAGEYGRGDLVGVVETL 672
Cdd:TIGR03896  140 RKVLFIFgelhesdvAWMMasgtpqkLPAGTILIHEGGTVDALYILLYGEASLSI-SPDGPGREVGSSRRGEILGETPFL 218

                          170       180
                   ....*....|....*....|..
gi 568913635   673 THQARAT-TVHAVRDSELAKLP 693
Cdd:TIGR03896  219 NGSLPGTaTVKAIENSVLLAID 240
Pat_PNPLA8 cd07211
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ...
 950-1115 7.45e-05

Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial phospholipase which maintains mitochondrial integrity. PNPLA8 is also known as iPLA2-gamma. In humans, it is predominantly expressed in heart tissue. iPLA2-gamma can catalyze both phospholipase A1 and A2 reactions (PLA1 and PLA2 respectively). This family includes PNPLA8 (iPLA2-gamma) from Homo sapiens and iPLA2-2 from Mus musculus.


Pssm-ID: 132850 [Multi-domain]  Cd Length: 308  Bit Score: 46.48  E-value: 7.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  950 LVLGGGGARGCAQVGILRAL-AECGVPV----DIIGGTSIGAFMGALFAEErsysqtRIRAKQWAEGMTSMMKTILDLTY 1024
Cdd:cd07211    11 LSIDGGGTRGVVALEILRKIeKLTGKPIhelfDYICGVSTGAILAFLLGLK------KMSLDECEELYRKLGKDVFSQNT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635 1025 PITSM----FSGTGFNSSI-SNIFK-----DRQIEDLWLP----YFAITTDITASAMRV--------------HTDGS-- 1074
Cdd:cd07211    85 YISGTsrlvLSHAYYDTETwEKILKemmgsDELIDTSADPncpkVACVSTQVNRTPLKPyvfrnynhppgtrsHYLGSck 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 568913635 1075 --LWRYVRASMSLSGYMPPLcdPKDGHLLMDGG-YINNlPADVA 1115
Cdd:cd07211   165 hkLWEAIRASSAAPGYFEEF--KLGNNLHQDGGlLANN-PTALA 205
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 950-1115 7.90e-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: 46.13  E-value: 7.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  950 LVLGGGGARGCAQVGILRALAECGvP-----VDIIGGTSIGAFMGALFAEERSYSQTRiraKQWAEgmtsMMKTILDLTY 1024
Cdd:cd07213     5 LSLDGGGVKGIVQLVLLKRLAEEF-PsfldqIDLFAGTSAGSLIALGLALGYSPRQVL---KLYEE----VGLKVFSKSS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635 1025 PITSMFSGTGFNSSISNIFKDRQIEDLWL---------PYFAITTDI-----TASAMRVHT-------DGSLWRYVRASM 1083
Cdd:cd07213    77 AGGGAGNNQYFAAGFLKAFAEVFFGDLTLgdlkrkvlvPSFQLDSGKddpnrRWKPKLFHNfpgepdlDELLVDVCLRSS 156

                         170       180       190
                  ....*....|....*....|....*....|...
gi 568913635 1084 SLSGYMPPLcdpkDGHLlmDGG-YINNlPADVA 1115
Cdd:cd07213   157 AAPTYFPSY----QGYV--DGGvFANN-PSLCA 182
Pat_PLPL cd07232
Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin ...
 949-993 1.19e-03

Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants and fungi. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have been found also in vertebrates.


Pssm-ID: 132870  Cd Length: 407  Bit Score: 43.02  E-value: 1.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568913635  949 ALVLGGGGARGCAQVGILRALAECGVPVDIIGGTSIGAFMGALFA 993
Cdd:cd07232    69 ALCLSGGAAFAYYHFGVVKALLDADLLPNVISGTSGGSLVAALLC 113
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 949-993 3.83e-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: 41.04  E-value: 3.83e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568913635  949 ALVLGGGGARGCAQVGILRALAECGVPVDIIGGTSIGAFMGALFA 993
Cdd:cd07206    71 ALMLSGGASLGLFHLGVVKALWEQDLLPRVISGSSAGAIVAALLG 115
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
625-735 4.97e-03

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 39.96  E-value: 4.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913635  625 IYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLVGVVETL-THQARATTVHAVRDSELAKLPAGALTSIKRR 703
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFeEGQERSAWVRAKTACEVAEISYKKFRQLIQV 110

                          90       100       110
                  ....*....|....*....|....*....|..
gi 568913635  704 YPqvvtRLIHLLGEKILGSLQQGSATGHQLGF 735
Cdd:PRK11753  111 NP----DILMALSAQMARRLQNTSRKVGDLAF 138
 
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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