NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|19075586|ref|NP_588086|]
View 

putative lysophospholipase [Schizosaccharomyces pombe]

Protein Classification

cyclic nucleotide-binding domain-containing protein( domain architecture ID 10035157)

cyclic nucleotide-binding domain-containing protein binds cyclic nucleotides (cAMP or cGMP) where binding of the effector leads to conformational changes; may be involved in regulating transcription, be present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK), or be part of vertebrate cyclic nucleotide-gated ion-channels.

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Pat_Fungal_NTE1 cd07227
Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy ...
 999-1268 0e+00

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: 576.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586  999 RLARRICGKAIALVLGGGGARGISQIGILYALEEAGIPFDIIGGTSIGAFNGGLYAWEADLVPMFGRAKKFCGRMANLWR 1078
Cdd:cd07227    1 RLARRLCGQAIGLVLGGGGARGISHIGILQALEEAGIPIDAIGGTSIGSFVGGLYAREADLVPIFGRAKKFAGRMASMWR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1079 FVLDVTYPQAAYTTGHEFNRGIWKTFGEIHIEDFWLPFYANTTNITHSRMDIHSSGYAWRYIRASMSLAGLVPPMlSDSG 1158
Cdd:cd07227   81 FLSDVTYPFASYTTGHEFNRGIWKTFGNTHIEDFWIPFYANSTNITHSRMEIHSSGYAWRYIRASMSLAGLLPPL-SDNG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1159 DMLLDGGYMDNLTVSHMQSLGASSIFAIDVGSEDSREPMHYGDTVSGVWALISRWIPFIPKTSFPSLAEIQSRLTYVTSV 1238
Cdd:cd07227  160 SMLLDGGYMDNLPVSPMRSLGIRDIFAVDVGSVDDRTPMDYGDSVSGVWIFFNRWNPFSSRPNVPSMAEIQSRLTYVSSV 239

                        250       260       270
                 ....*....|....*....|....*....|
gi 19075586 1239 ATGEKVKSMPGCFYMRPPVKDFPTLEFGSF 1268
Cdd:cd07227  240 KTLEKVKATPGCHYMRPPVQDFDTLDFGKF 269
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 641-756 2.38e-20

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: 87.77  E-value: 2.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586  641 LISLVPSLLLKLDFAVGWIHLNPDQVVYEKNDPSDCVYVVLNGRLRSIEDERGSARTQVDYfneYGKGDSVGELEMLLNN 720
Cdd:cd00038    2 FSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGF---LGPGDLFGELALLGNG 78

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 19075586  721 RRSSTLFAIRDSELAKIPETLFNALSLSHPAVGLQL 756
Cdd:cd00038   79 PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 522-638 4.00e-13

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: 66.97  E-value: 4.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586  522 KSTILEFAKEIEIIFYKKGTTIVRQGDHADGLYYIIDGFLDATcpskltfsTSYDTDLGMHSFMIKPGGIVNYQACVSNY 601
Cdd:cd00038    7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVY--------KLDEDGREQIVGFLGPGDLFGELALLGNG 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 19075586  602 RSFINVTARSDVLVGFLPRSCLERIIDQEPLISLTIA 638
Cdd:cd00038   79 PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
 
Name Accession Description Interval E-value
Pat_Fungal_NTE1 cd07227
Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy ...
 999-1268 0e+00

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: 576.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586  999 RLARRICGKAIALVLGGGGARGISQIGILYALEEAGIPFDIIGGTSIGAFNGGLYAWEADLVPMFGRAKKFCGRMANLWR 1078
Cdd:cd07227    1 RLARRLCGQAIGLVLGGGGARGISHIGILQALEEAGIPIDAIGGTSIGSFVGGLYAREADLVPIFGRAKKFAGRMASMWR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1079 FVLDVTYPQAAYTTGHEFNRGIWKTFGEIHIEDFWLPFYANTTNITHSRMDIHSSGYAWRYIRASMSLAGLVPPMlSDSG 1158
Cdd:cd07227   81 FLSDVTYPFASYTTGHEFNRGIWKTFGNTHIEDFWIPFYANSTNITHSRMEIHSSGYAWRYIRASMSLAGLLPPL-SDNG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1159 DMLLDGGYMDNLTVSHMQSLGASSIFAIDVGSEDSREPMHYGDTVSGVWALISRWIPFIPKTSFPSLAEIQSRLTYVTSV 1238
Cdd:cd07227  160 SMLLDGGYMDNLPVSPMRSLGIRDIFAVDVGSVDDRTPMDYGDSVSGVWIFFNRWNPFSSRPNVPSMAEIQSRLTYVSSV 239

                        250       260       270
                 ....*....|....*....|....*....|
gi 19075586 1239 ATGEKVKSMPGCFYMRPPVKDFPTLEFGSF 1268
Cdd:cd07227  240 KTLEKVKATPGCHYMRPPVQDFDTLDFGKF 269
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 1006-1285 1.18e-47

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 171.24  E-value: 1.18e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1006 GKAIALVLGGGGARGISQIGILYALEEAGIPFDIIGGTSIGAFNGGLYA--WEAD-LVPMFGR--AKKFCGRMANLWRFV 1080
Cdd:COG1752    4 RPKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAagYSADeLEELWRSldRRDLFDLSLPRRLLR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1081 LDVTYPQAAYTTGHEFNRGIWKTFGEIHIEDFWLPFYANTTNITHSRMDIHSSGYAWRYIRASMSLAGLVPPMLSDsGDM 1160
Cdd:COG1752   84 LDLGLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPVEID-GRL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1161 LLDGGYMDNLTVSHMQSLGASSIFAIDVGSEDSRepmhygdtvsgvwalisrwipfipktsFPSLAEIQSRLTYVTSVAT 1240
Cdd:COG1752  163 YVDGGVVNNLPVDPARALGADRVIAVDLNPPLRK---------------------------LPSLLDILGRALEIMFNSI 215

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 19075586 1241 GEKVKSMPGC-FYMRPPVKDFPTLEFGSFEKIYNVGYNYGKEYVEK 1285
Cdd:COG1752  216 LRRELALEPAdILIEPDLSGISLLDFSRAEELIEAGYEAARRALDE 261
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 1011-1172 4.42e-25

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


Pssm-ID: 396341  Cd Length: 190  Bit Score: 103.84  E-value: 4.42e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586   1011 LVLGGGGARGISQIGILYALEEAGIPFDIIGGTSIGAFNGGLYAWEADLVPMFGRAKKFC--------GRMANLWRFVLD 1082
Cdd:pfam01734    1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDlnlflsliRKRALSLLALLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586   1083 VTYPQAAYTTGHEFNRGIWKTFGEIHIEDFWLPF-----------------YANTTNITHSRMDIHSSGYAWRYIRASMS 1145
Cdd:pfam01734   81 GLIGEGGLFDGDALRELLRKLLGDLTLEELAARLslllvvalralltvistALGTRARILLPDDLDDDEDLADAVLASSA 160

                          170       180
                   ....*....|....*....|....*..
gi 19075586   1146 LAGLVPPMLSDsGDMLLDGGYMDNLTV 1172
Cdd:pfam01734  161 LPGVFPPVRLD-GELYVDGGLVDNVPV 186
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 641-756 2.38e-20

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: 87.77  E-value: 2.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586  641 LISLVPSLLLKLDFAVGWIHLNPDQVVYEKNDPSDCVYVVLNGRLRSIEDERGSARTQVDYfneYGKGDSVGELEMLLNN 720
Cdd:cd00038    2 FSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGF---LGPGDLFGELALLGNG 78

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 19075586  721 RRSSTLFAIRDSELAKIPETLFNALSLSHPAVGLQL 756
Cdd:cd00038   79 PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
PRK10279 PRK10279
patatin-like phospholipase RssA;
1009-1187 4.52e-17

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 83.61  E-value: 4.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586  1009 IALVLGGGGARGISQIGILYALEEAGIPFDIIGGTSIGAFNGGLYAweadlvpmfgrakkfCGRMANLWRFVLDVTYPQA 1088
Cdd:PRK10279    6 IGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYA---------------CDRLSALEDWVTSFSYWDV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586  1089 AYTTGHEFNRG-------IWKTFGEI----HIEDFWLPFYANTTNITHSRM------DIHSSgyawryIRASMSLAGLVP 1151
Cdd:PRK10279   71 LRLMDLSWQRGgllrgerVFNQYREImpetEIENCSRRFGAVATNLSTGRElwftegDLHLA------IRASCSMPGLMA 144

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 19075586  1152 PmLSDSGDMLLDGGYMDNLTVSHMQSLGASSIFAID 1187
Cdd:PRK10279  145 P-VAHNGYWLVDGAVVNPVPVSLTRALGADIVIAVD 179
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 659-769 1.80e-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: 1.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586  659 IHLNPDQVVYEKNDPSDCVYVVLNGRLR-SIEDERGsaRTQVDYFneYGKGDSVGELEMLLNNRRSSTLFAIRDSELAKI 737
Cdd:COG0664   19 RTLKKGEVLFREGDPADHLYFVLSGLVKlYRISEDG--REQILGF--LGPGDFFGELSLLGGEPSPATAEALEDSELLRI 94

                         90       100       110
                 ....*....|....*....|....*....|..
gi 19075586  738 PETLFNALSLSHPAVGLQLSKIIANRMNLLLN 769
Cdd:COG0664   95 PREDLEELLERNPELARALLRLLARRLRQLQE 126
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 659-749 7.61e-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: 68.40  E-value: 7.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586    659 IHLNPDQVVYEKNDPSDCVYVVLNGRLRsIEDERGSARTQVdyFNEYGKGDSVGELEMLLNNRRSSTLFAIRDSELAKIP 738
Cdd:pfam00027    2 RSYKAGEVIFREGDPADSLYIVLSGKVK-VYRTLEDGREQI--LAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIP 78

                           90
                   ....*....|.
gi 19075586    739 ETLFNALSLSH 749
Cdd:pfam00027   79 REDFLELLERD 89
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 522-638 4.00e-13

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: 66.97  E-value: 4.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586  522 KSTILEFAKEIEIIFYKKGTTIVRQGDHADGLYYIIDGFLDATcpskltfsTSYDTDLGMHSFMIKPGGIVNYQACVSNY 601
Cdd:cd00038    7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVY--------KLDEDGREQIVGFLGPGDLFGELALLGNG 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 19075586  602 RSFINVTARSDVLVGFLPRSCLERIIDQEPLISLTIA 638
Cdd:cd00038   79 PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 534-629 3.02e-10

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: 58.00  E-value: 3.02e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586    534 IIFYKKGTTIVRQGDHADGLYYIIDGFLDAtcpskltFSTSYDTDLGMHSFmIKPGGIVNYQACVSNYRSFINVTARSDV 613
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKV-------YRTLEDGREQILAV-LGPGDFFGELALLGGEPRSATVVALTDS 72

                           90
                   ....*....|....*.
gi 19075586    614 LVGFLPRSCLERIIDQ 629
Cdd:pfam00027   73 ELLVIPREDFLELLER 88
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 524-641 1.42e-09

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: 59.23  E-value: 1.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586  524 TILEFAKEIEIIFYKKGTTIVRQGDHADGLYYIIDGFLdatcpsKLTFSTSYDTDLGMHsfMIKPGGIVNYQACVSNYRS 603
Cdd:COG0664    8 ELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLV------KLYRISEDGREQILG--FLGPGDFFGELSLLGGEPS 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 19075586  604 FINVTARSDVLVGFLPRSCLERIIDQEPLISLTIAKRL 641
Cdd:COG0664   80 PATAEALEDSELLRIPREDLEELLERNPELARALLRLL 117
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 646-756 1.74e-08

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


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 53.94  E-value: 1.74e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586     646 PSLLLKLDFAVGWIHLNPDQVVYEKNDPSDCVYVVLNGRLR-SIEDERGsaRTQVdyFNEYGKGDSVGELEMLLNNRR-- 722
Cdd:smart00100    7 AEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEvYKVLEDG--EEQI--VGTLGPGDFFGELALLTNSRRaa 82

                            90       100       110
                    ....*....|....*....|....*....|....
gi 19075586     723 SSTLFAIRDSELAKIPETLFNALSLSHPAVGLQL 756
Cdd:smart00100   83 SAAAVALELATLLRIDFRDFLQLLPELPQLLLEL 116
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 522-644 4.90e-06

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: 47.01  E-value: 4.90e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586     522 KSTILEFAKEIEIIFYKKGTTIVRQGDHADGLYYIIDGFLDATcpskltfsTSYDTDLGMHSFMIKPGGIVNYQACVSNY 601
Cdd:smart00100    7 AEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVY--------KVLEDGEEQIVGTLGPGDFFGELALLTNS 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 19075586     602 RSFINVTARSDVLVgFLPRSCLERIIDQEPLISLTIAKRLISL 644
Cdd:smart00100   79 RRAASAAAVALELA-TLLRIDFRDFLQLLPELPQLLLELLLEL 120
 
Name Accession Description Interval E-value
Pat_Fungal_NTE1 cd07227
Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy ...
 999-1268 0e+00

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: 576.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586  999 RLARRICGKAIALVLGGGGARGISQIGILYALEEAGIPFDIIGGTSIGAFNGGLYAWEADLVPMFGRAKKFCGRMANLWR 1078
Cdd:cd07227    1 RLARRLCGQAIGLVLGGGGARGISHIGILQALEEAGIPIDAIGGTSIGSFVGGLYAREADLVPIFGRAKKFAGRMASMWR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1079 FVLDVTYPQAAYTTGHEFNRGIWKTFGEIHIEDFWLPFYANTTNITHSRMDIHSSGYAWRYIRASMSLAGLVPPMlSDSG 1158
Cdd:cd07227   81 FLSDVTYPFASYTTGHEFNRGIWKTFGNTHIEDFWIPFYANSTNITHSRMEIHSSGYAWRYIRASMSLAGLLPPL-SDNG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1159 DMLLDGGYMDNLTVSHMQSLGASSIFAIDVGSEDSREPMHYGDTVSGVWALISRWIPFIPKTSFPSLAEIQSRLTYVTSV 1238
Cdd:cd07227  160 SMLLDGGYMDNLPVSPMRSLGIRDIFAVDVGSVDDRTPMDYGDSVSGVWIFFNRWNPFSSRPNVPSMAEIQSRLTYVSSV 239

                        250       260       270
                 ....*....|....*....|....*....|
gi 19075586 1239 ATGEKVKSMPGCFYMRPPVKDFPTLEFGSF 1268
Cdd:cd07227  240 KTLEKVKATPGCHYMRPPVQDFDTLDFGKF 269
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 995-1297 2.76e-127

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: 394.85  E-value: 2.76e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586  995 SDFARLARRICGKAIALVLGGGGARGISQIGILYALEEAGIPFDIIGGTSIGAFNGGLYAWEADLVPMFGRAKKFCGRMA 1074
Cdd:cd07225    2 SDFSRLARVLTGNSIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKDMT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1075 NLWRFVLDVTYPQAAYTTGHEFNRGIWKTFGEIHIEDFWLPFYANTTNITHSRMDIHSSGYAWRYIRASMSLAGLVPPmL 1154
Cdd:cd07225   82 SIWKKLLDLTYPITSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPP-L 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1155 SD--SGDMLLDGGYMDNLTVSHMQSLGASSIFAIDVGSEDSREPMHYGDTVSGVWALISRWIPFIPKTSFPSLAEIQSRL 1232
Cdd:cd07225  161 CDpkDGHLLMDGGYINNLPADVARSMGAKTVIAIDVGSQDETDLTNYGDALSGWWLLWKRWNPLAEKVKVPNMAEIQSRL 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19075586 1233 TYVTSVATGEKVKSMPGCFYMRPPVKDFPTLEFGSFEKIYNVGYNYGKEYVEKLKTSHKLDDILS 1297
Cdd:cd07225  241 AYVSCVRQLEEVKSSDYCEYLRPPIDKYKTLDFGKFDEICEVGYQHGKTVFDGWKRSGVLEKMLQ 305
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 1009-1188 1.41e-59

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: 202.01  E-value: 1.41e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1009 IALVLGGGGARGISQIGILYALEEAGIPFDIIGGTSIGAFNGGLYAWEADLVPMFGRAKKFCGRMANLwrfvLDVTYPQA 1088
Cdd:cd07205    1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAGYSPEEIEERAKLRSTDLKAL----SDLTIPTA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1089 AYTTGHEFNRGIWKTFGEIHIEDFWLPFYANTTNITHSRMDIHSSGYAWRYIRASMSLAGLVPPMLSDsGDMLLDGGYMD 1168
Cdd:cd07205   77 GLLRGDKFLELLDEYFGDRDIEDLWIPFFIVATDLTSGKLVVFRSGSLVRAVRASMSIPGIFPPVKID-GQLLVDGGVLN 155

                        170       180
                 ....*....|....*....|
gi 19075586 1169 NLTVSHMQSLGASSIFAIDV 1188
Cdd:cd07205  156 NLPVDVLRELGADIIIAVDL 175
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 1006-1285 1.18e-47

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 171.24  E-value: 1.18e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1006 GKAIALVLGGGGARGISQIGILYALEEAGIPFDIIGGTSIGAFNGGLYA--WEAD-LVPMFGR--AKKFCGRMANLWRFV 1080
Cdd:COG1752    4 RPKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAagYSADeLEELWRSldRRDLFDLSLPRRLLR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1081 LDVTYPQAAYTTGHEFNRGIWKTFGEIHIEDFWLPFYANTTNITHSRMDIHSSGYAWRYIRASMSLAGLVPPMLSDsGDM 1160
Cdd:COG1752   84 LDLGLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPVEID-GRL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1161 LLDGGYMDNLTVSHMQSLGASSIFAIDVGSEDSRepmhygdtvsgvwalisrwipfipktsFPSLAEIQSRLTYVTSVAT 1240
Cdd:COG1752  163 YVDGGVVNNLPVDPARALGADRVIAVDLNPPLRK---------------------------LPSLLDILGRALEIMFNSI 215

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 19075586 1241 GEKVKSMPGC-FYMRPPVKDFPTLEFGSFEKIYNVGYNYGKEYVEK 1285
Cdd:COG1752  216 LRRELALEPAdILIEPDLSGISLLDFSRAEELIEAGYEAARRALDE 261
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 1011-1170 6.14e-37

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: 137.09  E-value: 6.14e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1011 LVLGGGGARGISQIGILYALEEAGIPFDIIGGTSIGAFNGGLYAWEADLVPMFGRAKkfcgRMANLWRFVLDVTYPQAAY 1090
Cdd:cd07198    1 LVLSGGGALGIYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASGRDLEEALLLLL----RLSREVRLRFDGAFPPTGR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1091 TTGHEFNRGIWKTFGEIHiEDFWLPFYANTTNITHSRMDIH---SSGYAWRYIRASMSLAGLVPPM-LSDSGDMLLDGGY 1166
Cdd:cd07198   77 LLGILRQPLLSALPDDAH-EDASGKLFISLTRLTDGENVLVsdtSKGELWSAVRASSSIPGYFGPVpLSFRGRRYGDGGL 155


                 ....
gi 19075586 1167 MDNL 1170
Cdd:cd07198  156 SNNL 159
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 1009-1188 1.60e-25

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: 104.66  E-value: 1.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1009 IALVLGGGGARGISQIGILYALEEAGIPFDIIGGTSIGAFNGGLYAweadlvpmFGRAKKFCGRMANL-WRFV---LDVT 1084
Cdd:cd07228    1 IGLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYA--------AGHLDALEEWVRSLsQRDVlrlLDLS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1085 YPQAAYTTGHEFNRGIWKTFGEIHIEDFWLPFYANTTNITHSRMDIHSSGYAWRYIRASMSLAGLVPPmLSDSGDMLLDG 1164
Cdd:cd07228   73 ASRSGLLKGEKVLEYLREIMGGVTIEELPIPFAAVATDLQTGKEVWFREGSLIDAIRASISIPGIFAP-VEHNGRLLVDG 151

                        170       180
                 ....*....|....*....|....
gi 19075586 1165 GYMDNLTVSHMQSLGASSIFAIDV 1188
Cdd:cd07228  152 GVVNPIPVSVARALGADIVIAVDL 175
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 1011-1172 4.42e-25

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


Pssm-ID: 396341  Cd Length: 190  Bit Score: 103.84  E-value: 4.42e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586   1011 LVLGGGGARGISQIGILYALEEAGIPFDIIGGTSIGAFNGGLYAWEADLVPMFGRAKKFC--------GRMANLWRFVLD 1082
Cdd:pfam01734    1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDlnlflsliRKRALSLLALLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586   1083 VTYPQAAYTTGHEFNRGIWKTFGEIHIEDFWLPF-----------------YANTTNITHSRMDIHSSGYAWRYIRASMS 1145
Cdd:pfam01734   81 GLIGEGGLFDGDALRELLRKLLGDLTLEELAARLslllvvalralltvistALGTRARILLPDDLDDDEDLADAVLASSA 160

                          170       180
                   ....*....|....*....|....*..
gi 19075586   1146 LAGLVPPMLSDsGDMLLDGGYMDNLTV 1172
Cdd:pfam01734  161 LPGVFPPVRLD-GELYVDGGLVDNVPV 186
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 1011-1232 2.05e-24

Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase similar to Z1214 protein of Escherichia coli. This family predominantly consists of bacterial patatin glycoproteins and some representatives from eukaryotes and archaea. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates.


Pssm-ID: 132848 [Multi-domain]  Cd Length: 215  Bit Score: 102.76  E-value: 2.05e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1011 LVLGGGGARGISQIGILYALEEAGIPFDIIGGTSIGAFNGGLYAWEADlvpmfGRAKkfcgRMANLWRfvlDVTYPQAAY 1090
Cdd:cd07209    1 LVLSGGGALGAYQAGVLKALAEAGIEPDIISGTSIGAINGALIAGGDP-----EAVE----RLEKLWR---ELSREDVFL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1091 tTGHEFNRGIWKTFGEIHIEDFWLPFYAntTNITHSRM---DIHSSGYAWRYIRASMSLAGLVPPMLSDsGDMLLDGGYM 1167
Cdd:cd07209   69 -RGLLDRALDFDTLRLLAILFAGLVIVA--VNVLTGEPvyfDDIPDGILPEHLLASAALPPFFPPVEID-GRYYWDGGVV 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19075586 1168 DNLTVSHMQSLGASSIFAIDVGsedsrePMHYGDTVSGVWALISRWIPFIPKTSFPSLAEIQSRL 1232
Cdd:cd07209  145 DNTPLSPAIDLGADEIIVVSLS------DKGRDDRKGTPPTTLIEILPRLFLRSGLDSERIRHNL 203
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 641-756 2.38e-20

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: 87.77  E-value: 2.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586  641 LISLVPSLLLKLDFAVGWIHLNPDQVVYEKNDPSDCVYVVLNGRLRSIEDERGSARTQVDYfneYGKGDSVGELEMLLNN 720
Cdd:cd00038    2 FSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGF---LGPGDLFGELALLGNG 78

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 19075586  721 RRSSTLFAIRDSELAKIPETLFNALSLSHPAVGLQL 756
Cdd:cd00038   79 PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
PRK10279 PRK10279
patatin-like phospholipase RssA;
1009-1187 4.52e-17

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 83.61  E-value: 4.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586  1009 IALVLGGGGARGISQIGILYALEEAGIPFDIIGGTSIGAFNGGLYAweadlvpmfgrakkfCGRMANLWRFVLDVTYPQA 1088
Cdd:PRK10279    6 IGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYA---------------CDRLSALEDWVTSFSYWDV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586  1089 AYTTGHEFNRG-------IWKTFGEI----HIEDFWLPFYANTTNITHSRM------DIHSSgyawryIRASMSLAGLVP 1151
Cdd:PRK10279   71 LRLMDLSWQRGgllrgerVFNQYREImpetEIENCSRRFGAVATNLSTGRElwftegDLHLA------IRASCSMPGLMA 144

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 19075586  1152 PmLSDSGDMLLDGGYMDNLTVSHMQSLGASSIFAID 1187
Cdd:PRK10279  145 P-VAHNGYWLVDGAVVNPVPVSLTRALGADIVIAVD 179
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 1009-1174 9.08e-15

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: 75.07  E-value: 9.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1009 IALVLGGGGARGISQIGILYALEEAGIPFDIIGGTSIGAFNGGLYAWEADLVPMFGRAKKFcgRMANLWRFVLDVTYPQA 1088
Cdd:cd07210    1 FALVLSSGFFGFYAHLGFLAALLEMGLEPSAISGTSAGALVGGLFASGISPDEMAELLLSL--ERKDFWMFWDPPLRGGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1089 AytTGHEFNRGIWKTFGEIHIEDFWLPFYANTTNITHSRMDIHSSGYAWRYIRASMSLAGLVPPMLSDsGDMLLDGGYMD 1168
Cdd:cd07210   79 L--SGDRFAALLREHLPPDRFEELRIPLAVSVVDLTSRETLLLSEGDLAEAVAASCAVPPLFQPVEIG-GRPFVDGGVAD 155


                 ....*.
gi 19075586 1169 NLTVSH 1174
Cdd:cd07210  156 RLPFDA 161
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
1009-1287 1.02e-14

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 75.97  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1009 IALVLGGGGARGISQIGILYALEEAGIPFDIIGGTSIGAFNGGLYaweadLVPMFGRAKKF------CGRMANLWRFV-- 1080
Cdd:COG4667    6 TALVLEGGGMRGIFTAGVLDALLEEGIPFDLVIGVSAGALNGASY-----LSRQPGRARRVitdyatDPRFFSLRNFLrg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1081 -----LDVTYpqaaYTTGHEFNRGIWKTFGEIHIEdfwlpFYANTTNIT------HSRMDIHssgYAW-RYIRASMSLAG 1148
Cdd:COG4667   81 gnlfdLDFLY----DEIPNELLPFDFETFKASPRE-----FYVVATNADtgeaeyFSKKDDD---YDLlDALRASSALPL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1149 LVPPMLSDsGDMLLDGGYMDNLTVSHMQSLGASSIFAIdvgsedsR-EPMHYGDTVSGVWALISRWIPfipktSFPSLAE 1227
Cdd:COG4667  149 LYPPVEID-GKRYLDGGVADSIPVREAIRDGADKIVVI-------LtRPRGYRKKPSKFKRLLRRLYR-----KYPKLVE 215

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19075586 1228 -IQSR-LTYVTSVatgEKVKSMPG---CFYMRPPVKdfptLEFGSFEK-------IYNVGYNYGKEYVEKLK 1287
Cdd:COG4667  216 aLLNRhERYNETL---EFIEQLEKegkIFVIRPPKP----LTVSRLERdpeklraLYELGYEDARKFLAELK 280
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 1011-1173 1.32e-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: 1.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1011 LVLGGGGARGISQIGILYALEEAGIPFDIIGGTSIGAFNGGLYA------------WEADLVPMFGrakKFCGRMANLWR 1078
Cdd:cd07207    2 LVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLAlgysaadikdilKETDFAKLLD---SPVGLLFLLPS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1079 FVLD-VTYPQAAYttgHEFNRGIWKTFGEIHIEDFWLPFYAN---------TTNITHSRMDIHSSGYA-----WRYIRAS 1143
Cdd:cd07207   79 LFKEgGLYKGDAL---EEWLRELLKEKTGNSFATSLLRDLDDdlgkdlkvvATDLTTGALVVFSAETTpdmpvAKAVRAS 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 19075586 1144 MSLAGLVPPMLSDSGDMLLDGGYMDNLTVS 1173
Cdd:cd07207  156 MSIPFVFKPVRLAKGDVYVDGGVLDNYPVW 185
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 659-769 1.80e-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: 1.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586  659 IHLNPDQVVYEKNDPSDCVYVVLNGRLR-SIEDERGsaRTQVDYFneYGKGDSVGELEMLLNNRRSSTLFAIRDSELAKI 737
Cdd:COG0664   19 RTLKKGEVLFREGDPADHLYFVLSGLVKlYRISEDG--REQILGF--LGPGDFFGELSLLGGEPSPATAEALEDSELLRI 94

                         90       100       110
                 ....*....|....*....|....*....|..
gi 19075586  738 PETLFNALSLSHPAVGLQLSKIIANRMNLLLN 769
Cdd:COG0664   95 PREDLEELLERNPELARALLRLLARRLRQLQE 126
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 659-749 7.61e-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: 68.40  E-value: 7.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586    659 IHLNPDQVVYEKNDPSDCVYVVLNGRLRsIEDERGSARTQVdyFNEYGKGDSVGELEMLLNNRRSSTLFAIRDSELAKIP 738
Cdd:pfam00027    2 RSYKAGEVIFREGDPADSLYIVLSGKVK-VYRTLEDGREQI--LAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIP 78

                           90
                   ....*....|.
gi 19075586    739 ETLFNALSLSH 749
Cdd:pfam00027   79 REDFLELLERD 89
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 522-638 4.00e-13

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: 66.97  E-value: 4.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586  522 KSTILEFAKEIEIIFYKKGTTIVRQGDHADGLYYIIDGFLDATcpskltfsTSYDTDLGMHSFMIKPGGIVNYQACVSNY 601
Cdd:cd00038    7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVY--------KLDEDGREQIVGFLGPGDLFGELALLGNG 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 19075586  602 RSFINVTARSDVLVGFLPRSCLERIIDQEPLISLTIA 638
Cdd:cd00038   79 PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 1011-1186 5.15e-13

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: 70.72  E-value: 5.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1011 LVLGGGGARGISQIGILYALEEAGI-PFDIIGGTSIGAFNGGLYaweadLVPMFGRA----------KKFCGrMANLWR- 1078
Cdd:cd07208    1 LVLEGGGMRGAYTAGVLDAFLEAGIrPFDLVIGVSAGALNAASY-----LSGQRGRAlrintkyatdPRYLG-LRSLLRt 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1079 ---FVLDVTYPQAAYtTGHEFNrgiWKTFGEIHIEdfwlpFYANTTNI-THSRM--DIHSSGYAW-RYIRASMSLAGLVP 1151
Cdd:cd07208   75 gnlFDLDFLYDELPD-GLDPFD---FEAFAASPAR-----FYVVATDAdTGEAVyfDKPDILDDLlDALRASSALPGLFP 145

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 19075586 1152 PMLSDsGDMLLDGGYMDNLTVSHMQSLGASSIFAI 1186
Cdd:cd07208  146 PVRID-GEPYVDGGLSDSIPVDKAIEDGADKIVVI 179
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 534-629 3.02e-10

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: 58.00  E-value: 3.02e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586    534 IIFYKKGTTIVRQGDHADGLYYIIDGFLDAtcpskltFSTSYDTDLGMHSFmIKPGGIVNYQACVSNYRSFINVTARSDV 613
Cdd:pfam00027    1 LRSYKAGEVIFREGDPADSLYIVLSGKVKV-------YRTLEDGREQILAV-LGPGDFFGELALLGGEPRSATVVALTDS 72

                           90
                   ....*....|....*.
gi 19075586    614 LVGFLPRSCLERIIDQ 629
Cdd:pfam00027   73 ELLVIPREDFLELLER 88
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 524-641 1.42e-09

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: 59.23  E-value: 1.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586  524 TILEFAKEIEIIFYKKGTTIVRQGDHADGLYYIIDGFLdatcpsKLTFSTSYDTDLGMHsfMIKPGGIVNYQACVSNYRS 603
Cdd:COG0664    8 ELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLV------KLYRISEDGREQILG--FLGPGDFFGELSLLGGEPS 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 19075586  604 FINVTARSDVLVGFLPRSCLERIIDQEPLISLTIAKRL 641
Cdd:COG0664   80 PATAEALEDSELLRIPREDLEELLERNPELARALLRLL 117
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 646-756 1.74e-08

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


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 53.94  E-value: 1.74e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586     646 PSLLLKLDFAVGWIHLNPDQVVYEKNDPSDCVYVVLNGRLR-SIEDERGsaRTQVdyFNEYGKGDSVGELEMLLNNRR-- 722
Cdd:smart00100    7 AEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEvYKVLEDG--EEQI--VGTLGPGDFFGELALLTNSRRaa 82

                            90       100       110
                    ....*....|....*....|....*....|....
gi 19075586     723 SSTLFAIRDSELAKIPETLFNALSLSHPAVGLQL 756
Cdd:smart00100   83 SAAAVALELATLLRIDFRDFLQLLPELPQLLLEL 116
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 1011-1179 2.32e-08

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: 54.73  E-value: 2.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1011 LVLGGGGARGISQIGILYALEEAGI--PFDIIGGTSIGAFNGGLyaweadLVPMFGrakKFCGRMANLWRFVLDvtypqa 1088
Cdd:cd01819    1 LSFSGGGFRGMYHAGVLSALAERGLldCVTYLAGTSGGAWVAAT------LYPPSS---SLDNKPRQSLEEALS------ 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1089 aYTTGHEFNRgiwktfgeihiedFWLPFYANTTnithsrmDIHSSGYAWRYIRASMSLA---GLVPP--------MLSDS 1157
Cdd:cd01819   66 -GKLWVSFTP-------------VTAGENVLVS-------RFVSKEELIRALFASGSWPsyfGLIPPaelytsksNLKEK 124

                        170       180
                 ....*....|....*....|..
gi 19075586 1158 GDMLLDGGYMDNLTVSHMQSLG 1179
Cdd:cd01819  125 GVRLVDGGVSNNLPAPVLLRPG 146
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 522-644 4.90e-06

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: 47.01  E-value: 4.90e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586     522 KSTILEFAKEIEIIFYKKGTTIVRQGDHADGLYYIIDGFLDATcpskltfsTSYDTDLGMHSFMIKPGGIVNYQACVSNY 601
Cdd:smart00100    7 AEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVY--------KVLEDGEEQIVGTLGPGDFFGELALLTNS 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 19075586     602 RSFINVTARSDVLVgFLPRSCLERIIDQEPLISLTIAKRLISL 644
Cdd:smart00100   79 RRAASAAAVALELA-TLLRIDFRDFLQLLPELPQLLLELLLEL 120
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 1011-1056 6.86e-05

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 46.44  E-value: 6.86e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 19075586 1011 LVLGGGGARGISQIGILYALEEA-GIP----FDIIGGTSIGAFNGGLYAWE 1056
Cdd:COG3621   10 LSLDGGGIRGLIPARILAELEERlGKPlaeyFDLIAGTSTGGIIALGLAAG 60
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
 1011-1048 7.47e-05

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


Pssm-ID: 132838 [Multi-domain]  Cd Length: 258  Bit Score: 45.79  E-value: 7.47e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 19075586 1011 LVLGGGGARGISQIGILYALEEA-GIP------FDIIGGTSIGAF 1048
Cdd:cd07199    2 LSLDGGGIRGIIPAEILAELEKRlGKPsriadlFDLIAGTSTGGI 46
Pat_PLPL cd07232
Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin ...
 968-1142 5.96e-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: 43.79  E-value: 5.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586  968 QNLHygfRKYIDWKHLHPVYQANRAQDSD-----FARLARRICGKAiALVLGGGGARGISQIGILYALEEAGIPFDIIGG 1042
Cdd:cd07232   26 KNLV---EEYIDEVEACLKYLRESSQLDLeekrrLFKRLSTNYGRT-ALCLSGGAAFAYYHFGVVKALLDADLLPNVISG 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075586 1043 TSIGAFNGGLYAWEAD------LVPMFGRAKKFCGR--MANLWRFVldvtypqaayTTGHEFN------RGIWKTFGEIH 1108
Cdd:cd07232  102 TSGGSLVAALLCTRTDeelkqlLVPELARKITACEPpwLVWIPRWL----------KTGARFDsvewarTCCWFTRGSMT 171

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 19075586 1109 IEDfwlpFYANT---TNITHSRMDIHSSGYAWRYIRA 1142
Cdd:cd07232  172 FEE----AYERTgriLNISVVPADPHSPTILLNYLTS 204
Pat_TGL4-5_like cd07230
Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in ...
 1001-1047 6.22e-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: 40.67  E-value: 6.22e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 19075586 1001 ARRICGKAiALVLGGGGARGISQIGILYALEEAGIPFDIIGGTSIGA 1047
Cdd:cd07230   67 TRKNFGRT-ALLLSGGGTFGMFHIGVLKALFEANLLPRIISGSSAGS 112
Pat_PNPLA9 cd07212
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ...
 1011-1048 7.96e-03

Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent phospholipase that catalyzes the hydrolysis of glycerophospholipids at the sn-2 position. PNPLA9 is also known as PLA2G6 (phospholipase A2 group VI) or iPLA2beta. PLA2G6 is stimulated by ATP and inhibited by bromoenol lactone (BEL). In humans, PNPLA9 in expressed ubiquitously and is involved in signal transduction, cell proliferation, and apoptotic cell death. Mutations in human PLA2G6 leads to infantile neuroaxonal dystrophy (INAD) and idiopathic neurodegeneration with brain iron accumulation (NBIA). This family includes PLA2G6 from Homo sapiens and Rattus norvegicus.


Pssm-ID: 132851 [Multi-domain]  Cd Length: 312  Bit Score: 40.01  E-value: 7.96e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 19075586 1011 LVLGGGGARGISQIGILYALE-EAGIP----FDIIGGTSIGAF 1048
Cdd:cd07212    2 LCLDGGGIRGLVLIQMLIAIEkALGRPirelFDWIAGTSTGGI 44
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH