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Conserved domains on  [gi|678007834|ref|XP_009079953|]
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PREDICTED: monoglyceride lipase [Acanthisitta chloris]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

alpha/beta hydrolase family protein may catalyze the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 30-297 1.41e-89

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member PHA02857:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 276  Bit Score: 268.29  E-value: 1.41e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834  30 IINADGQYLFCKYWKPAATPRALVFIAHGAGEHCGRYDDLAQKLTGLNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDSL 109
Cdd:PHA02857   5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834 110 QHIDLMKKEHPELPILILGHSMGGAISILTASERPSEFSGMLLISPLVVAspEVATPIKVFAAKVLNFVLPNLSLGSIDP 189
Cdd:PHA02857  85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLVNA--EAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834 190 SAISRNKKEIESYTSDPLVYHGGMKVSFVIQLMNAIARIERALPKLTLPILVLHG*****-----SYLLIDTVPSqDKTL 264
Cdd:PHA02857 163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEIsdvsgAYYFMQHANC-NREI 241

                        250       260       270
                 ....*....|....*....|....*....|...
gi 678007834 265 KVYEEAYHALHKELPEVSTSVFTEILTWIGQKV 297
Cdd:PHA02857 242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 30-297 1.41e-89

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 268.29  E-value: 1.41e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834  30 IINADGQYLFCKYWKPAATPRALVFIAHGAGEHCGRYDDLAQKLTGLNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDSL 109
Cdd:PHA02857   5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834 110 QHIDLMKKEHPELPILILGHSMGGAISILTASERPSEFSGMLLISPLVVAspEVATPIKVFAAKVLNFVLPNLSLGSIDP 189
Cdd:PHA02857  85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLVNA--EAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834 190 SAISRNKKEIESYTSDPLVYHGGMKVSFVIQLMNAIARIERALPKLTLPILVLHG*****-----SYLLIDTVPSqDKTL 264
Cdd:PHA02857 163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEIsdvsgAYYFMQHANC-NREI 241

                        250       260       270
                 ....*....|....*....|....*....|...
gi 678007834 265 KVYEEAYHALHKELPEVSTSVFTEILTWIGQKV 297
Cdd:PHA02857 242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 49-278 2.98e-84

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 253.29  E-value: 2.98e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834   49 PRALVFIAHGAGEHCGRYDDLAQKLTGLNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDSLQHIDLMKKEHPELPILILG 128
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834  129 HSMGGAISILTASERPSEFSGMLLISPLVVASPEVATPIKVFAAKVLNFVLPNLSL-GSIDPSAISRNKKEIESYTSDPL 207
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAADPL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 678007834  208 VyHGGMKVSFVIQLMNAIARIERALPKLTLPILVLHG**-----***SYLLIDTVPSQDKTLKVYEEAYHALHKEL 278
Cdd:pfam12146 163 V-HGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGAdrvvdPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
29-295 1.43e-40

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 140.91  E-value: 1.43e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834  29 HIINADGQYLFCKYWKPAATPRALVFIAHGAGEHCGRYDDLAQKLTGLNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDS 108
Cdd:COG2267    7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834 109 LQHIDLMKKEhPELPILILGHSMGGAISILTASERPSEFSGMLLISPLVVASPEVATPIKVFAAkvlnfvlpnlslgsid 188
Cdd:COG2267   87 RAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA---------------- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834 189 psaisrnkkeiesytsdplvyhggmkvsfviqlmnaiARIERALPKLTLPILVLHG*-----****SYLLIDTVPSqDKT 263
Cdd:COG2267  150 -------------------------------------LRLAEALARIDVPVLVLHGGadrvvPPEAARRLAARLSP-DVE 191

                        250       260       270
                 ....*....|....*....|....*....|..
gi 678007834 264 LKVYEEAYHALHKElpEVSTSVFTEILTWIGQ 295
Cdd:COG2267  192 LVLLPGARHELLNE--PAREEVLAAILAWLER 221
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 101-142 4.15e-04

Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238287 [Multi-domain]  Cd Length: 229  Bit Score: 40.92  E-value: 4.15e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 678007834 101 FHVFIRDSLQHIDLMKKEHPELPILILGHSMGGAISILTASE 142
Cdd:cd00519  107 YKSLYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 30-297 1.41e-89

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 268.29  E-value: 1.41e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834  30 IINADGQYLFCKYWKPAATPRALVFIAHGAGEHCGRYDDLAQKLTGLNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDSL 109
Cdd:PHA02857   5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834 110 QHIDLMKKEHPELPILILGHSMGGAISILTASERPSEFSGMLLISPLVVAspEVATPIKVFAAKVLNFVLPNLSLGSIDP 189
Cdd:PHA02857  85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLVNA--EAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834 190 SAISRNKKEIESYTSDPLVYHGGMKVSFVIQLMNAIARIERALPKLTLPILVLHG*****-----SYLLIDTVPSqDKTL 264
Cdd:PHA02857 163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEIsdvsgAYYFMQHANC-NREI 241

                        250       260       270
                 ....*....|....*....|....*....|...
gi 678007834 265 KVYEEAYHALHKELPEVSTSVFTEILTWIGQKV 297
Cdd:PHA02857 242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 49-278 2.98e-84

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 253.29  E-value: 2.98e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834   49 PRALVFIAHGAGEHCGRYDDLAQKLTGLNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDSLQHIDLMKKEHPELPILILG 128
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834  129 HSMGGAISILTASERPSEFSGMLLISPLVVASPEVATPIKVFAAKVLNFVLPNLSL-GSIDPSAISRNKKEIESYTSDPL 207
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAADPL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 678007834  208 VyHGGMKVSFVIQLMNAIARIERALPKLTLPILVLHG**-----***SYLLIDTVPSQDKTLKVYEEAYHALHKEL 278
Cdd:pfam12146 163 V-HGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGAdrvvdPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
29-295 1.43e-40

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 140.91  E-value: 1.43e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834  29 HIINADGQYLFCKYWKPAATPRALVFIAHGAGEHCGRYDDLAQKLTGLNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDS 108
Cdd:COG2267    7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834 109 LQHIDLMKKEhPELPILILGHSMGGAISILTASERPSEFSGMLLISPLVVASPEVATPIKVFAAkvlnfvlpnlslgsid 188
Cdd:COG2267   87 RAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA---------------- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834 189 psaisrnkkeiesytsdplvyhggmkvsfviqlmnaiARIERALPKLTLPILVLHG*-----****SYLLIDTVPSqDKT 263
Cdd:COG2267  150 -------------------------------------LRLAEALARIDVPVLVLHGGadrvvPPEAARRLAARLSP-DVE 191

                        250       260       270
                 ....*....|....*....|....*....|..
gi 678007834 264 LKVYEEAYHALHKElpEVSTSVFTEILTWIGQ 295
Cdd:COG2267  192 LVLLPGARHELLNE--PAREEVLAAILAWLER 221
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 32-298 1.40e-37

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 136.42  E-value: 1.40e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834  32 NADGQYLFCKYWKP-AATPRALVFIAHGAGEHCGRY-DDLAQKLTGLNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDSL 109
Cdd:PLN02385  68 NSRGVEIFSKSWLPeNSRPKAAVCFCHGYGDTCTFFfEGIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLVDDVI 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834 110 QHIDLMK--KEHPELPILILGHSMGGAISILTASERPSEFSGMLLISPLVVASPEVATP-----IKVFAAKVL--NFVLP 180
Cdd:PLN02385 148 EHYSKIKgnPEFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMCKIADDVVPPplvlqILILLANLLpkAKLVP 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834 181 NLSLGSI---DPSaisrnKKEIESYtsDPLVYHGGMKVSFVIQLMNAIARIERALPKLTLPILVLHG**-----***SYL 252
Cdd:PLN02385 228 QKDLAELafrDLK-----KRKMAEY--NVIAYKDKPRLRTAVELLRTTQEIEMQLEEVSLPLLILHGEAdkvtdPSVSKF 300

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 678007834 253 LIDTVPSQDKTLKVYEEAYHA-LHKELPEVSTSVFTEILTWIGQKVS 298
Cdd:PLN02385 301 LYEKASSSDKKLKLYEDAYHSiLEGEPDEMIFQVLDDIISWLDSHST 347
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 33-293 2.15e-34

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 128.86  E-value: 2.15e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834  33 ADGQYLFCKYWKPAATP-RALVFIAHGAGEHCGRYDDLAQKLTGLNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDSLQH 111
Cdd:PLN02652 118 ARRNALFCRSWAPAAGEmRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAF 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834 112 IDLMKKEHPELPILILGHSMGGAIsILTASERPS---EFSGMLLISPLVVASPevATPIKVFAAKVLNFVLPNLSLGSID 188
Cdd:PLN02652 198 LEKIRSENPGVPCFLFGHSTGGAV-VLKAASYPSiedKLEGIVLTSPALRVKP--AHPIVGAVAPIFSLVAPRFQFKGAN 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834 189 PSAI--SRNKKEIESYTSDPLVYHGGMKVSFVIQLMNAIARIERALPKLTLPILVLHG**-----***SYLLIDTVPSQD 261
Cdd:PLN02652 275 KRGIpvSRDPAALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTAdrvtdPLASQDLYNEAASRH 354

                        250       260       270
                 ....*....|....*....|....*....|..
gi 678007834 262 KTLKVYEEAYHALHKElPEvSTSVFTEILTWI 293
Cdd:PLN02652 355 KDIKLYDGFLHDLLFE-PE-REEVGRDIIDWM 384
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 35-305 1.88e-31

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 119.88  E-value: 1.88e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834  35 GQYLFCKYWKPAAT--PRALVFIAHGAGEHCG-RYDDLAQKLTGLNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDSLQH 111
Cdd:PLN02298  42 GLSLFTRSWLPSSSspPRALIFMVHGYGNDISwTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSF 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834 112 IDLMKK--EHPELPILILGHSMGGAISILTASERPSEFSGMLLISPLVVASPEVATPIKVfaAKVLNFV---LPNLSL-- 184
Cdd:PLN02298 122 FNSVKQreEFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCKISDKIRPPWPI--PQILTFVarfLPTLAIvp 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834 185 --GSIDPSAISRNKKEIESytSDPLVYHGGMKVSFVIQLMNAIARIERALPKLTLPILVLHG****-----*SYLLIDTV 257
Cdd:PLN02298 200 taDLLEKSVKVPAKKIIAK--RNPMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVvtdpdVSRALYEEA 277

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 678007834 258 PSQDKTLKVYEEAYHA-LHKELPEVSTSVFTEILTWIGQKVSAAGETSH 305
Cdd:PLN02298 278 KSEDKTIKIYDGMMHSlLFGEPDENIEIVRRDILSWLNERCTGKATPSE 326
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
46-298 2.59e-21

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 90.39  E-value: 2.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834  46 AATPRALVFIaHGAGehCGRYD--DLAQKLTGLNLFVFAHDHVGHGQSEGDrMVVSDFHVFIRDSLQHIDLMKKEHPElp 123
Cdd:COG1647   12 EGGRKGVLLL-HGFT--GSPAEmrPLAEALAKAGYTVYAPRLPGHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYDK-- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834 124 ILILGHSMGGAISILTASERPsEFSGMLLISPlvvaspevatpikvfAAKVLNFVLPNLSLGSIDPSAISRNKKEIESYT 203
Cdd:COG1647   86 VIVIGLSMGGLLALLLAARYP-DVAGLVLLSP---------------ALKIDDPSAPLLPLLKYLARSLRGIGSDIEDPE 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834 204 SDPLVYHgGMKVSFVIQLMNAIARIERALPKLTLPILVLHG**-----***SYLLIDTVPSQDKTLKVYEEAYHALH--K 276
Cdd:COG1647  150 VAEYAYD-RTPLRALAELQRLIREVRRDLPKITAPTLIIQSRKdevvpPESARYIYERLGSPDKELVWLEDSGHVITldK 228

                        250       260
                 ....*....|....*....|..
gi 678007834 277 ELPEvstsVFTEILTWIGQKVS 298
Cdd:COG1647  229 DREE----VAEEILDFLERLAA 246
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 23-273 6.07e-15

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 73.03  E-value: 6.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834  23 PYKDLPH----IINADGQYLFCKYWKPA--ATPRALVFIAHGAGEHCGRYDDLAQKLTGLNLFVFAHDHVGHGQSEGD-R 95
Cdd:COG1073    4 PSDKVNKedvtFKSRDGIKLAGDLYLPAgaSKKYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEpR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834  96 MVVS----DFHVFIrDSLQHidlmKKEHPELPILILGHSMGGAISILTASERPsEFSGMLLISPLVVASPEVATPIKVFA 171
Cdd:COG1073   84 EEGSperrDARAAV-DYLRT----LPGVDPERIGLLGISLGGGYALNAAATDP-RVKAVILDSPFTSLEDLAAQRAKEAR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834 172 AKVLNFV--LPNLSLGSidpsaisrnkkeiesytsdplvyhggmkvsfviqLMNAIARIERALPKLTLPILVLHG**--- 246
Cdd:COG1073  158 GAYLPGVpyLPNVRLAS----------------------------------LLNDEFDPLAKIEKISRPLLFIHGEKdea 203

                        250       260
                 ....*....|....*....|....*....
gi 678007834 247 --***SYLLIDTVPsQDKTLKVYEEAYHA 273
Cdd:COG1073  204 vpFYMSEDLYEAAA-EPKELLIVPGAGHV 231
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
29-295 1.27e-12

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 66.19  E-value: 1.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834  29 HIINADGQYLFCKYWKPAAT-PRALVFIAHGAGEH-CGRYDDLAQKLTGLNLFVFAHDHVGHGQSEGDRmvvsdFHVFIR 106
Cdd:COG1506    1 TFKSADGTTLPGWLYLPADGkKYPVVVYVHGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGESAGDW-----GGDEVD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834 107 DSLQHIDLMKkEHPELP---ILILGHSMGGAISILTASERPSEFSGMLLISPLVvaspevatpikvfaakvlnfvlpnlS 183
Cdd:COG1506   76 DVLAAIDYLA-ARPYVDpdrIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVS-------------------------D 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834 184 LGSIDPSAISRNKKEIESYTSDPLVYhggmkvsfviQLMNAIARIEralpKLTLPILVLHG**-----***SYLLIDTVP 258
Cdd:COG1506  130 LRSYYGTTREYTERLMGGPWEDPEAY----------AARSPLAYAD----KLKTPLLLIHGEAddrvpPEQAERLYEALK 195

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 678007834 259 SQ--DKTLKVYEEAYHALHKelpEVSTSVFTEILTWIGQ 295
Cdd:COG1506  196 KAgkPVELLVYPGEGHGFSG---AGAPDYLERILDFLDR 231
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 28-295 6.67e-12

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 63.87  E-value: 6.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834  28 PHIINADGQYLFCKYWKPAATPraLVFIaHGAGEHCGRYDDLAQKLTGlNLFVFAHDHVGHGQSEGDRMVVSdFHVFIRD 107
Cdd:COG0596    4 PRFVTVDGVRLHYREAGPDGPP--VVLL-HGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAGGYT-LDDLADD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834 108 SLQHIDLMKKEhpelPILILGHSMGGAISILTASERPSEFSGMLLISPLVVAspevatpikvfaakvlnfVLPNLSLGSI 187
Cdd:COG0596   79 LAALLDALGLE----RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAA------------------LAEPLRRPGL 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834 188 DPSAISRnkkeiesytsdplvyhggmkvsfviqLMNAIAR--IERALPKLTLPILVLHG-----*****SYLLIDTVPsq 260
Cdd:COG0596  137 APEALAA--------------------------LLRALARtdLRERLARITVPTLVIWGekdpiVPPALARRLAELLP-- 188

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 678007834 261 DKTLKVYEEAYHALHKELPEVstsVFTEILTWIGQ 295
Cdd:COG0596  189 NAELVVLPGAGHFPPLEQPEA---FAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 52-277 9.91e-07

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 49.04  E-value: 9.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834   52 LVFIAHGAGEHCGRYDDLAQKLTGLNLFVFAHDHVGHGQSEGdRMVVSDFHVFirDSLQHIDLMKKEHPELPILILGHSM 131
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSR-PKAQDDYRTD--DLAEDLEYILEALGLEKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834  132 GGAISILTASERPSEFSGMLLISPLVVASPEVATPIKVFAAK-------VLNFVLPNLSLGSIDPSAISR---------N 195
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFpgffdgfVADFAPNPLGRLVAKLLALLLlrlrllkalP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834  196 KKEIESYTSDPlvYHGGMKVSFVIQLMNAIARIERA--LPKLTLPILVLHG*-----****SYLLIDTVPSqdKTLKVYE 268
Cdd:pfam00561 159 LLNKRFPSGDY--ALAKSLVTGALLFIETWSTELRAkfLGRLDEPTLIIWGDqdplvPPQALEKLAQLFPN--ARLVVIP 234


                  ....*....
gi 678007834  269 EAYHALHKE 277
Cdd:pfam00561 235 DAGHFAFLE 243
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
29-167 1.13e-06

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 48.42  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834  29 HIINADGQYLFCKYWKPA-ATPRALVFIAHGAGEHCGRYDDLAQKLTGLNLFVFAHDHVGHGQSEGD------RMVVSDF 101
Cdd:COG0412    7 TIPTPDGVTLPGYLARPAgGGPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRGGPGDDpdearaLMGALDP 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 678007834 102 HVFIRDSLQHIDLMKKeHPEL---PILILGHSMGGAISILTASERPSE-----FSGMLLISPLVVASPEVATPI 167
Cdd:COG0412   87 ELLAADLRAALDWLKA-QPEVdagRVGVVGFCFGGGLALLAAARGPDLaaavsFYGGLPADDLLDLAARIKAPV 159
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 52-202 1.76e-05

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 44.77  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834   52 LVFIaHGAGEHCGRYDDLAQKltglNLFVFAHDHVGHGQSEGDRMVVSDFHvfirdslQHIDLMKKEHPELPILILGHSM 131
Cdd:pfam12697   1 VVLV-HGAGLSAAPLAALLAA----GVAVLAPDLPGHGSSSPPPLDLADLA-------DLAALLDELGAARPVVLVGHSL 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 678007834  132 GGAISILTAserPSEFSGMLLISPLVVASPEVATPIKVFAAKVLNFVLPNLSLGSIDPSAISRNKKEIESY 202
Cdd:pfam12697  69 GGAVALAAA---AAALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEW 136
PLN02578 PLN02578
hydrolase
 58-293 2.19e-04

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 42.52  E-value: 2.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834  58 GAGEHCGRYD--DLAQKLTglnlfVFAHDHVGHGQS-----EGDRMVVSDfhvfirdslQHIDLMKKEHPElPILILGHS 130
Cdd:PLN02578  96 GASAFHWRYNipELAKKYK-----VYALDLLGFGWSdkaliEYDAMVWRD---------QVADFVKEVVKE-PAVLVGNS 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834 131 MGGAISILTASERPSEFSGMLLISP-------------LVVASPEVAT-----PIK-VFAAKVLNFVLPNLSlgsiDPSA 191
Cdd:PLN02578 161 LGGFTALSTAVGYPELVAGVALLNSagqfgsesrekeeAIVVEETVLTrfvvkPLKeWFQRVVLGFLFWQAK----QPSR 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834 192 IS-------RNKKEIESY--------TSDP---LVYHGGMKvSFVIQLMNAIarIERALPKLTLPILVLHG*****sylL 253
Cdd:PLN02578 237 IEsvlksvyKDKSNVDDYlvesitepAADPnagEVYYRLMS-RFLFNQSRYT--LDSLLSKLSCPLLLLWGD-------L 306

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 678007834 254 IDTVPS----------QDKTLkVYEEAYHALHKELPEvstSVFTEILTWI 293
Cdd:PLN02578 307 DPWVGPakaekikafyPDTTL-VNLQAGHCPHDEVPE---QVNKALLEWL 352
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 101-142 4.15e-04

Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238287 [Multi-domain]  Cd Length: 229  Bit Score: 40.92  E-value: 4.15e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 678007834 101 FHVFIRDSLQHIDLMKKEHPELPILILGHSMGGAISILTASE 142
Cdd:cd00519  107 YKSLYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 51-155 4.17e-04

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 41.47  E-value: 4.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834  51 ALVFIaHG-AGEH---CGRYDDLAQKLTglnlfVFAHDHVGHGQSeGDRMVVSDFHvFIRDSLqhIDLMKKEHPELPILI 126
Cdd:PRK14875 133 PVVLI-HGfGGDLnnwLFNHAALAAGRP-----VIALDLPGHGAS-SKAVGAGSLD-ELAAAV--LAFLDALGIERAHLV 202

                         90       100
                 ....*....|....*....|....*....
gi 678007834 127 lGHSMGGAISILTASERPSEFSGMLLISP 155
Cdd:PRK14875 203 -GHSMGGAVALRLAARAPQRVASLTLIAP 230
Lipase_3 pfam01764
Lipase (class 3);
116-171 2.28e-03

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 37.63  E-value: 2.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 678007834  116 KKEHPELPILILGHSMGGAISILTASErpsefsgmllispLVVASPEVATPIKVFA 171
Cdd:pfam01764  57 LEKYPDYSIVVTGHSLGGALASLAALD-------------LVENGLRLSSRVTVVT 99
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
126-155 3.77e-03

Predicted hydrolase of the alpha/beta superfamily [General function prediction only];


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 38.04  E-value: 3.77e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 678007834 126 ILGHSMGGAISILTASERPSEFSGMLLISP 155
Cdd:COG2819  134 LIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 104-161 4.75e-03

Putative esterase; This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family.


Pssm-ID: 395613 [Multi-domain]  Cd Length: 246  Bit Score: 37.83  E-value: 4.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834  104 FIRDSLqhIDLMKKEHPELPI--LILGHSMGGAISILTASERPSEFSGMLLISPLVVASP 161
Cdd:pfam00756  92 FLTQEL--PPLLDANFPTAPDgrALAGQSMGGLGALYLALKYPDLFGSVSSFSPILNPSN 149
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 101-142 5.09e-03

Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 36.71  E-value: 5.09e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 678007834 101 FHVFIRDSLQHIDLMKKEHPELPILILGHSMGGAISILTASE 142
Cdd:cd00741    7 ARSLANLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLD 48
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
45-145 6.38e-03

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 37.78  E-value: 6.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834  45 PAATPRALVFIAHGAGEHCGRYDDLAQKLTGLNLFVFAHDHVGH-----GQSEGDRMVVSDFHVFI---RDSLQHIDLMK 116
Cdd:COG4188   57 PAGGPFPLVVLSHGLGGSREGYAYLAEHLASHGYVVAAPDHPGSnaadlSAALDGLADALDPEELWerpLDLSFVLDQLL 136

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 678007834 117 KEHPELPIL----------ILGHSMGGAISILTASERPS 145
Cdd:COG4188  137 ALNKSDPPLagrldldrigVIGHSLGGYTALALAGARLD 175
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 53-142 9.93e-03

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 36.60  E-value: 9.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678007834   53 VFIAHGAG--EHCgrYDDLAQKLTGLNLFVFAHDHvghGQSEGDRMVVSdfhvfiRDSL--QHIDLMKKEHPELPILILG 128
Cdd:pfam00975   3 LFCFPPAGgsASS--FRSLARRLPPPAEVLAVQYP---GRGRGEPPLNS------IEALadEYAEALRQIQPEGPYALFG 71

                          90
                  ....*....|....
gi 678007834  129 HSMGGAISILTASE 142
Cdd:pfam00975  72 HSMGGMLAFEVARR 85
 
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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