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Conserved domains on  [gi|1622922923|ref|XP_028701517|]
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protein ABHD11 isoform X2 [Macaca mulatta]

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 1001822)

alpha/beta fold hydrolase catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

CATH:  3.40.50.1820
Gene Ontology:  GO:0016787
PubMed:  12369917|15381402|1409539
SCOP:  3000102

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10673 super family cl30399
esterase;
23-201 4.55e-30

esterase;


The actual alignment was detected with superfamily member PRK10673:

Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 110.98  E-value: 4.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923  23 VVVGHSMGGRTAMLLALQRPELVERLIAVDISPVEGTGSSHFPAYvAAMRTVNIPDGLPRSHARKLADEQLssvvQNLAV 102
Cdd:PRK10673   84 TFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHVRRHDEIF-AAINAVSEAGATTRQQAAAIMRQHL----NEEGV 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923 103 RQYLLTNLVEVDgrlaWRLNLDALAQHLDKLLTFpQRQESYLGPTLFLLGGNSQFVHPSHHPEIIRLFPRAQIQTVPNAG 182
Cdd:PRK10673  159 IQFLLKSFVDGE----WRFNVPVLWDQYPHIVGW-EKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAG 233

                         170
                  ....*....|....*....
gi 1622922923 183 HWIHAERPQDFIDAIRGFL 201
Cdd:PRK10673  234 HWVHAEKPDAVLRAIRRYL 252
 
Name Accession Description Interval E-value
PRK10673 PRK10673
esterase;
23-201 4.55e-30

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 110.98  E-value: 4.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923  23 VVVGHSMGGRTAMLLALQRPELVERLIAVDISPVEGTGSSHFPAYvAAMRTVNIPDGLPRSHARKLADEQLssvvQNLAV 102
Cdd:PRK10673   84 TFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHVRRHDEIF-AAINAVSEAGATTRQQAAAIMRQHL----NEEGV 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923 103 RQYLLTNLVEVDgrlaWRLNLDALAQHLDKLLTFpQRQESYLGPTLFLLGGNSQFVHPSHHPEIIRLFPRAQIQTVPNAG 182
Cdd:PRK10673  159 IQFLLKSFVDGE----WRFNVPVLWDQYPHIVGW-EKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAG 233

                         170
                  ....*....|....*....
gi 1622922923 183 HWIHAERPQDFIDAIRGFL 201
Cdd:PRK10673  234 HWVHAEKPDAVLRAIRRYL 252
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 21-201 1.17e-21

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: 88.13  E-value: 1.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923  21 PCVVVGHSMGGRTAMLLALQRPELVERLIAVDispvegtgsshfPAYVAAMRTVNIPDGLPRSHARKLadeqlssvvqnl 100
Cdd:COG0596    90 RVVLVGHSMGGMVALELAARHPERVAGLVLVD------------EVLAALAEPLRRPGLAPEALAALL------------ 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923 101 avrqylltnlvevdgRLAWRLNLDALAQHLDKlltfpqrqesylgPTLFLLGGNSQFVHPSHHPEIIRLFPRAQIQTVPN 180
Cdd:COG0596   146 ---------------RALARTDLRERLARITV-------------PTLVIWGEKDPIVPPALARRLAELLPNAELVVLPG 197

                         170       180
                  ....*....|....*....|.
gi 1622922923 181 AGHWIHAERPQDFIDAIRGFL 201
Cdd:COG0596   198 AGHFPPLEQPEAFAAALRDFL 218
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 23-190 2.12e-14

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: 69.46  E-value: 2.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923  23 VVVGHSMGGRTAMLLALQRPELVERLIAVDI---SPVEGTGSSHFPAYVAAMRTVNIPDGLPRSHARKLADEQLSSVVQN 99
Cdd:pfam00561  72 NLVGHSMGGLIALAYAAKYPDRVKALVLLGAldpPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRL 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923 100 LAVrqYLLTNLVEVDGRLAWRLNLDALAQHLDKLLTFPQRQE-----SYLGPTLFLLGGNSQFVHPSHHPEIIRLFPRAQ 174
Cdd:pfam00561 152 RLL--KALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRakflgRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNAR 229

                         170
                  ....*....|....*.
gi 1622922923 175 IQTVPNAGHWIHAERP 190
Cdd:pfam00561 230 LVVIPDAGHFAFLEGP 245
protocat_pcaD TIGR02427
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
 23-201 1.92e-09

3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]


Pssm-ID: 131480 [Multi-domain]  Cd Length: 251  Bit Score: 55.44  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923  23 VVVGHSMGGRTAMLLALQRPELVERLIAVDISPVEGTGSSHFP--AYVAAMRTVNIPDG-LPR--SHARKLADEQLSSVV 97
Cdd:TIGR02427  82 VFCGLSLGGLIAQGLAARRPDRVRALVLSNTAAKIGTPESWNAriAAVRAEGLAALADAvLERwfTPGFREAHPARLDLY 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923  98 QNLAVRQylltnlvEVDGRLAwrlNLDALAQhldklLTFPQRQESYLGPTLFLLGGNSQFVHPSHHPEIIRLFPRAQIQT 177
Cdd:TIGR02427 162 RNMLVRQ-------PPDGYAG---CCAAIRD-----ADFRDRLGAIAVPTLCIAGDQDGSTPPELVREIADLVPGARFAE 226

                         170       180
                  ....*....|....*....|....
gi 1622922923 178 VPNAGHWIHAERPQDFIDAIRGFL 201
Cdd:TIGR02427 227 IRGAGHIPCVEQPEAFNAALRDFL 250
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 21-51 3.23e-05

Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.


Pssm-ID: 214007  Cd Length: 309  Bit Score: 43.39  E-value: 3.23e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1622922923  21 PCVVVGHSMGGRTAMLLALQRPELVERLIAV 51
Cdd:cd12808   189 PCIVVAHSQGGGFAFEAARARPDLVRAVVAL 219
 
Name Accession Description Interval E-value
PRK10673 PRK10673
esterase;
23-201 4.55e-30

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 110.98  E-value: 4.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923  23 VVVGHSMGGRTAMLLALQRPELVERLIAVDISPVEGTGSSHFPAYvAAMRTVNIPDGLPRSHARKLADEQLssvvQNLAV 102
Cdd:PRK10673   84 TFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHVRRHDEIF-AAINAVSEAGATTRQQAAAIMRQHL----NEEGV 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923 103 RQYLLTNLVEVDgrlaWRLNLDALAQHLDKLLTFpQRQESYLGPTLFLLGGNSQFVHPSHHPEIIRLFPRAQIQTVPNAG 182
Cdd:PRK10673  159 IQFLLKSFVDGE----WRFNVPVLWDQYPHIVGW-EKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAG 233

                         170
                  ....*....|....*....
gi 1622922923 183 HWIHAERPQDFIDAIRGFL 201
Cdd:PRK10673  234 HWVHAEKPDAVLRAIRRYL 252
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 21-201 1.17e-21

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: 88.13  E-value: 1.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923  21 PCVVVGHSMGGRTAMLLALQRPELVERLIAVDispvegtgsshfPAYVAAMRTVNIPDGLPRSHARKLadeqlssvvqnl 100
Cdd:COG0596    90 RVVLVGHSMGGMVALELAARHPERVAGLVLVD------------EVLAALAEPLRRPGLAPEALAALL------------ 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923 101 avrqylltnlvevdgRLAWRLNLDALAQHLDKlltfpqrqesylgPTLFLLGGNSQFVHPSHHPEIIRLFPRAQIQTVPN 180
Cdd:COG0596   146 ---------------RALARTDLRERLARITV-------------PTLVIWGEKDPIVPPALARRLAELLPNAELVVLPG 197

                         170       180
                  ....*....|....*....|.
gi 1622922923 181 AGHWIHAERPQDFIDAIRGFL 201
Cdd:COG0596   198 AGHFPPLEQPEAFAAALRDFL 218
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 23-190 2.12e-14

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: 69.46  E-value: 2.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923  23 VVVGHSMGGRTAMLLALQRPELVERLIAVDI---SPVEGTGSSHFPAYVAAMRTVNIPDGLPRSHARKLADEQLSSVVQN 99
Cdd:pfam00561  72 NLVGHSMGGLIALAYAAKYPDRVKALVLLGAldpPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRL 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923 100 LAVrqYLLTNLVEVDGRLAWRLNLDALAQHLDKLLTFPQRQE-----SYLGPTLFLLGGNSQFVHPSHHPEIIRLFPRAQ 174
Cdd:pfam00561 152 RLL--KALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRakflgRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNAR 229

                         170
                  ....*....|....*.
gi 1622922923 175 IQTVPNAGHWIHAERP 190
Cdd:pfam00561 230 LVVIPDAGHFAFLEGP 245
protocat_pcaD TIGR02427
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
 23-201 1.92e-09

3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]


Pssm-ID: 131480 [Multi-domain]  Cd Length: 251  Bit Score: 55.44  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923  23 VVVGHSMGGRTAMLLALQRPELVERLIAVDISPVEGTGSSHFP--AYVAAMRTVNIPDG-LPR--SHARKLADEQLSSVV 97
Cdd:TIGR02427  82 VFCGLSLGGLIAQGLAARRPDRVRALVLSNTAAKIGTPESWNAriAAVRAEGLAALADAvLERwfTPGFREAHPARLDLY 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923  98 QNLAVRQylltnlvEVDGRLAwrlNLDALAQhldklLTFPQRQESYLGPTLFLLGGNSQFVHPSHHPEIIRLFPRAQIQT 177
Cdd:TIGR02427 162 RNMLVRQ-------PPDGYAG---CCAAIRD-----ADFRDRLGAIAVPTLCIAGDQDGSTPPELVREIADLVPGARFAE 226

                         170       180
                  ....*....|....*....|....
gi 1622922923 178 VPNAGHWIHAERPQDFIDAIRGFL 201
Cdd:TIGR02427 227 IRGAGHIPCVEQPEAFNAALRDFL 250
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
21-201 2.38e-09

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 55.01  E-value: 2.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923  21 PCVVVGHSMGGRTAMLLALQRPELVERLIAVDispvegtgsshfPAYVAamrtvnipDGLPRSHARKLADEQLSSVVQNL 100
Cdd:COG2267   100 PVVLLGHSMGGLIALLYAARYPDRVAGLVLLA------------PAYRA--------DPLLGPSARWLRALRLAEALARI 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923 101 AVrqylltnlvevdgrlawrlnldalaqhldklltfpqrqesylgPTLFLLGGNSQFVHPSHHPEII-RLFPRAQIQTVP 179
Cdd:COG2267   160 DV-------------------------------------------PVLVLHGGADRVVPPEAARRLAaRLSPDVELVLLP 196

                         170       180
                  ....*....|....*....|...
gi 1622922923 180 NAGHWIHAERPQD-FIDAIRGFL 201
Cdd:COG2267   197 GARHELLNEPAREeVLAAILAWL 219
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 21-196 6.44e-07

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 47.85  E-value: 6.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923  21 PCVVVGHSMGGRTAMLLALqrpelVERLIAVDISPVeGTGSSHFPAYVAAMRTVNIPDGLPRSHARKLADEQLSSvvqnl 100
Cdd:pfam12697  60 PVVLVGHSLGGAVALAAAA-----AALVVGVLVAPL-AAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLD----- 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923 101 avrqylltnlvEVDGRLAWRLNLDALAQHLDKLLTFPQRQESYLGPTLFLLGGNSQFVHPsHHPEIIRLFPRAQIQTVPN 180
Cdd:pfam12697 129 -----------DLPADAEWAAALARLAALLAALALLPLAAWRDLPVPVLVLAEEDRLVPE-LAQRLLAALAGARLVVLPG 196

                         170
                  ....*....|....*.
gi 1622922923 181 AGHWIHaERPQDFIDA 196
Cdd:pfam12697 197 AGHLPL-DDPEEVAEA 211
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 21-201 7.21e-07

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 48.40  E-value: 7.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923  21 PCVVVGHSMGGRTAMLLALQRPELVERLIAvdISPVeGTGSSHFPAYVaamrtvnipDGLPRSHARKladeQLSSVVQNL 100
Cdd:PRK14875  198 RAHLVGHSMGGAVALRLAARAPQRVASLTL--IAPA-GLGPEINGDYI---------DGFVAAESRR----ELKPVLELL 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923 101 AVRQYLLTNLVeVDGRLAW-RLN-----LDALAQHLdklltFPQ-RQESYLG--------PTLFLLGGNSQFVhPSHHPE 165
Cdd:PRK14875  262 FADPALVTRQM-VEDLLKYkRLDgvddaLRALADAL-----FAGgRQRVDLRdrlaslaiPVLVIWGEQDRII-PAAHAQ 334

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622922923 166 iiRLFPRAQIQTVPNAGHWIHAERPQDFIDAIRGFL 201
Cdd:PRK14875  335 --GLPDGVAVHVLPGAGHMPQMEAAADVNRLLAEFL 368
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 20-189 1.33e-05

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: 44.51  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923  20 VPCVVVGHSMGGRTAMLLALQRPELVERLIAvdispvegtgsshfpayVAAMrtVNIPDGLPRSHARKLAdEQLSSVVQN 99
Cdd:pfam12146  76 LPLFLLGHSMGGLIAALYALRYPDKVDGLIL-----------------SAPA--LKIKPYLAPPILKLLA-KLLGKLFPR 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923 100 LAVRQYLLTNLVE--------------VDGRLAWRLNLDALaQHLDKLLtfpQRQESYLGPTLFLLGGNSQFVHPSHHPE 165
Cdd:pfam12146 136 LRVPNNLLPDSLSrdpevvaayaadplVHGGISARTLYELL-DAGERLL---RRAAAITVPLLLLHGGADRVVDPAGSRE 211

                         170       180
                  ....*....|....*....|....*.
gi 1622922923 166 IIRLFPRA--QIQTVPNAGHWIHAER 189
Cdd:pfam12146 212 FYERAGSTdkTLKLYPGLYHELLNEP 237
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 21-51 3.23e-05

Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.


Pssm-ID: 214007  Cd Length: 309  Bit Score: 43.39  E-value: 3.23e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1622922923  21 PCVVVGHSMGGRTAMLLALQRPELVERLIAV 51
Cdd:cd12808   189 PCIVVAHSQGGGFAFEAARARPDLVRAVVAL 219
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
23-201 9.24e-04

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 38.77  E-value: 9.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923  23 VVVGHSMGGRTAMLLALQRPElVERLIAvdISPvegtgsshfPAYVAAMRTVNIPDGLP-RSHARKLADEQLSSVVQNLA 101
Cdd:COG1647    87 IVIGLSMGGLLALLLAARYPD-VAGLVL--LSP---------ALKIDDPSAPLLPLLKYlARSLRGIGSDIEDPEVAEYA 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922923 102 VRQYLLTNLVEVdgrlaWRLnLDALAQHLDKLltfpqRQesylgPTLFLLGGNSQFVHPSHHPEIIRLF--PRAQIQTVP 179
Cdd:COG1647   155 YDRTPLRALAEL-----QRL-IREVRRDLPKI-----TA-----PTLIIQSRKDEVVPPESARYIYERLgsPDKELVWLE 218

                         170       180
                  ....*....|....*....|...
gi 1622922923 180 NAGHWIHAERPQDFI-DAIRGFL 201
Cdd:COG1647   219 DSGHVITLDKDREEVaEEILDFL 241
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 20-50 1.79e-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: 38.21  E-value: 1.79e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1622922923  20 VPCVVVGHSMGGRTAMLLALQRPELVERLIA 50
Cdd:pfam00756 110 DGRALAGQSMGGLGALYLALKYPDLFGSVSS 140
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 21-51 2.05e-03

Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.


Pssm-ID: 214008  Cd Length: 280  Bit Score: 37.98  E-value: 2.05e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1622922923  21 PCVVVGHSMGGRTAMLLALQRPELVERLIAV 51
Cdd:cd12809   172 PAILITHSQGGPFGWLAADARPDLVKAIVAI 202
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
24-44 9.50e-03

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 35.96  E-value: 9.50e-03
                          10        20
                  ....*....|....*....|.
gi 1622922923  24 VVGHSMGGRTAMLLALQRPEL 44
Cdd:COG0627   117 IAGLSMGGHGALTLALRHPDL 137
 
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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