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Conserved domains on  [gi|614458179|ref|NP_001096640|]
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arylacetamide deacetylase-like 3 [Homo sapiens]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11171394)

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

Gene Ontology:  GO:0016787
PubMed:  12369917|19508187

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
115-378 2.66e-51

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


:

Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 171.24  E-value: 2.66e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179  115 IVYYHGGGGVMGSLKTHHGICSRLCKESDSVVLAVGYRKLPKHKFPVPVRDCLVATIHFLKSLDAYGVDPARVVVCGDSF 194
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179  195 GGAIAAVVCQQLVDRpDLPRIRAQILIYAilqALDLQTPSFQQRKNIPLltwsficyfffqnldfssswqevimKGAHLP 274
Cdd:pfam07859  81 GGNLAAAVALRARDE-GLPKPAGQVLIYP---GTDLRTESPSYLAREFA-------------------------DGPLLT 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179  275 AEVWEKYRKwlgpeniperfkergyqlkphepmneaAYLEVSVVLDVMCSPLIAEDdiVSQLPETCIVSCEYDALRDNSL 354
Cdd:pfam07859 132 RAAMDWFWR---------------------------LYLPGADRDDPLASPLFASD--LSGLPPALVVVAEFDPLRDEGE 182
                         250       260
                  ....*....|....*....|....
gi 614458179  355 LYKKRLEDLGVPVTWHHMEDGFHG 378
Cdd:pfam07859 183 AYAERLRAAGVPVELIEYPGMPHG 206
 
Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
115-378 2.66e-51

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


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 171.24  E-value: 2.66e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179  115 IVYYHGGGGVMGSLKTHHGICSRLCKESDSVVLAVGYRKLPKHKFPVPVRDCLVATIHFLKSLDAYGVDPARVVVCGDSF 194
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179  195 GGAIAAVVCQQLVDRpDLPRIRAQILIYAilqALDLQTPSFQQRKNIPLltwsficyfffqnldfssswqevimKGAHLP 274
Cdd:pfam07859  81 GGNLAAAVALRARDE-GLPKPAGQVLIYP---GTDLRTESPSYLAREFA-------------------------DGPLLT 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179  275 AEVWEKYRKwlgpeniperfkergyqlkphepmneaAYLEVSVVLDVMCSPLIAEDdiVSQLPETCIVSCEYDALRDNSL 354
Cdd:pfam07859 132 RAAMDWFWR---------------------------LYLPGADRDDPLASPLFASD--LSGLPPALVVVAEFDPLRDEGE 182
                         250       260
                  ....*....|....*....|....
gi 614458179  355 LYKKRLEDLGVPVTWHHMEDGFHG 378
Cdd:pfam07859 183 AYAERLRAAGVPVELIEYPGMPHG 206
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
101-405 3.40e-44

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 152.33  E-value: 3.40e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179 101 LYQPKASTcTLKPGIVYYHGGGGVMGSLKTHHGICSRLCKESDSVVLAVGYRKLPKHKFPVPVRDCLVATIHFLKSLDAY 180
Cdd:COG0657    3 VYRPAGAK-GPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179 181 GVDPARVVVCGDSFGGAIAAVVCQQLVDRpDLPRIRAQILIYAilqaldlqtpsfqqrkniplltwsficyfffqnldfs 260
Cdd:COG0657   82 GIDPDRIAVAGDSAGGHLAAALALRARDR-GGPRPAAQVLIYP------------------------------------- 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179 261 sswqevimkgahlpaevwekyrkwlgpeniperfkergyqlkphepmneaaylevsvVLDVMCSPLIAEddiVSQLPETC 340
Cdd:COG0657  124 ---------------------------------------------------------VLDLTASPLRAD---LAGLPPTL 143
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 614458179 341 IVSCEYDALRDNSLLYKKRLEDLGVPVTWHHMEDGFHGvlrtiDMSFLHFPCSMRILSALVQFVK 405
Cdd:COG0657  144 IVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHG-----FGLLAGLPEARAALAEIAAFLR 203
PRK10162 PRK10162
acetyl esterase;
93-390 3.98e-19

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 87.47  E-value: 3.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179  93 RFGTIPVKLYQPKASTctlKPGIVYYHGGGGVMGSLKTHHGICSRLCKESDSVVLAVGYRKLPKHKFPVPVRDCLVATIH 172
Cdd:PRK10162  65 PYGQVETRLYYPQPDS---QATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCY 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179 173 FLKSLDAYGVDPARVVVCGDSFGGAIAAVVCQQLVDRP-DLPRIRAQILIYAILQALDlqtpsfqqrkniplltwsficy 251
Cdd:PRK10162 142 FHQHAEDYGINMSRIGFAGDSAGAMLALASALWLRDKQiDCGKVAGVLLWYGLYGLRD---------------------- 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179 252 fffqnldfSSSWQevimkgahLPAEVWEKYRKwlgpenipERFKergyqlkphepMNEAAYLEvsvvldvmcSPLIAE-- 329
Cdd:PRK10162 200 --------SVSRR--------LLGGVWDGLTQ--------QDLQ-----------MYEEAYLS---------NDADREsp 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 614458179 330 ------DDIVSQLPETCIVSCEYDALRDNSLLYKKRLEDLGVPVTWHHMEDGFHGvlrtidmsFLHF 390
Cdd:PRK10162 236 yyclfnNDLTRDVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHA--------FLHY 294
 
Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
115-378 2.66e-51

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


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 171.24  E-value: 2.66e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179  115 IVYYHGGGGVMGSLKTHHGICSRLCKESDSVVLAVGYRKLPKHKFPVPVRDCLVATIHFLKSLDAYGVDPARVVVCGDSF 194
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179  195 GGAIAAVVCQQLVDRpDLPRIRAQILIYAilqALDLQTPSFQQRKNIPLltwsficyfffqnldfssswqevimKGAHLP 274
Cdd:pfam07859  81 GGNLAAAVALRARDE-GLPKPAGQVLIYP---GTDLRTESPSYLAREFA-------------------------DGPLLT 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179  275 AEVWEKYRKwlgpeniperfkergyqlkphepmneaAYLEVSVVLDVMCSPLIAEDdiVSQLPETCIVSCEYDALRDNSL 354
Cdd:pfam07859 132 RAAMDWFWR---------------------------LYLPGADRDDPLASPLFASD--LSGLPPALVVVAEFDPLRDEGE 182
                         250       260
                  ....*....|....*....|....
gi 614458179  355 LYKKRLEDLGVPVTWHHMEDGFHG 378
Cdd:pfam07859 183 AYAERLRAAGVPVELIEYPGMPHG 206
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
101-405 3.40e-44

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 152.33  E-value: 3.40e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179 101 LYQPKASTcTLKPGIVYYHGGGGVMGSLKTHHGICSRLCKESDSVVLAVGYRKLPKHKFPVPVRDCLVATIHFLKSLDAY 180
Cdd:COG0657    3 VYRPAGAK-GPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179 181 GVDPARVVVCGDSFGGAIAAVVCQQLVDRpDLPRIRAQILIYAilqaldlqtpsfqqrkniplltwsficyfffqnldfs 260
Cdd:COG0657   82 GIDPDRIAVAGDSAGGHLAAALALRARDR-GGPRPAAQVLIYP------------------------------------- 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179 261 sswqevimkgahlpaevwekyrkwlgpeniperfkergyqlkphepmneaaylevsvVLDVMCSPLIAEddiVSQLPETC 340
Cdd:COG0657  124 ---------------------------------------------------------VLDLTASPLRAD---LAGLPPTL 143
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 614458179 341 IVSCEYDALRDNSLLYKKRLEDLGVPVTWHHMEDGFHGvlrtiDMSFLHFPCSMRILSALVQFVK 405
Cdd:COG0657  144 IVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHG-----FGLLAGLPEARAALAEIAAFLR 203
PRK10162 PRK10162
acetyl esterase;
93-390 3.98e-19

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 87.47  E-value: 3.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179  93 RFGTIPVKLYQPKASTctlKPGIVYYHGGGGVMGSLKTHHGICSRLCKESDSVVLAVGYRKLPKHKFPVPVRDCLVATIH 172
Cdd:PRK10162  65 PYGQVETRLYYPQPDS---QATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCY 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179 173 FLKSLDAYGVDPARVVVCGDSFGGAIAAVVCQQLVDRP-DLPRIRAQILIYAILQALDlqtpsfqqrkniplltwsficy 251
Cdd:PRK10162 142 FHQHAEDYGINMSRIGFAGDSAGAMLALASALWLRDKQiDCGKVAGVLLWYGLYGLRD---------------------- 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179 252 fffqnldfSSSWQevimkgahLPAEVWEKYRKwlgpenipERFKergyqlkphepMNEAAYLEvsvvldvmcSPLIAE-- 329
Cdd:PRK10162 200 --------SVSRR--------LLGGVWDGLTQ--------QDLQ-----------MYEEAYLS---------NDADREsp 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 614458179 330 ------DDIVSQLPETCIVSCEYDALRDNSLLYKKRLEDLGVPVTWHHMEDGFHGvlrtidmsFLHF 390
Cdd:PRK10162 236 yyclfnNDLTRDVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHA--------FLHY 294
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
96-238 4.08e-06

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 47.70  E-value: 4.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179  96 TIPVKLYQPKASTctLKPGIVYYHGGGGvmGSLKTHHGICSRLCKEsDSVVLAVGYR---KLPKHKFPVPVRDCLVAtIH 172
Cdd:COG1506    9 TLPGWLYLPADGK--KYPVVVYVHGGPG--SRDDSFLPLAQALASR-GYAVLAPDYRgygESAGDWGGDEVDDVLAA-ID 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 614458179 173 FLKSLDayGVDPARVVVCGDSFGGAIAAVVcqqLVDRPDlpRIRAQILIYAI--LQALDLQTPSFQQR 238
Cdd:COG1506   83 YLAARP--YVDPDRIGIYGHSYGGYMALLA---AARHPD--RFKAAVALAGVsdLRSYYGTTREYTER 143
Axe1 COG3458
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, ...
113-222 6.76e-05

Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442681 [Multi-domain]  Cd Length: 318  Bit Score: 44.41  E-value: 6.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179 113 PGIVYYHG-GGG------------------VMGSlkthHGICSRLCKESDSVVLAVG-----------------YRKLpk 156
Cdd:COG3458   83 PAVVEFHGyGGGrglphedldwaaagyavlVMDT----RGQGSSWGDTPDPGGYSGGalpgymtrgiddpdtyyYRRV-- 156
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 614458179 157 hkfpvpVRDCLVAtIHFLKSLDayGVDPARVVVCGDSFGGAIAAVVCqQLVdrpdlPRIRAQILIY 222
Cdd:COG3458  157 ------YLDAVRA-VDALRSLP--EVDGKRIGVTGGSQGGGLALAAA-ALD-----PRVKAAAADV 207
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
95-221 9.27e-05

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 43.42  E-value: 9.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179  95 GTIPVKLYQPKASTctLKPGIVYYHGGGGVmgslkTHH--GICSRLCKEsDSVVLAV---GYRKLPKH---------KFP 160
Cdd:COG0412   14 VTLPGYLARPAGGG--PRPGVVVLHEIFGL-----NPHirDVARRLAAA-GYVVLAPdlyGRGGPGDDpdearalmgALD 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 614458179 161 VP-VRDCLVATIHFLKSLDayGVDPARVVVCGDSFGGAIA-----------AVVC----QQLVDRPDL-PRIRAQILI 221
Cdd:COG0412   86 PElLAADLRAALDWLKAQP--EVDAGRVGVVGFCFGGGLAllaaargpdlaAAVSfyggLPADDLLDLaARIKAPVLL 161
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
95-246 1.88e-04

Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 43.07  E-value: 1.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179  95 GTIPVKLYQPKASTCTLKPG-IVYYHGGGGVMGSLKTHhgicSRLCKESDS----VVLAVGYRKLPKHKFPVPVRDCLVA 169
Cdd:COG3509   35 GTRTYRLYVPAGYDGGAPLPlVVALHGCGGSAADFAAG----TGLNALADRegfiVVYPEGTGRAPGRCWNWFDGRDQRR 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179 170 TI---HFLKSL-----DAYGVDPARVVVCGDSFGGAIAAVVcqqLVDRPDlpRIRAqILIYAILQALDLQTPSFQQRKNI 241
Cdd:COG3509  111 GRddvAFIAALvddlaARYGIDPKRVYVTGLSAGGAMAYRL---ACEYPD--VFAA-VAPVAGLPYGAASDAACAPGRPV 184

                 ....*
gi 614458179 242 PLLTW 246
Cdd:COG3509  185 PVLVI 189
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
101-221 1.40e-03

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 39.90  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614458179 101 LYQPKASTCTlKPGIVYYHGGGGVmgslKTHHGICSRLCKESDSVVLAVGYR------KLPKHKFPVPVRDcLVATIHFL 174
Cdd:COG1073   27 LYLPAGASKK-YPAVVVAHGNGGV----KEQRALYAQRLAELGFNVLAFDYRgygeseGEPREEGSPERRD-ARAAVDYL 100
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 614458179 175 KSLDayGVDPARVVVCGDSFGGAIAAVVCQQlvdrpdLPRIRAQILI 221
Cdd:COG1073  101 RTLP--GVDPERIGLLGISLGGGYALNAAAT------DPRVKAVILD 139
 
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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